P78559 · MAP1A_HUMAN
- ProteinMicrotubule-associated protein 1A
- GeneMAP1A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2803 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Structural protein involved in the filamentous cross-bridging between microtubules and other skeletal elements.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMicrotubule-associated protein 1A
- Short namesMAP-1A
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP78559
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_039705 | 72 | in dbSNP:rs2584695 | |||
Sequence: F → L | ||||||
Natural variant | VAR_039706 | 335 | in dbSNP:rs1060935 | |||
Sequence: A → S | ||||||
Natural variant | VAR_039707 | 336 | in dbSNP:rs1060936 | |||
Sequence: K → T | ||||||
Natural variant | VAR_039708 | 353 | in dbSNP:rs1060937 | |||
Sequence: A → S | ||||||
Natural variant | VAR_039709 | 357 | in dbSNP:rs1060938 | |||
Sequence: A → S | ||||||
Natural variant | VAR_039710 | 364 | in dbSNP:rs2602129 | |||
Sequence: K → Q | ||||||
Natural variant | VAR_039711 | 485 | in dbSNP:rs2584715 | |||
Sequence: K → Q | ||||||
Natural variant | VAR_039712 | 830 | in dbSNP:rs3803337 | |||
Sequence: T → A | ||||||
Natural variant | VAR_039713 | 1078 | in dbSNP:rs8034794 | |||
Sequence: N → S | ||||||
Natural variant | VAR_039714 | 1102 | in dbSNP:rs8036179 | |||
Sequence: I → T | ||||||
Natural variant | VAR_039715 | 1185 | in dbSNP:rs3803335 | |||
Sequence: R → H | ||||||
Natural variant | VAR_039716 | 1245 | in dbSNP:rs12912505 | |||
Sequence: D → N | ||||||
Natural variant | VAR_039717 | 1461 | in dbSNP:rs2245715 | |||
Sequence: D → N | ||||||
Natural variant | VAR_039718 | 1553 | in dbSNP:rs2584717 | |||
Sequence: Q → H | ||||||
Natural variant | VAR_039719 | 1605 | in dbSNP:rs2584697 | |||
Sequence: K → N | ||||||
Natural variant | VAR_039720 | 1650 | in dbSNP:rs1060943 | |||
Sequence: W → C | ||||||
Natural variant | VAR_039721 | 1690 | in dbSNP:rs1060946 | |||
Sequence: A → S | ||||||
Natural variant | VAR_039722 | 1827 | in dbSNP:rs2229014 | |||
Sequence: P → A | ||||||
Natural variant | VAR_039723 | 1881 | in dbSNP:rs1060950 | |||
Sequence: A → P | ||||||
Natural variant | VAR_039724 | 1912 | in dbSNP:rs2584718 | |||
Sequence: A → V | ||||||
Natural variant | VAR_039725 | 1938 | in dbSNP:rs2584719 | |||
Sequence: S → R | ||||||
Natural variant | VAR_039726 | 2056 | in dbSNP:rs1060953 | |||
Sequence: S → R | ||||||
Natural variant | VAR_039727 | 2214 | in dbSNP:rs1060955 | |||
Sequence: H → Y | ||||||
Natural variant | VAR_039728 | 2327 | in dbSNP:rs8026745 | |||
Sequence: D → V | ||||||
Natural variant | VAR_059432 | 2405 | in dbSNP:rs8027254 | |||
Sequence: T → I | ||||||
Natural variant | VAR_056122 | 2461 | in dbSNP:rs8028849 | |||
Sequence: I → T | ||||||
Natural variant | VAR_059433 | 2465 | in dbSNP:rs8027916 | |||
Sequence: D → N |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,915 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000418376 | 1-2566 | UniProt | MAP1A heavy chain | |||
Sequence: MDGVAEFSEYVSETVDVPSPFDLLEPPTSGGFLKLSKPCCYIFPGGRGDSALFAVNGFNILVDGGSDRKSCFWKLVRHLDRIDSVLLTHIGADNLPGINGLLQRKVAELEEEQSQGSSSYSDWVKNLISPELGVVFFNVPEKLRLPDASRKAKRSIEEACLTLQHLNRLGIQAEPLYRVVSNTIEPLTLFHKMGVGRLDMYVLNPVKDSKEMQFLMQKWAGNSKAKTGIVLPNGKEAEISVPYLTSITALVVWLPANPTEKIVRVLFPGNAPQNKILEGLEKLRHLDFLRYPVATQKDLASGAVPTNLKPSKIKQRADSKESLKATTKTAVSKLAKREEVVEEGAKEARSELAKELAKTEKKAKESSEKPPEKPAKPERVKTESSEALKAEKRKLIKDKVGKKHLKEKISKLEEKKDKEKKEIKKERKELKKDEGRKEEKKDAKKEEKRKDTKPELKKISKPDLKPFTPEVRKTLYKAKVPGRVKIDRSRAIRGEKELSSEPQTPPAQKGTVPLPTISGHRELVLSSPEDLTQDFEEMKREERALLAEQRDTGLGDKPFPLDTAEEGPPSTAIQGTPPSVPGLGQEEHVMKEKELVPEVPEEQGSKDRGLDSGAETEEEKDTWEEKKQREAERLPDRTEAREESEPEVKEDVIEKAELEEMEEVHPSDEEEEDATKAEGFYQKHMQEPLKVTPRSREAFGGRELGLQGKAPEKETSLFLSSLTTPAGATEHVSYIQDETIPGYSETEQTISDEEIHDEPEERPAPPRFHTSTYDLPGPEGAGPFEASQPADSAVPATSGKVYGTPETELTYPTNIVAAPLAEEEHVSSATSITECDKLSSFATSVAEDQSVASLTAPQTEETGKSSLLLDTVTSIPSSRTEATQGLDYVPSAGTISPTSSLEEDKGFKSPPCEDFSVTGESEKRGEIIGKGLSGERAVEEEEEETANVEMSEKLCSQYGTPVFSAPGHALHPGEPALGEAEERCLSPDDSTVKMASPPPSGPPSATHTPFHQSPVEEKSEPQDFQEADSWGDTKRTPGVGKEDAAEETVKPGPEEGTLEKEEKVPPPRSPQAQEAPVNIDEGLTGCTIQLLPAQDKAIVFEIMEAGEPTGPILGAEALPGGLRTLPQEPGKPQKDEVLRYPDRSLSPEDAESLSVLSVPSPDTANQEPTPKSPCGLTEQYLHKDRWPEVSPEDTQSLSLSEESPSKETSLDVSSKQLSPESLGTLQFGELNLGKEEMGHLMQAEDTSHHTAPMSVPEPHAATASPPTDGTTRYSAQTDITDDSLDRKSPASSFSHSTPSGNGKYLPGAITSPDEHILTPDSSFSKSPESLPGPALEDIAIKWEDKVPGLKDRTSEQKKEPEPKDEVLQQKDKTLEHKEVVEPKDTAIYQKDEALHVKNEAVKQQDKALEQKGRDLEQKDTALEQKDKALEPKDKDLEEKDKALEQKDKIPEEKDKALEQKDTALEQKDKALEPKDKDLEQKDRVLEQKEKIPEEKDKALDQKVRSVEHKAPEDTVAEMKDRDLEQTDKAPEQKHQAQEQKDKVSEKKDQALEQKYWALGQKDEALEQNIQALEENHQTQEQESLVQEDKTRKPKMLEEKSPEKVKAMEEKLEALLEKTKALGLEESLVQEGRAREQEEKYWRGQDVVQEWQETSPTREEPAGEQKELAPAWEDTSPEQDNRYWRGREDVALEQDTYWRELSCERKVWFPHELDGQGARPHYTEERESTFLDEGPDDEQEVPLREHATRSPWASDFKDFQESSPQKGLEVERWLAESPVGLPPEEEDKLTRSPFEIISPPASPPEMVGQRVPSAPGQESPIPDPKLMPHMKNEPTTPSWLADIPPWVPKDRPLPPAPLSPAPGPPTPAPESHTPAPFSWGTAEYDSVVAAVQEGAAELEGGPYSPLGKDYRKAEGEREEEGRAEAPDKSSHSSKVPEASKSHATTEPEQTEPEQREPTPYPDERSFQYADIYEQMMLTGLGPACPTREPPLGAAGDWPPCLSTKEAAAGRNTSAEKELSSPISPKSLQSDTPTFSYAALAGPTVPPRPEPGPSMEPSLTPPAVPPRAPILSKGPSPPLNGNILSCSPDRRSPSPKESGRSHWDDSTSDSELEKGAREQPEKEAQSPSPPHPIPMGSPTLWPETEAHVSPPLDSHLGPARPSLDFPASAFGFSSLQPAPPQLPSPAEPRSAPCGSLAFSGDRALALAPGPPTRTRHDEYLEVTKAPSLDSSLPQLPSPSSPGAPLLSNLPRPASPALSEGSSSEATTPVISSVAERFSPSLEAAEQESGELDPGMEPAAHSLWDLTPLSPAPPASLDLALAPAPSLPGDMGDGILPCHLECSEAATEKPSPFQVPSEDCAANGPTETSPNPPGPAPAKAENEEAAACPAWERGAWPEGAERSSRPDTLLSPEQPVCPAGGSGGPPSSASPEVEAGPQGCATEPRPHRGELSPSFLNPPLPPSIDDRDLSTEEVRLVGRGGRRRVGGPGTTGGPCPVTDETPPTSASDSGSSQSDSDVPPETEECPSITAEAALDSDEDGDFLPVDKAGGVSGTHHPRPGHDPPPLPQP | |||||||
Chain | PRO_0000018600 | 1-2803 | UniProt | Microtubule-associated protein 1A | |||
Sequence: MDGVAEFSEYVSETVDVPSPFDLLEPPTSGGFLKLSKPCCYIFPGGRGDSALFAVNGFNILVDGGSDRKSCFWKLVRHLDRIDSVLLTHIGADNLPGINGLLQRKVAELEEEQSQGSSSYSDWVKNLISPELGVVFFNVPEKLRLPDASRKAKRSIEEACLTLQHLNRLGIQAEPLYRVVSNTIEPLTLFHKMGVGRLDMYVLNPVKDSKEMQFLMQKWAGNSKAKTGIVLPNGKEAEISVPYLTSITALVVWLPANPTEKIVRVLFPGNAPQNKILEGLEKLRHLDFLRYPVATQKDLASGAVPTNLKPSKIKQRADSKESLKATTKTAVSKLAKREEVVEEGAKEARSELAKELAKTEKKAKESSEKPPEKPAKPERVKTESSEALKAEKRKLIKDKVGKKHLKEKISKLEEKKDKEKKEIKKERKELKKDEGRKEEKKDAKKEEKRKDTKPELKKISKPDLKPFTPEVRKTLYKAKVPGRVKIDRSRAIRGEKELSSEPQTPPAQKGTVPLPTISGHRELVLSSPEDLTQDFEEMKREERALLAEQRDTGLGDKPFPLDTAEEGPPSTAIQGTPPSVPGLGQEEHVMKEKELVPEVPEEQGSKDRGLDSGAETEEEKDTWEEKKQREAERLPDRTEAREESEPEVKEDVIEKAELEEMEEVHPSDEEEEDATKAEGFYQKHMQEPLKVTPRSREAFGGRELGLQGKAPEKETSLFLSSLTTPAGATEHVSYIQDETIPGYSETEQTISDEEIHDEPEERPAPPRFHTSTYDLPGPEGAGPFEASQPADSAVPATSGKVYGTPETELTYPTNIVAAPLAEEEHVSSATSITECDKLSSFATSVAEDQSVASLTAPQTEETGKSSLLLDTVTSIPSSRTEATQGLDYVPSAGTISPTSSLEEDKGFKSPPCEDFSVTGESEKRGEIIGKGLSGERAVEEEEEETANVEMSEKLCSQYGTPVFSAPGHALHPGEPALGEAEERCLSPDDSTVKMASPPPSGPPSATHTPFHQSPVEEKSEPQDFQEADSWGDTKRTPGVGKEDAAEETVKPGPEEGTLEKEEKVPPPRSPQAQEAPVNIDEGLTGCTIQLLPAQDKAIVFEIMEAGEPTGPILGAEALPGGLRTLPQEPGKPQKDEVLRYPDRSLSPEDAESLSVLSVPSPDTANQEPTPKSPCGLTEQYLHKDRWPEVSPEDTQSLSLSEESPSKETSLDVSSKQLSPESLGTLQFGELNLGKEEMGHLMQAEDTSHHTAPMSVPEPHAATASPPTDGTTRYSAQTDITDDSLDRKSPASSFSHSTPSGNGKYLPGAITSPDEHILTPDSSFSKSPESLPGPALEDIAIKWEDKVPGLKDRTSEQKKEPEPKDEVLQQKDKTLEHKEVVEPKDTAIYQKDEALHVKNEAVKQQDKALEQKGRDLEQKDTALEQKDKALEPKDKDLEEKDKALEQKDKIPEEKDKALEQKDTALEQKDKALEPKDKDLEQKDRVLEQKEKIPEEKDKALDQKVRSVEHKAPEDTVAEMKDRDLEQTDKAPEQKHQAQEQKDKVSEKKDQALEQKYWALGQKDEALEQNIQALEENHQTQEQESLVQEDKTRKPKMLEEKSPEKVKAMEEKLEALLEKTKALGLEESLVQEGRAREQEEKYWRGQDVVQEWQETSPTREEPAGEQKELAPAWEDTSPEQDNRYWRGREDVALEQDTYWRELSCERKVWFPHELDGQGARPHYTEERESTFLDEGPDDEQEVPLREHATRSPWASDFKDFQESSPQKGLEVERWLAESPVGLPPEEEDKLTRSPFEIISPPASPPEMVGQRVPSAPGQESPIPDPKLMPHMKNEPTTPSWLADIPPWVPKDRPLPPAPLSPAPGPPTPAPESHTPAPFSWGTAEYDSVVAAVQEGAAELEGGPYSPLGKDYRKAEGEREEEGRAEAPDKSSHSSKVPEASKSHATTEPEQTEPEQREPTPYPDERSFQYADIYEQMMLTGLGPACPTREPPLGAAGDWPPCLSTKEAAAGRNTSAEKELSSPISPKSLQSDTPTFSYAALAGPTVPPRPEPGPSMEPSLTPPAVPPRAPILSKGPSPPLNGNILSCSPDRRSPSPKESGRSHWDDSTSDSELEKGAREQPEKEAQSPSPPHPIPMGSPTLWPETEAHVSPPLDSHLGPARPSLDFPASAFGFSSLQPAPPQLPSPAEPRSAPCGSLAFSGDRALALAPGPPTRTRHDEYLEVTKAPSLDSSLPQLPSPSSPGAPLLSNLPRPASPALSEGSSSEATTPVISSVAERFSPSLEAAEQESGELDPGMEPAAHSLWDLTPLSPAPPASLDLALAPAPSLPGDMGDGILPCHLECSEAATEKPSPFQVPSEDCAANGPTETSPNPPGPAPAKAENEEAAACPAWERGAWPEGAERSSRPDTLLSPEQPVCPAGGSGGPPSSASPEVEAGPQGCATEPRPHRGELSPSFLNPPLPPSIDDRDLSTEEVRLVGRGGRRRVGGPGTTGGPCPVTDETPPTSASDSGSSQSDSDVPPETEECPSITAEAALDSDEDGDFLPVDKAGGVSGTHHPRPGHDPPPLPQPDPRPSPPRPDVCMADPEGLSSESGRVERLREKEKVQGRVGRRAPGKAKPASPARRLDLRGKRSPTPGKGPADRASRAPPRPRSTTSQVTPAEEKDGHSPMSKGLVNGLKAGPMALSSKGSSGAPVYVDLAYIPNHCSGKTADLDFFRRVRASYYVVSGNDPANGEPSRAVLDALLEGKAQWGENLQVTLIPTHDTEVTREWYQQTHEQQQQLNVLVLASSSTVVMQDESFPACKIEF | |||||||
Modified residue | 114 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 114 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 117 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 117 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 118 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 118 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 121 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 121 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 155 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 177 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 177 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 319 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 319 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 322 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 322 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 384 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 384 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 468 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 500 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 504 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 504 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 526 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 526 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 527 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 527 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 532 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 576 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 579 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 605 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 605 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 612 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 612 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 616 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 616 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 622 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 644 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 644 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 667 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 667 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 675 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 751 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 787 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 874 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 874 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 877 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 878 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 891 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 891 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 894 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 896 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 896 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 898 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 899 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 900 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 900 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 909 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 909 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 921 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 960 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 986 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 986 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 990 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 996 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 996 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1000 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1004 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1004 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1006 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1013 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1013 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1019 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1029 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1029 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1036 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1069 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1069 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1084 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1144 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1146 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1146 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1152 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1154 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1157 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1160 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1160 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1163 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1169 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1172 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1172 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1190 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1190 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1196 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1198 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1200 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1200 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1203 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1203 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1205 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1209 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1209 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1213 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1218 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1218 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1221 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1221 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1224 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1262 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1264 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1264 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1267 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1280 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1283 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1288 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1291 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1310 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1311 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1318 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1321 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1322 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1324 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1326 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1326 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1329 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1329 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1544 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1600 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1600 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1626 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1626 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1653 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1654 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1654 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1656 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1674 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1675 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1675 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1682 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1701 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1749 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1749 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1753 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1761 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1762 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1762 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1776 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1776 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1789 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1791 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1791 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1797 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1797 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1801 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1801 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1812 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1812 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1818 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1818 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1834 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1835 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1837 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1931 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1957 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1957 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2012 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2018 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2019 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2022 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2022 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2056 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2058 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2058 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2074 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2074 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2083 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2085 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2090 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2092 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2104 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2104 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2105 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2106 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2106 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2108 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2108 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2182 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2188 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2197 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2217 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 2235 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2235 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2237 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2238 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2252 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2252 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2256 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2256 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2259 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2259 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2260 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2307 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2366 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2425 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2427 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2449 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2449 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2451 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000018601 | 2567-2803 | UniProt | MAP1 light chain LC2 | |||
Sequence: DPRPSPPRPDVCMADPEGLSSESGRVERLREKEKVQGRVGRRAPGKAKPASPARRLDLRGKRSPTPGKGPADRASRAPPRPRSTTSQVTPAEEKDGHSPMSKGLVNGLKAGPMALSSKGSSGAPVYVDLAYIPNHCSGKTADLDFFRRVRASYYVVSGNDPANGEPSRAVLDALLEGKAQWGENLQVTLIPTHDTEVTREWYQQTHEQQQQLNVLVLASSSTVVMQDESFPACKIEF | |||||||
Modified residue (large scale data) | 2617 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2629 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2649 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2649 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2650 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2655 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2664 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2664 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2667 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2686 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by CSNK1D.
LC2 is generated from MAP1A by proteolytic processing.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins. Interacts with TIAM2. Interacts with guanylate kinase-like domain of DLG1, DLG2, DLG4. Binds to CSNK1D (By similarity).
MAP1 light chain LC2: Interacts with ELAVL4 (By similarity).
MAP1 light chain LC2: Interacts with ELAVL4 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P78559 | DISC1 Q9NRI5 | 3 | EBI-929047, EBI-529989 | |
BINARY | P78559 | SHANK3 Q9BYB0 | 2 | EBI-929047, EBI-1752330 |
Protein-protein interaction databases
Miscellaneous
Family & Domains
Features
Showing features for region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 302-466 | Disordered | ||||
Sequence: GAVPTNLKPSKIKQRADSKESLKATTKTAVSKLAKREEVVEEGAKEARSELAKELAKTEKKAKESSEKPPEKPAKPERVKTESSEALKAEKRKLIKDKVGKKHLKEKISKLEEKKDKEKKEIKKERKELKKDEGRKEEKKDAKKEEKRKDTKPELKKISKPDLKP | ||||||
Compositional bias | 331-395 | Basic and acidic residues | ||||
Sequence: VSKLAKREEVVEEGAKEARSELAKELAKTEKKAKESSEKPPEKPAKPERVKTESSEALKAEKRKL | ||||||
Compositional bias | 402-466 | Basic and acidic residues | ||||
Sequence: KKHLKEKISKLEEKKDKEKKEIKKERKELKKDEGRKEEKKDAKKEEKRKDTKPELKKISKPDLKP | ||||||
Repeat | 415-417 | 1 | ||||
Sequence: KKD | ||||||
Region | 415-541 | 9 X 3 AA repeats of K-K-[DE] | ||||
Sequence: KKDKEKKEIKKERKELKKDEGRKEEKKDAKKEEKRKDTKPELKKISKPDLKPFTPEVRKTLYKAKVPGRVKIDRSRAIRGEKELSSEPQTPPAQKGTVPLPTISGHRELVLSSPEDLTQDFEEMKRE | ||||||
Repeat | 420-422 | 2 | ||||
Sequence: KKE | ||||||
Repeat | 427-429 | 3 | ||||
Sequence: RKE | ||||||
Repeat | 431-433 | 4 | ||||
Sequence: KKD | ||||||
Repeat | 436-438 | 5 | ||||
Sequence: RKE | ||||||
Repeat | 440-442 | 6 | ||||
Sequence: KKD | ||||||
Repeat | 444-446 | 7 | ||||
Sequence: KKE | ||||||
Repeat | 449-451 | 8 | ||||
Sequence: RKD | ||||||
Region | 486-516 | Disordered | ||||
Sequence: IDRSRAIRGEKELSSEPQTPPAQKGTVPLPT | ||||||
Repeat | 539-541 | 9 | ||||
Sequence: KRE | ||||||
Region | 539-712 | Disordered | ||||
Sequence: KREERALLAEQRDTGLGDKPFPLDTAEEGPPSTAIQGTPPSVPGLGQEEHVMKEKELVPEVPEEQGSKDRGLDSGAETEEEKDTWEEKKQREAERLPDRTEAREESEPEVKEDVIEKAELEEMEEVHPSDEEEEDATKAEGFYQKHMQEPLKVTPRSREAFGGRELGLQGKAPE | ||||||
Compositional bias | 586-662 | Basic and acidic residues | ||||
Sequence: EEHVMKEKELVPEVPEEQGSKDRGLDSGAETEEEKDTWEEKKQREAERLPDRTEAREESEPEVKEDVIEKAELEEME | ||||||
Region | 734-806 | Disordered | ||||
Sequence: YIQDETIPGYSETEQTISDEEIHDEPEERPAPPRFHTSTYDLPGPEGAGPFEASQPADSAVPATSGKVYGTPE | ||||||
Compositional bias | 847-903 | Polar residues | ||||
Sequence: EDQSVASLTAPQTEETGKSSLLLDTVTSIPSSRTEATQGLDYVPSAGTISPTSSLEE | ||||||
Region | 847-1080 | Disordered | ||||
Sequence: EDQSVASLTAPQTEETGKSSLLLDTVTSIPSSRTEATQGLDYVPSAGTISPTSSLEEDKGFKSPPCEDFSVTGESEKRGEIIGKGLSGERAVEEEEEETANVEMSEKLCSQYGTPVFSAPGHALHPGEPALGEAEERCLSPDDSTVKMASPPPSGPPSATHTPFHQSPVEEKSEPQDFQEADSWGDTKRTPGVGKEDAAEETVKPGPEEGTLEKEEKVPPPRSPQAQEAPVNID | ||||||
Compositional bias | 917-937 | Basic and acidic residues | ||||
Sequence: VTGESEKRGEIIGKGLSGERA | ||||||
Compositional bias | 1013-1067 | Basic and acidic residues | ||||
Sequence: SPVEEKSEPQDFQEADSWGDTKRTPGVGKEDAAEETVKPGPEEGTLEKEEKVPPP | ||||||
Region | 1109-1548 | Disordered | ||||
Sequence: TGPILGAEALPGGLRTLPQEPGKPQKDEVLRYPDRSLSPEDAESLSVLSVPSPDTANQEPTPKSPCGLTEQYLHKDRWPEVSPEDTQSLSLSEESPSKETSLDVSSKQLSPESLGTLQFGELNLGKEEMGHLMQAEDTSHHTAPMSVPEPHAATASPPTDGTTRYSAQTDITDDSLDRKSPASSFSHSTPSGNGKYLPGAITSPDEHILTPDSSFSKSPESLPGPALEDIAIKWEDKVPGLKDRTSEQKKEPEPKDEVLQQKDKTLEHKEVVEPKDTAIYQKDEALHVKNEAVKQQDKALEQKGRDLEQKDTALEQKDKALEPKDKDLEEKDKALEQKDKIPEEKDKALEQKDTALEQKDKALEPKDKDLEQKDRVLEQKEKIPEEKDKALDQKVRSVEHKAPEDTVAEMKDRDLEQTDKAPEQKHQAQEQKDKVSEKKD | ||||||
Compositional bias | 1129-1146 | Basic and acidic residues | ||||
Sequence: PGKPQKDEVLRYPDRSLS | ||||||
Compositional bias | 1150-1173 | Polar residues | ||||
Sequence: AESLSVLSVPSPDTANQEPTPKSP | ||||||
Compositional bias | 1191-1225 | Polar residues | ||||
Sequence: PEDTQSLSLSEESPSKETSLDVSSKQLSPESLGTL | ||||||
Compositional bias | 1264-1278 | Polar residues | ||||
Sequence: SPPTDGTTRYSAQTD | ||||||
Compositional bias | 1286-1304 | Polar residues | ||||
Sequence: RKSPASSFSHSTPSGNGKY | ||||||
Compositional bias | 1338-1548 | Basic and acidic residues | ||||
Sequence: IAIKWEDKVPGLKDRTSEQKKEPEPKDEVLQQKDKTLEHKEVVEPKDTAIYQKDEALHVKNEAVKQQDKALEQKGRDLEQKDTALEQKDKALEPKDKDLEEKDKALEQKDKIPEEKDKALEQKDTALEQKDKALEPKDKDLEQKDRVLEQKEKIPEEKDKALDQKVRSVEHKAPEDTVAEMKDRDLEQTDKAPEQKHQAQEQKDKVSEKKD | ||||||
Region | 1573-1605 | Disordered | ||||
Sequence: EENHQTQEQESLVQEDKTRKPKMLEEKSPEKVK | ||||||
Compositional bias | 1580-1605 | Basic and acidic residues | ||||
Sequence: EQESLVQEDKTRKPKMLEEKSPEKVK | ||||||
Region | 1632-1684 | Disordered | ||||
Sequence: RAREQEEKYWRGQDVVQEWQETSPTREEPAGEQKELAPAWEDTSPEQDNRYWR | ||||||
Compositional bias | 1656-1684 | Basic and acidic residues | ||||
Sequence: TREEPAGEQKELAPAWEDTSPEQDNRYWR | ||||||
Compositional bias | 1713-1728 | Basic and acidic residues | ||||
Sequence: DGQGARPHYTEEREST | ||||||
Region | 1713-1879 | Disordered | ||||
Sequence: DGQGARPHYTEERESTFLDEGPDDEQEVPLREHATRSPWASDFKDFQESSPQKGLEVERWLAESPVGLPPEEEDKLTRSPFEIISPPASPPEMVGQRVPSAPGQESPIPDPKLMPHMKNEPTTPSWLADIPPWVPKDRPLPPAPLSPAPGPPTPAPESHTPAPFSWG | ||||||
Compositional bias | 1846-1871 | Pro residues | ||||
Sequence: VPKDRPLPPAPLSPAPGPPTPAPESH | ||||||
Region | 1892-2673 | Disordered | ||||
Sequence: EGAAELEGGPYSPLGKDYRKAEGEREEEGRAEAPDKSSHSSKVPEASKSHATTEPEQTEPEQREPTPYPDERSFQYADIYEQMMLTGLGPACPTREPPLGAAGDWPPCLSTKEAAAGRNTSAEKELSSPISPKSLQSDTPTFSYAALAGPTVPPRPEPGPSMEPSLTPPAVPPRAPILSKGPSPPLNGNILSCSPDRRSPSPKESGRSHWDDSTSDSELEKGAREQPEKEAQSPSPPHPIPMGSPTLWPETEAHVSPPLDSHLGPARPSLDFPASAFGFSSLQPAPPQLPSPAEPRSAPCGSLAFSGDRALALAPGPPTRTRHDEYLEVTKAPSLDSSLPQLPSPSSPGAPLLSNLPRPASPALSEGSSSEATTPVISSVAERFSPSLEAAEQESGELDPGMEPAAHSLWDLTPLSPAPPASLDLALAPAPSLPGDMGDGILPCHLECSEAATEKPSPFQVPSEDCAANGPTETSPNPPGPAPAKAENEEAAACPAWERGAWPEGAERSSRPDTLLSPEQPVCPAGGSGGPPSSASPEVEAGPQGCATEPRPHRGELSPSFLNPPLPPSIDDRDLSTEEVRLVGRGGRRRVGGPGTTGGPCPVTDETPPTSASDSGSSQSDSDVPPETEECPSITAEAALDSDEDGDFLPVDKAGGVSGTHHPRPGHDPPPLPQPDPRPSPPRPDVCMADPEGLSSESGRVERLREKEKVQGRVGRRAPGKAKPASPARRLDLRGKRSPTPGKGPADRASRAPPRPRSTTSQVTPAEEKDGHSPMSKGLVNG | ||||||
Compositional bias | 1908-1934 | Basic and acidic residues | ||||
Sequence: DYRKAEGEREEEGRAEAPDKSSHSSKV | ||||||
Compositional bias | 1943-1959 | Basic and acidic residues | ||||
Sequence: TTEPEQTEPEQREPTPY | ||||||
Compositional bias | 2005-2035 | Polar residues | ||||
Sequence: AAAGRNTSAEKELSSPISPKSLQSDTPTFSY | ||||||
Compositional bias | 2042-2071 | Pro residues | ||||
Sequence: TVPPRPEPGPSMEPSLTPPAVPPRAPILSK | ||||||
Compositional bias | 2076-2090 | Polar residues | ||||
Sequence: PLNGNILSCSPDRRS | ||||||
Compositional bias | 2091-2119 | Basic and acidic residues | ||||
Sequence: PSPKESGRSHWDDSTSDSELEKGAREQPE | ||||||
Compositional bias | 2252-2272 | Polar residues | ||||
Sequence: SPALSEGSSSEATTPVISSVA | ||||||
Compositional bias | 2463-2477 | Basic and acidic residues | ||||
Sequence: DRDLSTEEVRLVGRG | ||||||
Compositional bias | 2494-2517 | Polar residues | ||||
Sequence: VTDETPPTSASDSGSSQSDSDVPP | ||||||
Compositional bias | 2555-2577 | Pro residues | ||||
Sequence: RPGHDPPPLPQPDPRPSPPRPDV | ||||||
Compositional bias | 2587-2606 | Basic and acidic residues | ||||
Sequence: SESGRVERLREKEKVQGRVG |
Domain
The basic region containing the repeats may be responsible for the binding of MAP1A to microtubules.
Sequence similarities
Belongs to the MAP1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P78559-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length2,803
- Mass (Da)305,485
- Last updated2010-11-30 v6
- Checksum94733902420F1FFE
P78559-2
- Name2
- Differences from canonical
- 2752-2752: Q → QSV
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9PGC8 | E9PGC8_HUMAN | MAP1A | 3041 |
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 134-135 | in Ref. 5; CAA87104 | ||||
Sequence: VV → IP | ||||||
Sequence conflict | 249 | in Ref. 5; CAA87104 | ||||
Sequence: A → G | ||||||
Sequence conflict | 263 | in Ref. 5; CAA87104 | ||||
Sequence: V → A | ||||||
Sequence conflict | 296 | in Ref. 4; AAD00355 | ||||
Sequence: Q → H | ||||||
Sequence conflict | 311 | in Ref. 5; CAA87104 | ||||
Sequence: S → G | ||||||
Sequence conflict | 324 | in Ref. 4; AAD00355 | ||||
Sequence: K → Q | ||||||
Compositional bias | 331-395 | Basic and acidic residues | ||||
Sequence: VSKLAKREEVVEEGAKEARSELAKELAKTEKKAKESSEKPPEKPAKPERVKTESSEALKAEKRKL | ||||||
Compositional bias | 402-466 | Basic and acidic residues | ||||
Sequence: KKHLKEKISKLEEKKDKEKKEIKKERKELKKDEGRKEEKKDAKKEEKRKDTKPELKKISKPDLKP | ||||||
Sequence conflict | 414-419 | in Ref. 5; CAA87104 | ||||
Sequence: EKKDKE → KKKRNS | ||||||
Sequence conflict | 424 | in Ref. 1; AAB41132/AAB41133 | ||||
Sequence: K → P | ||||||
Sequence conflict | 426 | in Ref. 4; AAD00355 | ||||
Sequence: E → D | ||||||
Sequence conflict | 431 | in Ref. 4; AAD00355 | ||||
Sequence: K → Q | ||||||
Sequence conflict | 439 | in Ref. 4; AAD00355 | ||||
Sequence: E → D | ||||||
Sequence conflict | 444 | in Ref. 4; AAD00355 | ||||
Sequence: K → R | ||||||
Sequence conflict | 452-453 | in Ref. 4; AAD00355 | ||||
Sequence: TK → SS | ||||||
Sequence conflict | 457 | in Ref. 4; AAD00355 | ||||
Sequence: K → R | ||||||
Compositional bias | 586-662 | Basic and acidic residues | ||||
Sequence: EEHVMKEKELVPEVPEEQGSKDRGLDSGAETEEEKDTWEEKKQREAERLPDRTEAREESEPEVKEDVIEKAELEEME | ||||||
Sequence conflict | 682 | in Ref. 1; AAB41132/AAB41133 | ||||
Sequence: Q → P | ||||||
Compositional bias | 847-903 | Polar residues | ||||
Sequence: EDQSVASLTAPQTEETGKSSLLLDTVTSIPSSRTEATQGLDYVPSAGTISPTSSLEE | ||||||
Compositional bias | 917-937 | Basic and acidic residues | ||||
Sequence: VTGESEKRGEIIGKGLSGERA | ||||||
Compositional bias | 1013-1067 | Basic and acidic residues | ||||
Sequence: SPVEEKSEPQDFQEADSWGDTKRTPGVGKEDAAEETVKPGPEEGTLEKEEKVPPP | ||||||
Sequence conflict | 1025 | in Ref. 1; AAB41132/AAB41133 | ||||
Sequence: Q → K | ||||||
Compositional bias | 1129-1146 | Basic and acidic residues | ||||
Sequence: PGKPQKDEVLRYPDRSLS | ||||||
Compositional bias | 1150-1173 | Polar residues | ||||
Sequence: AESLSVLSVPSPDTANQEPTPKSP | ||||||
Compositional bias | 1191-1225 | Polar residues | ||||
Sequence: PEDTQSLSLSEESPSKETSLDVSSKQLSPESLGTL | ||||||
Compositional bias | 1264-1278 | Polar residues | ||||
Sequence: SPPTDGTTRYSAQTD | ||||||
Compositional bias | 1286-1304 | Polar residues | ||||
Sequence: RKSPASSFSHSTPSGNGKY | ||||||
Sequence conflict | 1303-1313 | in Ref. 4; AAD00355 | ||||
Sequence: KYLPGAITSPD → EVLTWGDHQALN | ||||||
Sequence conflict | 1335-1341 | in Ref. 4; AAD00355 | ||||
Sequence: Missing | ||||||
Compositional bias | 1338-1548 | Basic and acidic residues | ||||
Sequence: IAIKWEDKVPGLKDRTSEQKKEPEPKDEVLQQKDKTLEHKEVVEPKDTAIYQKDEALHVKNEAVKQQDKALEQKGRDLEQKDTALEQKDKALEPKDKDLEEKDKALEQKDKIPEEKDKALEQKDTALEQKDKALEPKDKDLEQKDRVLEQKEKIPEEKDKALDQKVRSVEHKAPEDTVAEMKDRDLEQTDKAPEQKHQAQEQKDKVSEKKD | ||||||
Sequence conflict | 1368 | in Ref. 4; AAD00355 | ||||
Sequence: Q → T | ||||||
Sequence conflict | 1470 | in Ref. 4; AAD00355 | ||||
Sequence: A → T | ||||||
Compositional bias | 1580-1605 | Basic and acidic residues | ||||
Sequence: EQESLVQEDKTRKPKMLEEKSPEKVK | ||||||
Compositional bias | 1656-1684 | Basic and acidic residues | ||||
Sequence: TREEPAGEQKELAPAWEDTSPEQDNRYWR | ||||||
Compositional bias | 1713-1728 | Basic and acidic residues | ||||
Sequence: DGQGARPHYTEEREST | ||||||
Sequence conflict | 1714 | in Ref. 1; AAB41132/AAB41133 | ||||
Sequence: G → V | ||||||
Compositional bias | 1846-1871 | Pro residues | ||||
Sequence: VPKDRPLPPAPLSPAPGPPTPAPESH | ||||||
Sequence conflict | 1869 | in Ref. 6; AAA81362 | ||||
Sequence: E → A | ||||||
Sequence conflict | 1879-1883 | in Ref. 6; AAA81362 | ||||
Sequence: GTAEY → AHSRV | ||||||
Compositional bias | 1908-1934 | Basic and acidic residues | ||||
Sequence: DYRKAEGEREEEGRAEAPDKSSHSSKV | ||||||
Compositional bias | 1943-1959 | Basic and acidic residues | ||||
Sequence: TTEPEQTEPEQREPTPY | ||||||
Compositional bias | 2005-2035 | Polar residues | ||||
Sequence: AAAGRNTSAEKELSSPISPKSLQSDTPTFSY | ||||||
Compositional bias | 2042-2071 | Pro residues | ||||
Sequence: TVPPRPEPGPSMEPSLTPPAVPPRAPILSK | ||||||
Compositional bias | 2076-2090 | Polar residues | ||||
Sequence: PLNGNILSCSPDRRS | ||||||
Compositional bias | 2091-2119 | Basic and acidic residues | ||||
Sequence: PSPKESGRSHWDDSTSDSELEKGAREQPE | ||||||
Sequence conflict | 2118 | in Ref. 1; AAB41132/AAB41133 | ||||
Sequence: P → A | ||||||
Sequence conflict | 2174 | in Ref. 1; AAB41132/AAB41133 | ||||
Sequence: Q → E | ||||||
Compositional bias | 2252-2272 | Polar residues | ||||
Sequence: SPALSEGSSSEATTPVISSVA | ||||||
Compositional bias | 2463-2477 | Basic and acidic residues | ||||
Sequence: DRDLSTEEVRLVGRG | ||||||
Compositional bias | 2494-2517 | Polar residues | ||||
Sequence: VTDETPPTSASDSGSSQSDSDVPP | ||||||
Compositional bias | 2555-2577 | Pro residues | ||||
Sequence: RPGHDPPPLPQPDPRPSPPRPDV | ||||||
Compositional bias | 2587-2606 | Basic and acidic residues | ||||
Sequence: SESGRVERLREKEKVQGRVG | ||||||
Sequence conflict | 2613 | in Ref. 1; AAB41132/AAB41133 | ||||
Sequence: A → D | ||||||
Sequence conflict | 2616 | in Ref. 1; AAB41132/AAB41133 | ||||
Sequence: A → V | ||||||
Sequence conflict | 2636 | in Ref. 1; AAB41132/AAB41133 | ||||
Sequence: P → S | ||||||
Sequence conflict | 2640 | in Ref. 1; AAB41132/AAB41133 | ||||
Sequence: A → V | ||||||
Sequence conflict | 2647 | in Ref. 1; AAB41132/AAB41133 | ||||
Sequence: P → S | ||||||
Sequence conflict | 2702 | in Ref. 1; AAB41132/AAB41133 | ||||
Sequence: C → W | ||||||
Alternative sequence | VSP_040240 | 2752 | in isoform 2 | |||
Sequence: Q → QSV | ||||||
Sequence conflict | 2753 | In isoform P78559-2; in Ref. 1; AAB41132/AAB41133 | ||||
Sequence: S → V | ||||||
Sequence conflict | 2754 | In isoform P78559-2; in Ref. 1; AAB41132/AAB41133 | ||||
Sequence: V → K |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U38291 EMBL· GenBank· DDBJ | AAB41132.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U38292 EMBL· GenBank· DDBJ | AAB41133.1 EMBL· GenBank· DDBJ | mRNA | ||
AC019011 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AF200415 EMBL· GenBank· DDBJ | AAF08305.2 EMBL· GenBank· DDBJ | mRNA | ||
U80458 EMBL· GenBank· DDBJ | AAD00355.1 EMBL· GenBank· DDBJ | mRNA | ||
Z47038 EMBL· GenBank· DDBJ | CAA87104.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U14577 EMBL· GenBank· DDBJ | AAA81362.1 EMBL· GenBank· DDBJ | mRNA |