P27546 · MAP4_MOUSE
- ProteinMicrotubule-associated protein 4
- GeneMap4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1125 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Non-neuronal microtubule-associated protein. Promotes microtubule assembly.
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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Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | cytoplasm | |
Cellular Component | microtubule | |
Cellular Component | microtubule organizing center | |
Cellular Component | mitotic spindle | |
Cellular Component | neuron projection | |
Cellular Component | postsynaptic density | |
Molecular Function | microtubule binding | |
Biological Process | cell division | |
Biological Process | establishment of spindle orientation | |
Biological Process | microtubule cytoskeleton organization | |
Biological Process | microtubule sliding | |
Biological Process | mitotic spindle organization | |
Biological Process | neuron projection development |
Names & Taxonomy
Protein names
- Recommended nameMicrotubule-associated protein 4
- Short namesMAP-4
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP27546
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Recruitment to microtubule is inhibited by microtubules polyglutamylation.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000072752 | 2-1125 | Microtubule-associated protein 4 | |||
Sequence: ADLSLVDALTEPPPEIEGEIKRDFMAALEAEPYDDIVGETVEKTEFIPLLDGDEKTGNSESKKKPCLDTSQVEGIPSSKPTLLANGDHGMEGNNTAGSPTDFLEERVDYPDYQSSQNWPEDASFCFQPQQVLDTDQAEPFNEHRDDGLADLLFVSSGPTNASAFTERDNPSEDSYGMLPCDSFASTAVVSQEWSVGAPNSPCSESCVSPEVTIETLQPATELSKAAEVESVKEQLPAKALETMAEQTTDVVHSPSTDTTPGPDTEAALAKDIEEITKPDVILANVTQPSTESDMFLAQDMELLTGTEAAHANNIILPTEPDESSTKDVAPPMEEEIVPGNDTTSPKETETTLPIKMDLAPPEDVLLTKETELAPAKGMVSLSEIEEALAKNDESSAEIPVAQETVVSETEVVLATEVVLPSDPITTLTKDVTLPLEAERPLVTDMTPSLETEMTLGKETAPPTETNLGMAKDMSPLPESEVTLGKDVVILPETKVAEFNNVTPLSEEEVTSVKDMSPSAETEAPLAKNADLHSGTELIVDNSMAPASDLALPLETKVATVPIKDKGTVQTEEKPREDSQLASMQHKGQSTVPPCTASPEPVKAAEQMSTLPIDAPSPLENLEQKETPGSQPSEPCSGVSRQEEAKAAVGVTGNDITTPPNKEPPPSPEKKAKPLATTQPAKTSTSKAKTQPTSLPKQPAPTTSGGLNKKPMSLASGSVPAAPHKRPAAATATARPSTLPARDVKPKPITEAKVAEKRTSPSKPSSAPALKPGPKTTPTVSKATSPSTLVSTGPSSRSPATTLPKRPTSIKTEGKPADVKRMTAKSASADLSRSKTTSASSVKRNTTPTGAAPPAGMTSTRVKPMSAPSRSSGALSVDKKPTSTKPSSSAPRVSRLATTVSAPDLKSVRSKVGSTENIKHQPGGGRAKVEKKTEAATTAGKPEPNAVTKAAGSIASAQKPPAGKVQIVSKKVSYSHIQSKCGSKDNIKHVPGGGNVQIQNKKVDISKVSSKCGSKANIKHKPGGGDVKIESQKLNFKEKAQAKVGSLDNVGHLPAGGAVKTEGGGSEALPCPGPPAGEEPVIPEAAPDAGAPTSASGLSGHTTLSGGGDQREPQTLDSQIQETSI | ||||||
Modified residue | 5 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 60 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 99 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 254 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 260 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 277 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 333 | In isoform P27546-4; Phosphoserine | ||||
Sequence: M | ||||||
Modified residue | 334 | In isoform P27546-4; Phosphoserine | ||||
Sequence: E | ||||||
Modified residue | 349 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 381 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 410 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 447 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 475 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 494 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 503 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 506 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 511 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 512 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 517 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 519 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 598 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 617 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 658 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 667 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 684 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 694 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 760 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 798 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 811 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 826 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 901 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 914 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 915 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 973 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1046 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1118 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1124 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing detachment from microtubules, and their disassembly (By similarity).
Phosphorylation on Ser-760 negatively regulates MAP4 activity to promote microtubule assembly. Isoform 4 is phosphorylated on Ser-333 and Ser-334 (By similarity).
Phosphorylation on Ser-760 negatively regulates MAP4 activity to promote microtubule assembly. Isoform 4 is phosphorylated on Ser-333 and Ser-334 (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for compositional bias, region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 49-63 | Basic and acidic residues | ||||
Sequence: PLLDGDEKTGNSESK | ||||||
Region | 49-103 | Disordered | ||||
Sequence: PLLDGDEKTGNSESKKKPCLDTSQVEGIPSSKPTLLANGDHGMEGNNTAGSPTDF | ||||||
Region | 245-265 | Disordered | ||||
Sequence: AEQTTDVVHSPSTDTTPGPDT | ||||||
Compositional bias | 247-263 | Polar residues | ||||
Sequence: QTTDVVHSPSTDTTPGP | ||||||
Region | 315-361 | Disordered | ||||
Sequence: IILPTEPDESSTKDVAPPMEEEIVPGNDTTSPKETETTLPIKMDLAP | ||||||
Region | 455-478 | Disordered | ||||
Sequence: TLGKETAPPTETNLGMAKDMSPLP | ||||||
Region | 508-529 | Disordered | ||||
Sequence: EEVTSVKDMSPSAETEAPLAKN | ||||||
Region | 563-964 | Disordered | ||||
Sequence: IKDKGTVQTEEKPREDSQLASMQHKGQSTVPPCTASPEPVKAAEQMSTLPIDAPSPLENLEQKETPGSQPSEPCSGVSRQEEAKAAVGVTGNDITTPPNKEPPPSPEKKAKPLATTQPAKTSTSKAKTQPTSLPKQPAPTTSGGLNKKPMSLASGSVPAAPHKRPAAATATARPSTLPARDVKPKPITEAKVAEKRTSPSKPSSAPALKPGPKTTPTVSKATSPSTLVSTGPSSRSPATTLPKRPTSIKTEGKPADVKRMTAKSASADLSRSKTTSASSVKRNTTPTGAAPPAGMTSTRVKPMSAPSRSSGALSVDKKPTSTKPSSSAPRVSRLATTVSAPDLKSVRSKVGSTENIKHQPGGGRAKVEKKTEAATTAGKPEPNAVTKAAGSIASAQKPPAGK | ||||||
Compositional bias | 567-581 | Basic and acidic residues | ||||
Sequence: GTVQTEEKPREDSQL | ||||||
Compositional bias | 582-596 | Polar residues | ||||
Sequence: ASMQHKGQSTVPPCT | ||||||
Compositional bias | 623-638 | Polar residues | ||||
Sequence: EQKETPGSQPSEPCSG | ||||||
Compositional bias | 677-711 | Polar residues | ||||
Sequence: TTQPAKTSTSKAKTQPTSLPKQPAPTTSGGLNKKP | ||||||
Compositional bias | 777-808 | Polar residues | ||||
Sequence: TPTVSKATSPSTLVSTGPSSRSPATTLPKRPT | ||||||
Compositional bias | 827-854 | Polar residues | ||||
Sequence: ASADLSRSKTTSASSVKRNTTPTGAAPP | ||||||
Compositional bias | 862-917 | Polar residues | ||||
Sequence: VKPMSAPSRSSGALSVDKKPTSTKPSSSAPRVSRLATTVSAPDLKSVRSKVGSTEN | ||||||
Repeat | 896-926 | Tau/MAP 1 | ||||
Sequence: LATTVSAPDLKSVRSKVGSTENIKHQPGGGR | ||||||
Compositional bias | 923-937 | Basic and acidic residues | ||||
Sequence: GGGRAKVEKKTEAAT | ||||||
Repeat | 965-995 | Tau/MAP 2 | ||||
Sequence: VQIVSKKVSYSHIQSKCGSKDNIKHVPGGGN | ||||||
Repeat | 996-1026 | Tau/MAP 3 | ||||
Sequence: VQIQNKKVDISKVSSKCGSKANIKHKPGGGD | ||||||
Repeat | 1027-1058 | Tau/MAP 4 | ||||
Sequence: VKIESQKLNFKEKAQAKVGSLDNVGHLPAGGA | ||||||
Region | 1047-1125 | Disordered | ||||
Sequence: LDNVGHLPAGGAVKTEGGGSEALPCPGPPAGEEPVIPEAAPDAGAPTSASGLSGHTTLSGGGDQREPQTLDSQIQETSI | ||||||
Compositional bias | 1095-1125 | Polar residues | ||||
Sequence: ASGLSGHTTLSGGGDQREPQTLDSQIQETSI |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
P27546-1
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
- Length1,125
- Mass (Da)117,429
- Last updated2007-06-12 v3
- ChecksumE948B7F1F5B903E9
P27546-2
- Name2
- Differences from canonical
- 1124-1125: SI → N
P27546-3
- Name3
- Differences from canonical
- 927-964: Missing
- 1124-1125: SI → N
P27546-4
- Name4
- Differences from canonical
- 1-26: MADLSLVDALTEPPPEIEGEIKRDFM → MSLPEKQPAALT
- 30-259: EAEPYDDIVGETVEKTEFIPLLDGDEKTGNSESKKKPCLDTSQVEGIPSSKPTLLANGDHGMEGNNTAGSPTDFLEERVDYPDYQSSQNWPEDASFCFQPQQVLDTDQAEPFNEHRDDGLADLLFVSSGPTNASAFTERDNPSEDSYGMLPCDSFASTAVVSQEWSVGAPNSPCSESCVSPEVTIETLQPATELSKAAEVESVKEQLPAKALETMAEQTTDVVHSPSTDT → AAEDEQLSKGNPPECGMDSRKEIGQDGFEWQRTEGKLNEIGLNVSMDGQLKDRLVKNSSFLEQNKLGFFEGKLDKELSIEKPNKAYQETSGHLESGYVISGTCQPSEGNLVHQKAAEFHPGLTEGKDKAATVQGKVAGKSGLEIKSQPDLNFPGAADTLTQHGEEQETSAWNANFYSVTQSPQAA
- 263-419: PDTEAALAKDIEEITKPDVILANVTQPSTESDMFLAQDMELLTGTEAAHANNIILPTEPDESSTKDVAPPMEEEIVPGNDTTSPKETETTLPIKMDLAPPEDVLLTKETELAPAKGMVSLSEIEEALAKNDESSAEIPVAQETVVSETEVVLATEVV → KEKNGLVSSCSVTGVMSDNSGQLNNKSPLLVAITHPDPTSEHLPTTSPPITMVEFTQENLNAGQDKELEKLRSSEEGPMLDQVPQQKKAIRRALSECYHLSVPPAVNLVDKYPELPAREE
- 424-531: PITTLTKDVTLPLEAERPLVTDMTPSLETEMTLGKETAPPTETNLGMAKDMSPLPESEVTLGKDVVILPETKVAEFNNVTPLSEEEVTSVKDMSPSAETEAPLAKNAD → LLPPTSSPMPSPMPRKLGVPAMRRSMTVAEDQSASCRLSAGELASLSASQVPTALTFEEPVAKEREEQIHFSNDSNSSGKKELGIAGLY
- 535-625: GTELIVDNSMAPASDLALPLETKVATVPIKDKGTVQTEEKPREDSQLASMQHKGQSTVPPCTASPEPVKAAEQMSTLPIDAPSPLENLEQK → KLEQIPEGSHKGKGQKNTGETRVDSCPFICLGGEKQLMALAGKKEIEVTATQSIPSLLLE
- 629-637: GSQPSEPCS → RD
- 927-964: Missing
- 965-995: Missing
- 1124-1125: SI → N
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A140T8T5 | A0A140T8T5_MOUSE | Map4 | 414 | ||
E9PZ43 | E9PZ43_MOUSE | Map4 | 933 | ||
Q78TF3 | Q78TF3_MOUSE | Map4 | 99 | ||
A0A0G2JFH2 | A0A0G2JFH2_MOUSE | Map4 | 1441 | ||
A0A0G2JFK3 | A0A0G2JFK3_MOUSE | Map4 | 207 | ||
A0A0G2JFT4 | A0A0G2JFT4_MOUSE | Map4 | 276 | ||
A0A0G2JG35 | A0A0G2JG35_MOUSE | Map4 | 290 | ||
A0A0G2JDY5 | A0A0G2JDY5_MOUSE | Map4 | 220 | ||
A0A0G2JDU1 | A0A0G2JDU1_MOUSE | Map4 | 116 | ||
A0A0G2JE57 | A0A0G2JE57_MOUSE | Map4 | 81 | ||
A0A0G2JDN7 | A0A0G2JDN7_MOUSE | Map4 | 902 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_026089 | 1-26 | in isoform 4 | |||
Sequence: MADLSLVDALTEPPPEIEGEIKRDFM → MSLPEKQPAALT | ||||||
Alternative sequence | VSP_026090 | 30-259 | in isoform 4 | |||
Sequence: EAEPYDDIVGETVEKTEFIPLLDGDEKTGNSESKKKPCLDTSQVEGIPSSKPTLLANGDHGMEGNNTAGSPTDFLEERVDYPDYQSSQNWPEDASFCFQPQQVLDTDQAEPFNEHRDDGLADLLFVSSGPTNASAFTERDNPSEDSYGMLPCDSFASTAVVSQEWSVGAPNSPCSESCVSPEVTIETLQPATELSKAAEVESVKEQLPAKALETMAEQTTDVVHSPSTDT → AAEDEQLSKGNPPECGMDSRKEIGQDGFEWQRTEGKLNEIGLNVSMDGQLKDRLVKNSSFLEQNKLGFFEGKLDKELSIEKPNKAYQETSGHLESGYVISGTCQPSEGNLVHQKAAEFHPGLTEGKDKAATVQGKVAGKSGLEIKSQPDLNFPGAADTLTQHGEEQETSAWNANFYSVTQSPQAA | ||||||
Compositional bias | 49-63 | Basic and acidic residues | ||||
Sequence: PLLDGDEKTGNSESK | ||||||
Sequence conflict | 225 | in Ref. 3; AAH55364 | ||||
Sequence: K → E | ||||||
Compositional bias | 247-263 | Polar residues | ||||
Sequence: QTTDVVHSPSTDTTPGP | ||||||
Sequence conflict | 252 | in Ref. 3; AAH55364 | ||||
Sequence: V → A | ||||||
Alternative sequence | VSP_026091 | 263-419 | in isoform 4 | |||
Sequence: PDTEAALAKDIEEITKPDVILANVTQPSTESDMFLAQDMELLTGTEAAHANNIILPTEPDESSTKDVAPPMEEEIVPGNDTTSPKETETTLPIKMDLAPPEDVLLTKETELAPAKGMVSLSEIEEALAKNDESSAEIPVAQETVVSETEVVLATEVV → KEKNGLVSSCSVTGVMSDNSGQLNNKSPLLVAITHPDPTSEHLPTTSPPITMVEFTQENLNAGQDKELEKLRSSEEGPMLDQVPQQKKAIRRALSECYHLSVPPAVNLVDKYPELPAREE | ||||||
Sequence conflict | 394-395 | in Ref. 1; AAA16372 | ||||
Sequence: ES → VR | ||||||
Sequence conflict | 416 | in Ref. 3; AAH55332 | ||||
Sequence: T → I | ||||||
Alternative sequence | VSP_026092 | 424-531 | in isoform 4 | |||
Sequence: PITTLTKDVTLPLEAERPLVTDMTPSLETEMTLGKETAPPTETNLGMAKDMSPLPESEVTLGKDVVILPETKVAEFNNVTPLSEEEVTSVKDMSPSAETEAPLAKNAD → LLPPTSSPMPSPMPRKLGVPAMRRSMTVAEDQSASCRLSAGELASLSASQVPTALTFEEPVAKEREEQIHFSNDSNSSGKKELGIAGLY | ||||||
Sequence conflict | 435 | In isoform P27546-4; in Ref. 2; BAE23650/BAE22377 | ||||
Sequence: K → E | ||||||
Alternative sequence | VSP_026093 | 535-625 | in isoform 4 | |||
Sequence: GTELIVDNSMAPASDLALPLETKVATVPIKDKGTVQTEEKPREDSQLASMQHKGQSTVPPCTASPEPVKAAEQMSTLPIDAPSPLENLEQK → KLEQIPEGSHKGKGQKNTGETRVDSCPFICLGGEKQLMALAGKKEIEVTATQSIPSLLLE | ||||||
Compositional bias | 567-581 | Basic and acidic residues | ||||
Sequence: GTVQTEEKPREDSQL | ||||||
Compositional bias | 582-596 | Polar residues | ||||
Sequence: ASMQHKGQSTVPPCT | ||||||
Compositional bias | 623-638 | Polar residues | ||||
Sequence: EQKETPGSQPSEPCSG | ||||||
Alternative sequence | VSP_026094 | 629-637 | in isoform 4 | |||
Sequence: GSQPSEPCS → RD | ||||||
Compositional bias | 677-711 | Polar residues | ||||
Sequence: TTQPAKTSTSKAKTQPTSLPKQPAPTTSGGLNKKP | ||||||
Compositional bias | 777-808 | Polar residues | ||||
Sequence: TPTVSKATSPSTLVSTGPSSRSPATTLPKRPT | ||||||
Compositional bias | 827-854 | Polar residues | ||||
Sequence: ASADLSRSKTTSASSVKRNTTPTGAAPP | ||||||
Compositional bias | 862-917 | Polar residues | ||||
Sequence: VKPMSAPSRSSGALSVDKKPTSTKPSSSAPRVSRLATTVSAPDLKSVRSKVGSTEN | ||||||
Compositional bias | 923-937 | Basic and acidic residues | ||||
Sequence: GGGRAKVEKKTEAAT | ||||||
Alternative sequence | VSP_026095 | 927-964 | in isoform 3 and isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 955 | in Ref. 3; AAH55364 | ||||
Sequence: A → V | ||||||
Alternative sequence | VSP_026096 | 965-995 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 982 | in Ref. 1; AAA16372 | ||||
Sequence: G → V | ||||||
Sequence conflict | 993 | in Ref. 1; AAA16372 | ||||
Sequence: G → C | ||||||
Sequence conflict | 1053 | in Ref. 1; AAA16372 | ||||
Sequence: L → F | ||||||
Sequence conflict | 1060 | in Ref. 3; AAH44654/AAH55364 | ||||
Sequence: K → KV | ||||||
Sequence conflict | 1089 | in Ref. 1; AAA16372 | ||||
Sequence: A → R | ||||||
Compositional bias | 1095-1125 | Polar residues | ||||
Sequence: ASGLSGHTTLSGGGDQREPQTLDSQIQETSI | ||||||
Alternative sequence | VSP_026097 | 1124-1125 | in isoform 2, isoform 3 and isoform 4 | |||
Sequence: SI → N |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M72414 EMBL· GenBank· DDBJ | AAA16372.1 EMBL· GenBank· DDBJ | mRNA | ||
AK134996 EMBL· GenBank· DDBJ | BAE22377.1 EMBL· GenBank· DDBJ | mRNA | ||
AK138416 EMBL· GenBank· DDBJ | BAE23650.1 EMBL· GenBank· DDBJ | mRNA | ||
AK146790 EMBL· GenBank· DDBJ | BAE27434.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC042645 EMBL· GenBank· DDBJ | AAH42645.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC044654 EMBL· GenBank· DDBJ | AAH44654.1 EMBL· GenBank· DDBJ | mRNA | ||
BC050893 EMBL· GenBank· DDBJ | AAH50893.1 EMBL· GenBank· DDBJ | mRNA | ||
BC055332 EMBL· GenBank· DDBJ | AAH55332.1 EMBL· GenBank· DDBJ | mRNA | ||
BC055364 EMBL· GenBank· DDBJ | AAH55364.1 EMBL· GenBank· DDBJ | mRNA |