Q12955 · ANK3_HUMAN
- ProteinAnkyrin-3
- GeneANK3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids4377 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments (PubMed:7836469).
In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity).
Regulates KCNA1 channel activity in function of dietary Mg2+ levels, and thereby contributes to the regulation of renal Mg2+ reabsorption (PubMed:23903368).
Required for intracellular adhesion and junctional conductance in myocytes, potentially via stabilization of GJA1/CX43 protein abundance and promotion of PKP2, GJA1/CX43, and SCN5A/Nav1.5 localization to cell-cell junctions (By similarity).
In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity).
Regulates KCNA1 channel activity in function of dietary Mg2+ levels, and thereby contributes to the regulation of renal Mg2+ reabsorption (PubMed:23903368).
Required for intracellular adhesion and junctional conductance in myocytes, potentially via stabilization of GJA1/CX43 protein abundance and promotion of PKP2, GJA1/CX43, and SCN5A/Nav1.5 localization to cell-cell junctions (By similarity).
Isoform 5
May be part of a Golgi-specific membrane cytoskeleton in association with beta-spectrin.
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
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAnkyrin-3
- Short namesANK-3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ12955
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In skeletal muscle, localized at costameres and neuromuscular junctions. In macrophages, associated with lysosomes.
Isoform 5
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Intellectual developmental disorder, autosomal recessive 37 (MRT37)
- Note
- DescriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT37 patients manifest delayed global development with speech delay, hypotonia, spasticity, and a sleep disorder. Severe behavioral abnormalities include aggression, hyperactivity, and grinding of the teeth.
- See alsoMIM:615493
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_077912 | 968 | found in a patient with Gillessen-Kaesbach-Nishimura syndrome; uncertain significance; dbSNP:rs730882195 | |||
Sequence: D → H | ||||||
Natural variant | VAR_068702 | 1569 | found in a patient with autism; uncertain significance; dbSNP:rs375050420 | |||
Sequence: S → A | ||||||
Natural variant | VAR_061013 | 2318 | in dbSNP:rs59021407 | |||
Sequence: K → R | ||||||
Natural variant | VAR_059115 | 2885 | in dbSNP:rs11599164 | |||
Sequence: H → Q | ||||||
Natural variant | VAR_061014 | 2996 | in dbSNP:rs41274672 | |||
Sequence: Q → H | ||||||
Natural variant | VAR_059116 | 3117 | in dbSNP:rs28932171 | |||
Sequence: I → V | ||||||
Natural variant | VAR_059117 | 3123 | in dbSNP:rs10821668 | |||
Sequence: K → R | ||||||
Natural variant | VAR_068703 | 3720 | found in a patient with autism; uncertain significance; dbSNP:rs201547988 | |||
Sequence: T → M | ||||||
Natural variant | VAR_068704 | 4255 | found in a patient with autism; uncertain significance; dbSNP:rs769573528 | |||
Sequence: T → P | ||||||
Natural variant | VAR_054333 | 4257 | in dbSNP:rs12261793 | |||
Sequence: I → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 4,431 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
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_0000066886 | 1-4377 | UniProt | Ankyrin-3 | |||
Sequence: MAHAASQLKKNRDLEINAEEEPEKKRKHRKRSRDRKKKSDANASYLRAARAGHLEKALDYIKNGVDINICNQNGLNALHLASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVKFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENDTKGKVRLPALHIAARKDDTKAAALLLQNDNNADVESKSGFTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRAAPILSKTKNGLSPLHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIKVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVAAFLLDHGASLSITTKKGFTPLHVAAKYGKLEVANLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQMDIATTLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLGRNANVNLSNKSGLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQNNASPNELTVNGNTALGIARRLGYISVVDTLKIVTEETMTTTTVTEKHKMNVPETMNEVLDMSDDEVRKANAPEMLSDGEYISDVEEGEDAMTGDTDKYLGPQDLKELGDDSLPAEGYMGFSLGARSASLRSFSSDRSYTLNRSSYARDSMMIEELLVPSKEQHLTFTREFDSDSLRHYSWAADTLDNVNLVSSPIHSGFLVSFMVDARGGSMRGSRHHGMRIIIPPRKCTAPTRITCRLVKRHKLANPPPMVEGEGLASRLVEMGPAGAQFLGPVIVEIPHFGSMRGKERELIVLRSENGETWKEHQFDSKNEDLTELLNGMDEELDSPEELGKKRICRIITKDFPQYFAVVSRIKQESNQIGPEGGILSSTTVPLVQASFPEGALTKRIRVGLQAQPVPDEIVKKILGNKATFSPIVTVEPRRRKFHKPITMTIPVPPPSGEGVSNGYKGDTTPNLRLLCSITGGTSPAQWEDITGTTPLTFIKDCVSFTTNVSARFWLADCHQVLETVGLATQLYRELICVPYMAKFVVFAKMNDPVESSLRCFCMTDDKVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNFYSFKENRLPFSIKIRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLPAHKKETESDQDDEIEKTDRRQSFASLALRKRYSYLTEPGMIERSTGATRSLPTTYSYKPFFSTRPYQSWTTAPITVPGPAKSGFTSLSSSSSNTPSASPLKSIWSVSTPSPIKSTLGASTTSSVKSISDVASPIRSFRTMSSPIKTVVSQSPYNIQVSSGTLARAPAVTEATPLKGLASNSTFSSRTSPVTTAGSLLERSSITMTPPASPKSNINMYSSSLPFKSIITSAAPLISSPLKSVVSPVKSAVDVISSAKITMASSLSSPVKQMPGHAEVALVNGSISPLKYPSSSTLINGCKATATLQEKISSATNSVSSVVSAATDTVEKVFSTTTAMPFSPLRSYVSAAPSAFQSLRTPSASALYTSLGSSISATTSSVTSSIITVPVYSVVNVLPEPALKKLPDSNSFTKSAAALLSPIKTLTTETHPQPHFSRTSSPVKSSLFLAPSALKLSTPSSLSSSQEILKDVAEMKEDLMRMTAILQTDVPEEKPFQPELPKEGRIDDEEPFKIVEKVKEDLVKVSEILKKDVCVDNKGSPKSPKSDKGHSPEDDWIEFSSEEIREARQQAAASQSPSLPERVQVKAKAASEKDYNLTKVIDYLTNDIGSSSLTNLKYKFEDAKKDGEERQKRVLKPAIALQEHKLKMPPASMRTSTSEKELCKMADSFFGTDTILESPDDFSQHDQDKSPLSDSGFETRSEKTPSAPQSAESTGPKPLFHEVPIPPVITETRTEVVHVIRSYDPSAGDVPQTQPEEPVSPKPSPTFMELEPKPTTSSIKEKVKAFQMKASSEEDDHNRVLSKGMRVKEETHITTTTRMVYHSPPGGEGASERIEETMSVHDIMKAFQSGRDPSKELAGLFEHKSAVSPDVHKSAAETSAQHAEKDNQMKPKLERIIEVHIEKGNQAEPTEVIIRETKKHPEKEMYVYQKDLSRGDINLKDFLPEKHDAFPCSEEQGQQEEEELTAEESLPSYLESSRVNTPVSQEEDSRPSSAQLISDDSYKTLKLLSQHSIEYHDDELSELRGESYRFAEKMLLSEKLDVSHSDTEESVTDHAGPPSSELQGSDKRSREKIATAPKKEILSKIYKDVSENGVGKVSKDEHFDKVTVLHYSGNVSSPKHAMWMRFTEDRLDRGREKLIYEDRVDRTVKEAEEKLTEVSQFFRDKTEKLNDELQSPEKKARPKNGKEYSSQSPTSSSPEKVLLTELLASNDEWVKARQHGPDGQGFPKAEEKAPSLPSSPEKMVLSQQTEDSKSTVEAKGSISQSKAPDGPQSGFQLKQSKLSSIRLKFEQGTHAKSKDMSQEDRKSDGQSRIPVKKIQESKLPVYQVFAREKQQKAIDLPDESVSVQKDFMVLKTKDEHAQSNEIVVNDSGSDNVKKQRTEMSSKAMPDSFSEQQAKDLACHITSDLATRGPWDKKVFRTWESSGATNNKSQKEKLSHVLVHDVRENHIGHPESKSVDQKNEFMSVTERERKLLTNGSLSEIKEMTVKSPSKKVLYREYVVKEGDHPGGLLDQPSRRSESSAVSHIPVRVADERRMLSSNIPDGFCEQSAFPKHELSQKLSQSSMSKETVETQHFNSIEDEKVTYSEISKVSKHQSYVGLCPPLEETETSPTKSPDSLEFSPGKESPSSDVFDHSPIDGLEKLAPLAQTEGGKEIKTLPVYVSFVQVGKQYEKEIQQGGVKKIISQECKTVQETRGTFYTTRQQKQPPSPQGSPEDDTLEQVSFLDSSGKSPLTPETPSSEEVSYEFTSKTPDSLIAYIPGKPSPIPEVSEESEEEEQAKSTSLKQTTVEETAVEREMPNDVSKDSNQRPKNNRVAYIEFPPPPPLDADQIESDKKHHYLPEKEVDMIEVNLQDEHDKYQLAEPVIRVQPPSPVPPGADVSDSSDDESIYQPVPVKKYTFKLKEVDDEQKEKPKASAEKASNQKELESNGSGKDNEFGLGLDSPQNEIAQNGNNDQSITECSIATTAEFSHDTDATEIDSLDGYDLQDEDDGLTESDSKLPIQAMEIKKDIWNTEGILKPADRSFSQSKLEVIEEEGKVGPDEDKPPSKSSSSEKTPDKTDQKSGAQFFTLEGRHPDRSVFPDTYFSYKVDEEFATPFKTVATKGLDFDPWSNNRGDDEVFDSKSREDETKPFGLAVEDRSPATTPDTTPARTPTDESTPTSEPNPFPFHEGKMFEMTRSGAIDMSKRDFVEERLQFFQIGEHTSEGKSGDQGEGDKSMVTATPQPQSGDTTVETNLERNVETPTVEPNPSIPTSGECQEGTSSSGSLEKSAAATNTSKVDPKLRTPIKMGISASTMTMKKEGPGEITDKIEAVMTSCQGLENETITMISNTANSQMGVRPHEKHDFQKDNFNNNNNLDSSTIQTDNIMSNIVLTEHSAPTCTTEKDNPVKVSSGKKTGVLQGHCVRDKQKVLGEQQKTKELIGIRQKSKLPIKATSPKDTFPPNHMSNTKASKMKQVSQSEKTKALTTSSCVDVKSRIPVKNTHRDNIIAVRKACATQKQGQPEKGKAKQLPSKLPVKVRSTCVTTTTTTATTTTTTTTTTTTSCTVKVRKSQLKEVCKHSIEYFKGISGETLKLVDRLSEEEKKMQSELSDEEESTSRNTSLSETSRGGQPSVTTKSARDKKTEAAPLKSKSEKAGSEKRSSRRTGPQSPCERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLEGPIFDYGNISGTRSFADENNVFHDPVDGWQNETSSGNLESCAQARRVTGGLLDRLDDSPDQCRDSITSYLKGEAGKFEANGSHTEITPEAKTKSYFPESQNDVGKQSTKETLKPKIHGSGHVEEPASPLAAYQKSLEETSKLIIEETKPCVPVSMKKMSRTSPADGKPRLSLHEEEGSSGSEQKQGEGFKVKTKKEIRHVEKKSHS | |||||||
Modified residue | 39 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 39 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 468 | UniProt | In isoform Q12955-7; Phosphoserine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 531 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 533 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 623 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 623 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 765 | UniProt | In isoform Q12955-6; Phosphoserine | ||||
Sequence: T | |||||||
Modified residue | 791 | UniProt | In isoform Q12955-6; Phosphoserine | ||||
Sequence: E | |||||||
Modified residue | 847 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 847 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 861 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 861 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 867 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 867 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 896 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 911 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 913 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 913 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 916 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 916 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 922 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 934 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 957 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 959 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 959 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1113 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1405 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1443 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1445 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1445 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1459 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1459 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1462 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1470 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1622 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1625 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1625 | UniProt | In isoform Q12955-5; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1632 | UniProt | In isoform Q12955-4; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1651 | UniProt | In isoform Q12955-5; Phosphoserine | ||||
Sequence: I | |||||||
Modified residue | 1658 | UniProt | In isoform Q12955-4; Phosphoserine | ||||
Sequence: L | |||||||
Modified residue | 1984 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1984 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2009 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2111 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2123 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2126 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2445 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3055 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3355 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4181 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 4211 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 4229 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4229 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4258 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 4290 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4290 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 4298 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4298 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4325 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4332 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 4333 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4342 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4349 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 4350 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4350 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in brain, neurons, muscles and other tissues.
Developmental stage
Up-regulated during muscle cell differentiation.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Directly interacts with DMD and betaDAG1. This interaction does not interfere with binding between DMD and betaDAG1. It is also required for DMD and betaDAG1 retention at costameres (By similarity).
Interacts (via N-terminal ANK repeats) with SCHIP1 isoform 5 (via C-terminus); this interaction is required for the localization at axon initial segments (AISs) and nodes of Ranvier (NRs) (By similarity).
May be a constituent of a NFASC/NRCAM/ankyrin G complex. Interacts with RHBG (PubMed:15611082).
Interacts with PLEC and FLNC (PubMed:21223964).
Interacts with KCNA1; this inhibits channel activity (PubMed:23903368).
Interacts (via ANK repeats) with IQCJ-SCHIP1; required for IQCJ-SCHIP1 localization at axon initial segments (AIS) and nodes of Ranvier (PubMed:25950943).
Interacts with SCHIP1 (PubMed:25950943).
Interacts with SCN5A (PubMed:15579534).
Interacts with PKP2 and GJA1/CX43 (By similarity).
Interacts (via N-terminal ANK repeats) with SCHIP1 isoform 5 (via C-terminus); this interaction is required for the localization at axon initial segments (AISs) and nodes of Ranvier (NRs) (By similarity).
May be a constituent of a NFASC/NRCAM/ankyrin G complex. Interacts with RHBG (PubMed:15611082).
Interacts with PLEC and FLNC (PubMed:21223964).
Interacts with KCNA1; this inhibits channel activity (PubMed:23903368).
Interacts (via ANK repeats) with IQCJ-SCHIP1; required for IQCJ-SCHIP1 localization at axon initial segments (AIS) and nodes of Ranvier (PubMed:25950943).
Interacts with SCHIP1 (PubMed:25950943).
Interacts with SCN5A (PubMed:15579534).
Interacts with PKP2 and GJA1/CX43 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q12955 | AP3B1 O00203-1 | 2 | EBI-2691178, EBI-15816315 | |
BINARY | Q12955 | RAPGEF5 Q92565 | 2 | EBI-2691178, EBI-3921741 | |
BINARY | Q12955 | SMAD2 Q15796 | 2 | EBI-2691178, EBI-1040141 | |
BINARY | Q12955-5 | NAB2 Q15742 | 3 | EBI-12154305, EBI-8641936 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-27 | Basic and acidic residues | ||||
Sequence: MAHAASQLKKNRDLEINAEEEPEKKRK | ||||||
Region | 1-44 | Disordered | ||||
Sequence: MAHAASQLKKNRDLEINAEEEPEKKRKHRKRSRDRKKKSDANAS | ||||||
Repeat | 73-102 | ANK 1 | ||||
Sequence: NGLNALHLASKEGHVEVVSELLQREANVDA | ||||||
Repeat | 106-135 | ANK 2 | ||||
Sequence: KGNTALHIASLAGQAEVVKVLVTNGANVNA | ||||||
Repeat | 139-168 | ANK 3 | ||||
Sequence: NGFTPLYMAAQENHLEVVKFLLDNGASQSL | ||||||
Repeat | 172-201 | ANK 4 | ||||
Sequence: DGFTPLAVALQQGHDQVVSLLLENDTKGKV | ||||||
Repeat | 203-230 | ANK 5 | ||||
Sequence: LPALHIAARKDDTKAAALLLQNDNNADV | ||||||
Repeat | 234-263 | ANK 6 | ||||
Sequence: SGFTPLHIAAHYGNINVATLLLNRAAAVDF | ||||||
Repeat | 267-296 | ANK 7 | ||||
Sequence: NDITPLHVASKRGNANMVKLLLDRGAKIDA | ||||||
Repeat | 300-329 | ANK 8 | ||||
Sequence: DGLTPLHCGARSGHEQVVEMLLDRAAPILS | ||||||
Repeat | 333-362 | ANK 9 | ||||
Sequence: NGLSPLHMATQGDHLNCVQLLLQHNVPVDD | ||||||
Repeat | 366-395 | ANK 10 | ||||
Sequence: DYLTALHVAAHCGHYKVAKVLLDKKANPNA | ||||||
Repeat | 399-428 | ANK 11 | ||||
Sequence: NGFTPLHIACKKNRIKVMELLLKHGASIQA | ||||||
Repeat | 432-461 | ANK 12 | ||||
Sequence: SGLTPIHVAAFMGHVNIVSQLMHHGASPNT | ||||||
Repeat | 465-494 | ANK 13 | ||||
Sequence: RGETALHMAARSGQAEVVRYLVQDGAQVEA | ||||||
Repeat | 498-527 | ANK 14 | ||||
Sequence: DDQTPLHISARLGKADIVQQLLQQGASPNA | ||||||
Repeat | 531-560 | ANK 15 | ||||
Sequence: SGYTPLHLSAREGHEDVAAFLLDHGASLSI | ||||||
Repeat | 564-593 | ANK 16 | ||||
Sequence: KGFTPLHVAAKYGKLEVANLLLQKSASPDA | ||||||
Repeat | 597-626 | ANK 17 | ||||
Sequence: SGLTPLHVAAHYDNQKVALLLLDQGASPHA | ||||||
Repeat | 630-659 | ANK 18 | ||||
Sequence: NGYTPLHIAAKKNQMDIATTLLEYGADANA | ||||||
Repeat | 663-692 | ANK 19 | ||||
Sequence: QGIASVHLAAQEGHVDMVSLLLGRNANVNL | ||||||
Repeat | 696-725 | ANK 20 | ||||
Sequence: SGLTPLHLAAQEDRVNVAEVLVNQGAHVDA | ||||||
Repeat | 729-758 | ANK 21 | ||||
Sequence: MGYTPLHVGCHYGNIKIVNFLLQHSAKVNA | ||||||
Repeat | 762-791 | ANK 22 | ||||
Sequence: NGYTPLHQAAQQGHTHIINVLLQNNASPNE | ||||||
Repeat | 795-825 | ANK 23 | ||||
Sequence: NGNTALGIARRLGYISVVDTLKIVTEETMTT | ||||||
Domain | 984-1139 | ZU5 1 | ||||
Sequence: FLVSFMVDARGGSMRGSRHHGMRIIIPPRKCTAPTRITCRLVKRHKLANPPPMVEGEGLASRLVEMGPAGAQFLGPVIVEIPHFGSMRGKERELIVLRSENGETWKEHQFDSKNEDLTELLNGMDEELDSPEELGKKRICRIITKDFPQYFAVVSR | ||||||
Domain | 1141-1288 | ZU5 2 | ||||
Sequence: KQESNQIGPEGGILSSTTVPLVQASFPEGALTKRIRVGLQAQPVPDEIVKKILGNKATFSPIVTVEPRRRKFHKPITMTIPVPPPSGEGVSNGYKGDTTPNLRLLCSITGGTSPAQWEDITGTTPLTFIKDCVSFTTNVSARFWLADC | ||||||
Region | 1273-1407 | UPA domain | ||||
Sequence: VSFTTNVSARFWLADCHQVLETVGLATQLYRELICVPYMAKFVVFAKMNDPVESSLRCFCMTDDKVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNFYSFKENRLPFSIKIRDTSQE | ||||||
Region | 1519-1540 | Disordered | ||||
Sequence: SGFTSLSSSSSNTPSASPLKSI | ||||||
Region | 1968-1987 | Disordered | ||||
Sequence: VDNKGSPKSPKSDKGHSPED | ||||||
Region | 2107-2159 | Disordered | ||||
Sequence: TILESPDDFSQHDQDKSPLSDSGFETRSEKTPSAPQSAESTGPKPLFHEVPIP | ||||||
Compositional bias | 2112-2129 | Basic and acidic residues | ||||
Sequence: PDDFSQHDQDKSPLSDSG | ||||||
Compositional bias | 2130-2146 | Polar residues | ||||
Sequence: FETRSEKTPSAPQSAES | ||||||
Region | 2176-2245 | Disordered | ||||
Sequence: YDPSAGDVPQTQPEEPVSPKPSPTFMELEPKPTTSSIKEKVKAFQMKASSEEDDHNRVLSKGMRVKEETH | ||||||
Compositional bias | 2219-2245 | Basic and acidic residues | ||||
Sequence: FQMKASSEEDDHNRVLSKGMRVKEETH | ||||||
Region | 2299-2322 | Disordered | ||||
Sequence: AVSPDVHKSAAETSAQHAEKDNQM | ||||||
Region | 2383-2433 | Disordered | ||||
Sequence: FPCSEEQGQQEEEELTAEESLPSYLESSRVNTPVSQEEDSRPSSAQLISDD | ||||||
Compositional bias | 2403-2433 | Polar residues | ||||
Sequence: LPSYLESSRVNTPVSQEEDSRPSSAQLISDD | ||||||
Region | 2474-2508 | Disordered | ||||
Sequence: DVSHSDTEESVTDHAGPPSSELQGSDKRSREKIAT | ||||||
Compositional bias | 2588-2618 | Basic and acidic residues | ||||
Sequence: LTEVSQFFRDKTEKLNDELQSPEKKARPKNG | ||||||
Region | 2588-2751 | Disordered | ||||
Sequence: LTEVSQFFRDKTEKLNDELQSPEKKARPKNGKEYSSQSPTSSSPEKVLLTELLASNDEWVKARQHGPDGQGFPKAEEKAPSLPSSPEKMVLSQQTEDSKSTVEAKGSISQSKAPDGPQSGFQLKQSKLSSIRLKFEQGTHAKSKDMSQEDRKSDGQSRIPVKKI | ||||||
Compositional bias | 2619-2636 | Polar residues | ||||
Sequence: KEYSSQSPTSSSPEKVLL | ||||||
Compositional bias | 2673-2720 | Polar residues | ||||
Sequence: PEKMVLSQQTEDSKSTVEAKGSISQSKAPDGPQSGFQLKQSKLSSIRL | ||||||
Compositional bias | 2724-2748 | Basic and acidic residues | ||||
Sequence: QGTHAKSKDMSQEDRKSDGQSRIPV | ||||||
Region | 2795-2824 | Disordered | ||||
Sequence: QSNEIVVNDSGSDNVKKQRTEMSSKAMPDS | ||||||
Region | 3036-3067 | Disordered | ||||
Sequence: PPLEETETSPTKSPDSLEFSPGKESPSSDVFD | ||||||
Compositional bias | 3041-3058 | Polar residues | ||||
Sequence: TETSPTKSPDSLEFSPGK | ||||||
Compositional bias | 3131-3185 | Polar residues | ||||
Sequence: TFYTTRQQKQPPSPQGSPEDDTLEQVSFLDSSGKSPLTPETPSSEEVSYEFTSKT | ||||||
Region | 3131-3272 | Disordered | ||||
Sequence: TFYTTRQQKQPPSPQGSPEDDTLEQVSFLDSSGKSPLTPETPSSEEVSYEFTSKTPDSLIAYIPGKPSPIPEVSEESEEEEQAKSTSLKQTTVEETAVEREMPNDVSKDSNQRPKNNRVAYIEFPPPPPLDADQIESDKKHH | ||||||
Compositional bias | 3224-3242 | Basic and acidic residues | ||||
Sequence: EETAVEREMPNDVSKDSNQ | ||||||
Region | 3298-3516 | Disordered | ||||
Sequence: PVIRVQPPSPVPPGADVSDSSDDESIYQPVPVKKYTFKLKEVDDEQKEKPKASAEKASNQKELESNGSGKDNEFGLGLDSPQNEIAQNGNNDQSITECSIATTAEFSHDTDATEIDSLDGYDLQDEDDGLTESDSKLPIQAMEIKKDIWNTEGILKPADRSFSQSKLEVIEEEGKVGPDEDKPPSKSSSSEKTPDKTDQKSGAQFFTLEGRHPDRSVFP | ||||||
Compositional bias | 3333-3355 | Basic and acidic residues | ||||
Sequence: TFKLKEVDDEQKEKPKASAEKAS | ||||||
Compositional bias | 3378-3405 | Polar residues | ||||
Sequence: PQNEIAQNGNNDQSITECSIATTAEFSH | ||||||
Compositional bias | 3462-3495 | Basic and acidic residues | ||||
Sequence: SKLEVIEEEGKVGPDEDKPPSKSSSSEKTPDKTD | ||||||
Region | 3538-3607 | Disordered | ||||
Sequence: KGLDFDPWSNNRGDDEVFDSKSREDETKPFGLAVEDRSPATTPDTTPARTPTDESTPTSEPNPFPFHEGK | ||||||
Compositional bias | 3545-3569 | Basic and acidic residues | ||||
Sequence: WSNNRGDDEVFDSKSREDETKPFGL | ||||||
Compositional bias | 3576-3599 | Polar residues | ||||
Sequence: PATTPDTTPARTPTDESTPTSEPN | ||||||
Region | 3635-3718 | Disordered | ||||
Sequence: GEHTSEGKSGDQGEGDKSMVTATPQPQSGDTTVETNLERNVETPTVEPNPSIPTSGECQEGTSSSGSLEKSAAATNTSKVDPKL | ||||||
Compositional bias | 3650-3716 | Polar residues | ||||
Sequence: DKSMVTATPQPQSGDTTVETNLERNVETPTVEPNPSIPTSGECQEGTSSSGSLEKSAAATNTSKVDP | ||||||
Region | 3868-3897 | Disordered | ||||
Sequence: KATSPKDTFPPNHMSNTKASKMKQVSQSEK | ||||||
Compositional bias | 3875-3897 | Polar residues | ||||
Sequence: TFPPNHMSNTKASKMKQVSQSEK | ||||||
Compositional bias | 4019-4034 | Basic and acidic residues | ||||
Sequence: KKMQSELSDEEESTSR | ||||||
Region | 4019-4090 | Disordered | ||||
Sequence: KKMQSELSDEEESTSRNTSLSETSRGGQPSVTTKSARDKKTEAAPLKSKSEKAGSEKRSSRRTGPQSPCERT | ||||||
Compositional bias | 4035-4052 | Polar residues | ||||
Sequence: NTSLSETSRGGQPSVTTK | ||||||
Compositional bias | 4053-4077 | Basic and acidic residues | ||||
Sequence: SARDKKTEAAPLKSKSEKAGSEKRS | ||||||
Domain | 4090-4174 | Death | ||||
Sequence: TDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLEGPI | ||||||
Region | 4251-4298 | Disordered | ||||
Sequence: NGSHTEITPEAKTKSYFPESQNDVGKQSTKETLKPKIHGSGHVEEPAS | ||||||
Compositional bias | 4256-4278 | Polar residues | ||||
Sequence: EITPEAKTKSYFPESQNDVGKQS | ||||||
Region | 4323-4377 | Disordered | ||||
Sequence: PVSMKKMSRTSPADGKPRLSLHEEEGSSGSEQKQGEGFKVKTKKEIRHVEKKSHS | ||||||
Compositional bias | 4338-4366 | Basic and acidic residues | ||||
Sequence: KPRLSLHEEEGSSGSEQKQGEGFKVKTKK |
Domain
The tandem configuration of the two ZU5 and the UPA domains forms a structural supramodule termed ZZU. ZU5-1 mediates interaction with beta-spectrin, and the ZU5-1/UPA interface is required for ankyrin's function other than binding to spectrin (By similarity).
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
Q12955-3
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
- Length4,377
- Mass (Da)480,410
- Last updated2009-09-01 v3
- ChecksumF6F9FABD09F15C13
Q12955-4
- Name2
- Differences from canonical
- 1-36: MAHAASQLKKNRDLEINAEEEPEKKRKHRKRSRDRK → MSEEPKEKNAKPAHRKRKG
- 872-872: G → GNRCTWYKIPKVQEFTVKS
- 1442-1450: Missing
- 1478-4081: Missing
- 4082-4082: G → S
- 4199-4199: G → GYPSLQVELETPTGLHYTPPTPFQQDDYFSDISSIESPLRTPSRLSDGLVPSQGNIEHSADGPPVVTAEDASLEDSKLEDSVPLTEMPEAVDVDESQLENVCLS
Q12955-5
- Name3
- Differences from canonical
- 1-37: MAHAASQLKKNRDLEINAEEEPEKKRKHRKRSRDRKK → MASSASSSPAGTEDSAPAQGGFGSDYSRSSR
- 1442-1450: Missing
- 1478-4081: Missing
- 4082-4082: G → S
- 4199-4199: G → GYPSLQVELETPTGLHYTPPTPFQQDDYFSDISSIESPLRTPSRLSDGLVPSQGNIEHSADGPPVVTAEDASLEDSKLEDSVPLTEMPEAVDVDESQLENVCLS
Q12955-6
- Name4
- Differences from canonical
- 1-866: Missing
- 867-872: SDVEEG → MALPQS
- 1442-1450: Missing
- 1478-4081: Missing
- 4082-4082: G → S
- 4199-4199: G → GYPSLQVELETPTGLHYTPPTPFQQDDYFSDISSIESPLRTPSRLSDGLVPSQGNIEHSADGPPVVTAEDASLEDSKLEDSVPLTEMPEAVDVDESQLENVCLS
Q12955-7
- Name5
- SynonymsAnkG119, Golgi ankyrin
- NoteAvidly binds beta spectrin.
- Differences from canonical
- 1-6: MAHAAS → MNLRCD
- 7-385: Missing
- 850-870: Missing
- 913-918: Missing
- 1036-1043: MVEGEGLA → HGERRGIS
- 1442-1450: Missing
- 1478-1880: IERSTGATRSLPTTYSYKPFFSTRPYQSWTTAPITVPGPAKSGFTSLSSSSSNTPSASPLKSIWSVSTPSPIKSTLGASTTSSVKSISDVASPIRSFRTMSSPIKTVVSQSPYNIQVSSGTLARAPAVTEATPLKGLASNSTFSSRTSPVTTAGSLLERSSITMTPPASPKSNINMYSSSLPFKSIITSAAPLISSPLKSVVSPVKSAVDVISSAKITMASSLSSPVKQMPGHAEVALVNGSISPLKYPSSSTLINGCKATATLQEKISSATNSVSSVVSAATDTVEKVFSTTTAMPFSPLRSYVSAAPSAFQSLRTPSASALYTSLGSSISATTSSVTSSIITVPVYSVVNVLPEPALKKLPDSNSFTKSAAALLSPIKTLTTETHPQPHFSRTSSPVKSSL → TSCTVKVRKSQLKEVCKHSIEYFKGISGETLKLVDRLSEEEKKMQSELSDEEESTSRNTSLSETSRGGQPSVTTKSARDKKTEAAPLKSKSEKAGSEKRSSRRTGPQSPCERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLEGPIFDYGNISGTRSFADENNVFHDPVDGWQNETSSGNLESCAQARRVTGGLLDRLDDSPDQCRDSITSYLKGEAGKFEANGSHTEITPEAKTKSYFPESQNDVGKQSTKETLKPKIHGSGHVEEPASPLAAYQKSLEETSKLSKLIIEETKPCVPVSMKKMSRTSPADGKPRLSLHEEEGSSGSEQKQGEGFKVKTKKEIRHVEKKSHS
- 1881-4377: Missing
Computationally mapped potential isoform sequences
There are 22 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D6RFK6 | D6RFK6_HUMAN | ANK3 | 159 | ||
D6RF31 | D6RF31_HUMAN | ANK3 | 86 | ||
D6RHY3 | D6RHY3_HUMAN | ANK3 | 273 | ||
H0YA66 | H0YA66_HUMAN | ANK3 | 187 | ||
H0YAH5 | H0YAH5_HUMAN | ANK3 | 217 | ||
D6RBY7 | D6RBY7_HUMAN | ANK3 | 72 | ||
H0Y9E9 | H0Y9E9_HUMAN | ANK3 | 1792 | ||
H0Y8Z4 | H0Y8Z4_HUMAN | ANK3 | 114 | ||
H0Y951 | H0Y951_HUMAN | ANK3 | 166 | ||
H0Y3A4 | H0Y3A4_HUMAN | ANK3 | 459 | ||
B1AQT1 | B1AQT1_HUMAN | ANK3 | 195 | ||
A0A087X0L3 | A0A087X0L3_HUMAN | ANK3 | 63 | ||
A0A087X0B4 | A0A087X0B4_HUMAN | ANK3 | 450 | ||
A0A087WTE8 | A0A087WTE8_HUMAN | ANK3 | 241 | ||
A0A087WTF3 | A0A087WTF3_HUMAN | ANK3 | 1643 | ||
A0A087WTP5 | A0A087WTP5_HUMAN | ANK3 | 868 | ||
A0A087WVC2 | A0A087WVC2_HUMAN | ANK3 | 322 | ||
A0A087WWI5 | A0A087WWI5_HUMAN | ANK3 | 96 | ||
A0A087WX55 | A0A087WX55_HUMAN | ANK3 | 175 | ||
A0A087WY90 | A0A087WY90_HUMAN | ANK3 | 178 | ||
A0A087WZ26 | A0A087WZ26_HUMAN | ANK3 | 201 | ||
A0A087WZ65 | A0A087WZ65_HUMAN | ANK3 | 973 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_053753 | 1-6 | in isoform 5 | |||
Sequence: MAHAAS → MNLRCD | ||||||
Compositional bias | 1-27 | Basic and acidic residues | ||||
Sequence: MAHAASQLKKNRDLEINAEEEPEKKRK | ||||||
Alternative sequence | VSP_044349 | 1-36 | in isoform 2 | |||
Sequence: MAHAASQLKKNRDLEINAEEEPEKKRKHRKRSRDRK → MSEEPKEKNAKPAHRKRKG | ||||||
Alternative sequence | VSP_044348 | 1-37 | in isoform 3 | |||
Sequence: MAHAASQLKKNRDLEINAEEEPEKKRKHRKRSRDRKK → MASSASSSPAGTEDSAPAQGGFGSDYSRSSR | ||||||
Alternative sequence | VSP_046885 | 1-866 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_053754 | 7-385 | in isoform 5 | |||
Sequence: Missing | ||||||
Sequence conflict | 197 | in Ref. 5; CAI56716 | ||||
Sequence: T → A | ||||||
Sequence conflict | 222 | in Ref. 5; CAD97900 | ||||
Sequence: L → P | ||||||
Sequence conflict | 327 | in Ref. 5; CAD97900 | ||||
Sequence: I → V | ||||||
Sequence conflict | 338 | in Ref. 4; BAG58523 | ||||
Sequence: L → W | ||||||
Sequence conflict | 523 | in Ref. 5; CAD97900 | ||||
Sequence: A → T | ||||||
Sequence conflict | 578 | in Ref. 5; CAI56716 | ||||
Sequence: L → P | ||||||
Alternative sequence | VSP_053755 | 850-870 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_046886 | 867-872 | in isoform 4 | |||
Sequence: SDVEEG → MALPQS | ||||||
Alternative sequence | VSP_044350 | 872 | in isoform 2 | |||
Sequence: G → GNRCTWYKIPKVQEFTVKS | ||||||
Alternative sequence | VSP_053756 | 913-918 | in isoform 5 | |||
Sequence: Missing | ||||||
Sequence conflict | 921 | in Ref. 3; CAB66645 | ||||
Sequence: R → G | ||||||
Sequence conflict | 977 | in Ref. 3; CAB66645 | ||||
Sequence: S → P | ||||||
Alternative sequence | VSP_053757 | 1036-1043 | in isoform 5 | |||
Sequence: MVEGEGLA → HGERRGIS | ||||||
Sequence conflict | 1237 | in Ref. 5; CAI56716 | ||||
Sequence: D → G | ||||||
Sequence conflict | 1418 | in Ref. 1; AAA64834 | ||||
Sequence: P → R | ||||||
Alternative sequence | VSP_044351 | 1442-1450 | in isoform 2, isoform 3, isoform 4 and isoform 5 | |||
Sequence: Missing | ||||||
Sequence conflict | 1455 | in Ref. 4; BAG58523 | ||||
Sequence: D → E | ||||||
Alternative sequence | VSP_053758 | 1478-1880 | in isoform 5 | |||
Sequence: IERSTGATRSLPTTYSYKPFFSTRPYQSWTTAPITVPGPAKSGFTSLSSSSSNTPSASPLKSIWSVSTPSPIKSTLGASTTSSVKSISDVASPIRSFRTMSSPIKTVVSQSPYNIQVSSGTLARAPAVTEATPLKGLASNSTFSSRTSPVTTAGSLLERSSITMTPPASPKSNINMYSSSLPFKSIITSAAPLISSPLKSVVSPVKSAVDVISSAKITMASSLSSPVKQMPGHAEVALVNGSISPLKYPSSSTLINGCKATATLQEKISSATNSVSSVVSAATDTVEKVFSTTTAMPFSPLRSYVSAAPSAFQSLRTPSASALYTSLGSSISATTSSVTSSIITVPVYSVVNVLPEPALKKLPDSNSFTKSAAALLSPIKTLTTETHPQPHFSRTSSPVKSSL → TSCTVKVRKSQLKEVCKHSIEYFKGISGETLKLVDRLSEEEKKMQSELSDEEESTSRNTSLSETSRGGQPSVTTKSARDKKTEAAPLKSKSEKAGSEKRSSRRTGPQSPCERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLEGPIFDYGNISGTRSFADENNVFHDPVDGWQNETSSGNLESCAQARRVTGGLLDRLDDSPDQCRDSITSYLKGEAGKFEANGSHTEITPEAKTKSYFPESQNDVGKQSTKETLKPKIHGSGHVEEPASPLAAYQKSLEETSKLSKLIIEETKPCVPVSMKKMSRTSPADGKPRLSLHEEEGSSGSEQKQGEGFKVKTKKEIRHVEKKSHS | ||||||
Alternative sequence | VSP_044352 | 1478-4081 | in isoform 2, isoform 3 and isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 1574 | in Ref. 1; AAA64834 | ||||
Sequence: F → L | ||||||
Sequence conflict | 1685 | in Ref. 1; AAA64834 | ||||
Sequence: A → R | ||||||
Sequence conflict | 1726 | in Ref. 1; AAA64834 | ||||
Sequence: P → A | ||||||
Alternative sequence | VSP_053759 | 1881-4377 | in isoform 5 | |||
Sequence: Missing | ||||||
Sequence conflict | 2062-2063 | in Ref. 1; AAA64834 | ||||
Sequence: ER → GG | ||||||
Compositional bias | 2112-2129 | Basic and acidic residues | ||||
Sequence: PDDFSQHDQDKSPLSDSG | ||||||
Compositional bias | 2130-2146 | Polar residues | ||||
Sequence: FETRSEKTPSAPQSAES | ||||||
Sequence conflict | 2146 | in Ref. 1; AAA64834 | ||||
Sequence: S → T | ||||||
Compositional bias | 2219-2245 | Basic and acidic residues | ||||
Sequence: FQMKASSEEDDHNRVLSKGMRVKEETH | ||||||
Compositional bias | 2403-2433 | Polar residues | ||||
Sequence: LPSYLESSRVNTPVSQEEDSRPSSAQLISDD | ||||||
Compositional bias | 2588-2618 | Basic and acidic residues | ||||
Sequence: LTEVSQFFRDKTEKLNDELQSPEKKARPKNG | ||||||
Compositional bias | 2619-2636 | Polar residues | ||||
Sequence: KEYSSQSPTSSSPEKVLL | ||||||
Compositional bias | 2673-2720 | Polar residues | ||||
Sequence: PEKMVLSQQTEDSKSTVEAKGSISQSKAPDGPQSGFQLKQSKLSSIRL | ||||||
Compositional bias | 2724-2748 | Basic and acidic residues | ||||
Sequence: QGTHAKSKDMSQEDRKSDGQSRIPV | ||||||
Compositional bias | 3041-3058 | Polar residues | ||||
Sequence: TETSPTKSPDSLEFSPGK | ||||||
Compositional bias | 3131-3185 | Polar residues | ||||
Sequence: TFYTTRQQKQPPSPQGSPEDDTLEQVSFLDSSGKSPLTPETPSSEEVSYEFTSKT | ||||||
Compositional bias | 3224-3242 | Basic and acidic residues | ||||
Sequence: EETAVEREMPNDVSKDSNQ | ||||||
Compositional bias | 3333-3355 | Basic and acidic residues | ||||
Sequence: TFKLKEVDDEQKEKPKASAEKAS | ||||||
Compositional bias | 3378-3405 | Polar residues | ||||
Sequence: PQNEIAQNGNNDQSITECSIATTAEFSH | ||||||
Compositional bias | 3462-3495 | Basic and acidic residues | ||||
Sequence: SKLEVIEEEGKVGPDEDKPPSKSSSSEKTPDKTD | ||||||
Compositional bias | 3545-3569 | Basic and acidic residues | ||||
Sequence: WSNNRGDDEVFDSKSREDETKPFGL | ||||||
Compositional bias | 3576-3599 | Polar residues | ||||
Sequence: PATTPDTTPARTPTDESTPTSEPN | ||||||
Compositional bias | 3650-3716 | Polar residues | ||||
Sequence: DKSMVTATPQPQSGDTTVETNLERNVETPTVEPNPSIPTSGECQEGTSSSGSLEKSAAATNTSKVDP | ||||||
Compositional bias | 3875-3897 | Polar residues | ||||
Sequence: TFPPNHMSNTKASKMKQVSQSEK | ||||||
Sequence conflict | 3919 | in Ref. 1; AAA64834 | ||||
Sequence: H → P | ||||||
Compositional bias | 4019-4034 | Basic and acidic residues | ||||
Sequence: KKMQSELSDEEESTSR | ||||||
Compositional bias | 4035-4052 | Polar residues | ||||
Sequence: NTSLSETSRGGQPSVTTK | ||||||
Compositional bias | 4053-4077 | Basic and acidic residues | ||||
Sequence: SARDKKTEAAPLKSKSEKAGSEKRS | ||||||
Alternative sequence | VSP_044353 | 4082 | in isoform 2, isoform 3 and isoform 4 | |||
Sequence: G → S | ||||||
Sequence conflict | 4137 | in Ref. 3; CAB66645 | ||||
Sequence: L → F | ||||||
Alternative sequence | VSP_044354 | 4199 | in isoform 2, isoform 3 and isoform 4 | |||
Sequence: G → GYPSLQVELETPTGLHYTPPTPFQQDDYFSDISSIESPLRTPSRLSDGLVPSQGNIEHSADGPPVVTAEDASLEDSKLEDSVPLTEMPEAVDVDESQLENVCLS | ||||||
Compositional bias | 4256-4278 | Polar residues | ||||
Sequence: EITPEAKTKSYFPESQNDVGKQS | ||||||
Compositional bias | 4338-4366 | Basic and acidic residues | ||||
Sequence: KPRLSLHEEEGSSGSEQKQGEGFKVKTKK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U13616 EMBL· GenBank· DDBJ | AAA64834.1 EMBL· GenBank· DDBJ | mRNA | ||
U43965 EMBL· GenBank· DDBJ | AAB08437.1 EMBL· GenBank· DDBJ | mRNA | ||
AL136710 EMBL· GenBank· DDBJ | CAB66645.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK295661 EMBL· GenBank· DDBJ | BAG58523.1 EMBL· GenBank· DDBJ | mRNA | ||
BX537917 EMBL· GenBank· DDBJ | CAD97900.2 EMBL· GenBank· DDBJ | mRNA | ||
BX648574 EMBL· GenBank· DDBJ | CAI56716.1 EMBL· GenBank· DDBJ | mRNA | ||
AC022390 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC023904 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL359267 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL359377 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL391707 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL592430 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL607065 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |