Q7Z4S6 · KI21A_HUMAN
- ProteinKinesin-like protein KIF21A
- GeneKIF21A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1674 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Features
Showing features for binding site.
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 | axonal growth cone | |
Cellular Component | cytosol | |
Cellular Component | dendrite | |
Cellular Component | kinesin complex | |
Cellular Component | microtubule | |
Molecular Function | ankyrin repeat binding | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | microtubule binding | |
Molecular Function | microtubule motor activity | |
Molecular Function | plus-end-directed microtubule motor activity | |
Biological Process | cortical microtubule organization | |
Biological Process | microtubule-based movement | |
Biological Process | regulation of axon guidance | |
Biological Process | regulation of microtubule depolymerization | |
Biological Process | regulation of microtubule polymerization |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKinesin-like protein KIF21A
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ7Z4S6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Fibrosis of extraocular muscles, congenital, 1 (CFEOM1)
- Note
- DescriptionA congenital ocular motility disorder marked by restrictive ophthalmoplegia affecting extraocular muscles innervated by the oculomotor and/or trochlear nerves. It is clinically characterized by anchoring of the eyes in downward gaze, ptosis, and backward tilt of the head. Patients affected by congenital fibrosis of extraocular muscles type 1 show an absence of the superior division of the oculomotor nerve (cranial nerve III) and corresponding oculomotor subnuclei.
- See alsoMIM:135700
Natural variants in CFEOM1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_089555 | 28 | C>W | in CFEOM1; prevents the interaction between the motor domain and the coiled-coil domain, expected to cause loss of autoinhibition and gain of function | |
VAR_074031 | 352 | D>E | in CFEOM1; de novo mutation | |
VAR_019399 | 356 | M>T | in CFEOM1; prevents the interaction between the motor domain and the coiled-coil domain expected to cause loss of autoinhibition and gain of function; dbSNP:rs121912588 | |
VAR_074032 | 944 | E>Q | in CFEOM1 | |
VAR_019400 | 947 | M>R | in CFEOM1; dbSNP:rs121912590 | |
VAR_027021 | 947 | M>T | in CFEOM1 | |
VAR_019401 | 947 | M>V | in CFEOM1; dbSNP:rs121912589 | |
VAR_074033 | 954 | R>L | in CFEOM1 | |
VAR_019402 | 954 | R>Q | in CFEOM1; dbSNP:rs121912586 | |
VAR_019403 | 954 | R>W | in CFEOM1; enhances plus-end-directed motor activity due to loss of autoinhibition; gain of function; dbSNP:rs121912585 | |
VAR_074034 | 1008 | A>P | in CFEOM1 | |
VAR_019404 | 1010 | I>T | in CFEOM1; dbSNP:rs121912587 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_089555 | 28 | in CFEOM1; prevents the interaction between the motor domain and the coiled-coil domain, expected to cause loss of autoinhibition and gain of function | |||
Sequence: C → W | ||||||
Natural variant | VAR_074031 | 352 | in CFEOM1; de novo mutation | |||
Sequence: D → E | ||||||
Natural variant | VAR_019399 | 356 | in CFEOM1; prevents the interaction between the motor domain and the coiled-coil domain expected to cause loss of autoinhibition and gain of function; dbSNP:rs121912588 | |||
Sequence: M → T | ||||||
Natural variant | VAR_074032 | 944 | in CFEOM1 | |||
Sequence: E → Q | ||||||
Natural variant | VAR_019400 | 947 | in CFEOM1; dbSNP:rs121912590 | |||
Sequence: M → R | ||||||
Natural variant | VAR_027021 | 947 | in CFEOM1 | |||
Sequence: M → T | ||||||
Natural variant | VAR_019401 | 947 | in CFEOM1; dbSNP:rs121912589 | |||
Sequence: M → V | ||||||
Natural variant | VAR_074033 | 954 | in CFEOM1 | |||
Sequence: R → L | ||||||
Natural variant | VAR_019402 | 954 | in CFEOM1; dbSNP:rs121912586 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_019403 | 954 | in CFEOM1; enhances plus-end-directed motor activity due to loss of autoinhibition; gain of function; dbSNP:rs121912585 | |||
Sequence: R → W | ||||||
Natural variant | VAR_074034 | 1008 | in CFEOM1 | |||
Sequence: A → P | ||||||
Natural variant | VAR_019404 | 1010 | in CFEOM1; dbSNP:rs121912587 | |||
Sequence: I → T | ||||||
Mutagenesis | 1154 | Very weak binding affinity for KANK1 and KANK2. | ||||
Sequence: R → A | ||||||
Mutagenesis | 1164 | Does not bind to KANK1 or KANK2. | ||||
Sequence: L → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,719 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000125462 | 1-1674 | UniProt | Kinesin-like protein KIF21A | |||
Sequence: MLGAPDESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMGTGFDVNIVEEELGIISRAVKHLFKSIEEKKHIAIKNGLPAPDFKVNAQFLELYNEEVLDLFDTTRDIDAKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIDADNATDNKIISESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQDRASQQINALRSEITRLQMELMEYKTGKRIIDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRSRITQLVSDQANHVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARAPYFSGSSTFSPTILSSDKETIEIIDLAKKDLEKLKRKEKRKKKRLQKLEESNREERSVAGKEDNTDTDQEKKEEKGVSERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERRVTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDVTAVINACTLTEARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQTEITSATQNQLLFHMLKEKAELNPELDALLGHALQDLDSVPLENVEDSTDEDAPLNSPGSEGSTLSSDLMKLCGEVKPKNKARRRTTTQMELLYADSSELASDTSTGDASLPGPLTPVAEGQEIGMNTETSGTSAREKELSPPPGLPSKIGSISRQSSLSEKKIPEPSPVTRRKAYEKAEKSKAKEQKHSDSGTSEASLSPPSSPPSRPRNELNVFNRLTVSQGNTSVQQDKSDESDSSLSEVHRSSRRGIINPFPASKGIRAFPLQCIHIAEGHTKAVLCVDSTDDLLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVSTSYIKVWDIRDSAKCIRTLTSSGQVTLGDACSASTSRTVAIPSGENQINQIALNPTGTFLYAASGNAVRMWDLKRFQSTGKLTGHLGPVMCLTVDQISSGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNFEPPHYDGIEALTIQGDNLFSGSRDNGIKKWDLTQKDLLQQVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICVNSTHIFTAADDRTVRIWKARNLQDGQISDTGDLGEDIASN | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 9 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 186 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 518 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 520 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 524 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 524 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 529 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 530 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 571 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 579 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 581 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 710 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 853 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 855 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 862 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1212 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1212 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1225 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1225 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1228 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1229 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1229 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1231 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1239 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1239 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1269 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1271 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1274 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1275 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1293 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1298 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1304 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1307 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1310 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1662 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1662 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1664 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1664 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1673 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1673 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts (via residues 1146-1167) with KANK1 (via ankyrin repeats 1-5) and KANK2 (via ankyrin repeats 1-5) (PubMed:24120883, PubMed:29183992).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q7Z4S6 | ARFGEF1 Q9Y6D6 | 7 | EBI-2691397, EBI-1044254 | |
BINARY | Q7Z4S6 | KANK1 Q14678 | 5 | EBI-2691397, EBI-2556221 | |
BINARY | Q7Z4S6 | KANK1 Q14678-2 | 3 | EBI-2691397, EBI-6173812 | |
BINARY | Q7Z4S6-2 | ARFGEF1 Q9Y6D6 | 4 | EBI-6251716, EBI-1044254 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, coiled coil, region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 9-371 | Kinesin motor | ||||
Sequence: SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMGTGFDVNIVEEELGIISRAVKHLFKSIEEKKHIAIKNGLPAPDFKVNAQFLELYNEEVLDLFDTTRDIDAKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIDADNATDNKIISESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI | ||||||
Coiled coil | 365-575 | |||||
Sequence: ANRARNIKNKVMVNQDRASQQINALRSEITRLQMELMEYKTGKRIIDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRSRITQLVSDQANHVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARAPYFSGSSTFSPTILSSDKETIEIIDLAKKDLEKLKRKEKRKKKRLQKLEESNREERSVAGK | ||||||
Region | 556-641 | Disordered | ||||
Sequence: KKRLQKLEESNREERSVAGKEDNTDTDQEKKEEKGVSERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKA | ||||||
Compositional bias | 558-603 | Basic and acidic residues | ||||
Sequence: RLQKLEESNREERSVAGKEDNTDTDQEKKEEKGVSERENNELEVEE | ||||||
Compositional bias | 604-635 | Acidic residues | ||||
Sequence: SQEVSDHEDEEEEEEEEEDDIDGGESSDESDS | ||||||
Region | 779-804 | Disordered | ||||
Sequence: EEQEKARLTESRRNREIAQLKKDQRK | ||||||
Region | 841-881 | Disordered | ||||
Sequence: SDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQK | ||||||
Compositional bias | 853-878 | Polar residues | ||||
Sequence: SSSDAPAQDTGSSAAAVETDASRTGA | ||||||
Coiled coil | 931-1019 | |||||
Sequence: TDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEE | ||||||
Coiled coil | 1053-1083 | |||||
Sequence: LQAAQKEAQIKVLEGRLKQTEITSATQNQLL | ||||||
Region | 1116-1138 | Disordered | ||||
Sequence: VEDSTDEDAPLNSPGSEGSTLSS | ||||||
Compositional bias | 1122-1138 | Polar residues | ||||
Sequence: EDAPLNSPGSEGSTLSS | ||||||
Region | 1146-1167 | Interaction with KANK1 and KANK2 | ||||
Sequence: EVKPKNKARRRTTTQMELLYAD | ||||||
Region | 1170-1318 | Disordered | ||||
Sequence: ELASDTSTGDASLPGPLTPVAEGQEIGMNTETSGTSAREKELSPPPGLPSKIGSISRQSSLSEKKIPEPSPVTRRKAYEKAEKSKAKEQKHSDSGTSEASLSPPSSPPSRPRNELNVFNRLTVSQGNTSVQQDKSDESDSSLSEVHRSS | ||||||
Compositional bias | 1194-1208 | Polar residues | ||||
Sequence: EIGMNTETSGTSARE | ||||||
Compositional bias | 1221-1235 | Polar residues | ||||
Sequence: IGSISRQSSLSEKKI | ||||||
Compositional bias | 1237-1263 | Basic and acidic residues | ||||
Sequence: EPSPVTRRKAYEKAEKSKAKEQKHSDS | ||||||
Compositional bias | 1280-1305 | Polar residues | ||||
Sequence: PRNELNVFNRLTVSQGNTSVQQDKSD | ||||||
Repeat | 1345-1382 | WD 1 | ||||
Sequence: GHTKAVLCVDSTDDLLFTGSKDRTCKVWNLVTGQEIMS | ||||||
Repeat | 1385-1423 | WD 2 | ||||
Sequence: GHPNNVVSVKYCNYTSLVFTVSTSYIKVWDIRDSAKCIR | ||||||
Repeat | 1449-1487 | WD 3 | ||||
Sequence: SGENQINQIALNPTGTFLYAASGNAVRMWDLKRFQSTGK | ||||||
Repeat | 1490-1532 | WD 4 | ||||
Sequence: GHLGPVMCLTVDQISSGQDLIITGSKDHYIKMFDVTEGALGTV | ||||||
Repeat | 1541-1578 | WD 5 | ||||
Sequence: PHYDGIEALTIQGDNLFSGSRDNGIKKWDLTQKDLLQQ | ||||||
Repeat | 1582-1621 | WD 6 | ||||
Sequence: AHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGE | ||||||
Repeat | 1624-1661 | WD 7 | ||||
Sequence: GHDSPINAICVNSTHIFTAADDRTVRIWKARNLQDGQI |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 6 isoforms produced by Alternative splicing.
Q7Z4S6-1
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
- Length1,674
- Mass (Da)187,179
- Last updated2004-07-19 v2
- Checksum292AFA5F2C0C6F9A
Q7Z4S6-2
- Name2
- Differences from canonical
- 558-570: Missing
Q7Z4S6-3
- Name3
- Differences from canonical
- 1260-1319: HSDSGTSEASLSPPSSPPSRPRNELNVFNRLTVSQGNTSVQQDKSDESDSSLSEVHRSSR → QSDESDSSLSEVH
Q7Z4S6-4
- Name4
- Differences from canonical
- 1315-1315: H → HS
Q7Z4S6-5
- Name5
- Differences from canonical
- 558-570: Missing
- 1107-1113: Missing
- 1304-1320: Missing
Q7Z4S6-6
- Name6
- Differences from canonical
- 558-570: Missing
- 807-829: Missing
- 1304-1320: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 172 | in Ref. 2; CAJ45483 | ||||
Sequence: K → R | ||||||
Sequence conflict | 176 | in Ref. 2; CAJ45483 | ||||
Sequence: R → G | ||||||
Sequence conflict | 215 | in Ref. 2; CAJ45483 | ||||
Sequence: A → G | ||||||
Sequence conflict | 315 | in Ref. 2; CAJ45483 | ||||
Sequence: S → C | ||||||
Alternative sequence | VSP_010870 | 558-570 | in isoform 2, isoform 5 and isoform 6 | |||
Sequence: Missing | ||||||
Compositional bias | 558-603 | Basic and acidic residues | ||||
Sequence: RLQKLEESNREERSVAGKEDNTDTDQEKKEEKGVSERENNELEVEE | ||||||
Sequence conflict | 596-597 | in Ref. 3; AAP97680 and 8; AAD42883 | ||||
Sequence: NN → TQ | ||||||
Compositional bias | 604-635 | Acidic residues | ||||
Sequence: SQEVSDHEDEEEEEEEEEDDIDGGESSDESDS | ||||||
Sequence conflict | 653 | in Ref. 3; AAP97680 | ||||
Sequence: E → D | ||||||
Sequence conflict | 801 | in Ref. 2; CAJ45483 | ||||
Sequence: D → G | ||||||
Sequence conflict | 801-802 | in Ref. 3; AAP97680 | ||||
Sequence: DQ → AP | ||||||
Alternative sequence | VSP_046790 | 807-829 | in isoform 6 | |||
Sequence: Missing | ||||||
Sequence conflict | 813 | in Ref. 3; AAP97680 | ||||
Sequence: E → G | ||||||
Sequence conflict | 826 | in Ref. 3; AAP97680 | ||||
Sequence: K → Q | ||||||
Compositional bias | 853-878 | Polar residues | ||||
Sequence: SSSDAPAQDTGSSAAAVETDASRTGA | ||||||
Sequence conflict | 875 | in Ref. 2; CAJ45483 | ||||
Sequence: R → G | ||||||
Sequence conflict | 892 | in Ref. 2; CAJ45483 | ||||
Sequence: L → S | ||||||
Sequence conflict | 1071 | in Ref. 2; CAJ45483 | ||||
Sequence: Q → R | ||||||
Alternative sequence | VSP_046791 | 1107-1113 | in isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 1122-1138 | Polar residues | ||||
Sequence: EDAPLNSPGSEGSTLSS | ||||||
Sequence conflict | 1167 | in Ref. 2; CAJ45483 | ||||
Sequence: D → G | ||||||
Compositional bias | 1194-1208 | Polar residues | ||||
Sequence: EIGMNTETSGTSARE | ||||||
Compositional bias | 1221-1235 | Polar residues | ||||
Sequence: IGSISRQSSLSEKKI | ||||||
Sequence conflict | 1237 | in Ref. 7; AAI36415 | ||||
Sequence: E → D | ||||||
Compositional bias | 1237-1263 | Basic and acidic residues | ||||
Sequence: EPSPVTRRKAYEKAEKSKAKEQKHSDS | ||||||
Alternative sequence | VSP_010871 | 1260-1319 | in isoform 3 | |||
Sequence: HSDSGTSEASLSPPSSPPSRPRNELNVFNRLTVSQGNTSVQQDKSDESDSSLSEVHRSSR → QSDESDSSLSEVH | ||||||
Compositional bias | 1280-1305 | Polar residues | ||||
Sequence: PRNELNVFNRLTVSQGNTSVQQDKSD | ||||||
Alternative sequence | VSP_046792 | 1304-1320 | in isoform 5 and isoform 6 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_010872 | 1315 | in isoform 4 | |||
Sequence: H → HS | ||||||
Sequence conflict | 1341 | in Ref. 2; CAJ45483 | ||||
Sequence: H → N | ||||||
Sequence conflict | 1378-1379 | in Ref. 2; CAJ45483 | ||||
Sequence: QE → HR | ||||||
Sequence conflict | 1429 | in Ref. 2; CAJ45483 | ||||
Sequence: G → A | ||||||
Sequence conflict | 1503 | in Ref. 11; CAD97863 | ||||
Sequence: I → T | ||||||
Sequence conflict | 1511 | in Ref. 11; CAD97863 | ||||
Sequence: I → T |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY368076 EMBL· GenBank· DDBJ | AAR04774.1 EMBL· GenBank· DDBJ | mRNA | ||
AM177179 EMBL· GenBank· DDBJ | CAJ45483.1 EMBL· GenBank· DDBJ | mRNA | ||
AF450487 EMBL· GenBank· DDBJ | AAP97680.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AB290166 EMBL· GenBank· DDBJ | BAG06720.1 EMBL· GenBank· DDBJ | mRNA | ||
AC084373 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC090668 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC121334 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AF155117 EMBL· GenBank· DDBJ | AAD42883.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK000059 EMBL· GenBank· DDBJ | BAA90916.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
CH471111 EMBL· GenBank· DDBJ | EAW57803.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC041430 EMBL· GenBank· DDBJ | AAH41430.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC047572 EMBL· GenBank· DDBJ | AAH47572.1 EMBL· GenBank· DDBJ | mRNA | ||
BC136414 EMBL· GenBank· DDBJ | AAI36415.1 EMBL· GenBank· DDBJ | mRNA | ||
AB051495 EMBL· GenBank· DDBJ | BAB21799.2 EMBL· GenBank· DDBJ | mRNA | ||
BX537855 EMBL· GenBank· DDBJ | CAD97863.1 EMBL· GenBank· DDBJ | mRNA |