P30622 · CLIP1_HUMAN
- ProteinCAP-Gly domain-containing linker protein 1
- GeneCLIP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1438 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 | cell cortex | |
Cellular Component | centrosome | |
Cellular Component | cytoplasmic vesicle membrane | |
Cellular Component | cytosol | |
Cellular Component | intermediate filament | |
Cellular Component | kinetochore | |
Cellular Component | microtubule | |
Cellular Component | microtubule cytoskeleton | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Cellular Component | ruffle | |
Molecular Function | identical protein binding | |
Molecular Function | microtubule binding | |
Molecular Function | microtubule plus-end binding | |
Molecular Function | tubulin binding | |
Molecular Function | zinc ion binding | |
Biological Process | cytoplasmic microtubule organization | |
Biological Process | microtubule bundle formation | |
Biological Process | mitotic cell cycle | |
Biological Process | positive regulation of microtubule polymerization |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCAP-Gly domain-containing linker protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP30622
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Localizes preferentially to the ends of tyrosinated microtubules (By similarity).
Accumulates in plasma membrane regions with ruffling and protrusions. Associates with the membranes of intermediate macropinocytic vesicles (PubMed:12433698).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 98-99 | Abolishes interaction with tubulin. Abolishes localization at the microtubule plus end. | ||||
Sequence: KN → EE | ||||||
Natural variant | VAR_059206 | 162 | in dbSNP:rs7963597 | |||
Sequence: S → P | ||||||
Natural variant | VAR_048672 | 780 | in dbSNP:rs3741447 | |||
Sequence: R → W | ||||||
Natural variant | VAR_048673 | 941 | in dbSNP:rs17883517 | |||
Sequence: S → P | ||||||
Natural variant | VAR_020398 | 1080 | in dbSNP:rs1129167 | |||
Sequence: D → E | ||||||
Natural variant | VAR_036446 | 1213 | in a breast cancer sample; somatic mutation; dbSNP:rs1183319975 | |||
Sequence: M → I | ||||||
Natural variant | VAR_048674 | 1224 | in dbSNP:rs17881033 | |||
Sequence: A → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,351 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000083527 | 1-1438 | UniProt | CAP-Gly domain-containing linker protein 1 | |||
Sequence: MSMLKPSGLKAPTKILKPGSTALKTPTAVVAPVEKTISSEKASSTPSSETQEEFVDDFRVGERVWVNGNKPGFIQFLGETQFAPGQWAGIVLDEPIGKNDGSVAGVRYFQCEPLKGIFTRPSKLTRKVQAEDEANGLQTTPASRATSPLCTSTASMVSSSPSTPSNIPQKPSQPAAKEPSATPPISNLTKTASESISNLSEAGSIKKGERELKIGDRVLVGGTKAGVVRFLGETDFAKGEWCGVELDEPLGKNDGAVAGTRYFQCQPKYGLFAPVHKVTKIGFPSTTPAKAKANAVRRVMATTSASLKRSPSASSLSSMSSVASSVSSRPSRTGLLTETSSRYARKISGTTALQEALKEKQQHIEQLLAERDLERAEVAKATSHVGEIEQELALARDGHDQHVLELEAKMDQLRTMVEAADREKVELLNQLEEEKRKVEDLQFRVEEESITKGDLEQKSQISEDPENTQTKLEHARIKELEQSLLFEKTKADKLQRELEDTRVATVSEKSRIMELEKDLALRVQEVAELRRRLESNKPAGDVDMSLSLLQEISSLQEKLEVTRTDHQREITSLKEHFGAREETHQKEIKALYTATEKLSKENESLKSKLEHANKENSDVIALWKSKLETAIASHQQAMEELKVSFSKGLGTETAEFAELKTQIEKMRLDYQHEIENLQNQQDSERAAHAKEMEALRAKLMKVIKEKENSLEAIRSKLDKAEDQHLVEMEDTLNKLQEAEIKVKELEVLQAKCNEQTKVIDNFTSQLKATEEKLLDLDALRKASSEGKSEMKKLRQQLEAAEKQIKHLEIEKNAESSKASSITRELQGRELKLTNLQENLSEVSQVKETLEKELQILKEKFAEASEEAVSVQRSMQETVNKLHQKEEQFNMLSSDLEKLRENLADMEAKFREKDEREEQLIKAKEKLENDIAEIMKMSGDNSSQLTKMNDELRLKERDVEELQLKLTKANENASFLQKSIEDMTVKAEQSQQEAAKKHEEEKKELERKLSDLEKKMETSHNQCQELKARYERATSETKTKHEEILQNLQKTLLDTEDKLKGAREENSGLLQELEELRKQADKAKAAQTAEDAMQIMEQMTKEKTETLASLEDTKQTNAKLQNELDTLKENNLKNVEELNKSKELLTVENQKMEEFRKEIETLKQAAAQKSQQLSALQEENVKLAEELGRSRDEVTSHQKLEEERSVLNNQLLEMKKRESKFIKDADEEKASLQKSISITSALLTEKDAELEKLRNEVTVLRGENASAKSLHSVVQTLESDKVKLELKVKNLELQLKENKRQLSSSSGNTDTQADEDERAQESQIDFLNSVIVDLQRKNQDLKMKVEMMSEAALNGNGDDLNNYDSDDQEKQSKKKPRLFCDICDCFDLHDTEDCPTQAQMSEDPPHSTHHGSRGEERPYCEICEMFGHWATNCNDDETF | |||||||
Modified residue (large scale data) | 20 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 25 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 44 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 45 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 48 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 48 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 50 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 50 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 140 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 140 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 143 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 143 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 146 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 147 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 147 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 151 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 155 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 160 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 162 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 163 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 180 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 182 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 182 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 193 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 195 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 195 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 197 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 197 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 200 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 200 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 204 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 204 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 285 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 286 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 287 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 304 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 306 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 310 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 310 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 312 | UniProt | Phosphoserine; by PKA | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 312 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 314 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 315 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 315 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 348 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 348 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 350 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 973 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1140 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1236 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1236 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1268 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1271 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1305 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1310 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1364 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1364 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation by MTOR may positively regulate CLIP1 association with microtubules (PubMed:12231510).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts (via CAP-Gly domains) with tubulin (PubMed:17563362, PubMed:17889670).
Interacts with SLAIN2 (PubMed:21646404).
Interacts (via zinc finger) with DCTN1 (PubMed:17828275, PubMed:20679239).
Interacts with TUBA1B, MAPRE1 and MAPRE3 (PubMed:17563362).
Binds preferentially to tyrosinated microtubules, and only marginally to detyrosinated microtubules (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P30622 | MAPRE1 Q15691 | 3 | EBI-2683569, EBI-1004115 | |
BINARY | P30622 | REL Q04864-2 | 3 | EBI-2683569, EBI-10829018 | |
BINARY | P30622 | TUBA4A P68366 | 3 | EBI-2683569, EBI-351772 | |
BINARY | P30622-1 | CLIP1 P30622-1 | 12 | EBI-9640673, EBI-9640673 | |
BINARY | P30622-1 | DCTN1 Q14203 | 7 | EBI-9640673, EBI-724352 | |
BINARY | P30622-1 | MAPRE1 Q15691 | 2 | EBI-9640673, EBI-1004115 | |
BINARY | P30622-2 | MAPRE1 Q15691 | 4 | EBI-6479976, EBI-1004115 | |
BINARY | P30622-2 | TUBA1A Q71U36 | 3 | EBI-6479976, EBI-302552 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, coiled coil, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 78-120 | CAP-Gly 1 | ||||
Sequence: GETQFAPGQWAGIVLDEPIGKNDGSVAGVRYFQCEPLKGIFTR | ||||||
Region | 97-101 | Important for tubulin binding | ||||
Sequence: GKNDG | ||||||
Region | 129-188 | Disordered | ||||
Sequence: QAEDEANGLQTTPASRATSPLCTSTASMVSSSPSTPSNIPQKPSQPAAKEPSATPPISNL | ||||||
Compositional bias | 132-188 | Polar residues | ||||
Sequence: DEANGLQTTPASRATSPLCTSTASMVSSSPSTPSNIPQKPSQPAAKEPSATPPISNL | ||||||
Domain | 232-274 | CAP-Gly 2 | ||||
Sequence: GETDFAKGEWCGVELDEPLGKNDGAVAGTRYFQCQPKYGLFAP | ||||||
Region | 302-340 | Disordered | ||||
Sequence: TTSASLKRSPSASSLSSMSSVASSVSSRPSRTGLLTETS | ||||||
Coiled coil | 350-1353 | |||||
Sequence: TTALQEALKEKQQHIEQLLAERDLERAEVAKATSHVGEIEQELALARDGHDQHVLELEAKMDQLRTMVEAADREKVELLNQLEEEKRKVEDLQFRVEEESITKGDLEQKSQISEDPENTQTKLEHARIKELEQSLLFEKTKADKLQRELEDTRVATVSEKSRIMELEKDLALRVQEVAELRRRLESNKPAGDVDMSLSLLQEISSLQEKLEVTRTDHQREITSLKEHFGAREETHQKEIKALYTATEKLSKENESLKSKLEHANKENSDVIALWKSKLETAIASHQQAMEELKVSFSKGLGTETAEFAELKTQIEKMRLDYQHEIENLQNQQDSERAAHAKEMEALRAKLMKVIKEKENSLEAIRSKLDKAEDQHLVEMEDTLNKLQEAEIKVKELEVLQAKCNEQTKVIDNFTSQLKATEEKLLDLDALRKASSEGKSEMKKLRQQLEAAEKQIKHLEIEKNAESSKASSITRELQGRELKLTNLQENLSEVSQVKETLEKELQILKEKFAEASEEAVSVQRSMQETVNKLHQKEEQFNMLSSDLEKLRENLADMEAKFREKDEREEQLIKAKEKLENDIAEIMKMSGDNSSQLTKMNDELRLKERDVEELQLKLTKANENASFLQKSIEDMTVKAEQSQQEAAKKHEEEKKELERKLSDLEKKMETSHNQCQELKARYERATSETKTKHEEILQNLQKTLLDTEDKLKGAREENSGLLQELEELRKQADKAKAAQTAEDAMQIMEQMTKEKTETLASLEDTKQTNAKLQNELDTLKENNLKNVEELNKSKELLTVENQKMEEFRKEIETLKQAAAQKSQQLSALQEENVKLAEELGRSRDEVTSHQKLEEERSVLNNQLLEMKKRESKFIKDADEEKASLQKSISITSALLTEKDAELEKLRNEVTVLRGENASAKSLHSVVQTLESDKVKLELKVKNLELQLKENKRQLSSSSGNTDTQADEDERAQESQIDFLNSVIVDLQRKNQDLKMKVEMMSEAALN | ||||||
Region | 987-1006 | Disordered | ||||
Sequence: EQSQQEAAKKHEEEKKELER | ||||||
Compositional bias | 990-1006 | Basic and acidic residues | ||||
Sequence: QQEAAKKHEEEKKELER | ||||||
Region | 1298-1319 | Disordered | ||||
Sequence: KRQLSSSSGNTDTQADEDERAQ | ||||||
Region | 1395-1414 | Disordered | ||||
Sequence: TQAQMSEDPPHSTHHGSRGE | ||||||
Zinc finger | 1417-1434 | CCHC-type | ||||
Sequence: PYCEICEMFGHWATNCND |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P30622-3
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
- Length1,438
- Mass (Da)162,246
- Last updated2009-10-13 v2
- ChecksumA7F125F7A96DBDDB
P30622-1
- Name2
- SynonymsLong
- Differences from canonical
- 457-467: Missing
P30622-2
- Name3
- SynonymsShort
- Differences from canonical
- 457-502: Missing
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
J3KP58 | J3KP58_HUMAN | CLIP1 | 1316 | ||
A0A3B3IS27 | A0A3B3IS27_HUMAN | CLIP1 | 107 | ||
A0A3B3ISJ8 | A0A3B3ISJ8_HUMAN | CLIP1 | 867 | ||
A0A3B3ITA2 | A0A3B3ITA2_HUMAN | CLIP1 | 791 | ||
F5H6A0 | F5H6A0_HUMAN | CLIP1 | 802 | ||
F5H367 | F5H367_HUMAN | CLIP1 | 83 | ||
F5H0N7 | F5H0N7_HUMAN | CLIP1 | 1063 | ||
F5H1T5 | F5H1T5_HUMAN | CLIP1 | 350 | ||
F5H270 | F5H270_HUMAN | CLIP1 | 108 |
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 132-188 | Polar residues | ||||
Sequence: DEANGLQTTPASRATSPLCTSTASMVSSSPSTPSNIPQKPSQPAAKEPSATPPISNL | ||||||
Sequence conflict | 193 | in Ref. 3; AAI14214 | ||||
Sequence: S → G | ||||||
Sequence conflict | 324 | in Ref. 3; AAI14214 | ||||
Sequence: S → P | ||||||
Alternative sequence | VSP_038201 | 457-467 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_000765 | 457-502 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 651 | in Ref. 3; AAI14214 | ||||
Sequence: T → A | ||||||
Sequence conflict | 682 | in Ref. 3; AAI14214 | ||||
Sequence: D → N | ||||||
Sequence conflict | 766 | in Ref. 3; AAI14214 | ||||
Sequence: L → P | ||||||
Compositional bias | 990-1006 | Basic and acidic residues | ||||
Sequence: QQEAAKKHEEEKKELER | ||||||
Sequence conflict | 1432 | in Ref. 3; AAI14214 | ||||
Sequence: C → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X64838 EMBL· GenBank· DDBJ | CAA46050.1 EMBL· GenBank· DDBJ | mRNA | ||
M97501 EMBL· GenBank· DDBJ | AAA35693.1 EMBL· GenBank· DDBJ | mRNA | ||
BC114213 EMBL· GenBank· DDBJ | AAI14214.1 EMBL· GenBank· DDBJ | mRNA | ||
BC117209 EMBL· GenBank· DDBJ | AAI17210.1 EMBL· GenBank· DDBJ | mRNA | ||
BC126305 EMBL· GenBank· DDBJ | AAI26306.1 EMBL· GenBank· DDBJ | mRNA |