P09055 · ITB1_MOUSE
- ProteinIntegrin beta-1
- GeneItgb1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids798 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Integrin alpha-4/beta-1 is a receptor for VCAM1 and recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition (PubMed:12941630).
Involved in promoting endothelial cell motility and angiogenesis (PubMed:15181153).
Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules (PubMed:21768292).
May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis (PubMed:18804435).
ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (By similarity).
ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (By similarity).
ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (By similarity).
ITGA5:ITGB1 acts as a receptor for fibronectin FN1 and mediates R-G-D-dependent cell adhesion to FN1 (By similarity).
ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling (By similarity).
ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling (By similarity).
Plays an important role in myoblast differentiation and fusion during skeletal myogenesis (By similarity).
ITGA9:ITGB1 may play a crucial role in SVEP1/polydom-mediated myoblast cell adhesion (PubMed:22654117).
Integrins ITGA9:ITGB1 and ITGA4:ITGB1 repress PRKCA-mediated L-type voltage-gated channel Ca2+ influx and ROCK-mediated calcium sensitivity in vascular smooth muscle cells via their interaction with SVEP1, thereby inhibit vasocontraction (PubMed:35802072).
Isoform 2
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 152 | Mg2+ (UniProtKB | ChEBI); in MIDAS binding site | ||||
Sequence: S | ||||||
Binding site | 154 | Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site | ||||
Sequence: S | ||||||
Binding site | 154 | Mg2+ (UniProtKB | ChEBI); in MIDAS binding site | ||||
Sequence: S | ||||||
Binding site | 157 | Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site | ||||
Sequence: D | ||||||
Binding site | 158 | Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site | ||||
Sequence: D | ||||||
Binding site | 189 | Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: E | ||||||
Binding site | 244 | Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: N | ||||||
Binding site | 246 | Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: D | ||||||
Binding site | 248 | Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: P | ||||||
Binding site | 249 | Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: E | ||||||
Binding site | 249 | Mg2+ (UniProtKB | ChEBI); in MIDAS binding site | ||||
Sequence: E | ||||||
Binding site | 362 | Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site | ||||
Sequence: G |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIntegrin beta-1
- Alternative names
- CD Antigen Name
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 accessionP09055
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform 2
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 21-728 | Extracellular | ||||
Sequence: QTDKNRCLKANAKSCGECIQAGPNCGWCTNTTFLQEGMPTSARCDDLEALKKKGCQPSDIENPRGSQTIKKNKNVTNRSKGMAEKLRPEDITQIQPQQLLLKLRSGEPQKFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTDRGEFFNELVGQQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNVYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSGNSSNVIQLIIDAYNSLSSEVILENSKLPDGVTINYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITANKCPNKESETIKIKPLGFTEEVEVVLQFICKCNCQSHGIPASPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCRCRVCECYPNYTGSACDCSLDTGPCLASNGQICNGRGICECGACKCTDPKFQGPTCETCQTCLGVCAEHKECVQCRAFNKGEKKDTCAQECSHFNLTKVESREKLPQPVQVDPVTHCKEKDIDDCWFYFTYSVNGNNEAIVHVVETPDCPTGPD | ||||||
Transmembrane | 729-751 | Helical | ||||
Sequence: IIPIVAGVVAGIVLIGLALLLIW | ||||||
Topological domain | 752-798 | Cytoplasmic | ||||
Sequence: KLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGK |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 783 | Reduced endocytosis; when associated with F-795. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 795 | Reduced endocytosis; when associated with F-783. | ||||
Sequence: Y → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 31 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MNLQLVSWIGLISLICSVFG | ||||||
Chain | PRO_0000016335 | 21-798 | Integrin beta-1 | |||
Sequence: QTDKNRCLKANAKSCGECIQAGPNCGWCTNTTFLQEGMPTSARCDDLEALKKKGCQPSDIENPRGSQTIKKNKNVTNRSKGMAEKLRPEDITQIQPQQLLLKLRSGEPQKFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTDRGEFFNELVGQQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNVYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSGNSSNVIQLIIDAYNSLSSEVILENSKLPDGVTINYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITANKCPNKESETIKIKPLGFTEEVEVVLQFICKCNCQSHGIPASPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCRCRVCECYPNYTGSACDCSLDTGPCLASNGQICNGRGICECGACKCTDPKFQGPTCETCQTCLGVCAEHKECVQCRAFNKGEKKDTCAQECSHFNLTKVESREKLPQPVQVDPVTHCKEKDIDDCWFYFTYSVNGNNEAIVHVVETPDCPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGK | ||||||
Disulfide bond | 27↔45 | |||||
Sequence: CLKANAKSCGECIQAGPNC | ||||||
Disulfide bond | 35↔464 | |||||
Sequence: CGECIQAGPNCGWCTNTTFLQEGMPTSARCDDLEALKKKGCQPSDIENPRGSQTIKKNKNVTNRSKGMAEKLRPEDITQIQPQQLLLKLRSGEPQKFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTDRGEFFNELVGQQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNVYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSGNSSNVIQLIIDAYNSLSSEVILENSKLPDGVTINYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITANKCPNKESETIKIKPLGFTEEVEVVLQFICKC | ||||||
Disulfide bond | 38↔64 | |||||
Sequence: CIQAGPNCGWCTNTTFLQEGMPTSARC | ||||||
Disulfide bond | 48↔75 | |||||
Sequence: CTNTTFLQEGMPTSARCDDLEALKKKGC | ||||||
Glycosylation | 50 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 94 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 97 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 207↔213 | |||||
Sequence: CTSEQNC | ||||||
Glycosylation | 212 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 261↔301 | |||||
Sequence: CGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQC | ||||||
Glycosylation | 269 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 363 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 401↔415 | |||||
Sequence: CKNGVNGTGENGRKC | ||||||
Glycosylation | 406 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 417 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 435↔462 | |||||
Sequence: CPNKESETIKIKPLGFTEEVEVVLQFIC | ||||||
Disulfide bond | 466↔486 | |||||
Sequence: CQSHGIPASPKCHEGNGTFEC | ||||||
Disulfide bond | 477↔489 | |||||
Sequence: CHEGNGTFECGAC | ||||||
Glycosylation | 481 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 491↔500 | |||||
Sequence: CNEGRVGRHC | ||||||
Disulfide bond | 502↔533 | |||||
Sequence: CSTDEVNSEDMDAYCRKENSSEICSNNGECVC | ||||||
Disulfide bond | 516↔531 | |||||
Sequence: CRKENSSEICSNNGEC | ||||||
Glycosylation | 520 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 525↔536 | |||||
Sequence: CSNNGECVCGQC | ||||||
Disulfide bond | 538↔553 | |||||
Sequence: CRKRDNTNEIYSGKFC | ||||||
Disulfide bond | 555↔576 | |||||
Sequence: CDNFNCDRSNGLICGGNGVCRC | ||||||
Disulfide bond | 560↔574 | |||||
Sequence: CDRSNGLICGGNGVC | ||||||
Disulfide bond | 568↔579 | |||||
Sequence: CGGNGVCRCRVC | ||||||
Disulfide bond | 581↔590 | |||||
Sequence: CYPNYTGSAC | ||||||
Glycosylation | 584 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 592↔615 | |||||
Sequence: CSLDTGPCLASNGQICNGRGICEC | ||||||
Disulfide bond | 599↔613 | |||||
Sequence: CLASNGQICNGRGIC | ||||||
Disulfide bond | 607↔618 | |||||
Sequence: CNGRGICECGAC | ||||||
Disulfide bond | 620↔630 | |||||
Sequence: CTDPKFQGPTC | ||||||
Disulfide bond | 633↔636 | |||||
Sequence: CQTC | ||||||
Disulfide bond | 640↔691 | |||||
Sequence: CAEHKECVQCRAFNKGEKKDTCAQECSHFNLTKVESREKLPQPVQVDPVTHC | ||||||
Disulfide bond | 646↔665 | |||||
Sequence: CVQCRAFNKGEKKDTCAQEC | ||||||
Disulfide bond | 649↔661 | |||||
Sequence: CRAFNKGEKKDTC | ||||||
Glycosylation | 669 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 699↔723 | |||||
Sequence: CWFYFTYSVNGNNEAIVHVVETPDC | ||||||
Modified residue | 777 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 783 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 785 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 789 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 794 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 794 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform 1
Isoform 2
Developmental stage
Expression is down-regulated during myodifferentiation in culture (PubMed:8567725).
Isoform 2
Gene expression databases
Interaction
Subunit
Heterodimer of an alpha and a beta subunit. Beta-1 associates with either alpha-1, alpha-2, alpha-3, alpha-4, alpha-5, alpha-6, alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or alpha-V. ITGA6:ITGB1 is found in a complex with CD9; interaction takes place in oocytes and is involved in sperm-egg fusion (PubMed:10634791).
Binds LGALS3BP and NMRK2, when associated with alpha-7, but not with alpha-5. Interacts with FLNA, FLNB, FLNC and RANBP9. Interacts with KRT1 in the presence of RACK1 and SRC. Interacts with JAML; integrin alpha-4/beta-1 may regulate leukocyte to endothelial cells adhesion by controlling JAML homodimerization. Interacts with RAB21. Interacts (via the cytoplasmic region) with RAB25 (via the hypervariable C-terminal region). Interacts with MYO10. Interacts with ITGB1BP1 (via C-terminal region); the interaction is a prerequisite for focal adhesion disassembly. Interacts with TLN1; the interaction is prevented by competitive binding of ITGB1BP1. Interacts with ACAP1; required for ITGB1 recycling. Interacts with ASAP3. Interacts with FERMT2; the interaction is inhibited in presence of ITGB1BP1. Interacts with DAB2. Interacts with FGR and HCK. Isoform 2 interacts with alpha-7A and alpha-7B in adult skeletal muscle. Isoform 2 interacts with alpha-7B in cardiomyocytes of adult heart. Interacts with EMP2; the interaction may be direct or indirect and ITGB1 has a heterodimer form (PubMed:12189152).
ITGA5:ITGB1 interacts with CCN3 (By similarity).
ITGA4:ITGB1 is found in a ternary complex with CX3CR1 and CX3CL1 (By similarity).
ITGA5:ITGB1 interacts with FBN1 (By similarity).
ITGA5:ITGB1 interacts with IL1B. Interacts with MDK (PubMed:15466886).
ITGA4:ITGB1 interacts with MDK; this interaction mediates MDK-induced osteoblast cells migration through PXN phosphorylation (PubMed:15466886).
ITGA6:ITGB1 interacts with MDK; this interaction mediates MDK-induced neurite-outgrowth (PubMed:15466886).
ITGA5:ITGB1 interacts with ACE2 (By similarity).
Interacts with TMEM182 (By similarity).
Interacts with LAMB1 (PubMed:34427057).
Interacts with tensin TNS3; TNS3 also interacts with PEAK1, thus acting as an adapter molecule to bridge the association of PEAK1 with ITGB1 (PubMed:35687021).
Interacts with tensin TNS4; the interaction displaces tensin TNS3 from the ITGB1 cytoplasmic tail and promotes ITGB1 stability (By similarity).
Integrin ITGA9:ITGB1 interacts with SPP1/OPN (via N-terminus) (PubMed:22654117).
Integrin ITGA9:ITGB1 interacts with TNC/TNFN3 (via the 3rd Fibronectin type-III domain) (PubMed:22654117).
Integrins ITGA4:ITGB1 and ITGA9:ITGB1 interact with SVEP1 (via Sushi domain 21); thereby inhibit Ca2+ intracellular signaling and as a result repress vasocontraction (PubMed:22654117, PubMed:28179430).
ITGA4:ITGB1 and ITGA5:ITGB1 interacts with SELP (By similarity).
Interacts with CD248 (PubMed:38061240).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P09055 | Csf2rb P26955 | 2 | EBI-644224, EBI-1810026 | |
BINARY | P09055 | Nme2 Q01768 | 3 | EBI-644224, EBI-642573 | |
BINARY | P09055 | Tmem158 Q6F5E0 | 3 | EBI-644224, EBI-645317 | |
BINARY | P09055 | Wasl Q91YD9 | 2 | EBI-644224, EBI-642417 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 26-76 | PSI | ||||
Sequence: RCLKANAKSCGECIQAGPNCGWCTNTTFLQEGMPTSARCDDLEALKKKGCQ | ||||||
Region | 76-104 | Disordered | ||||
Sequence: QPSDIENPRGSQTIKKNKNVTNRSKGMAE | ||||||
Compositional bias | 80-96 | Polar residues | ||||
Sequence: IENPRGSQTIKKNKNVT | ||||||
Domain | 140-378 | VWFA | ||||
Sequence: DYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTDRGEFFNELVGQQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNVYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSGNSSNVIQLIIDAYNSL | ||||||
Region | 207-213 | CX3CL1-binding | ||||
Sequence: CTSEQNC | ||||||
Region | 295-314 | CX3CL1-binding | ||||
Sequence: LPNDGQCHLENNVYTMSHYY | ||||||
Region | 383-465 | Interaction with TMEM182 | ||||
Sequence: ILENSKLPDGVTINYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITANKCPNKESETIKIKPLGFTEEVEVVLQFICKCN | ||||||
Domain | 439-501 | EGF-like 1 | ||||
Sequence: ESETIKIKPLGFTEEVEVVLQFICKCNCQSHGIPASPKCHEGNGTFECGACRCNEGRVGRHCE | ||||||
Domain | 502-554 | EGF-like 2 | ||||
Sequence: CSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCE | ||||||
Domain | 555-591 | EGF-like 3 | ||||
Sequence: CDNFNCDRSNGLICGGNGVCRCRVCECYPNYTGSACD | ||||||
Domain | 592-635 | EGF-like 4 | ||||
Sequence: CSLDTGPCLASNGQICNGRGICECGACKCTDPKFQGPTCETCQT | ||||||
Region | 762-767 | Signal for sorting from recycling endosomes; interaction with ACAP1 | ||||
Sequence: EFAKFE | ||||||
Region | 785-792 | Interaction with ITGB1BP1 | ||||
Sequence: SAVTTVVN |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P09055-1
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
- SynonymsBeta-1A
- Length798
- Mass (Da)88,231
- Last updated1988-11-01 v1
- Checksum26788F7F0A168B56
P09055-2
- Name2
- SynonymsBeta-1D
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0A0MQJ3 | A0A0A0MQJ3_MOUSE | Itgb1 | 112 | ||
D6RJL5 | D6RJL5_MOUSE | Itgb1 | 58 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 5 | in Ref. 2; BAC40532 | ||||
Sequence: L → Q | ||||||
Sequence conflict | 72 | in Ref. 2; BAE35290 | ||||
Sequence: K → E | ||||||
Compositional bias | 80-96 | Polar residues | ||||
Sequence: IENPRGSQTIKKNKNVT | ||||||
Sequence conflict | 385 | in Ref. 2; BAC36379 | ||||
Sequence: E → D | ||||||
Sequence conflict | 385 | in Ref. 6; CAA33272 | ||||
Sequence: E → P | ||||||
Sequence conflict | 392 | in Ref. 6; CAA33272 | ||||
Sequence: G → A | ||||||
Sequence conflict | 407 | in Ref. 2; BAC36379 | ||||
Sequence: G → E | ||||||
Sequence conflict | 443-445 | in Ref. 6; CAA33272 | ||||
Sequence: IKI → HSKL | ||||||
Alternative sequence | VSP_053581 | 778 | in isoform 2 | |||
Sequence: G → Q | ||||||
Alternative sequence | VSP_053582 | 786-798 | in isoform 2 | |||
Sequence: AVTTVVNPKYEGK → PINNFKNPNYGRKAGL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y00769 EMBL· GenBank· DDBJ | CAA68738.1 EMBL· GenBank· DDBJ | mRNA | ||
AK076526 EMBL· GenBank· DDBJ | BAC36379.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK088729 EMBL· GenBank· DDBJ | BAC40532.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159689 EMBL· GenBank· DDBJ | BAE35290.1 EMBL· GenBank· DDBJ | mRNA | ||
AK167682 EMBL· GenBank· DDBJ | BAE39731.1 EMBL· GenBank· DDBJ | mRNA | ||
AC156608 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH466525 EMBL· GenBank· DDBJ | EDL11832.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC050906 EMBL· GenBank· DDBJ | AAH50906.1 EMBL· GenBank· DDBJ | mRNA | ||
X15202 EMBL· GenBank· DDBJ | CAA33272.1 EMBL· GenBank· DDBJ | mRNA | ||
U37029 EMBL· GenBank· DDBJ | AAA80243.1 EMBL· GenBank· DDBJ | mRNA | ||
U47283 EMBL· GenBank· DDBJ | AAA88821.1 EMBL· GenBank· DDBJ | Genomic DNA |