P05107 · ITB2_HUMAN
- ProteinIntegrin beta-2
- GeneITGB2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids769 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrin ITGAL/ITGB2 is also a receptor for the secreted form of ubiquitin-like protein ISG15; the interaction is mediated by ITGAL (PubMed:29100055).
Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin ITGAX/ITGB2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin ITGAM/ITGB2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin ITGAM/ITGB2 is also a receptor for factor X. Integrin ITGAD/ITGB2 is a receptor for ICAM3 and VCAM1. Contributes to natural killer cell cytotoxicity (PubMed:15356110).
Involved in leukocyte adhesion and transmigration of leukocytes including T-cells and neutrophils (PubMed:11812992, PubMed:28807980).
Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation (PubMed:18587400).
Integrin ITGAL/ITGB2 in association with ICAM3, contributes to apoptotic neutrophil phagocytosis by macrophages (PubMed:23775590).
In association with alpha subunit ITGAM/CD11b, required for CD177-PRTN3-mediated activation of TNF primed neutrophils (PubMed:21193407).
Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin ITGAX/ITGB2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin ITGAM/ITGB2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin ITGAM/ITGB2 is also a receptor for factor X. Integrin ITGAD/ITGB2 is a receptor for ICAM3 and VCAM1. Contributes to natural killer cell cytotoxicity (PubMed:15356110).
Involved in leukocyte adhesion and transmigration of leukocytes including T-cells and neutrophils (PubMed:11812992, PubMed:28807980).
Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation (PubMed:18587400).
Integrin ITGAL/ITGB2 in association with ICAM3, contributes to apoptotic neutrophil phagocytosis by macrophages (PubMed:23775590).
In association with alpha subunit ITGAM/CD11b, required for CD177-PRTN3-mediated activation of TNF primed neutrophils (PubMed:21193407).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 136 | Mg2+ (UniProtKB | ChEBI); in MIDAS binding site | ||||
Sequence: S | ||||||
Binding site | 138 | Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site | ||||
Sequence: S | ||||||
Binding site | 138 | Mg2+ (UniProtKB | ChEBI); in MIDAS binding site | ||||
Sequence: S | ||||||
Binding site | 141 | Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site | ||||
Sequence: D | ||||||
Binding site | 142 | Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site | ||||
Sequence: D | ||||||
Binding site | 173 | Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: D | ||||||
Binding site | 229 | Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: N | ||||||
Binding site | 231 | Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: D | ||||||
Binding site | 233 | Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: P | ||||||
Binding site | 234 | Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: E | ||||||
Binding site | 234 | Mg2+ (UniProtKB | ChEBI); in MIDAS binding site | ||||
Sequence: E | ||||||
Binding site | 264 | Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site and liganded-open conformation | ||||
Sequence: D | ||||||
Binding site | 347 | Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site and unliganded-closed conformation | ||||
Sequence: E |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIntegrin beta-2
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP05107
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Membrane raft ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 23-700 | Extracellular | ||||
Sequence: QECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRCDTRPQLLMRGCAADDIMDPTSLAETQEDHNGGQKQLSPQKVTLYLRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLRNVKKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPDKLRNPCPNKEKECQPPFAFRHVLKLTNNSNQFQTEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKRSNEFDYPSVGQLAHKLAENNIQPIFAVTSRMVKTYEKLTEIIPKSAVGELSEDSSNVVHLIKNAYNKLSSRVFLDHNALPDTLKVTYDSFCSNGVTHRNQPRGDCDGVQINVPITFQVKVTATECIQEQSFVIRALGFTDIVTVQVLPQCECRCRDQSRDRSLCHGKGFLECGICRCDTGYIGKNCECQTQGRSSQELEGSCRKDNNSIICSGLGDCVCGQCLCHTSDVPGKLIYGQYCECDTINCERYNGQVCGGPGRGLCFCGKCRCHPGFEGSACQCERTTEGCLNPRRVECSGRGRCRCNVCECHSGYQLPLCQECPGCPSPCGKYISCAECLKFEKGPFGKNCSAACPGLQLSNNPVKGRTCKERDSEGCWVAYTLEQQDGMDRYLIYVDESRECVAGPN | ||||||
Transmembrane | 701-723 | Helical | ||||
Sequence: IAAIVGGTVAGIVLIGILLLVIW | ||||||
Topological domain | 724-769 | Cytoplasmic | ||||
Sequence: KALIHLSDLREYRRFEKEKLKSQWNNDNPLFKSATTTVMNPKFAES |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Leukocyte adhesion deficiency 1 (LAD1)
- Note
- DescriptionLAD1 patients have recurrent bacterial infections and their leukocytes are deficient in a wide range of adhesion-dependent functions.
- See alsoMIM:116920
Natural variants in LAD1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_003984 | 128 | D>N | in LAD1; dbSNP:rs137852615 | |
VAR_065661 | 128 | D>Y | in LAD1; dbSNP:rs137852615 | |
VAR_013402 | 138 | S>P | in LAD1; dbSNP:rs137852617 | |
VAR_003985 | 149 | L>P | in LAD1; dbSNP:rs137852611 | |
VAR_003986 | 169 | G>R | in LAD1; dbSNP:rs137852612 | |
VAR_003987 | 178 | P>L | in LAD1; dbSNP:rs137852614 | |
VAR_003988 | 196 | K>T | in LAD1; dbSNP:rs137852610 | |
VAR_065662 | 239 | A>T | in LAD1; dbSNP:rs179363873 | |
VAR_013403 | 273 | G>R | in LAD1; dbSNP:rs137852618 | |
VAR_003989 | 284 | G>S | in LAD1; dbSNP:rs137852616 | |
VAR_065663 | 300 | D>V | in LAD1; dbSNP:rs179363874 | |
VAR_003990 | 351 | N>S | in LAD1; dbSNP:rs137852613 | |
VAR_003991 | 586 | R>W | in LAD1; dbSNP:rs5030672 | |
VAR_003992 | 593 | R>C | in LAD1; dbSNP:rs137852609 | |
VAR_065664 | 716 | G>A | in LAD1; dbSNP:rs179363872 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_003984 | 128 | in LAD1; dbSNP:rs137852615 | |||
Sequence: D → N | ||||||
Natural variant | VAR_065661 | 128 | in LAD1; dbSNP:rs137852615 | |||
Sequence: D → Y | ||||||
Natural variant | VAR_013402 | 138 | in LAD1; dbSNP:rs137852617 | |||
Sequence: S → P | ||||||
Natural variant | VAR_003985 | 149 | in LAD1; dbSNP:rs137852611 | |||
Sequence: L → P | ||||||
Natural variant | VAR_003986 | 169 | in LAD1; dbSNP:rs137852612 | |||
Sequence: G → R | ||||||
Natural variant | VAR_003987 | 178 | in LAD1; dbSNP:rs137852614 | |||
Sequence: P → L | ||||||
Natural variant | VAR_003988 | 196 | in LAD1; dbSNP:rs137852610 | |||
Sequence: K → T | ||||||
Natural variant | VAR_065662 | 239 | in LAD1; dbSNP:rs179363873 | |||
Sequence: A → T | ||||||
Natural variant | VAR_013403 | 273 | in LAD1; dbSNP:rs137852618 | |||
Sequence: G → R | ||||||
Natural variant | VAR_003989 | 284 | in LAD1; dbSNP:rs137852616 | |||
Sequence: G → S | ||||||
Natural variant | VAR_065663 | 300 | in LAD1; dbSNP:rs179363874 | |||
Sequence: D → V | ||||||
Natural variant | VAR_003990 | 351 | in LAD1; dbSNP:rs137852613 | |||
Sequence: N → S | ||||||
Natural variant | VAR_030035 | 354 | in dbSNP:rs235330 | |||
Sequence: H → Q | ||||||
Natural variant | VAR_003991 | 586 | in LAD1; dbSNP:rs5030672 | |||
Sequence: R → W | ||||||
Natural variant | VAR_003992 | 593 | in LAD1; dbSNP:rs137852609 | |||
Sequence: R → C | ||||||
Natural variant | VAR_065664 | 716 | in LAD1; dbSNP:rs179363872 | |||
Sequence: G → A | ||||||
Mutagenesis | 758 | Abolishes phosphorylation. Reduces COS cell adhesion to ICAM1. | ||||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,038 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 signal, modified residue, chain, disulfide bond, glycosylation, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-22 | UniProt | |||||
Sequence: MLGLRPPLLALVGLLSLGCVLS | |||||||
Modified residue | 23 | UniProt | Pyrrolidone carboxylic acid | ||||
Sequence: Q | |||||||
Chain | PRO_0000016341 | 23-769 | UniProt | Integrin beta-2 | |||
Sequence: QECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRCDTRPQLLMRGCAADDIMDPTSLAETQEDHNGGQKQLSPQKVTLYLRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLRNVKKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPDKLRNPCPNKEKECQPPFAFRHVLKLTNNSNQFQTEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKRSNEFDYPSVGQLAHKLAENNIQPIFAVTSRMVKTYEKLTEIIPKSAVGELSEDSSNVVHLIKNAYNKLSSRVFLDHNALPDTLKVTYDSFCSNGVTHRNQPRGDCDGVQINVPITFQVKVTATECIQEQSFVIRALGFTDIVTVQVLPQCECRCRDQSRDRSLCHGKGFLECGICRCDTGYIGKNCECQTQGRSSQELEGSCRKDNNSIICSGLGDCVCGQCLCHTSDVPGKLIYGQYCECDTINCERYNGQVCGGPGRGLCFCGKCRCHPGFEGSACQCERTTEGCLNPRRVECSGRGRCRCNVCECHSGYQLPLCQECPGCPSPCGKYISCAECLKFEKGPFGKNCSAACPGLQLSNNPVKGRTCKERDSEGCWVAYTLEQQDGMDRYLIYVDESRECVAGPNIAAIVGGTVAGIVLIGILLLVIWKALIHLSDLREYRRFEKEKLKSQWNNDNPLFKSATTTVMNPKFAES | |||||||
Disulfide bond | 25↔43 | UniProt | |||||
Sequence: CTKFKVSSCRECIESGPGC | |||||||
Disulfide bond | 33↔447 | UniProt | |||||
Sequence: CRECIESGPGCTWCQKLNFTGPGDPDSIRCDTRPQLLMRGCAADDIMDPTSLAETQEDHNGGQKQLSPQKVTLYLRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLRNVKKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPDKLRNPCPNKEKECQPPFAFRHVLKLTNNSNQFQTEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKRSNEFDYPSVGQLAHKLAENNIQPIFAVTSRMVKTYEKLTEIIPKSAVGELSEDSSNVVHLIKNAYNKLSSRVFLDHNALPDTLKVTYDSFCSNGVTHRNQPRGDCDGVQINVPITFQVKVTATECIQEQSFVIRALGFTDIVTVQVLPQCEC | |||||||
Disulfide bond | 36↔62 | UniProt | |||||
Sequence: CIESGPGCTWCQKLNFTGPGDPDSIRC | |||||||
Disulfide bond | 46↔73 | UniProt | |||||
Sequence: CQKLNFTGPGDPDSIRCDTRPQLLMRGC | |||||||
Glycosylation | 50 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 116 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 191↔198 | UniProt | |||||
Sequence: CPNKEKEC | |||||||
Glycosylation | 212 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 246↔286 | UniProt | |||||
Sequence: CPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRC | |||||||
Glycosylation | 254 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 386↔400 | UniProt | |||||
Sequence: CSNGVTHRNQPRGDC | |||||||
Disulfide bond | 420↔445 | UniProt | |||||
Sequence: CIQEQSFVIRALGFTDIVTVQVLPQC | |||||||
Disulfide bond | 449↔467 | UniProt | |||||
Sequence: CRDQSRDRSLCHGKGFLEC | |||||||
Disulfide bond | 459↔470 | UniProt | |||||
Sequence: CHGKGFLECGIC | |||||||
Disulfide bond | 472↔481 | UniProt | |||||
Sequence: CDTGYIGKNC | |||||||
Disulfide bond | 483↔514 | UniProt | |||||
Sequence: CQTQGRSSQELEGSCRKDNNSIICSGLGDCVC | |||||||
Disulfide bond | 497↔512 | UniProt | |||||
Sequence: CRKDNNSIICSGLGDC | |||||||
Glycosylation | 501 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 506↔517 | UniProt | |||||
Sequence: CSGLGDCVCGQC | |||||||
Disulfide bond | 519↔534 | UniProt | |||||
Sequence: CHTSDVPGKLIYGQYC | |||||||
Disulfide bond | 536↔559 | UniProt | |||||
Sequence: CDTINCERYNGQVCGGPGRGLCFC | |||||||
Disulfide bond | 541↔557 | UniProt | |||||
Sequence: CERYNGQVCGGPGRGLC | |||||||
Disulfide bond | 549↔562 | UniProt | |||||
Sequence: CGGPGRGLCFCGKC | |||||||
Disulfide bond | 564↔573 | UniProt | |||||
Sequence: CHPGFEGSAC | |||||||
Disulfide bond | 575↔598 | UniProt | |||||
Sequence: CERTTEGCLNPRRVECSGRGRCRC | |||||||
Disulfide bond | 582↔596 | UniProt | |||||
Sequence: CLNPRRVECSGRGRC | |||||||
Disulfide bond | 590↔601 | UniProt | |||||
Sequence: CSGRGRCRCNVC | |||||||
Disulfide bond | 603↔612 | UniProt | |||||
Sequence: CHSGYQLPLC | |||||||
Disulfide bond | 615↔618 | UniProt | |||||
Sequence: CPGC | |||||||
Disulfide bond | 622↔662 | UniProt | |||||
Sequence: CGKYISCAECLKFEKGPFGKNCSAACPGLQLSNNPVKGRTC | |||||||
Disulfide bond | 628↔647 | UniProt | |||||
Sequence: CAECLKFEKGPFGKNCSAAC | |||||||
Disulfide bond | 631↔643 | UniProt | |||||
Sequence: CLKFEKGPFGKNC | |||||||
Glycosylation | 642 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 670↔695 | UniProt | |||||
Sequence: CWVAYTLEQQDGMDRYLIYVDESREC | |||||||
Modified residue | 745 | UniProt | Phosphoserine; by PKC | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 745 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 756 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 756 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 758 | UniProt | Phosphothreonine; by PKC; in vitro | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 758 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 759 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 760 | UniProt | Phosphothreonine; by PKC/PRKCA; in vitro | ||||
Sequence: T |
Post-translational modification
Both Ser-745 and Ser-756 become phosphorylated when T-cells are exposed to phorbol esters (PubMed:11700305).
Phosphorylation on Thr-758 (but not on Ser-756) allows interaction with 14-3-3 proteins (PubMed:11700305, PubMed:16301335).
Phosphorylation on Thr-758 (but not on Ser-756) allows interaction with 14-3-3 proteins (PubMed:11700305, PubMed:16301335).
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Heterodimer of an alpha and a beta subunit (PubMed:20033057).
The ITGB2 beta subunit associates with the ITGAL, ITGAM, ITGAX or ITGAD alpha subunits. Found in a complex with CD177 and ITGAM/CD11b (PubMed:21193407, PubMed:28807980).
Interacts with FGR (By similarity).
Interacts with COPS5 and RANBP9 (PubMed:10766246, PubMed:14722085).
Interacts with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and 23) (PubMed:19828450).
Interacts with THBD (PubMed:27055590).
The ITGB2 beta subunit associates with the ITGAL, ITGAM, ITGAX or ITGAD alpha subunits. Found in a complex with CD177 and ITGAM/CD11b (PubMed:21193407, PubMed:28807980).
Interacts with FGR (By similarity).
Interacts with COPS5 and RANBP9 (PubMed:10766246, PubMed:14722085).
Interacts with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and 23) (PubMed:19828450).
Interacts with THBD (PubMed:27055590).
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-74 | PSI | ||||
Sequence: ECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRCDTRPQLLMRGCA | ||||||
Domain | 124-363 | VWFA | ||||
Sequence: GYPIDLYYLMDLSYSMLDDLRNVKKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPDKLRNPCPNKEKECQPPFAFRHVLKLTNNSNQFQTEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKRSNEFDYPSVGQLAHKLAENNIQPIFAVTSRMVKTYEKLTEIIPKSAVGELSEDSSNVVHLIKNAYNKL | ||||||
Motif | 397-399 | Cell attachment site | ||||
Sequence: RGD | ||||||
Domain | 449-496 | EGF-like 1 | ||||
Sequence: CRDQSRDRSLCHGKGFLECGICRCDTGYIGKNCECQTQGRSSQELEGS | ||||||
Domain | 497-540 | EGF-like 2 | ||||
Sequence: CRKDNNSIICSGLGDCVCGQCLCHTSDVPGKLIYGQYCECDTIN | ||||||
Domain | 541-581 | EGF-like 3 | ||||
Sequence: CERYNGQVCGGPGRGLCFCGKCRCHPGFEGSACQCERTTEG | ||||||
Domain | 582-617 | EGF-like 4 | ||||
Sequence: CLNPRRVECSGRGRCRCNVCECHSGYQLPLCQECPG |
Domain
The VWFA domain (or beta I domain) contains three cation-binding sites: the ligand-associated metal ion-binding site (LIMBS or SyMBS), the metal ion-dependent adhesion site (MIDAS), and the adjacent MIDAS site (ADMIDAS). This domain is also part of the ligand-binding site.
Sequence similarities
Belongs to the integrin beta chain family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length769
- Mass (Da)84,791
- Last updated2024-01-24 v3
- Checksum0390BD89F1E71E98
Computationally mapped potential isoform sequences
There are 14 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A8MVG7 | A8MVG7_HUMAN | ITGB2 | 108 | ||
J3KNI6 | J3KNI6_HUMAN | ITGB2 | 322 | ||
D3DSM0 | D3DSM0_HUMAN | ITGB2 | 712 | ||
E7EVZ9 | E7EVZ9_HUMAN | ITGB2 | 166 | ||
A0AAA9WZN5 | A0AAA9WZN5_HUMAN | ITGB2 | 793 | ||
A0A494C0X7 | A0A494C0X7_HUMAN | ITGB2 | 769 | ||
E5RIG7 | E5RIG7_HUMAN | ITGB2 | 120 | ||
E5RIE4 | E5RIE4_HUMAN | ITGB2 | 93 | ||
E5RK25 | E5RK25_HUMAN | ITGB2 | 160 | ||
E5RK54 | E5RK54_HUMAN | ITGB2 | 49 | ||
E5RGK9 | E5RGK9_HUMAN | ITGB2 | 71 | ||
E5RHE6 | E5RHE6_HUMAN | ITGB2 | 37 | ||
E5RHT0 | E5RHT0_HUMAN | ITGB2 | 49 | ||
E5RFI0 | E5RFI0_HUMAN | ITGB2 | 70 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 199 | in Ref. 8; CAA68266 | ||||
Sequence: Q → P | ||||||
Sequence conflict | 279 | in Ref. 4; BAD96225 | ||||
Sequence: L → P | ||||||
Sequence conflict | 526 | in Ref. 3; BAG53190 | ||||
Sequence: G → C | ||||||
Sequence conflict | 630 | in Ref. 3; BAG53190 | ||||
Sequence: E → K |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M15395 EMBL· GenBank· DDBJ | AAA59490.1 EMBL· GenBank· DDBJ | mRNA | ||
X64072 EMBL· GenBank· DDBJ | CAA45427.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X64073 EMBL· GenBank· DDBJ | CAA45427.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X64074 EMBL· GenBank· DDBJ | CAA45427.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X64075 EMBL· GenBank· DDBJ | CAA45427.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X64076 EMBL· GenBank· DDBJ | CAA45427.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X64077 EMBL· GenBank· DDBJ | CAA45427.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X64078 EMBL· GenBank· DDBJ | CAA45427.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X64079 EMBL· GenBank· DDBJ | CAA45427.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X64080 EMBL· GenBank· DDBJ | CAA45427.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X64081 EMBL· GenBank· DDBJ | CAA45427.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X64082 EMBL· GenBank· DDBJ | CAA45427.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X64083 EMBL· GenBank· DDBJ | CAA45427.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X63924 EMBL· GenBank· DDBJ | CAA45427.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X63925 EMBL· GenBank· DDBJ | CAA45427.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X63926 EMBL· GenBank· DDBJ | CAA45427.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK095992 EMBL· GenBank· DDBJ | BAG53190.1 EMBL· GenBank· DDBJ | mRNA | ||
AK222505 EMBL· GenBank· DDBJ | BAD96225.1 EMBL· GenBank· DDBJ | mRNA | ||
AL163300 EMBL· GenBank· DDBJ | CAB90553.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09381.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09382.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09385.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC005861 EMBL· GenBank· DDBJ | AAH05861.1 EMBL· GenBank· DDBJ | mRNA | ||
Y00057 EMBL· GenBank· DDBJ | CAA68266.1 EMBL· GenBank· DDBJ | mRNA | ||
S81234 EMBL· GenBank· DDBJ | AAB21404.1 EMBL· GenBank· DDBJ | mRNA |