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Reviewed, UniProtKB/Swiss-Prot P05556 (ITB1_HUMAN)

Last modified September 2, 2008. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Integrin beta-1
Alternative name(s):
    Fibronectin receptor subunit beta
    Integrin VLA-4 subunit beta
    CD_antigen=CD29
Gene names
Name: ITGB1
Synonyms: FNRB, MDF2, MSK12
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length798 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-4/beta-1 is a receptor for VCAM1. It 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. 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. Isoform beta-1B interferes with isoform beta-1A resulting in a dominant negative effect on cell adhesion and migration (in vitro). In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.

Subunit structure

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. Interacts with FLNA. Binds LGALS3BP and ITGB1BP3, when associated with alpha-7, but not with alpha-5 By similarity. Interacts with FLNB and RANBP9. Isoform Beta-1D interacts with ACE2. Isoform Beta-1A interacts with the C-terminal region of FLNC. Interacts with HIV-1 Tat. Binds to human echoviruses 1 and 8 capsid proteins and acts as a receptor for these viruses.

Subcellular location

Cell membrane; Single-pass type I membrane protein. Melanosome. Note= Isoform beta-1B does not localize to focal adhesions. Highly enriched in stage I melanosomes.

Tissue specificity

Isoform beta-1A is widely expressed, other isoforms are generally coexpressed with a more restricted distribution. Isoform beta-1B is expressed in skin, liver, skeletal muscle, cardiac muscle, placenta, umbelical vein endothelial cells, neuroblastoma cells, lymphoma cells, hepatoma cells and astrocytoma cells. Isoform beta-1C and isoform beta-1C-2 are expressed in muscle, kidney, liver, placenta, cervical epithelium, umbilical vein endothelial cells, fibroblast cells, embryonal kidney cells, platelets and several blood cell lines. Isoform beta-C-2, rather than isoform beta-1C, is selectively expressed in primary T-cells. Isoform beta-1C is expressed in nonproliferating and differentiated prostate gland epithelial cells. Isoform beta-1D is expressed specifically in striated muscle (skeletal and cardiac muscle).

Sequence similarities

Belongs to the integrin beta chain family.

Contains 1 VWFA domain.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-703066,EBI-703066

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Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform Beta-1A (identifier: P05556-1)

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.
Isoform Beta-1B (identifier: P05556-2)

The sequence of this isoform differs from the canonical sequence as follows:
     778-798: GENPIYKSAVTTVVNPKYEGK → VSYKTSKKQSGL
Isoform Beta-1C (identifier: P05556-3)

The sequence of this isoform differs from the canonical sequence as follows:
     778-798: GENPIYKSAVTTVVNPKYEGK → SLSVAQPGVQWCDISSLQPLTSRFQQFSCLSLPSTWDYRVKILFIRVP
Isoform Beta-1C-2 (identifier: P05556-4)

The sequence of this isoform differs from the canonical sequence as follows:
     778-798: GENPIYKSAVTTVVNPKYEGK → PGVQWCDISSLQPLTSRFQQFSCLSLPSTWDYRVKILFIRVP
Isoform Beta-1D (identifier: P05556-5)

The sequence of this isoform differs from the canonical sequence as follows:
     778-798: GENPIYKSAVTTVVNPKYEGK → QENPIYKSPINNFKNPNYGRKAGL

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 2020
Chain21 – 798778Integrin beta-1

Regions

Topological domain21 – 728708Extracellular Potential
Transmembrane729 – 75123 Potential
Topological domain752 – 79847Cytoplasmic Potential
Domain140 – 378239VWFA
Repeat466 – 51550I
Repeat516 – 55944II
Repeat560 – 59839III
Repeat599 – 63537IV
Region466 – 635170Cysteine-rich tandem repeats

Amino acid modifications

Modified residue7831Phosphotyrosine
Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation2121N-linked (GlcNAc...) Potential
Glycosylation2691N-linked (GlcNAc...) Potential
Glycosylation3631N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...)
Glycosylation4171N-linked (GlcNAc...) Potential
Glycosylation4811N-linked (GlcNAc...) Potential
Glycosylation5201N-linked (GlcNAc...) Potential
Glycosylation5841N-linked (GlcNAc...) Potential
Glycosylation6691N-linked (GlcNAc...) Potential
Disulfide bond27 ↔ 464 By similarity
Disulfide bond35 ↔ 45 By similarity
Disulfide bond38 ↔ 75 By similarity
Disulfide bond48 ↔ 64 By similarity
Disulfide bond207 ↔ 213 By similarity
Disulfide bond261 ↔ 301 By similarity
Disulfide bond401 ↔ 415 By similarity
Disulfide bond435 ↔ 691 By similarity
Disulfide bond462 ↔ 466 By similarity
Disulfide bond477 ↔ 489 By similarity
Disulfide bond486 ↔ 525 By similarity
Disulfide bond491 ↔ 500 By similarity
Disulfide bond502 ↔ 516 By similarity
Disulfide bond531 ↔ 536 By similarity
Disulfide bond533 ↔ 568 By similarity
Disulfide bond538 ↔ 553 By similarity
Disulfide bond555 ↔ 560 By similarity
Disulfide bond574 ↔ 579 By similarity
Disulfide bond576 ↔ 607 By similarity
Disulfide bond581 ↔ 590 By similarity
Disulfide bond592 ↔ 599 By similarity
Disulfide bond613 ↔ 618 By similarity
Disulfide bond615 ↔ 661 By similarity
Disulfide bond620 ↔ 630 By similarity
Disulfide bond633 ↔ 636 By similarity
Disulfide bond640 ↔ 649 By similarity
Disulfide bond646 ↔ 723 By similarity
Disulfide bond665 ↔ 699 By similarity

Natural variations

Alternative sequence778 – 79821GENPI…KYEGK → VSYKTSKKQSGL in isoform Beta-1B.
Alternative sequence778 – 79821GENPI…KYEGK → SLSVAQPGVQWCDISSLQPL TSRFQQFSCLSLPSTWDYRV KILFIRVP in isoform Beta-1C.
Alternative sequence778 – 79821GENPI…KYEGK → PGVQWCDISSLQPLTSRFQQ FSCLSLPSTWDYRVKILFIR VP in isoform Beta-1C-2.
Alternative sequence778 – 79821GENPI…KYEGK → QENPIYKSPINNFKNPNYGR KAGL in isoform Beta-1D.

Experimental info

Mutagenesis7781G → Q: Loss of beta-1A interaction with FLNA and FLNB
Mutagenesis7861A → P: Loss of beta-1A interaction with FLNA and FLNB

Secondary structure

1 ............................................................................... 798
Helix Strand Turn

Details...