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P05556 (ITB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 181. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Integrin beta-1
Alternative name(s):
Fibronectin receptor subunit beta
Glycoprotein IIa
Short name=GPIIA
VLA-4 subunit beta
CD_antigen=CD29
Gene names
Name:ITGB1
Synonyms:FNRB, MDF2, MSK12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

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 2 interferes with isoform 1 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. When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and GNB2L1/RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis. Ref.8 Ref.24 Ref.28 Ref.33 Ref.35 Ref.36 Ref.44

Isoform 5:Isoform 5 displaces isoform 1 in striated muscles By similarity. Ref.8 Ref.24 Ref.28 Ref.33 Ref.35 Ref.36 Ref.44

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. Binds LGALS3BP and NMRK2, when associated with alpha-7, but not with alpha-5. Interacts with FGR and HCK. Interacts (via the cytoplasmic region) with RAB25 (via the hypervariable C-terminal region). Interacts with RAB21. Interacts with KRT1 in the presence of GNB2L1 and SRC. Interacts with AMICA1; integrin alpha-4/beta-1 may regulate leukocyte to endothelial cells adhesion by controlling AMICA1 homodimerization. Interacts with HIV-1 Tat. Binds to human echoviruses 1 and 8 capsid proteins and acts as a receptor for these viruses. Interacts with FLNA, FLNB and RANBP9. Isoform 5 interacts with ACE2. Isoform 1 interacts with the C-terminal region of FLNC. Interacts with MYO10. Interacts with DAB2. Interacts with FERMT2; the interaction is inhibited in presence of ITGB1BP1. Interacts with ITGB1BP1 (via C-terminus region); the interaction is a prerequisite for focal adhesion disassembly. Interacts with TLN1; the interaction is prevented by competitive binding of ITGB1BP1. Interacts with human cytomegalovirus/HHV-5 envelope glycoprotein B/gB. Interacts with ACAP1; required for ITGB1 recycling. Interacts with ASAP3. Isoform 5 interacts with alpha-7A and alpha-7B in adult skeletal muscle. Isoform 5 interacts with alpha-7B in cardiomyocytes of adult heart. Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.31 Ref.33 Ref.34 Ref.36 Ref.41 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48

Subcellular location

Cell membrane; Single-pass type I membrane protein. Recycling endosome. Melanosome. Cleavage furrow. Cell projectionlamellipodium. Cell projectionruffle. Note: Isoform 2 does not localize to focal adhesions. Highly enriched in stage I melanosomes. Located on plasma membrane of neuroblastoma NMB7 cells. In a lung cancer cell line, in prometaphase and metaphase, localizes diffusely at the membrane and in a few intracellular vesicles. In early telophase, detected mainly on the matrix-facing side of the cells. By mid-telophase, concentrated to the ingressing cleavage furrow, mainly to the basal side of the furrow. In late telophase, concentrated to the extending protrusions formed at the opposite ends of the spreading daughter cells, in vesicles at the base of the lamellipodia formed by the separating daughter cells. Colocalizes with ITGB1BP1 and metastatic suppressor protein NME2 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen. Translocates from peripheral focal adhesions sites to fibrillar adhesions in a ITGB1BP1-dependent manner. Ref.7 Ref.10 Ref.16 Ref.21 Ref.28 Ref.32 Ref.33 Ref.35 Ref.46

Isoform 5: Cell membranesarcolemma By similarity. Cell junction By similarity. Note: In cardiac muscle, isoform 5 is found in costameres and intercalated disks By similarity. Ref.7 Ref.10 Ref.16 Ref.21 Ref.28 Ref.32 Ref.33 Ref.35 Ref.46

Tissue specificity

Isoform 1 is widely expressed, other isoforms are generally coexpressed with a more restricted distribution. Isoform 2 is expressed in skin, liver, skeletal muscle, cardiac muscle, placenta, umbilical vein endothelial cells, neuroblastoma cells, lymphoma cells, hepatoma cells and astrocytoma cells. Isoform 3 and isoform 4 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 4, rather than isoform 3, is selectively expressed in peripheral T-cells. Isoform 3 is expressed in non-proliferating and differentiated prostate gland epithelial cells and in platelets, on the surface of erythroleukemia cells and in various hematopoietic cell lines. Isoform 5 is expressed specifically in striated muscle (skeletal and cardiac muscle). Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Post-translational modification

The cysteine residues are involved in intrachain disulfide bonds By similarity.

Sequence similarities

Belongs to the integrin beta chain family.

Contains 1 VWFA domain.

Sequence caution

The sequence CAD97649.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCell adhesion
Host-virus interaction
   Cellular componentCell junction
Cell membrane
Cell projection
Endosome
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Magnesium
Metal-binding
   Molecular functionHost cell receptor for virus entry
Integrin
Receptor
   PTMAcetylation
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred by curator PubMed 1715889. Source: BHF-UCL

G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

calcium-independent cell-matrix adhesion

Inferred from genetic interaction PubMed 19651211. Source: MGI

cardiac muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

cell fate specification

Inferred from electronic annotation. Source: Ensembl

cell junction assembly

Traceable author statement. Source: Reactome

cell migration

Traceable author statement Ref.21. Source: HGNC

cell migration involved in sprouting angiogenesis

Inferred from electronic annotation. Source: Ensembl

cell-cell adhesion mediated by integrin

Inferred from expression pattern PubMed 17704059. Source: BHF-UCL

cell-matrix adhesion

Inferred from mutant phenotype PubMed 18156211. Source: BHF-UCL

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular defense response

Traceable author statement PubMed 10201960. Source: ProtInc

cellular response to ionizing radiation

Inferred from electronic annotation. Source: Ensembl

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to vitamin D

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Traceable author statement. Source: Reactome

formation of radial glial scaffolds

Inferred from electronic annotation. Source: Ensembl

germ cell migration

Inferred from electronic annotation. Source: Ensembl

homophilic cell adhesion

Traceable author statement PubMed 10201960. Source: ProtInc

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

leukocyte cell-cell adhesion

Inferred from direct assay PubMed 1715889. Source: BHF-UCL

leukocyte migration

Traceable author statement. Source: Reactome

maternal process involved in female pregnancy

Inferred from electronic annotation. Source: Ensembl

negative regulation of anoikis

Inferred from mutant phenotype PubMed 15006356. Source: UniProtKB

negative regulation of cell projection organization

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAPK cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from genetic interaction PubMed 19364818. Source: MGI

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell-substrate adhesion

Inferred from electronic annotation. Source: Ensembl

positive regulation of endocytosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

protein transport within lipid bilayer

Inferred from electronic annotation. Source: Ensembl

regulation of G-protein coupled receptor protein signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

regulation of immune response

Traceable author statement. Source: Reactome

response to activity

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to gonadotropin

Inferred from electronic annotation. Source: Ensembl

response to transforming growth factor beta

Inferred from electronic annotation. Source: Ensembl

sarcomere organization

Inferred from electronic annotation. Source: Ensembl

tight junction assembly

Inferred from electronic annotation. Source: Ensembl

tissue homeostasis

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

alpha3-beta1 integrin complex

Inferred from electronic annotation. Source: Ensembl

alpha7-beta1 integrin complex

Inferred from electronic annotation. Source: Ensembl

alpha8-beta1 integrin complex

Traceable author statement PubMed 21335239. Source: BHF-UCL

alpha9-beta1 integrin complex

Inferred from electronic annotation. Source: Ensembl

basement membrane

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 1715889PubMed 21310825. Source: BHF-UCL

cleavage furrow

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay PubMed 16803572. Source: BHF-UCL

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

filopodium

Inferred from direct assay PubMed 16803572. Source: BHF-UCL

focal adhesion

Inferred from direct assay PubMed 12417594. Source: MGI

hemidesmosome

Inferred from electronic annotation. Source: Ensembl

integrin complex

Non-traceable author statement PubMed 9552005. Source: UniProtKB

intercalated disc

Inferred from electronic annotation. Source: Ensembl

lamellipodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane raft

Inferred from direct assay PubMed 14559243. Source: BHF-UCL

myelin sheath abaxonal region

Inferred from electronic annotation. Source: Ensembl

neuromuscular junction

Inferred from direct assay PubMed 9415431. Source: MGI

plasma membrane

Inferred from direct assay PubMed 12869515. Source: UniProtKB

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

recycling endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

ruffle

Traceable author statement Ref.21. Source: HGNC

sarcolemma

Inferred from direct assay PubMed 9415431. Source: MGI

   Molecular_functionactin binding

Inferred from direct assay PubMed 16803572. Source: BHF-UCL

cell adhesion molecule binding

Inferred from physical interaction PubMed 12869515. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptide binding

Inferred from electronic annotation. Source: Ensembl

protein heterodimerization activity

Non-traceable author statement PubMed 9552005. Source: UniProtKB

virus receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

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

Also known as: Beta-1A;

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 2 (identifier: P05556-2)

Also known as: Beta-1B;

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

Also known as: Beta-1C;

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

Also known as: Beta-1C-2;

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

Also known as: Beta-1D;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Chain21 – 798778Integrin beta-1
PRO_0000016334

Regions

Topological domain21 – 728708Extracellular Potential
Transmembrane729 – 75123Helical; Potential
Topological domain752 – 79847Cytoplasmic Potential
Domain140 – 378239VWFA
Repeat466 – 51550I
Repeat516 – 55944II
Repeat560 – 59839III
Repeat599 – 63537IV
Region466 – 635170Cysteine-rich tandem repeats
Region762 – 7676Signal for sorting from recycling endosomes; interaction with ACAP1
Region785 – 7928Interaction with ITGB1BP1

Sites

Metal binding1521Magnesium
Metal binding1541Calcium 1; via carbonyl oxygen
Metal binding1561Calcium 1
Metal binding1571Calcium 1
Metal binding1891Calcium 2
Metal binding2441Calcium 2
Metal binding2461Calcium 2
Metal binding2481Calcium 2; via carbonyl oxygen
Metal binding2491Calcium 2
Metal binding2491Magnesium
Metal binding3621Calcium 1; via carbonyl oxygen

Amino acid modifications

Modified residue7771Phosphothreonine Ref.39
Modified residue7831Phosphotyrosine By similarity
Modified residue7941N6-acetyllysine Ref.40
Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation2121N-linked (GlcNAc...) Ref.37
Glycosylation2691N-linked (GlcNAc...) Ref.47
Glycosylation3631N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...); atypical Ref.38
Glycosylation4061N-linked (GlcNAc...) Ref.30 Ref.38 Ref.47
Glycosylation4111N-linked (GlcNAc...); atypical Ref.38
Glycosylation4171N-linked (GlcNAc...) Potential
Glycosylation4811N-linked (GlcNAc...) Ref.37
Glycosylation5201N-linked (GlcNAc...) Potential
Glycosylation5841N-linked (GlcNAc...) Potential
Glycosylation6691N-linked (GlcNAc...) Ref.37
Disulfide bond27 ↔ 45 Ref.47
Disulfide bond35 ↔ 464 Ref.47
Disulfide bond38 ↔ 64 Ref.47
Disulfide bond48 ↔ 75 Ref.47
Disulfide bond207 ↔ 213 Ref.47
Disulfide bond261 ↔ 301 Ref.47
Disulfide bond401 ↔ 415 Ref.47
Disulfide bond435 ↔ 462 Ref.47
Disulfide bond466 ↔ 691 Probable
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 2.
VSP_002741
Alternative sequence778 – 79821GENPI…KYEGK → SLSVAQPGVQWCDISSLQPL TSRFQQFSCLSLPSTWDYRV KILFIRVP in isoform 3.
VSP_002742
Alternative sequence778 – 79821GENPI…KYEGK → PGVQWCDISSLQPLTSRFQQ FSCLSLPSTWDYRVKILFIR VP in isoform 4.
VSP_002743
Alternative sequence778 – 79821GENPI…KYEGK → QENPIYKSPINNFKNPNYGR KAGL in isoform 5.
VSP_002744

Experimental info

Mutagenesis760 – 7612RR → AA: No effect on interaction with ACAP1.
Mutagenesis762 – 7676EFAKFE → AAAAAA: Strongly reduces interaction with ACAP1 and ability to recycle; does not affect heterodimerization with ITGA5. Ref.46
Mutagenesis762 – 7632EF → AA: Slightly reduces interaction with ACAP1.
Mutagenesis7651K → A: Reduces interaction with ACAP1.
Mutagenesis766 – 7672FE → AA: Slightly reduces interaction with ACAP1.
Mutagenesis768 – 7692KE → AA: No effect on interaction with ACAP1.
Mutagenesis7781G → Q: Loss of beta-1A interaction with FLNA and FLNB. Ref.22
Mutagenesis786 – 7916AVTTVV → PINNFK: Does not interact with ITGB1BP1. Ref.22 Ref.23
Mutagenesis7861A → P: Loss of beta-1A interaction with FLNA and FLNB. Ref.22
Mutagenesis7871V → T: Reduces interaction with ITGB1BP1, but not with FERMT2 or TLN1. Inhibits fibronectin deposition and mineralized bone nodules formation. Ref.44
Mutagenesis7881T → D: Strongly reduces ITGB1BP1 binding; when associated with D-790. Ref.48
Mutagenesis7901V → D: Strongly reduces ITGB1BP1 binding; when associated with D-788. Ref.48
Mutagenesis7921N → A: Strongly reduces ITGB1BP1 binding; when associated with A-795. Ref.48
Mutagenesis7951Y → A: Strongly reduces ITGB1BP1 binding; when associated with A-792. Ref.48
Sequence conflict1121T → H in CAA30790. Ref.1
Sequence conflict2151S → T in CAA30790. Ref.1
Sequence conflict261 – 2655CGSLI → VWMLL in AAI13902. Ref.6
Sequence conflict385 – 3862EN → DG in AAI13902. Ref.6
Sequence conflict4631E → V in BAF84386. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Beta-1A) [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: DE35979C1625578C

FASTA79888,415
        10         20         30         40         50         60 
MNLQPIFWIG LISSVCCVFA QTDENRCLKA NAKSCGECIQ AGPNCGWCTN STFLQEGMPT 

        70         80         90        100        110        120 
SARCDDLEAL KKKGCPPDDI ENPRGSKDIK KNKNVTNRSK GTAEKLKPED ITQIQPQQLV 

       130        140        150        160        170        180 
LRLRSGEPQT FTLKFKRAED YPIDLYYLMD LSYSMKDDLE NVKSLGTDLM NEMRRITSDF 

       190        200        210        220        230        240 
RIGFGSFVEK TVMPYISTTP AKLRNPCTSE QNCTSPFSYK NVLSLTNKGE VFNELVGKQR 

       250        260        270        280        290        300 
ISGNLDSPEG GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ 

       310        320        330        340        350        360 
CHLENNMYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN LIPKSAVGTL 

       370        380        390        400        410        420 
SANSSNVIQL IIDAYNSLSS EVILENGKLS EGVTISYKSY CKNGVNGTGE NGRKCSNISI 

       430        440        450        460        470        480 
GDEVQFEISI TSNKCPKKDS DSFKIRPLGF TEEVEVILQY ICECECQSEG IPESPKCHEG 

       490        500        510        520        530        540 
NGTFECGACR CNEGRVGRHC ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK 

       550        560        570        580        590        600 
RDNTNEIYSG KFCECDNFNC DRSNGLICGG NGVCKCRVCE CNPNYTGSAC DCSLDTSTCE 

       610        620        630        640        650        660 
ASNGQICNGR GICECGVCKC TDPKFQGQTC EMCQTCLGVC AEHKECVQCR AFNKGEKKDT 

       670        680        690        700        710        720 
CTQECSYFNI TKVESRDKLP QPVQPDPVSH CKEKDVDDCW FYFTYSVNGN NEVMVHVVEN 

       730        740        750        760        770        780 
PECPTGPDII PIVAGVVAGI VLIGLALLLI WKLLMIIHDR REFAKFEKEK MNAKWDTGEN 

       790 
PIYKSAVTTV VNPKYEGK 

« Hide

Isoform 2 (Beta-1B) [UniParc].

Checksum: 75834A92490CFBB0
Show »

FASTA78987,446
Isoform 3 (Beta-1C) [UniParc].

Checksum: D5DCB510A049FBEC
Show »

FASTA82591,620
Isoform 4 (Beta-1C-2) [UniParc].

Checksum: 5838866B6DA6CECC
Show »

FASTA81991,034
Isoform 5 (Beta-1D) [UniParc].

Checksum: 5A2DA413650A16BE
Show »

FASTA80188,884

References

« Hide 'large scale' references
[1]"Amino acid sequence of the human fibronectin receptor."
Argraves W.S., Suzuki S., Arai H., Thompson K., Pierschbacher M.D., Ruoslahti E.
J. Cell Biol. 105:1183-1190(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Endometrium.
[4]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Skin.
[7]"Expression and functional analysis of a cytoplasmic domain variant of the beta 1 integrin subunit."
Balzac F., Belkin A.M., Koteliansky V.E., Balabanov Y.V., Altruda F., Silengo L., Tarone G.
J. Cell Biol. 121:171-178(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 717-757, CHARACTERIZATION OF BETA-1B, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"Expression of beta 1B integrin isoform in CHO cells results in a dominant negative effect on cell adhesion and motility."
Balzac F., Retta S.F., Albini A., Melchiorri A., Koteliansky V.E., Geuna M., Silengo L., Tarone G.
J. Cell Biol. 127:557-565(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 717-757, FUNCTION.
[9]"A human integrin beta 1 subunit with a unique cytoplasmic domain generated by alternative mRNA processing."
Altruda F., Cervella P., Tarone G., Botta C., Balzac F., Stefanuto G., Silengo L.
Gene 95:261-266(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
Tissue: Skeletal muscle.
[10]"An alternative form of the integrin beta 1 subunit with a variant cytoplasmic domain."
Languino L.R., Ruoslahti E.
J. Biol. Chem. 267:7116-7120(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Cervix carcinoma.
[11]"Novel isoform of beta 1 integrin expressed in skeletal and cardiac muscle."
Zhidkova N.I., Belkin A.M., Mayne R.
Biochem. Biophys. Res. Commun. 214:279-285(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
Tissue: Skeletal muscle.
[12]"A novel beta 1 integrin isoform produced by alternative splicing: unique expression in cardiac and skeletal muscle."
van der Flier A., Kuikman I., Baudoin C., van der Neut R., Sonnenberg A.
FEBS Lett. 369:340-344(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY.
[13]"Identification of beta1C-2, a novel variant of the integrin beta1 subunit generated by utilization of an alternative splice acceptor site in exon C."
Svineng G., Faessler R., Johansson S.
Biochem. J. 330:1255-1263(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM 4), TISSUE SPECIFICITY.
[14]"Interaction of ACE2 and integrin beta1 in failing human heart."
Lin Q., Keller R.S., Weaver B., Zisman L.S.
Biochim. Biophys. Acta 1689:175-178(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 775-784 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ACE2.
[15]"Infection by echoviruses 1 and 8 depends on the alpha 2 subunit of human VLA-2."
Bergelson J.M., St John N., Kawaguchi S., Chan M., Stubdal H., Modlin J., Finberg R.W.
J. Virol. 67:6847-6852(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ECHOVIRUS 1 AND HUMAN ECHOVIRUS 8 CAPSID PROTEINS.
[16]"Beta 1D integrin displaces the beta 1A isoform in striated muscles: localization at junctional structures and signaling potential in nonmuscle cells."
Belkin A.M., Zhidkova N.I., Balzac F., Altruda F., Tomatis D., Maier A., Tarone G., Koteliansky V.E., Burridge K.
J. Cell Biol. 132:211-226(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[17]"Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds beta1 integrins, collagens and fibronectin."
Sasaki T., Brakebusch C., Engel J., Timpl R.
EMBO J. 17:1606-1613(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LGALS3BP.
[18]"The Tat protein of human immunodeficiency virus type-1 promotes vascular cell growth and locomotion by engaging the alpha5beta1 and alphavbeta3 integrins and by mobilizing sequestered basic fibroblast growth factor."
Barillari G., Sgadari C., Fiorelli V., Samaniego F., Colombini S., Manzari V., Modesti A., Nair B.C., Cafaro A., Stuerzl M., Ensoli B.
Blood 94:663-672(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 TAT.
[19]"A novel muscle-specific beta 1 integrin binding protein (MIBP) that modulates myogenic differentiation."
Li J., Mayne R., Wu C.
J. Cell Biol. 147:1391-1398(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NMRK2.
Tissue: Heart.
[20]"Interaction between krit1 and icap1alpha infers perturbation of integrin beta1-mediated angiogenesis in the pathogenesis of cerebral cavernous malformation."
Zhang J., Clatterbuck R.E., Rigamonti D., Chang D.D., Dietz H.C.
Hum. Mol. Genet. 10:2953-2960(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGB1BP1.
[21]"Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement."
Fournier H.N., Dupe-Manet S., Bouvard D., Lacombe M.L., Marie C., Block M.R., Albiges-Rizo C.
J. Biol. Chem. 277:20895-20902(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[22]"Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin (beta) subunits."
van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M., Takafuta T., Shapiro S.S., Sonnenberg A.
J. Cell Biol. 156:361-376(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FLNA AND FLNB, MUTAGENESIS OF GLY-778 AND ALA-786.
[23]"The integrin cytoplasmic domain-associated protein ICAP-1 binds and regulates Rho family GTPases during cell spreading."
Degani S., Balzac F., Brancaccio M., Guazzone S., Retta S.F., Silengo L., Eva A., Tarone G.
J. Cell Biol. 156:377-387(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGB1BP1, MUTAGENESIS OF 786-ALA--VAL-791.
[24]"Disruption of focal adhesions by integrin cytoplasmic domain-associated protein-1 alpha."
Bouvard D., Vignoud L., Dupe-Manet S., Abed N., Fournier H.N., Vincent-Monegat C., Retta S.F., Fassler R., Block M.R.
J. Biol. Chem. 278:6567-6574(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ITGB1BP1.
[25]"RanBPM is a phosphoprotein that associates with the plasma membrane and interacts with the integrin LFA-1."
Denti S., Sirri A., Cheli A., Rogge L., Innamorati G., Putignano S., Fabbri M., Pardi R., Bianchi E.
J. Biol. Chem. 279:13027-13034(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RANBP9.
[26]"NG2 proteoglycan promotes endothelial cell motility and angiogenesis via engagement of galectin-3 and alpha3beta1 integrin."
Fukushi J., Makagiansar I.T., Stallcup W.B.
Mol. Biol. Cell 15:3580-3590(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGA3; LGALS3 AND CSPG4.
[27]"Myosin-X provides a motor-based link between integrins and the cytoskeleton."
Zhang H., Berg J.S., Li Z., Wang Y., Lang P., Sousa A.D., Bhaskar A., Cheney R.E., Stromblad S.
Nat. Cell Biol. 6:523-531(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYO10.
[28]"Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent recycling of integrin beta1 to control cell migration."
Li J., Ballif B.A., Powelka A.M., Dai J., Gygi S.P., Hsu V.W.
Dev. Cell 9:663-673(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ACAP1, SUBCELLULAR LOCATION.
[29]"The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins."
Gontier Y., Taivainen A., Fontao L., Sonnenberg A., van der Flier A., Carpen O., Faulkner G., Borradori L.
J. Cell Sci. 118:3739-3749(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FLNB AND FLNC.
[30]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406.
Tissue: Plasma.
[31]"Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic of beta1-integrins."
Pellinen T., Arjonen A., Vuoriluoto K., Kallio K., Fransen J.A.M., Ivaska J.
J. Cell Biol. 173:767-780(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB21.
[32]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[33]"Interaction of integrin beta1 with cytokeratin 1 in neuroblastoma NMB7 cells."
Chuang N.N., Huang C.C.
Biochem. Soc. Trans. 35:1292-1294(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KRT1, SUBCELLULAR LOCATION.
[34]"Rab25 associates with alpha5beta1 integrin to promote invasive migration in 3D microenvironments."
Caswell P.T., Spence H.J., Parsons M., White D.P., Clark K., Cheng K.W., Mills G.B., Humphries M.J., Messent A.J., Anderson K.I., McCaffrey M.W., Ozanne B.W., Norman J.C.
Dev. Cell 13:496-510(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB25.
[35]"Integrin trafficking regulated by Rab21 is necessary for cytokinesis."
Pellinen T., Tuomi S., Arjonen A., Wolf M., Edgren H., Meyer H., Grosse R., Kitzing T., Rantala J.K., Kallioniemi O., Faessler R., Kallio M., Ivaska J.
Dev. Cell 15:371-385(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[36]"JAM-L-mediated leukocyte adhesion to endothelial cells is regulated in cis by alpha4beta1 integrin activation."
Luissint A.C., Lutz P.G., Calderwood D.A., Couraud P.O., Bourdoulous S.
J. Cell Biol. 183:1159-1173(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN LEUKOCYTE TO ENDOTHELIAL CELLS ADHESION, INTERACTION WITH AMICA1.
[37]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212; ASN-481 AND ASN-669.
Tissue: Liver.
[38]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-403; ASN-406 AND ASN-411.
Tissue: Leukemic T-cell.
[39]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-777, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[40]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-794, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"The glycoprotein B disintegrin-like domain binds beta 1 integrin to mediate cytomegalovirus entry."
Feire A.L., Roy R.M., Manley K., Compton T.
J. Virol. 84:10026-10037(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-5 GB.
[42]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[43]"ACAP4 protein cooperates with Grb2 protein to orchestrate epidermal growth factor-stimulated integrin beta1 recycling in cell migration."
Yu X., Wang F., Liu H., Adams G., Aikhionbare F., Liu D., Cao X., Fan L., Hu G., Chen Y., Frost A., Partridge E., Ding X., Yao X.
J. Biol. Chem. 286:43735-43747(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ASAP3.
[44]"Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent fibronectin deposition."
Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.
J. Cell Biol. 194:307-322(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FERMT2 AND TLN1, MUTAGENESIS OF VAL-787.
[45]"Kindlin-2 regulates podocyte adhesion and fibronectin matrix deposition through interactions with phosphoinositides and integrins."
Qu H., Tu Y., Shi X., Larjava H., Saleem M.A., Shattil S.J., Fukuda K., Qin J., Kretzler M., Wu C.
J. Cell Sci. 124:879-891(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FERMT2.
[46]"Mechanistic insights into regulated cargo binding by ACAP1 protein."
Bai M., Pang X., Lou J., Zhou Q., Zhang K., Ma J., Li J., Sun F., Hsu V.W.
J. Biol. Chem. 287:28675-28685(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 758-769 IN COMPLEX WITH ACAP1, INTERACTION WITH ACAP1 AND ITGA5, SUBCELLULAR LOCATION, MUTAGENESIS OF 760-ARG-ARG-761; 762-GLU--PHE-767 AND 768-LYS-GLU-769.
[47]"Crystal structure of alpha5beta1 integrin ectodomain: atomic details of the fibronectin receptor."
Nagae M., Re S., Mihara E., Nogi T., Sugita Y., Takagi J.
J. Cell Biol. 197:131-140(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 21-465 IN COMPLEX WITH ANTIBODY; ITGA5 AND RGD PEPTIDE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-269 AND ASN-406, METAL-BINDING SITES, SUBUNIT.
[48]"Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin activation."
Liu W., Draheim K.M., Zhang R., Calderwood D.A., Boggon T.J.
Mol. Cell 49:719-729(2013)
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 784-798 IN COMPLEX WITH ITGB1BP1, INTERACTION WITH ITGB1BP1, MUTAGENESIS OF THR-788; VAL-790; ASN-792 AND TYR-795.
+Additional computationally mapped references.

Web resources

Wikipedia

CD29 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07979 mRNA. Translation: CAA30790.1.
AK291697 mRNA. Translation: BAF84386.1.
BX537407 mRNA. Translation: CAD97649.1. Different initiation.
AL365203 Genomic DNA. Translation: CAI14426.1.
CH471072 Genomic DNA. Translation: EAW85948.1.
CH471072 Genomic DNA. Translation: EAW85949.1.
CH471072 Genomic DNA. Translation: EAW85950.1.
CH471072 Genomic DNA. Translation: EAW85951.1.
CH471072 Genomic DNA. Translation: EAW85952.1.
CH471072 Genomic DNA. Translation: EAW85953.1.
CH471072 Genomic DNA. Translation: EAW85954.1.
CH471072 Genomic DNA. Translation: EAW85955.1.
CH471072 Genomic DNA. Translation: EAW85957.1.
CH471072 Genomic DNA. Translation: EAW85958.1.
CH471072 Genomic DNA. Translation: EAW85959.1.
BC020057 mRNA. Translation: AAH20057.1.
BC113901 mRNA. Translation: AAI13902.1.
U33879 Genomic DNA. Translation: AAA79832.1.
U33880, U33879 Genomic DNA. Translation: AAA79833.1.
U33882, U33879, U33881 Genomic DNA. Translation: AAA79834.1.
U33882, U33879 Genomic DNA. Translation: AAA79835.1.
M34189 mRNA. Translation: AAA59182.1.
M84237 mRNA. Translation: AAA74402.1.
M84237 mRNA. Translation: AAA74403.1.
U28252 mRNA. Translation: AAA81366.1.
PIRB27079.
RefSeqNP_002202.2. NM_002211.3.
NP_391988.1. NM_033668.2.
NP_596867.1. NM_133376.2.
XP_005252505.1. XM_005252448.1.
UniGeneHs.643813.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K11model-B786-797[»]
1LHAmodel-A86-543[»]
3G9WX-ray2.16C/D752-785[»]
3T9KX-ray2.30A/B758-769[»]
3VI3X-ray2.90B/D21-465[»]
3VI4X-ray2.90B/D21-465[»]
4DX9X-ray3.006/7/8/9/B/D/F/H/J/L/N/P/R/T/V/X/Z/b/d/f/h/j/l/n/p/r/t/v/x/z784-798[»]
ProteinModelPortalP05556.
SMRP05556. Positions 23-797.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109894. 61 interactions.
DIPDIP-312N.
IntActP05556. 38 interactions.
MINTMINT-140089.

Chemistry

BindingDBP05556.
ChEMBLCHEMBL1907599.

PTM databases

PhosphoSiteP05556.

Polymorphism databases

DMDM218563324.

Proteomic databases

PaxDbP05556.
PRIDEP05556.

Protocols and materials databases

DNASU3688.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302278; ENSP00000303351; ENSG00000150093. [P05556-1]
ENST00000374956; ENSP00000364094; ENSG00000150093. [P05556-3]
ENST00000396033; ENSP00000379350; ENSG00000150093. [P05556-1]
ENST00000423113; ENSP00000388694; ENSG00000150093. [P05556-5]
GeneID3688.
KEGGhsa:3688.
UCSCuc001iwr.4. human. [P05556-5]
uc001iws.4. human. [P05556-1]

Organism-specific databases

CTD3688.
GeneCardsGC10M033189.
HGNCHGNC:6153. ITGB1.
HPACAB003434.
MIM135630. gene.
neXtProtNX_P05556.
PharmGKBPA29953.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG287997.
HOVERGENHBG006190.
KOK05719.
OMAENNVYTM.
OrthoDBEOG7T7GSB.
PhylomeDBP05556.
TreeFamTF105392.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111155. Cell-Cell communication.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SABIO-RKP05556.
SignaLinkP05556.

Gene expression databases

ArrayExpressP05556.
BgeeP05556.
GenevestigatorP05556.

Family and domain databases

Gene3D1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProIPR013111. EGF_extracell.
IPR027071. Integrin_beta-1.
IPR015812. Integrin_bsu.
IPR014836. Integrin_bsu_cyt_dom.
IPR002369. Integrin_bsu_N.
IPR012896. Integrin_bsu_tail.
IPR016201. Plexin-like_fold.
IPR002035. VWF_A.
[Graphical view]
PANTHERPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF28. PTHR10082:SF28. 1 hit.
PfamPF07974. EGF_2. 1 hit.
PF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
[Graphical view]
PIRSFPIRSF002512. Integrin_B. 1 hit.
PRINTSPR01186. INTEGRINB.
SMARTSM00187. INB. 1 hit.
SM00423. PSI. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF103575. SSF103575. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEPS00022. EGF_1. 2 hits.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSITGB1. human.
EvolutionaryTraceP05556.
GeneWikiCD29.
GenomeRNAi3688.
NextBio14435.
PMAP-CutDBQ8WUM6.
PROP05556.
SOURCESearch...

Entry information

Entry nameITB1_HUMAN
AccessionPrimary (citable) accession number: P05556
Secondary accession number(s): A8K6N2 expand/collapse secondary AC list , D3DRX9, D3DRY3, D3DRY4, D3DRY5, P78466, P78467, Q13089, Q13090, Q13091, Q13212, Q14622, Q14647, Q29RW2, Q7Z3V1, Q8WUM6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: December 16, 2008
Last modified: April 16, 2014
This is version 181 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries