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Reviewed, UniProtKB/Swiss-Prot P05556 (ITB1_HUMAN)

Last modified February 9, 2010. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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
    VLA-4 subunit beta
    CD_antigen=CD29
Gene names
Name: ITGB1
Synonyms: FNRB, MDF2, MSK12
OrganismHomo sapiens (Human) [Complete proteome]
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. When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. 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.26 Ref.28

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 ITGB1BP3, when associated with alpha-7, but not with alpha-5. Interacts with FLNA, FLNB and RANBP9. Isoform Beta-1D interacts with ACE2. Isoform Beta-1A interacts with the C-terminal region of FLNC. Interacts with KRT1 in the presence of GNB2L1 and SRC. Interacts with HIV-1 Tat. Binds to human echoviruses 1 and 8 capsid proteins and acts as a receptor for these viruses. Interacts with RAB21. Ref.26 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24

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. 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 afew 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. Ref.26 Ref.28 Ref.7 Ref.10 Ref.25

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 peripheral T-cells. Isoform beta-1C 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 beta-1D is expressed specifically in striated muscle (skeletal and cardiac muscle). Ref.7 Ref.10 Ref.9 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.

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Ontologies

Keywords
   Biological processCell adhesion
Host-virus interaction
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
   Molecular functionIntegrin
Receptor
   PTMAcetylation
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processB cell differentiation

Inferred by curator. Source: UniProtKB

cell migration

Traceable author statement. Source: HGNC

cell-cell adhesion mediated by integrin

Inferred from expression pattern. Source: UniProtKB

cell-matrix adhesion

Inferred from electronic annotation. Source: InterPro

cellular defense response

Traceable author statement. Source: ProtInc

homophilic cell adhesion

Traceable author statement. Source: ProtInc

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

interspecies interaction between organisms

Inferred from electronic annotation. Source: UniProtKB-KW

leukocyte adhesion

Inferred from direct assay. Source: UniProtKB

   Cellular componentcell surface

Inferred from direct assay. Source: UniProtKB

integrin complex

Non-traceable author statement. Source: UniProtKB

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuromuscular junction

Inferred from direct assay. Source: MGI

ruffle

Traceable author statement. Source: HGNC

sarcolemma

Inferred from direct assay. Source: MGI

   Molecular functionidentical protein binding

Inferred from physical interaction. Source: IntAct

protein heterodimerization activity

Non-traceable author statement. Source: UniProtKB

receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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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 viewFeature identifier

Molecule processing

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

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 residue1861Phosphoserine By similarity
Modified residue7771Phosphothreonine Ref.33
Modified residue7831Phosphotyrosine Ref.27 Ref.31
Modified residue7941N6-acetyllysine Ref.34
Modified residue7951Phosphotyrosine Ref.31
Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation2121N-linked (GlcNAc...) Ref.30
Glycosylation2691N-linked (GlcNAc...) Potential
Glycosylation3631N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Ref.32
Glycosylation4061N-linked (GlcNAc...) Ref.32 Ref.23
Glycosylation4111N-linked (GlcNAc...) Ref.32
Glycosylation4171N-linked (GlcNAc...) Potential
Glycosylation4811N-linked (GlcNAc...) Ref.30
Glycosylation5201N-linked (GlcNAc...) Potential
Glycosylation5841N-linked (GlcNAc...) Potential
Glycosylation6691N-linked (GlcNAc...) Ref.30
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.
VSP_002741
Alternative sequence778 – 79821GENPI…KYEGK → SLSVAQPGVQWCDISSLQPL TSRFQQFSCLSLPSTWDYRV KILFIRVP in isoform Beta-1C.
VSP_002742
Alternative sequence778 – 79821GENPI…KYEGK → PGVQWCDISSLQPLTSRFQQ FSCLSLPSTWDYRVKILFIR VP in isoform Beta-1C-2.
VSP_002743
Alternative sequence778 – 79821GENPI…KYEGK → QENPIYKSPINNFKNPNYGR KAGL in isoform Beta-1D.
VSP_002744

Experimental info

Mutagenesis7781G → Q: Loss of beta-1A interaction with FLNA and FLNB. Ref.19
Mutagenesis7861A → P: Loss of beta-1A interaction with FLNA and FLNB. Ref.19
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

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

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform 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

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Isoform Beta-1B.

Checksum: 75834A92490CFBB0
Show »

FASTA78987,446
Isoform Beta-1C.

Checksum: D5DCB510A049FBEC
Show »

FASTA82591,620
Isoform Beta-1C-2.

Checksum: 5838866B6DA6CECC
Show »

FASTA81991,034
Isoform Beta-1D.

Checksum: 5A2DA413650A16BE
Show »

FASTA80188,884

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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: 2958481] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1A).
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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1A).
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: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1A).
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: 15164054] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1A).
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: 7681433] [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: 7523423] [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: 2249781] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1B), 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: 1551917] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-1A AND BETA-1C), 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: 7545396] [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: 7544298] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1D), 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: 9494094] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM BETA-1C-2), 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: 15276642] [Abstract]
Cited for: PROTEIN SEQUENCE OF 775-784 (ISOFORM BETA-1D), 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: 8411387] [Abstract]
Cited for: INTERACTION WITH HUMAN ECHOVIRUS 1 AND HUMAN ECHOVIRUS 8 CAPSID PROTEINS.
[16]"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: 9501082] [Abstract]
Cited for: INTERACTION WITH LGALS3BP.
[17]"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: 10397733] [Abstract]
Cited for: INTERACTION WITH HIV-1 TAT.
[18]"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: 10613898] [Abstract]
Cited for: INTERACTION WITH ITGB1BP3.
Tissue: Heart.
[19]"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: 11807098] [Abstract]
Cited for: INTERACTION WITH FLNA AND FLNB, MUTAGENESIS OF GLY-778 AND ALA-786.
[20]"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: 14722085] [Abstract]
Cited for: INTERACTION WITH RANBP9.
[21]"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: 15181153] [Abstract]
Cited for: INTERACTION WITH ITGA3; LGALS3 AND CSPG4.
[22]"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: 16076904] [Abstract]
Cited for: INTERACTION WITH FLNB AND FLNC.
[23]"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: 16335952] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406, MASS SPECTROMETRY.
Tissue: Plasma.
[24]"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: 16754960] [Abstract]
Cited for: INTERACTION WITH RAB21.
[25]"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: 17081065] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[26]"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: 17956333] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KRT1, SUBCELLULAR LOCATION.
[27]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-783, MASS SPECTROMETRY.
[28]"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: 18804435] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[29]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[30]"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: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212; ASN-481 AND ASN-669, MASS SPECTROMETRY.
Tissue: Liver.
[31]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-783 AND TYR-795, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[32]"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: 19349973] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-403; ASN-406 AND ASN-411, MASS SPECTROMETRY.
[33]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-777, MASS SPECTROMETRY.
Tissue: T-cell.
[34]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-794, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Web resources

Wikipedia

CD29 entry

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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.
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.
IPIIPI00217561.
IPI00217562.
IPI00217563.
IPI00293305.
IPI00549336.
PIRB27079.
RefSeqNP_002202.2.
NP_389647.1.
NP_391987.1.
NP_391988.1.
NP_391989.1.
NP_596867.1.
UniGeneHs.643813

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K11model-B786-797[»]
1LHAmodel-A86-543[»]
3G9WX-ray2.16C/D752-785[»]
SMRP05556. Positions 26-137, 81-726, 721-763, 752-797.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-312N.
IntActP05556. 6 interactions.
STRINGP05556.

PTM databases

PhosphoSiteP05556.

Proteomic databases

PRIDEP05556.

Genome annotation databases

EnsemblENST00000302278; ENSP00000303351; ENSG00000150093; Homo sapiens. [Genome view]
ENST00000396033; ENSP00000379350; ENSG00000150093; Homo sapiens. [Genome view]
GeneID3688.
KEGGhsa:3688.
UCSCuc001iwp.2. human.
uc001iwq.2. human.
uc001iwr.2. human.
uc001iwu.1. human.

Organism-specific databases

CTD3688.
GeneCardsGC10M033229.
HGNCHGNC:6153. ITGB1.
HPACAB003434.
MIM135630. gene.
PharmGKBPA29953.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG10838.
HOVERGENP05556.
OMAVDPLSHC.
OrthoDBEOG9M3CVK.

Enzyme and pathway databases

Pathway_Interaction_DBa4b1_a4b7_pathway. a4b1 and a4b7 Integrin signaling.
a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
arf6_traffickingpathway. Arf6 trafficking events.
a4b1_paxdep_pathway. Paxillin-dependent events mediated by a4b1.
a4b1_paxindep_pathway. Paxillin-independent events mediated by a4b1 and a4b7.
reelinpathway. Reelin signaling pathway.
prlsignalingeventspathway. Signaling events mediated by PRL.
syndecan_2_pathway. Syndecan-2-mediated signaling events.
syndecan_4_pathway. Syndecan-4-mediated signaling events.
lymphangiogenesis_pathway. VEGFR3 signaling in lymphatic endothelium.
ReactomeREACT_13552. Integrin cell surface interactions.
REACT_18266. Axon guidance.
REACT_20676. Cell junction organization.
REACT_604. Hemostasis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressP05556.
BgeeP05556.
GenevestigatorP05556.
GermOnlineENSG00000150093. Homo sapiens.

Family and domain databases

InterProIPR015812. Integrin_bsu.
IPR015438. Integrin_bsu-1_C.
IPR001169. Integrin_bsu_C.
IPR014836. Integrin_bsu_cyt.
IPR002369. Integrin_bsu_N.
IPR012012. Integrin_bsu_subgr.
IPR012896. Integrin_bsu_tail.
IPR003659. Plexin-like.
IPR002035. VWF_A.
[Graphical view]
Gene3DG3DSA:1.20.5.630. Integrin_bsu_cyt. 1 hit.
PANTHERPTHR10082. Integrin_beta_C. 1 hit.
PTHR10082:SF14. Integrin_bsu-1_C. 1 hit.
PfamPF08725. 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]
PROSITEPS00022. EGF_1. 2 hits. Uncertain.
PS00243. INTEGRIN_BETA. 3 hits.
PS50234. VWFA. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

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Entry information

Entry nameITB1_HUMAN
AccessionPrimary (citable) accession number: P05556
Secondary accession number(s): A8K6N2 expand/collapse secondary AC list , 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: February 9, 2010
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Relevant documents

Human cell differentiation molecules

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

Human chromosome 10

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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