Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P09055 (ITB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 and recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition. 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, 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.11 Ref.12 Ref.15 Ref.19 Ref.20

Isoform 2:Isoform 2 displaces isoform 1 in striated muscles. Ref.8 Ref.11 Ref.12 Ref.15 Ref.19 Ref.20

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 FLNA, FLNB, FLNC and RANBP9. 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 RAB21. Interacts (via the cytoplasmic region) with RAB25 (via the hypervariable C-terminal region). Interacts with MYO10. 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 ACAP1; required for ITGB1 recycling. Interacts with ASAP3. Interacts with FERMT2; the interaction is inhibited in presence of ITGB1BP1. Interacts with DAB2. Interacts with FGR and HCK. Isoform 2 interacts with alpha-7A and alpha-7B in adult skeletal muscle. Isoform 2 interacts with alpha-7B in cardiomyocytes of adult heart. Ref.8 Ref.11 Ref.12 Ref.13 Ref.16 Ref.19

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity. Recycling endosome. Melanosome By similarity. Cell projectionlamellipodium By similarity. Cell projectionruffle By similarity. Note: 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 to fibrillar adhesions in an ITGB1BP1-dependent manner By similarity. Ref.8 Ref.20

Isoform 2: Cell membranesarcolemma. Cell junction. Note: In cardiac muscle, isoform 2 is found in costameres and intercalated disks. Ref.8 Ref.20

Tissue specificity

Isoform 2 is expressed in skeletal and cardiac muscles only (at protein level). Isoform 1 is very weakly expressed in striated muscles and not detected in adult skeletal muscle fibers and cardiomyocytes. Ref.8

Developmental stage

Isoform 2 is not detected in proliferating myoblasts, but it appears immediately after myoblast fusion and its amount continues to rise during myotube growth and maturation reaching its highest level at day 9 through day 10, when mature differentiated myotubes appear in cell culture. Isoform 1 expression is down-regulated during myodifferentiation in culture and it is completely displaced by isoform 2 in mature differentiated myotubes. Ref.8

Post-translational modification

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

Disruption phenotype

Isoform 2 knockout mice are viable and fertile, but male mice display a mild abnormality of cardiac function reflected by an increased expression of atrial natriuretic peptide and beta myosin heavy chain. Muscles do not show any histological or ultrastructural alterations. Replacement of isoform 1 by isoform 2 results in embryonic lethality before 16.5 dpc with a plethora of developmental defects including open neural tube, which is abnormally waved both rostrally and caudally. Some embryos lack part of the hindbrain and in most embryos the first branchial arch is shortened, which in some of the embryos leaves the tongue exposed. Abnormally strong fibronectin staining is seen in the mesenchyme under the open neural tube. Extravasation of red blood cells is evident in various tissues and they are also found in the pericardial cavity. Choroid plexus is virtually absent correlating with the presence of an abnormally smooth head and small brain cavities. At later developmental stages, a striking feature is the lack of a lower jaw and a dysmorphic lower face. These defects are in part caused by the abnormal migration of neuroepithelial cells. Ref.10

Sequence similarities

Belongs to the integrin beta chain family.

Contains 1 VWFA domain.

Sequence caution

The sequence BAC36379.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Cell projection
Endosome
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandMagnesium
Metal-binding
   Molecular functionIntegrin
Receptor
   PTMAcetylation
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 12957148. Source: MGI

axon extension

Inferred from mutant phenotype PubMed 12879062. Source: MGI

calcium-independent cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

cardiac muscle cell differentiation

Inferred from mutant phenotype PubMed 9004034. Source: MGI

cardiac muscle tissue development

Inferred from mutant phenotype Ref.10. Source: MGI

cell fate specification

Inferred from mutant phenotype PubMed 9004034. Source: MGI

cell migration

Inferred from mutant phenotype Ref.10. Source: MGI

cell migration involved in sprouting angiogenesis

Inferred from mutant phenotype PubMed 16424942. Source: MGI

cell-cell adhesion mediated by integrin

Inferred from electronic annotation. Source: Ensembl

cell-matrix adhesion

Inferred from mutant phenotype PubMed 21185282. Source: MGI

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

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

formation of radial glial scaffolds

Inferred from mutant phenotype PubMed 21185282. Source: MGI

germ cell migration

Inferred from mutant phenotype PubMed 10079228. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 7544313. Source: MGI

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

leukocyte cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

maternal process involved in female pregnancy

Inferred from electronic annotation. Source: Ensembl

negative regulation of anoikis

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell differentiation

Inferred from mutant phenotype PubMed 15056720. Source: MGI

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

neuron projection development

Inferred from mutant phenotype PubMed 19118221. Source: MGI

positive regulation of MAPK cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 15056720. Source: MGI

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 mutant phenotype PubMed 14522949. Source: MGI

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 mutant phenotype PubMed 9004034. Source: MGI

tight junction assembly

Inferred from electronic annotation. Source: Ensembl

tissue homeostasis

Inferred from electronic annotation. Source: Ensembl

   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 direct assay PubMed 18611855. Source: MGI

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 8306881. Source: MGI

external side of plasma membrane

Inferred from direct assay PubMed 19487454PubMed 20103531Ref.10. Source: MGI

filopodium

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Inferred from electronic annotation. Source: Ensembl

hemidesmosome

Inferred from electronic annotation. Source: Ensembl

intercalated disc

Inferred from direct assay PubMed 11732910. Source: MGI

lamellipodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane raft

Inferred from electronic annotation. Source: Ensembl

myelin sheath abaxonal region

Inferred from direct assay PubMed 20237282. Source: BHF-UCL

neuromuscular junction

Inferred from direct assay PubMed 9415431. Source: MGI

plasma membrane

Inferred from direct assay PubMed 12591243PubMed 12670870PubMed 14522949. Source: MGI

receptor complex

Inferred from sequence orthology PubMed 23382219. Source: MGI

recycling endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

ruffle membrane

Inferred from electronic annotation. Source: Ensembl

sarcolemma

Inferred from direct assay PubMed 9415431. Source: MGI

synapse

Inferred from direct assay PubMed 12904471. Source: MGI

   Molecular_functionintegrin binding

Inferred from physical interaction PubMed 1833411PubMed 8601592. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptide binding

Inferred from electronic annotation. Source: Ensembl

receptor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P09055-1)

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: P09055-2)

Also known as: Beta-1D;

The sequence of this isoform differs from the canonical sequence as follows:
     778-778: G → Q
     786-798: AVTTVVNPKYEGK → PINNFKNPNYGRKAGL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Chain21 – 798778Integrin beta-1
PRO_0000016335

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 By similarity
Region785 – 7928Interaction with ITGB1BP1 By similarity

Sites

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

Amino acid modifications

Modified residue7771Phosphothreonine Ref.17
Modified residue7831Phosphotyrosine Ref.14
Modified residue7941N6-acetyllysine By similarity
Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation2121N-linked (GlcNAc...) Potential
Glycosylation2691N-linked (GlcNAc...) Potential
Glycosylation3631N-linked (GlcNAc...) Ref.18
Glycosylation3661N-linked (GlcNAc...); atypical Ref.18
Glycosylation3761N-linked (GlcNAc...); atypical Ref.18
Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation4171N-linked (GlcNAc...) Potential
Glycosylation4811N-linked (GlcNAc...) Potential
Glycosylation5201N-linked (GlcNAc...) Potential
Glycosylation5841N-linked (GlcNAc...) Potential
Glycosylation6691N-linked (GlcNAc...) Ref.18
Disulfide bond27 ↔ 45 By similarity
Disulfide bond35 ↔ 464 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 ↔ 462 By similarity
Disulfide bond466 ↔ 691 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 sequence7781G → Q in isoform 2.
VSP_053581
Alternative sequence786 – 79813AVTTV…KYEGK → PINNFKNPNYGRKAGL in isoform 2.
VSP_053582

Experimental info

Mutagenesis7831Y → F: Reduced endocytosis; when associated with F-795. Ref.15
Mutagenesis7951Y → F: Reduced endocytosis; when associated with F-783. Ref.15
Sequence conflict51L → Q in BAC40532. Ref.2
Sequence conflict721K → E in BAE35290. Ref.2
Sequence conflict3851E → D in BAC36379. Ref.2
Sequence conflict3851E → P in CAA33272. Ref.6
Sequence conflict3921G → A in CAA33272. Ref.6
Sequence conflict4071G → E in BAC36379. Ref.2
Sequence conflict443 – 4453IKI → HSKL in CAA33272. Ref.6

Sequences

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

Last modified November 1, 1988. Version 1.
Checksum: 26788F7F0A168B56

FASTA79888,231
        10         20         30         40         50         60 
MNLQLVSWIG LISLICSVFG QTDKNRCLKA NAKSCGECIQ AGPNCGWCTN TTFLQEGMPT 

        70         80         90        100        110        120 
SARCDDLEAL KKKGCQPSDI ENPRGSQTIK KNKNVTNRSK GMAEKLRPED ITQIQPQQLL 

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

       190        200        210        220        230        240 
RIGFGSFVEK TVMPYISTTP AKLRNPCTSE QNCTSPFSYK NVLSLTDRGE FFNELVGQQR 

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

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

       370        380        390        400        410        420 
SGNSSNVIQL IIDAYNSLSS EVILENSKLP DGVTINYKSY CKNGVNGTGE NGRKCSNISI 

       430        440        450        460        470        480 
GDEVQFEISI TANKCPNKES ETIKIKPLGF TEEVEVVLQF ICKCNCQSHG IPASPKCHEG 

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

       550        560        570        580        590        600 
RDNTNEIYSG KFCECDNFNC DRSNGLICGG NGVCRCRVCE CYPNYTGSAC DCSLDTGPCL 

       610        620        630        640        650        660 
ASNGQICNGR GICECGACKC TDPKFQGPTC ETCQTCLGVC AEHKECVQCR AFNKGEKKDT 

       670        680        690        700        710        720 
CAQECSHFNL TKVESREKLP QPVQVDPVTH CKEKDIDDCW FYFTYSVNGN NEAIVHVVET 

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

       790 
PIYKSAVTTV VNPKYEGK 

« Hide

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

Checksum: 7559450B2812F5A2
Show »

FASTA80188,700

References

« Hide 'large scale' references
[1]"Murine mRNA for the beta-subunit of integrin is increased in BALB/c-3T3 cells entering the G1 phase from the G0 state."
Tominaga S.
FEBS Lett. 238:315-319(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: BALB/c.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J and NOD.
Tissue: Head, Osteoclast, Placenta and Thymocyte.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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).
Strain: C57BL/6.
Tissue: Brain.
[6]"Molecular cloning of a murine fibronectin receptor and its expression during inflammation. Expression of VLA-5 is increased in activated peritoneal macrophages in a manner discordant from major histocompatibility complex class II."
Holers V.M., Ruff T.G., Parks D.L., McDonald J.A., Ballard L.L., Brown E.J.
J. Exp. Med. 169:1589-1605(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-798 (ISOFORM 1).
Strain: BALB/c.
[7]"Coordinate induction of fibronectin, fibronectin receptor, tropomyosin, and actin genes in serum-stimulated fibroblasts."
Ryseck R.P., MacDonald-Bravo H., Zerial M., Bravo R.
Exp. Cell Res. 180:537-545(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 595-798 (ISOFORM 1).
[8]"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: NUCLEOTIDE SEQUENCE [MRNA] OF 718-798 (ISOFORM 2), FUNCTION, INTERACTION WITH ITGA7, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Myoblast.
[9]"Genomic organization of the mouse beta 1 gene: conservation of the beta 1D but not of the beta 1B and beta 1C integrin splice variants."
Baudoin C., Van der Flier A., Borradori L., Sonnenberg A.
Cell Adhes. Commun. 4:1-11(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 723-798.
Tissue: Skeletal muscle.
[10]"Knockout and knockin of the beta1 exon D define distinct roles for integrin splice variants in heart function and embryonic development."
Baudoin C., Goumans M.J., Mummery C., Sonnenberg A.
Genes Dev. 12:1202-1216(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[11]"The muscle integrin binding protein (MIBP) interacts with alpha7beta1 integrin and regulates cell adhesion and laminin matrix deposition."
Li J., Rao H., Burkin D., Kaufman S.J., Wu C.
Dev. Biol. 261:209-219(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NMRK2.
[12]"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: FUNCTION, INTERACTION WITH ITGA3; LGALS3 AND CSPG4.
[13]"Disabled-2 (Dab2) is required for transforming growth factor beta-induced epithelial to mesenchymal transition (EMT)."
Prunier C., Howe P.H.
J. Biol. Chem. 280:17540-17548(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAB2.
[14]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[15]"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, MUTAGENESIS OF TYR-783 AND TYR-795.
[16]"Kindlin-2 controls bidirectional signaling of integrins."
Montanez E., Ussar S., Schifferer M., Bosl M., Zent R., Moser M., Fassler R.
Genes Dev. 22:1325-1330(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FERMT2.
[17]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-777, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-363; ASN-366; ASN-376 AND ASN-669.
Tissue: Myoblast.
[19]"c-Abl and Src-family kinases cross-talk in regulation of myeloid cell migration."
Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G., Berton G.
FEBS Lett. 584:15-21(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FGR AND HCK.
[20]"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, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00769 mRNA. Translation: CAA68738.1.
AK076526 mRNA. Translation: BAC36379.1. Different initiation.
AK088729 mRNA. Translation: BAC40532.1.
AK159689 mRNA. Translation: BAE35290.1.
AK167682 mRNA. Translation: BAE39731.1.
AC156608 Genomic DNA. No translation available.
CH466525 Genomic DNA. Translation: EDL11832.1.
BC050906 mRNA. Translation: AAH50906.1.
X15202 mRNA. Translation: CAA33272.1.
U37029 mRNA. Translation: AAA80243.1.
U47283 Genomic DNA. Translation: AAA88821.1.
PIRIJMSFB. PL0104.
S01659.
RefSeqNP_034708.1. NM_010578.2.
UniGeneMm.263396.

3D structure databases

ProteinModelPortalP09055.
SMRP09055. Positions 23-797.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200826. 6 interactions.
DIPDIP-46247N.
IntActP09055. 19 interactions.
MINTMINT-1573412.

PTM databases

PhosphoSiteP09055.

Proteomic databases

PaxDbP09055.
PRIDEP09055.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000090006; ENSMUSP00000087457; ENSMUSG00000025809. [P09055-1]
GeneID16412.
KEGGmmu:16412.
UCSCuc009nzv.2. mouse. [P09055-1]

Organism-specific databases

CTD3688.
MGIMGI:96610. Itgb1.

Phylogenomic databases

eggNOGNOG287997.
GeneTreeENSGT00730000110513.
HOGENOMHOG000252936.
HOVERGENHBG006190.
InParanoidQ8BTU0.
KOK05719.
OMAENNVYTM.
OrthoDBEOG7T7GSB.
PhylomeDBP09055.
TreeFamTF105392.

Enzyme and pathway databases

ReactomeREACT_188576. Developmental Biology.

Gene expression databases

ArrayExpressP09055.
BgeeP09055.
CleanExMM_ITGB1.
GenevestigatorP09055.

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

NextBio289597.
PROP09055.
SOURCESearch...

Entry information

Entry nameITB1_MOUSE
AccessionPrimary (citable) accession number: P09055
Secondary accession number(s): F6R105 expand/collapse secondary AC list , Q3TIW5, Q3TWH6, Q60993, Q61126, Q8BTU0, Q8BVU1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: April 16, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot