P09055 (ITB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Integrin beta-1

Alternative name(s):
Fibronectin receptor subunit beta
VLA-4 subunit beta
CD_antigen=CD29

Gene names

Name:

Itgb1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	798 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. 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.7 Ref.8 Ref.11 Ref.14
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 By similarity. Interacts with RAB21. Interacts (via the cytoplasmic region) with RAB25 (via the hypervariable C-terminal region). Interacts with MYO10. Interacts with ITGB1BP1 By similarity. Interacts with FGR and HCK. Interacts with DAB2. Ref.7 Ref.8 Ref.9 Ref.14
Subcellular location	Cell membrane; Single-pass type I membrane protein By similarity. Melanosome By similarity.
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 BAC36379.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell membrane Membrane
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Magnesium Metal-binding
Molecular function	Integrin Receptor
PTM	Acetylation Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Inferred from mutant phenotype PubMed 12957148. Source: MGI calcium-independent cell-matrix adhesion Inferred from electronic annotation. Source: Compara cardiac muscle cell differentiation Inferred from mutant phenotype PubMed 9004034. Source: MGI cell fate specification Inferred from mutant phenotype PubMed 9004034. 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: Compara cell-matrix adhesion Inferred from genetic interaction PubMed 17099249. Source: MGI cellular calcium ion homeostasis Inferred from electronic annotation. Source: Compara cellular response to ionizing radiation Inferred from electronic annotation. Source: Compara cellular response to mechanical stimulus Inferred from electronic annotation. Source: Compara cellular response to vitamin D Inferred from electronic annotation. Source: Compara 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: Compara maternal process involved in female pregnancy Inferred from electronic annotation. Source: Compara negative regulation of anoikis Inferred from electronic annotation. Source: Compara negative regulation of cell differentiation Inferred from mutant phenotype PubMed 15056720. Source: MGI negative regulation of cell projection organization Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of neuron differentiation Inferred from electronic annotation. Source: Compara neuron projection development Inferred from mutant phenotype PubMed 19118221. Source: MGI positive regulation of MAPK cascade Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of cell migration Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from mutant phenotype PubMed 15056720. Source: MGI positive regulation of cell-substrate adhesion Inferred from electronic annotation. Source: Compara positive regulation of endocytosis Inferred from electronic annotation. Source: Compara positive regulation of neuron differentiation Inferred from electronic annotation. Source: Compara positive regulation of neuron projection development Inferred from electronic annotation. Source: Compara positive regulation of peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara protein transport within lipid bilayer Inferred from electronic annotation. Source: Compara regulation of G-protein coupled receptor protein signaling pathway Inferred from electronic annotation. Source: Compara regulation of cell cycle Inferred from mutant phenotype PubMed 14522949. Source: MGI response to activity Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to gonadotropin stimulus Inferred from electronic annotation. Source: Compara response to transforming growth factor beta stimulus Inferred from electronic annotation. Source: Compara sarcomere organization Inferred from mutant phenotype PubMed 9004034. Source: MGI tight junction assembly Inferred from electronic annotation. Source: Compara tissue homeostasis Inferred from electronic annotation. Source: Compara
Cellular_component	acrosomal vesicle Inferred from electronic annotation. Source: Compara alpha3-beta1 integrin complex Inferred from electronic annotation. Source: Compara alpha9-beta1 integrin complex Inferred from electronic annotation. Source: Compara basement membrane Inferred from electronic annotation. Source: Compara external side of plasma membrane Inferred from direct assay PubMed 19487454PubMed 20103531. Source: MGI focal adhesion Inferred from electronic annotation. Source: Compara hemidesmosome Inferred from electronic annotation. Source: Compara intercalated disc Inferred from direct assay PubMed 11732910. Source: MGI melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell membrane raft Inferred from electronic annotation. Source: Compara myelin sheath abaxonal region Inferred from direct assay PubMed 20237282. Source: BHF-UCL neuromuscular junction Inferred from direct assay PubMed 9415431. Source: MGI ruffle membrane Inferred from electronic annotation. Source: Compara sarcolemma Inferred from direct assay PubMed 9415431. Source: MGI
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW peptide binding Inferred from electronic annotation. Source: Compara receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Csf2rb	P26955	2	EBI-644224,EBI-1810026
Nme2	Q01768	3	EBI-644224,EBI-642573
Tmem158	Q6F5E0	3	EBI-644224,EBI-645317

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20
	Chain	21 – 798	778	Integrin beta-1		PRO_0000016335
Regions
	Topological domain	21 – 728	708	Extracellular Potential
	Transmembrane	729 – 751	23	Helical; Potential
	Topological domain	752 – 798	47	Cytoplasmic Potential
	Domain	140 – 378	239	VWFA
	Repeat	466 – 515	50	I
	Repeat	516 – 559	44	II
	Repeat	560 – 598	39	III
	Repeat	599 – 635	37	IV
	Region	466 – 635	170	Cysteine-rich tandem repeats
	Region	785 – 792	8	Interaction with ITGB1BP1 By similarity
Sites
	Metal binding	152	1	Magnesium By similarity
	Metal binding	154	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	156	1	Calcium 1 By similarity
	Metal binding	157	1	Calcium 1 By similarity
	Metal binding	189	1	Calcium 2 By similarity
	Metal binding	244	1	Calcium 2 By similarity
	Metal binding	246	1	Calcium 2 By similarity
	Metal binding	248	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	249	1	Calcium 2 By similarity
	Metal binding	249	1	Magnesium By similarity
Amino acid modifications
	Modified residue	186	1	Phosphoserine Ref.12
	Modified residue	777	1	Phosphothreonine Ref.12
	Modified residue	783	1	Phosphotyrosine Ref.10
	Modified residue	794	1	N6-acetyllysine By similarity
	Glycosylation	50	1	N-linked (GlcNAc...) Potential
	Glycosylation	94	1	N-linked (GlcNAc...) Potential
	Glycosylation	97	1	N-linked (GlcNAc...) Potential
	Glycosylation	212	1	N-linked (GlcNAc...) Potential
	Glycosylation	269	1	N-linked (GlcNAc...) Potential
	Glycosylation	363	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	366	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	376	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	406	1	N-linked (GlcNAc...) Potential
	Glycosylation	417	1	N-linked (GlcNAc...) Potential
	Glycosylation	481	1	N-linked (GlcNAc...) Potential
	Glycosylation	520	1	N-linked (GlcNAc...) Potential
	Glycosylation	584	1	N-linked (GlcNAc...) Potential
	Glycosylation	669	1	N-linked (GlcNAc...) Ref.13
	Disulfide bond	27 ↔ 45		By similarity
	Disulfide bond	35 ↔ 464		By similarity
	Disulfide bond	38 ↔ 75		By similarity
	Disulfide bond	48 ↔ 64		By similarity
	Disulfide bond	207 ↔ 213		By similarity
	Disulfide bond	261 ↔ 301		By similarity
	Disulfide bond	401 ↔ 415		By similarity
	Disulfide bond	435 ↔ 462		By similarity
	Disulfide bond	466 ↔ 691		By similarity
	Disulfide bond	477 ↔ 489		By similarity
	Disulfide bond	486 ↔ 525		By similarity
	Disulfide bond	491 ↔ 500		By similarity
	Disulfide bond	502 ↔ 516		By similarity
	Disulfide bond	531 ↔ 536		By similarity
	Disulfide bond	533 ↔ 568		By similarity
	Disulfide bond	538 ↔ 553		By similarity
	Disulfide bond	555 ↔ 560		By similarity
	Disulfide bond	574 ↔ 579		By similarity
	Disulfide bond	576 ↔ 607		By similarity
	Disulfide bond	581 ↔ 590		By similarity
	Disulfide bond	592 ↔ 599		By similarity
	Disulfide bond	613 ↔ 618		By similarity
	Disulfide bond	615 ↔ 661		By similarity
	Disulfide bond	620 ↔ 630		By similarity
	Disulfide bond	633 ↔ 636		By similarity
	Disulfide bond	640 ↔ 649		By similarity
	Disulfide bond	646 ↔ 723		By similarity
	Disulfide bond	665 ↔ 699		By similarity
Experimental info
	Mutagenesis	783	1	Y → F: Reduced endocytosis; when associated with F-795. Ref.11
	Mutagenesis	795	1	Y → F: Reduced endocytosis; when associated with F-783. Ref.11
	Sequence conflict	5	1	L → Q in BAC40532. Ref.2
	Sequence conflict	72	1	K → E in BAE35290. Ref.2
	Sequence conflict	385	1	E → D in BAC36379. Ref.2
	Sequence conflict	385	1	E → P in CAA33272. Ref.5
	Sequence conflict	392	1	G → A in CAA33272. Ref.5
	Sequence conflict	407	1	G → E in BAC36379. Ref.2
	Sequence conflict	443 – 445	3	IKI → HSKL in CAA33272. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P09055 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 26788F7F0A168B56	FASTA	798	88,231
	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

References

	« Hide 'large scale' referencesShow '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]. 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. , 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]. Strain: C57BL/6J and NOD. Tissue: Head, Osteoclast, Placenta and Thymocyte.
[3]	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].
[4]	"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]. Strain: C57BL/6. Tissue: Brain.
[5]	"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. Strain: BALB/c.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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, MASS SPECTROMETRY. Tissue: Mast cell.
[11]	"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.
[12]	"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 SER-186 AND THR-777, MASS SPECTROMETRY. Tissue: Macrophage.
[13]	"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, MASS SPECTROMETRY. Tissue: Myoblast.
[14]	"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.
+	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. CH466525 Genomic DNA. Translation: EDL11832.1. BC050906 mRNA. Translation: AAH50906.1. X15202 mRNA. Translation: CAA33272.1.
IPI	IPI00132474.
PIR	IJMSFB. PL0104. S01659.
RefSeq	NP_034708.1. NM_010578.2.
UniGene	Mm.263396.
3D structure databases
ProteinModelPortal	P09055.
SMR	P09055. Positions 25-787.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-46247N.
IntAct	P09055. 10 interactions.
MINT	MINT-1573412.
PTM databases
PhosphoSite	P09055.
Proteomic databases
PaxDb	P09055.
PRIDE	P09055.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000090006; ENSMUSP00000087457; ENSMUSG00000025809.
GeneID	16412.
KEGG	mmu:16412.
UCSC	uc009nzv.2. mouse.
Organism-specific databases
CTD	3688.
MGI	MGI:96610. Itgb1.
Phylogenomic databases
eggNOG	NOG287997.
GeneTree	ENSGT00700000104375.
HOGENOM	HOG000252936.
HOVERGEN	HBG006190.
InParanoid	Q8BTU0.
KO	K05719.
OMA	KVENRDK.
OrthoDB	EOG4K9BBM.
Enzyme and pathway databases
Reactome	REACT_127416. Developmental Biology.
Gene expression databases
ArrayExpress	P09055.
Bgee	P09055.
CleanEx	MM_ITGB1.
Genevestigator	P09055.
GermOnline	ENSMUSG00000025809. Mus musculus.
Family and domain databases
Gene3D	1.20.5.630. 1 hit.
InterPro	IPR013111. EGF_extracell. IPR027071. Integrin_beta-1. IPR015812. Integrin_bsu. IPR014836. Integrin_bsu_cyt_dom. IPR002369. Integrin_bsu_N. IPR012896. Integrin_bsu_tail. IPR003659. Plexin-like. IPR016201. Plexin-like_fold. IPR002035. VWF_A. [Graphical view]
PANTHER	PTHR10082. PTHR10082. 1 hit. PTHR10082:SF28. PTHR10082:SF28. 1 hit.
Pfam	PF07974. EGF_2. 1 hit. PF08725. Integrin_b_cyt. 1 hit. PF07965. Integrin_B_tail. 1 hit. PF00362. Integrin_beta. 1 hit. [Graphical view]
PIRSF	PIRSF002512. Integrin_B. 1 hit.
PRINTS	PR01186. INTEGRINB.
SMART	SM00187. INB. 1 hit. SM00423. PSI. 1 hit. SM00327. VWA. 1 hit. [Graphical view]
SUPFAM	SSF69687. Integrin_bsu_tail. 1 hit. SSF103575. Plexin-like_fold. 1 hit.
PROSITE	PS00022. EGF_1. 2 hits. Uncertain. PS00243. INTEGRIN_BETA. 3 hits. PS50234. VWFA. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	289597.
SOURCE	Search...

Entry information

Entry name

ITB1_MOUSE

Accession

Primary (citable) accession number: P09055
Secondary accession number(s): Q3TIW5 , Q3TWH6, Q8BTU0, Q8BVU1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	May 1, 2013
This is version 146 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program