Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
logos LINCs Logo Mt Sinai Logo NIH Logo NCI Logo
Protein Page:
ITGB1 (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
ITGB1 an integral membrane protein that heterodimerizes with an alpha-3 chain, forming a receptor for many extracellular-matrix proteins including fibronectin, laminin, collagen, epiligrin and thrombospondin. . Beta 1 integrins recognize the amino-acid motif RGD in a wide array of ligands. Five alternatively spliced variants with alternate carboxy termini have been described. Two alternatively spliced isoforms have been described. Isoform beta-1a is widely expressed; other isoforms are generally expressed with a more restricted distribution. Isoform beta-1b is expressed in skin, liver, skeletal muscle, cardiac muscle, placenta, umbilical vein endothelial cells, neuroblastoma cells, lymphoma cells, hepatoma cells and astrocytoma cells. Isoforms beta-1c and beta-1c-2 are expressed in muscle, kidney, liver, placenta, cervical epithelium, umbilical vein endothelial cells, fibroblast cells, embryonal kidney cells, platelets and several blood cell lines. Isoform beta-c-2, rather than isoform beta-1c, is selectively expressed in primary t-cells. Isoform beta-1c is expressed in nonproliferating and differentiated prostate gland epithelial cells. Isoform beta-1d is expressed specifically in striated muscle (skeletal and cardiac muscle). Note: This description may include information from UniProtKB.
Protein type: Receptor, misc.; Membrane protein, integral; Motility/polarity/chemotaxis; Cell adhesion; Cell surface
Chromosomal Location of Human Ortholog: 10p11.2
Cellular Component: acrosome; basement membrane; cell surface; cleavage furrow; cytoplasm; dendritic spine; external side of plasma membrane; filopodium; focal adhesion; hemidesmosome; integrin complex; lamellipodium; lipid raft; melanosome; membrane; neuromuscular junction; perinuclear region of cytoplasm; plasma membrane; receptor complex; recycling endosome; ruffle; sarcolemma
Molecular Function: actin binding; alpha-actinin binding; cell adhesion molecule binding; fibronectin binding; glycoprotein binding; integrin binding; laminin binding; metal ion binding; peptide binding; protease binding; protein binding; protein complex binding; protein domain specific binding; protein heterodimerization activity; protein kinase binding; viral receptor activity
Biological Process: axon extension; axon guidance; B cell differentiation; blood coagulation; calcium-independent cell-matrix adhesion; cardiac muscle cell differentiation; cell fate specification; cell migration; cell migration during sprouting angiogenesis; cell-cell adhesion mediated by integrin; cell-matrix adhesion; cell-substrate adhesion; cellular calcium ion homeostasis; cellular defense response; dendrite morphogenesis; entry of virus into host cell; extracellular matrix organization and biogenesis; formation of radial glial scaffolds; G1/S transition of mitotic cell cycle; germ cell migration; heterotypic cell-cell adhesion; homophilic cell adhesion; in utero embryonic development; integrin-mediated signaling pathway; leukocyte adhesion; leukocyte migration; leukocyte tethering or rolling; maternal process involved in pregnancy; mesodermal cell differentiation; negative regulation of cell projection organization and biogenesis; negative regulation of cell proliferation; negative regulation of neuron differentiation; negative regulation of Rho protein signal transduction; positive regulation of apoptosis; positive regulation of cell migration; positive regulation of cell proliferation; positive regulation of endocytosis; positive regulation of GTPase activity; positive regulation of MAPKKK cascade; positive regulation of peptidyl-tyrosine phosphorylation; protein transport within lipid bilayer; receptor internalization; regulation of cell cycle; regulation of G-protein coupled receptor protein signaling pathway; regulation of immune response; response to activity; response to drug; sarcomere organization; small GTPase mediated signal transduction; stress fiber formation; tissue homeostasis; transforming growth factor beta receptor signaling pathway; visual learning
Reference #:  P05556 (UniProtKB)
Alt. Names/Synonyms: CD29; fibronectin receptor beta subunit; Fibronectin receptor subunit beta; FNRB; GPIIA; Integrin beta-1; integrin VLA-4 beta subunit; integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12); ITB1; ITGB1; MDF2; MSK12; VLA-4 subunit beta; VLA-BETA; VLAB
Gene Symbols: ITGB1
Molecular weight: 88,415 Da
Basal Isoelectric point: 5.27  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  GPCR Signaling to MAPKs  |  Growth And Differentiation Control by MAPKs  |  PI3K/Akt Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

ITGB1

Protein Structure Not Found.


STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Sites Implicated In
cell adhesion, altered: T788‑p, T789‑p
cell motility, altered: T788‑p, T789‑p
cytoskeletal reorganization: S785‑p
activity, induced: T788‑p, T789‑p
molecular association, regulation: Y783‑p, T788‑p, T789‑p, Y795‑p
protein conformation: T788‑p, T789‑p

Modification Sites and Domains  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 R122 QPQQLVLRLRSGEPQ
0 1 S125 QLVLRLRSGEPQtFT
0 1 T130‑p LRSGEPQtFTLkFKR
0 1 T130 LRSGEPQTFTLkFKR
0 3 K134‑ac EPQtFTLkFKRAEDy
0 2 Y141‑p kFKRAEDyPIDLYyL
0 2 Y147‑p DyPIDLYyLMDLSYS
0 1 K163‑ub KDDLENVkSLGTDLM
0 2 S186‑p DFRIGFGsFVEkTVM
0 1 K190‑ub GFGsFVEkTVMPYIs
0 1 S197‑p kTVMPYIsTTPAkLR
0 2 K202‑ub YIsTTPAkLRNPCTS
0 2 S224‑p FSYKNVLsLtNkGEV
0 2 T226‑p YKNVLsLtNkGEVFN
0 1 K228‑ub NVLsLtNkGEVFNEL
0 1 K238‑ub VFNELVGkQRISGNL
0 1 K289‑ac FHFAGDGkLGGIVLP
0 1 K349 QPVYKELKNLIPKSA
0 1 T394‑ga GKLSEGVtISYKSYC
0 2 S549‑p DNTNEIYsGKFCECD
0 1 K672‑ub CSYFNITkVESRDKL
0 24 K774‑ub EKEKMNAkWDtGENP
0 21 T777‑p KMNAkWDtGENPIyk
6 1178 Y783‑p DtGENPIyksAVttV
0 1 - gap
0 42 K784‑ub tGENPIyksAVttVV
5 25 S785‑p GENPIyksAVttVVN
11 1 T788‑p PIyksAVttVVNPky
10 2 T789‑p IyksAVttVVNPkyE
0 4 K794‑ac VttVVNPkyEGk___
0 28 K794‑ub VttVVNPkyEGk___
0 1 - gap
7 220 Y795‑p ttVVNPkyEGk____
0 6 K798‑ub VNPkyEGk_______
  ITGB1 iso2  
R122 QPQQLVLRLRSGEPQ
S125 QLVLRLRSGEPQTFT
T130 LRSGEPQTFTLKFKR
T130 LRSGEPQTFTLKFKR
K134 EPQTFTLKFKRAEDY
Y141 KFKRAEDYPIDLYYL
Y147 DYPIDLYYLMDLSYS
K163 KDDLENVKSLGTDLM
S186 DFRIGFGSFVEKTVM
K190 GFGSFVEKTVMPYIS
S197 KTVMPYISTTPAKLR
K202 YISTTPAKLRNPCTS
S224 FSYKNVLSLTNKGEV
T226 YKNVLSLTNKGEVFN
K228 NVLSLTNKGEVFNEL
K238 VFNELVGKQRISGNL
K289 FHFAGDGKLGGIVLP
K349 QPVYKELKNLIPKSA
T394 GKLSEGVTISYKSYC
S549 DNTNEIYSGKFCECD
K672 CSYFNITKVESRDKL
K774 EKEKMNAKWDTVSyK
T777 KMNAKWDTVSyKTSK
- gap
Y780‑p AKWDTVSyKTSKKQS
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  ITGB1 iso3  
R122 QPQQLVLRLRSGEPQ
S125 QLVLRLRSGEPQTFT
T130 LRSGEPQTFTLKFKR
T130 LRSGEPQTFTLKFKR
K134 EPQTFTLKFKRAEDY
Y141 KFKRAEDYPIDLYYL
Y147 DYPIDLYYLMDLSYS
K163 KDDLENVKSLGTDLM
S186 DFRIGFGSFVEKTVM
K190 GFGSFVEKTVMPYIS
S197 KTVMPYISTTPAKLR
K202 YISTTPAKLRNPCTS
S224 FSYKNVLSLTNKGEV
T226 YKNVLSLTNKGEVFN
K228 NVLSLTNKGEVFNEL
K238 VFNELVGKQRISGNL
K289 FHFAGDGKLGGIVLP
K349 QPVYKELKNLIPKSA
T394 GKLSEGVTISYKSYC
S549 DNTNEIYSGKFCECD
K672 CSYFNITKVESRDKL
K774 EKEKMNAKWDTSLSV
T777 KMNAKWDTSLSVAQP
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  ITGB1 iso5  
R122 QPQQLVLRLRSGEPQ
S125 QLVLRLRSGEPQTFT
T130 LRSGEPQTFTLKFKR
T130 LRSGEPQTFTLKFKR
K134 EPQTFTLKFKRAEDY
Y141 KFKRAEDYPIDLYYL
Y147 DYPIDLYYLMDLSYS
K163 KDDLENVKSLGTDLM
S186 DFRIGFGSFVEKTVM
K190 GFGSFVEKTVMPYIS
S197 KTVMPYISTTPAKLR
K202 YISTTPAKLRNPCTS
S224 FSYKNVLSLTNKGEV
T226 YKNVLSLTNKGEVFN
K228 NVLSLTNKGEVFNEL
K238 VFNELVGKQRISGNL
K289 FHFAGDGKLGGIVLP
K349 QPVYKELKNLIPKSA
T394 GKLSEGVTISYKSYC
S549 DNTNEIYSGKFCECD
K672 CSYFNITKVESRDKL
K774 EKEKMNAKWDTQENP
T777 KMNAKWDTQENPIyK
Y783‑p DTQENPIyKSPINNF
- gap
K784 TQENPIyKSPINNFK
S785 QENPIyKSPINNFKN
- gap
- gap
- gap
- gap
K791 KSPINNFKNPNYGRK
Y795 NNFKNPNYGRKAGL_
K798 KNPNYGRKAGL____
  mouse

► Hide Isoforms
 
K122 QPQQLLLKLRsGEPQ
S125‑p QLLLKLRsGEPQKFT
K130 LRsGEPQKFTLKFKR
K130 LRsGEPQKFTLKFKR
K134 EPQKFTLKFKRAEDY
Y141 KFKRAEDYPIDLYYL
Y147 DYPIDLYYLMDLSYS
K163 KDDLENVKSLGTDLM
S186‑p DFRIGFGsFVEKTVM
K190 GFGsFVEKTVMPYIS
S197 KTVMPYISTTPAkLR
K202‑ub YISTTPAkLRNPCTS
S224 FSYKNVLSLTDRGEF
T226 YKNVLSLTDRGEFFN
R228 NVLSLTDRGEFFNEL
Q238 FFNELVGQQRISGNL
K289 FHFAGDGKLGGIVLP
K349 QPVYKELKNLIPKSA
T394 SKLPDGVTINYKSYC
S549 DNTNEIYSGKFCECD
K672 CSHFNLTKVESREKL
K774‑ub EKEKMNAkWDtGENP
T777‑p KMNAkWDtGENPIyk
Y783‑p DtGENPIyksAVttV
- gap
K784‑ub tGENPIyksAVttVV
S785‑p GENPIyksAVttVVN
T788‑p PIyksAVttVVNPky
T789‑p IyksAVttVVNPkyE
K794‑ac VttVVNPkyEGk___
K794‑ub VttVVNPkyEGk___
- gap
Y795‑p ttVVNPkyEGk____
K798‑ub VNPkyEGk_______
  ITGB1 iso5  
K122 QPQQLLLKLRSGEPQ
S125 QLLLKLRSGEPQKFT
K130 LRSGEPQKFTLKFKR
K130 LRSGEPQKFTLKFKR
K134 EPQKFTLKFKRAEDY
Y141 KFKRAEDYPIDLYYL
Y147 DYPIDLYYLMDLSYS
K163 KDDLENVKSLGTDLM
S186 DFRIGFGSFVEKTVM
K190 GFGSFVEKTVMPYIS
S197 KTVMPYISTTPAKLR
K202 YISTTPAKLRNPCTS
S224 FSYKNVLSLTDRGEF
T226 YKNVLSLTDRGEFFN
R228 NVLSLTDRGEFFNEL
Q238 FFNELVGQQRISGNL
K289 FHFAGDGKLGGIVLP
K349 QPVYKELKNLIPKSA
T394 SKLPDGVTINYKSYC
S549 DNTNEIYSGKFCECD
K672 CSHFNLTKVESREKL
K774‑ub EKEKMNAkWDTQENP
T777 KMNAkWDTQENPIYk
Y783 DTQENPIYksPINNF
- gap
K784‑ub TQENPIYksPINNFk
S785‑p QENPIYksPINNFkN
- gap
- gap
- gap
- gap
K791‑ub ksPINNFkNPNYGRK
Y795 NNFkNPNYGRKAGL_
K798 kNPNYGRKAGL____
  rat

 
K122‑ac QPQQLLLkLRSGEPQ
S125 QLLLkLRSGEPQkFT
K130 LRSGEPQKFTLKFKR
K130‑ac LRSGEPQkFTLKFKR
K134 EPQkFTLKFKRAEDY
Y141 KFKRAEDYPIDLYYL
Y147 DYPIDLYYLMDLSYS
K163 KDDLENVKSLGTDLM
S186 DFRIGFGSFVEKTVM
K190 GFGSFVEKTVMPYIS
S197 KTVMPYISTTPAKLR
K202 YISTTPAKLRNPCTS
S224 FSYKNVLSLTDRGEF
T226 YKNVLSLTDRGEFFN
R228 NVLSLTDRGEFFNEL
Q238 FFNELVGQQRISGNL
K289 FHFAGDGKLGGIVLP
K349‑ac QPVYKELkNLIPKSA
T394 SKLPDGVTINYKSYC
S550‑p ENTNEIYsGKFCECD
K673 CSHFNLTKVESREKL
K775 EKEKMNAKWDTGENP
T778 KMNAKWDTGENPIyK
Y784‑p DTGENPIyKSAVTTV
- gap
K785 TGENPIyKSAVTTVV
S786 GENPIyKSAVTTVVN
T789 PIyKSAVTTVVNPky
T790 IyKSAVTTVVNPkyE
K795‑ac VTTVVNPkyEGK___
K795 VTTVVNPKyEGK___
- gap
Y796‑p TTVVNPkyEGK____
K799 VNPkyEGK_______
  chicken

 
Q126 QPQKLVLQLRVGEPQ
V129 KLVLQLRVGEPQTFS
T134 LRVGEPQTFSLKFKR
T134 LRVGEPQTFSLKFKR
K138 EPQTFSLKFKRAEDY
Y145 KFKRAEDYPIDLYYL
Y151 DYPIDLYYLMDLSYS
K167 KDDLENVKSLGTALM
S190 DFRIGFGSFVEKTVM
K194 GFGSFVEKTVMPYIS
S201 KTVMPYISTTPAKLR
K206 YISTTPAKLRNPCTG
S228 FSYKNVLSLTSEGNK
T230 YKNVLSLTSEGNKFN
E232 NVLSLTSEGNKFNEL
K242 KFNELVGKQHISGNL
K293 FHFAGDGKLGGIVLP
K353 QAVYKELKNLIPKSA
T398 SKLPKEVTISYKSYC
S554 ENTNEVYSGKYCECD
R677 CMHFNMTRVESRGKL
K779 EKEKMNAKWDTGENP
T782 KMNAKWDTGENPIYK
Y788 DTGENPIYKsAVTTV
- gap
K789 TGENPIYKsAVTTVV
S790‑p GENPIYKsAVTTVVN
T793 PIYKsAVTTVVNPKY
T794 IYKsAVTTVVNPKYE
K799 VTTVVNPKYEGK___
K799 VTTVVNPKYEGK___
- gap
Y800 TTVVNPKYEGK____
K803 VNPKYEGK_______
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.