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Protein Page:
ITGB1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
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.; Cell surface; Motility/polarity/chemotaxis; Cell adhesion; Membrane protein, integral
Chromosomal Location of Human Ortholog: 10p11.2
Cellular Component: focal adhesion; cell surface; dendritic spine; acrosome; lipid raft; ruffle; recycling endosome; membrane; hemidesmosome; lamellipodium; cytoplasm; melanosome; plasma membrane; basement membrane; integrin complex; neuromuscular junction; sarcolemma; receptor complex; cleavage furrow; external side of plasma membrane; filopodium
Molecular Function: protein domain specific binding; protease binding; metal ion binding; laminin binding; actin binding; alpha-actinin binding; protein kinase binding; peptide binding; integrin binding; viral receptor activity; protein binding; protein heterodimerization activity; fibronectin binding; cell adhesion molecule binding; glycoprotein binding
Biological Process: extracellular matrix organization and biogenesis; maternal process involved in pregnancy; positive regulation of apoptosis; regulation of cell cycle; axon extension; mesodermal cell differentiation; positive regulation of endocytosis; cardiac muscle cell differentiation; leukocyte adhesion; transforming growth factor beta receptor signaling pathway; germ cell migration; tissue homeostasis; response to drug; dendrite morphogenesis; protein transport within lipid bilayer; negative regulation of neuron differentiation; positive regulation of peptidyl-tyrosine phosphorylation; cell migration during sprouting angiogenesis; B cell differentiation; cell-cell adhesion mediated by integrin; response to activity; leukocyte migration; regulation of G-protein coupled receptor protein signaling pathway; G1/S transition of mitotic cell cycle; axon guidance; entry of virus into host cell; cell-matrix adhesion; cell fate specification; negative regulation of cell proliferation; positive regulation of MAPKKK cascade; positive regulation of cell proliferation; visual learning; negative regulation of cell projection organization and biogenesis; integrin-mediated signaling pathway; cell migration; regulation of immune response; in utero embryonic development; sarcomere organization; cell-substrate adhesion; cellular calcium ion homeostasis; formation of radial glial scaffolds; heterotypic cell-cell adhesion; negative regulation of Rho protein signal transduction; stress fiber formation; calcium-independent cell-matrix adhesion; cellular defense response; blood coagulation; leukocyte tethering or rolling; homophilic cell adhesion; positive regulation of cell migration
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
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

ITGB1

Protein Structure Not Found.


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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, Y795‑p
protein conformation: T788‑p, T789‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: 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.


 MS 

MS: 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 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 23 K774-ub EKEKMNAkWDtGENP
0 17 T777-p KMNAkWDtGENPIyk
0 1 - gap
6 1172 Y783-p DtGENPIyksAVttV
0 41 K784-ub tGENPIyksAVttVV
5 23 S785-p GENPIyksAVttVVN
11 1 T788-p PIyksAVttVVNPky
10 2 T789-p IyksAVttVVNPkyE
0 1 - gap
0 4 K794-ac VttVVNPkyEGk___
0 27 K794-ub VttVVNPkyEGk___
7 219 Y795-p ttVVNPkyEGk____
0 6 K798-ub VNPkyEGk_______
  ITGB1 iso2  
R122 QPQQLVLRLRSGEPQ
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
Y780-p AKWDTVSyKTSKKQS
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  ITGB1 iso3  
R122 QPQQLVLRLRSGEPQ
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
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
- gap
Y783-p DTQENPIyKSPINNF
K784 TQENPIyKSPINNFK
S785 QENPIyKSPINNFKN
- gap
- gap
K791 KSPINNFKNPNYGRK
- gap
- gap
Y795 NNFKNPNYGRKAGL_
K798 KNPNYGRKAGL____
  mouse

► Hide Isoforms
 
K122 QPQQLLLKLRSGEPQ
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
- gap
Y783-p DtGENPIyksAVttV
K784-ub tGENPIyksAVttVV
S785-p GENPIyksAVttVVN
T788-p PIyksAVttVVNPky
T789-p IyksAVttVVNPkyE
- gap
K794-ac VttVVNPkyEGk___
K794-ub VttVVNPkyEGk___
Y795-p ttVVNPkyEGk____
K798-ub VNPkyEGk_______
  ITGB1 iso5  
K122 QPQQLLLKLRSGEPQ
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
- gap
Y783 DTQENPIYkSPINNF
K784-ub TQENPIYkSPINNFk
S785 QENPIYkSPINNFkN
- gap
- gap
K791-ub kSPINNFkNPNYGRK
- gap
- gap
Y795 NNFkNPNYGRKAGL_
K798 kNPNYGRKAGL____
  rat

 
K122-ac QPQQLLLkLRSGEPQ
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
- gap
Y784-p DTGENPIyKSAVTTV
K785 TGENPIyKSAVTTVV
S786 GENPIyKSAVTTVVN
T789 PIyKSAVTTVVNPky
T790 IyKSAVTTVVNPkyE
- gap
K795-ac VTTVVNPkyEGK___
K795 VTTVVNPKyEGK___
Y796-p TTVVNPkyEGK____
K799 VNPkyEGK_______
  chicken

 
Q126 QPQKLVLQLRVGEPQ
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
- gap
Y788 DTGENPIYKsAVTTV
K789 TGENPIYKsAVTTVV
S790-p GENPIYKsAVTTVVN
T793 PIYKsAVTTVVNPKY
T794 IYKsAVTTVVNPKYE
- gap
K799 VTTVVNPKYEGK___
K799 VTTVVNPKYEGK___
Y800 TTVVNPKYEGK____
K803 VNPKYEGK_______
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