dbPTM

ITBP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ITBP1_HUMAN
UniProt AC	O14713
Protein Name	Integrin beta-1-binding protein 1
Gene Name	ITGB1BP1
Organism	Homo sapiens (Human).
Sequence Length	200
Subcellular Localization	Nucleus. Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane. Cell projection, lamellipodium. Cell projection, ruffle. Nucleocytoplasmic shuttling protein shuttles between nucleus and cytoplasm in a integrin-dependent manner probably sequestered in t
Protein Description	Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration in the context of mineralization and bone development and angiogenesis. Stimulates cellular proliferation in a fibronectin-dependent manner. Involved in the regulation of beta-1 integrin-containing focal adhesion (FA) site dynamics by controlling its assembly rate during cell adhesion; inhibits beta-1 integrin clustering within FA by directly competing with talin TLN1, and hence stimulates osteoblast spreading and migration in a fibronectin-and/or collagen-dependent manner. Acts as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho family GTPases during integrin-mediated cell matrix adhesion; reduces the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon cell adhesion to fibronectin. Stimulates the release of active CDC42 from the membranes to maintain it in an inactive cytoplasmic pool. Participates in the translocation of the Rho-associated protein kinase ROCK1 to membrane ruffles at cell leading edges of the cell membrane, leading to an increase of myoblast cell migration on laminin. Plays a role in bone mineralization at a late stage of osteoblast differentiation; modulates the dynamic formation of focal adhesions into fibrillar adhesions, which are adhesive structures responsible for fibronectin deposition and fibrillogenesis. Plays a role in blood vessel development; acts as a negative regulator of angiogenesis by attenuating endothelial cell proliferation and migration, lumen formation and sprouting angiogenesis by promoting AKT phosphorylation and inhibiting ERK1/2 phosphorylation through activation of the Notch signaling pathway. Promotes transcriptional activity of the MYC promoter..
Protein Sequence	MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNNNSDTCAEFRIKYVGAIEKLKLSEGKGLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIRMVCYDDGLGAGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSEKP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	RKGKKRHSSSSSQSS CCCCCCCCCCCCCCC	35.63	30576142
11	Phosphorylation	KGKKRHSSSSSQSSE CCCCCCCCCCCCCCH	28.28	25849741
12	Phosphorylation	GKKRHSSSSSQSSEI CCCCCCCCCCCCCHH	36.70	30576142
13	Phosphorylation	KKRHSSSSSQSSEIS CCCCCCCCCCCCHHH	34.05	25159151
14	Phosphorylation	KRHSSSSSQSSEIST CCCCCCCCCCCHHHH	35.71	30576142
16	Phosphorylation	HSSSSSQSSEISTKS CCCCCCCCCHHHHCC	31.70	30576142
17	Phosphorylation	SSSSSQSSEISTKSK CCCCCCCCHHHHCCC	31.17	30576142
20	Phosphorylation	SSQSSEISTKSKSVD CCCCCHHHHCCCCCC	26.23	25072903
21	Phosphorylation	SQSSEISTKSKSVDS CCCCHHHHCCCCCCC	45.02	28985074
23	Phosphorylation	SSEISTKSKSVDSSL CCHHHHCCCCCCCCC	30.19	23312004
25	Phosphorylation	EISTKSKSVDSSLGG HHHHCCCCCCCCCCC	37.94	25159151
28	Phosphorylation	TKSKSVDSSLGGLSR HCCCCCCCCCCCCCC	25.88	29255136
29	Phosphorylation	KSKSVDSSLGGLSRS CCCCCCCCCCCCCCC	26.94	29255136
34	Phosphorylation	DSSLGGLSRSSTVAS CCCCCCCCCCCCEEE	33.13	29255136
36	Phosphorylation	SLGGLSRSSTVASLD CCCCCCCCCCEEEEC	27.30	23403867
37	Phosphorylation	LGGLSRSSTVASLDT CCCCCCCCCEEEECC	26.28	23403867
38	Phosphorylation	GGLSRSSTVASLDTD CCCCCCCCEEEECCC	22.72	28348404
41	Phosphorylation	SRSSTVASLDTDSTK CCCCCEEEECCCCCC	23.57	23401153
44	Phosphorylation	STVASLDTDSTKSSG CCEEEECCCCCCCCC	36.82	25159151
46	Phosphorylation	VASLDTDSTKSSGQS EEEECCCCCCCCCCC	39.57	25159151
47	Phosphorylation	ASLDTDSTKSSGQSN EEECCCCCCCCCCCC	37.44	25159151
49	Phosphorylation	LDTDSTKSSGQSNNN ECCCCCCCCCCCCCC	39.53	28450419
50	Phosphorylation	DTDSTKSSGQSNNNS CCCCCCCCCCCCCCC	42.27	28450419
53	Phosphorylation	STKSSGQSNNNSDTC CCCCCCCCCCCCCCC	45.08	30576142
59	Phosphorylation	QSNNNSDTCAEFRIK CCCCCCCCCHHHHHH	17.28	30576142
66	Ubiquitination	TCAEFRIKYVGAIEK CCHHHHHHEHHHEEE	29.63	-
73	Ubiquitination	KYVGAIEKLKLSEGK HEHHHEEEEECCCCC	44.82	-
117	Phosphorylation	FIMGVSKYGIKVSTS EEECHHHCCEEEECC	19.31	22817900
127	Phosphorylation	KVSTSDQYDVLHRHA EEECCCCHHHHHHHH	17.01	22817900
136	Phosphorylation	VLHRHALYLIIRMVC HHHHHHHHHHHHHHH	9.17	22817900
153	Phosphorylation	DGLGAGKSLLALKTT CCCCCCCEEEEEEEC	27.91	25003641
158	Ubiquitination	GKSLLALKTTDASNE CCEEEEEEECCCCCC	43.71	-
199	Ubiquitination	DSVLTSEKP------ HHHHHCCCC------	56.65	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
38	T	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
38	T	Phosphorylation	Kinase	CAMK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
38	T	Phosphorylation		9813144
Phosphorylation at Thr-38 seems to enhance integrin alpha5beta1-mediated cell adhesion.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of ITBP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ITB1_HUMAN	ITGB1	physical	9281591
LRP1_HUMAN	LRP1	physical	10827173
LRP2_HUMAN	LRP2	physical	10827173
ITB1_HUMAN	ITGB1	physical	11741908
KRIT1_HUMAN	KRIT1	physical	11741838
TANK_HUMAN	TANK	physical	8710854
KRIT1_HUMAN	KRIT1	physical	11854171
EF1A1_HUMAN	EEF1A1	physical	21900206
FAF1_HUMAN	FAF1	physical	21900206
A4_HUMAN	APP	physical	21832049
FIGL1_HUMAN	FIGNL1	physical	25416956
PGRC1_HUMAN	PGRMC1	physical	25814554
KRIT1_HUMAN	KRIT1	physical	25814554
ITB1_HUMAN	ITGB1	physical	28049720
SMUF1_HUMAN	SMURF1	physical	28049720

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ITBP1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND MASSSPECTROMETRY.	19690332 [Abstract]

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