ITB1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ITB1_RAT
• UniProt AC: P49134
• Protein Name: Integrin beta-1
• Gene Name: Itgb1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 799
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein . Cell projection, invadopodium membrane ; Single-pass type I membrane protein . Cell projection, ruffle membrane ; Single-pass type I membrane protein . Recycling endosome . Melanosome . Cell projection
• Protein Description: 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. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. 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 RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling..
• Protein Sequence: MNLQLVFWIGLISLICSVFGQTDKNRCLKANAKSCGECIQAGPNCGWCTNTTFLQEGMPTSARCDDLEALKKKGCHPSDIENPRGSQTIKKNKNVTNRSKGMAEKLRPEDITQIQPQQLLLKLRSGEPQKFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTDRGEFFNELVGQQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNVYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSGNSSNVIQLIIDAYNSLSSEVILENSKLPDGVTINYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITANKCPNKESENQLKLNPLGFTEEVEVVLQFICKCNCQSHGIPASPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRENTNEIYSGKFCECDNFNCDRSNGLICGGNGVCRCRVCECYPNYTGSACDCSLDTVPCVATNGQICNGRGICECGACKCTDPKFQGPTCETCQTCLGVCAEHKECVQCRAFNKGEKKDTCAQECSHFNLTKVESREKLPQPVQVDPVTHCKEKDIDDCWFYFTYSVNSKGEAHVHVVETPDCPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGK

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
50	N-linked_Glycosylation	PNCGWCTNTTFLQEG CCCCCCCCCHHHHCC	33.70	-
94	N-linked_Glycosylation	QTIKKNKNVTNRSKG CCCCCCCCCCCCCCC	56.06	-
97	N-linked_Glycosylation	KKNKNVTNRSKGMAE CCCCCCCCCCCCHHH	41.78	-
122	Acetylation	QPQQLLLKLRSGEPQ CHHHHHHHHHCCCCC	41.65	22902405
130	Acetylation	LRSGEPQKFTLKFKR HHCCCCCEEEEEEEE	51.54	22902405
212	N-linked_Glycosylation	NPCTSEQNCTSPFSY CCCCCCCCCCCCCCC	27.29	-
269	N-linked_Glycosylation	GSLIGWRNVTRLLVF HHHHCCCCCEEEEEE	32.76	-
349	Acetylation	QPVYKELKNLIPKSA HHHHHHHHHHCCHHH	51.29	22902405
363	N-linked_Glycosylation	AVGTLSGNSSNVIQL HCCCCCCCCCCHHHH	38.60	-
406	N-linked_Glycosylation	SYCKNGVNGTGENGR HHHCCCCCCCCCCCC	43.64	-
417	N-linked_Glycosylation	ENGRKCSNISIGDEV CCCCCCCCCCCCCEE	41.31	-
482	N-linked_Glycosylation	SPKCHEGNGTFECGA CCCCCCCCCEEECCC	43.26	-
521	N-linked_Glycosylation	DAYCRKENSSEICSN HHHHHHCCCCCCCCC	54.60	-
550	Phosphorylation	ENTNEIYSGKFCECD CCCCCCCCCCCCCCC	40.96	-
585	N-linked_Glycosylation	RVCECYPNYTGSACD EEEEECCCCCCCCCC	22.11	-
670	N-linked_Glycosylation	AQECSHFNLTKVESR HHHCCCCCCCCCCCC	41.18	-
778	Phosphorylation	KMNAKWDTGENPIYK HHHCCCCCCCCCCCC	45.33	22108457
784	Phosphorylation	DTGENPIYKSAVTTV CCCCCCCCCCCEEEE	10.51	27097102
786	Phosphorylation	GENPIYKSAVTTVVN CCCCCCCCCEEEECC	15.82	23984901
789	Phosphorylation	PIYKSAVTTVVNPKY CCCCCCEEEECCCCC	17.37	23984901
790	Phosphorylation	IYKSAVTTVVNPKYE CCCCCEEEECCCCCC	18.83	-
795	Acetylation	VTTVVNPKYEGK--- EEEECCCCCCCC---	51.21	22902405
796	Phosphorylation	TTVVNPKYEGK---- EEECCCCCCCC----	31.04	-

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

Oops, there are no upstream regulatory protein records of ITB1_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ITB1_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ITB1_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PAXI_RAT	Pxn	physical	16935300
FAK1_RAT	Ptk2	physical	16935300
ACTB_RAT	Actb	physical	16935300

Drug and Disease Associations

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