ITA5_MOUSE - dbPTM
ITA5_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITA5_MOUSE
UniProt AC P11688
Protein Name Integrin alpha-5
Gene Name Itga5
Organism Mus musculus (Mouse).
Sequence Length 1053
Subcellular Localization Membrane
Single-pass type I membrane protein. Cell junction, focal adhesion . Cell surface .
Protein Description Integrin alpha-5/beta-1 (ITGA5:ITGB1) is a receptor for fibronectin and fibrinogen. It recognizes the sequence R-G-D in its ligands. ITGA5:ITGB1 binds 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 MGSWTPRSPRSPLHAVLLRWGPRRLPPLLPLLLLLWPPPLQVGGFNLDAEAPAVLSGPPGSLFGFSVEFYRPGRDGVSVLVGAPKANTSQPGVLQGGAVYVCPWGTSPIQCTTIQFDSKGSRILESSLYSAKGEEPVEYKSLQWFGATVRAHGSSILACAPLYSWRTEKDPQNDPVGTCYLSTENFTRILEYAPCRSDFGSAAGQGYCQGGFSAEFTKTGRVVLGGPGSYFWQGQILSATQEQISESYYPEYLINPVQGQLQTRQASSVYDDSYLGYSVAVGEFSGDDTEDFVAGVPKGNLTYGYVTVLNGSDIHSLYNVSGEQMASYFGYAVAATDTNGDGLDDLLVGAPLLMERTADGRPQEVGRVYIYLQRPAGIDPTPTLTLTGQDEFSRFGSSLTPLGDLDQDGYNDVAIGAPFGGEAQQGVVFIFPGGPGGLSTKPSQVLQPLWAAGRTPDFFGSALRGGRDLDGNGYPDLIVGSFGVDKALVYRGRPIISASASLTIFPSMFNPEERSCSLEGNPVSCINLSFCLNASGKHVPNSIGFEVELQLDWQKQKGGVRRALFLTSKQATLTQTLLIQNGAREDCREMKIYLRNESEFRDKLSPIHIALNFSLDPKAPMDSHGLRPVLHYQSKSRIEDKAQILLDCGEDNICVPDLQLDVYGEKKHVYLGDKNALNLTFHAQNLGEGGAYEAELRVTAPLEAEYSGLVRHPGNFSSLSCDYFAVNQSRQLVCDLGNPMKAGTSLWGGLRFTVPHLQDTKKTIQFDFQILSKNLNNSQSNVVSFPLSVEAQAQVSLNGVSKPEAVIFPVSDWNPQDQPQKEEDLGPAVHHVYELINQGPSSISQGVLELSCPQALEGQQLLYVTKVTGLSNCTSNYTPNSQGLELDPETSPHHLQKREAPGRSSTASGTQVLKCPEAKCFRLRCEFGPLHRQESRSLQLHFRVWAKTFLQREYQPFSLQCEAVYEALKMPYQILPRQLPQKKLQVATAVQWTKAEGSNGVPLWIIILAILFGLLLLGLLIYVLYKLGFFKRSLPYGTAMEKAQLKPPATSDA
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 Orthologous
Protein Cluster
87N-linked_GlycosylationLVGAPKANTSQPGVL
EECCCCCCCCCCCEE		46.52-
130PhosphorylationILESSLYSAKGEEPV
EEEEECEECCCCCCC		28.88-
185N-linked_GlycosylationTCYLSTENFTRILEY
EEEEECCCCCHHHHH		43.6119349973
197PhosphorylationLEYAPCRSDFGSAAG
HHHCCCCCCCCCCCC		43.9728285833
201PhosphorylationPCRSDFGSAAGQGYC
CCCCCCCCCCCCCCC		18.2328285833
300N-linked_GlycosylationVAGVPKGNLTYGYVT
CCCCCCCCEEEEEEE		35.0219656770
310N-linked_GlycosylationYGYVTVLNGSDIHSL
EEEEEEECCCCCHHE		43.5219656770
319N-linked_GlycosylationSDIHSLYNVSGEQMA
CCCHHEEECCHHHHH		27.11-
527N-linked_GlycosylationGNPVSCINLSFCLNA
CCCEEEEEEEEEECC		33.68-
533N-linked_GlycosylationINLSFCLNASGKHVP
EEEEEEECCCCCCCC		32.99-
596N-linked_GlycosylationEMKIYLRNESEFRDK
HCEEEECCHHHHHHH		55.3319656770
598PhosphorylationKIYLRNESEFRDKLS
EEEECCHHHHHHHCC		45.65-
612N-linked_GlycosylationSPIHIALNFSLDPKA
CCCEEEEECCCCCCC		18.5519656770
675N-linked_GlycosylationHVYLGDKNALNLTFH
EEEECCCCEEEEEEE		55.1719656770
678N-linked_GlycosylationLGDKNALNLTFHAQN
ECCCCEEEEEEEEEE		34.3219656770
685N-linked_GlycosylationNLTFHAQNLGEGGAY
EEEEEEEECCCCCEE		51.2819656770
715N-linked_GlycosylationGLVRHPGNFSSLSCD
CCCCCCCCCCCCCCC		37.7719349973
727N-linked_GlycosylationSCDYFAVNQSRQLVC
CCCEEEEECCCCEEE		30.5819349973
776N-linked_GlycosylationQILSKNLNNSQSNVV
HHHHHCCCCCCCCEE		56.34-
872N-linked_GlycosylationTKVTGLSNCTSNYTP
EEECCCCCCCCCCCC		37.82-
876N-linked_GlycosylationGLSNCTSNYTPNSQG
CCCCCCCCCCCCCCC		26.9219349973
961GlutathionylationYQPFSLQCEAVYEAL
CCCCCHHHHHHHHHH		4.3824333276
1036PhosphorylationFFKRSLPYGTAMEKA
CCCCCCCCCCHHHHC		32.19-
1042UbiquitinationPYGTAMEKAQLKPPA
CCCCHHHHCCCCCCC		28.4822790023
1050PhosphorylationAQLKPPATSDA----
CCCCCCCCCCC----		32.6730635358
1051PhosphorylationQLKPPATSDA-----
CCCCCCCCCC-----		33.3830635358
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

Oops, there are no upstream regulatory protein records of ITA5_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITA5_MOUSE !!
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 ITA5_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SHRPN_MOUSESharpinphysical
21947080
AP2B1_HUMANAP2B1physical
26496610
CAPZB_HUMANCAPZBphysical
26496610
DAPK3_HUMANDAPK3physical
26496610
FLNA_HUMANFLNAphysical
26496610
ITB1_HUMANITGB1physical
26496610
MYO5A_HUMANMYO5Aphysical
26496610
MYO6_HUMANMYO6physical
26496610
PP1B_HUMANPPP1CBphysical
26496610
RBBP6_HUMANRBBP6physical
26496610
TMOD1_HUMANTMOD1physical
26496610
TPM1_HUMANTPM1physical
26496610
TPM2_HUMANTPM2physical
26496610
TPM3_HUMANTPM3physical
26496610
LUZP1_HUMANLUZP1physical
26496610
OGT1_HUMANOGTphysical
26496610
LRRF2_HUMANLRRFIP2physical
26496610
ARPC5_HUMANARPC5physical
26496610
ARC1B_HUMANARPC1Bphysical
26496610
ARP3_HUMANACTR3physical
26496610
ARP2_HUMANACTR2physical
26496610
LIMC1_HUMANLIMCH1physical
26496610
CYTSA_HUMANSPECC1Lphysical
26496610
TMOD3_HUMANTMOD3physical
26496610
MICA3_HUMANMICAL3physical
26496610
ARP5L_HUMANARPC5Lphysical
26496610
CYTSB_HUMANSPECC1physical
26496610
TPRN_HUMANTPRNphysical
26496610
MY18A_HUMANMYO18Aphysical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ITA5_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185; ASN-596; ASN-612;ASN-678; ASN-715; ASN-727 AND ASN-876, AND MASS SPECTROMETRY.
"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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-300; ASN-310; ASN-596;ASN-612; ASN-675; ASN-678 AND ASN-685, AND MASS SPECTROMETRY.

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