ITA2_HUMAN - dbPTM
ITA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITA2_HUMAN
UniProt AC P17301
Protein Name Integrin alpha-2
Gene Name ITGA2
Organism Homo sapiens (Human).
Sequence Length 1181
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Integrin alpha-2/beta-1 is a receptor for laminin, collagen, collagen C-propeptides, fibronectin and E-cadherin. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. It is responsible for adhesion of platelets and other cells to collagens, modulation of collagen and collagenase gene expression, force generation and organization of newly synthesized extracellular matrix.; (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for Human rotavirus A.; (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for Human echoviruses 1 and 8..
Protein Sequence MGPERTGAAPLPLLLVLALSQGILNCCLAYNVGLPEAKIFSGPSSEQFGYAVQQFINPKGNWLLVGSPWSGFPENRMGDVYKCPVDLSTATCEKLNLQTSTSIPNVTEMKTNMSLGLILTRNMGTGGFLTCGPLWAQQCGNQYYTTGVCSDISPDFQLSASFSPATQPCPSLIDVVVVCDESNSIYPWDAVKNFLEKFVQGLDIGPTKTQVGLIQYANNPRVVFNLNTYKTKEEMIVATSQTSQYGGDLTNTFGAIQYARKYAYSAASGGRRSATKVMVVVTDGESHDGSMLKAVIDQCNHDNILRFGIAVLGYLNRNALDTKNLIKEIKAIASIPTERYFFNVSDEAALLEKAGTLGEQIFSIEGTVQGGDNFQMEMSQVGFSADYSSQNDILMLGAVGAFGWSGTIVQKTSHGHLIFPKQAFDQILQDRNHSSYLGYSVAAISTGESTHFVAGAPRANYTGQIVLYSVNENGNITVIQAHRGDQIGSYFGSVLCSVDVDKDTITDVLLVGAPMYMSDLKKEEGRVYLFTIKKGILGQHQFLEGPEGIENTRFGSAIAALSDINMDGFNDVIVGSPLENQNSGAVYIYNGHQGTIRTKYSQKILGSDGAFRSHLQYFGRSLDGYGDLNGDSITDVSIGAFGQVVQLWSQSIADVAIEASFTPEKITLVNKNAQIILKLCFSAKFRPTKQNNQVAIVYNITLDADGFSSRVTSRGLFKENNERCLQKNMVVNQAQSCPEHIIYIQEPSDVVNSLDLRVDISLENPGTSPALEAYSETAKVFSIPFHKDCGEDGLCISDLVLDVRQIPAAQEQPFIVSNQNKRLTFSVTLKNKRESAYNTGIVVDFSENLFFASFSLPVDGTEVTCQVAASQKSVACDVGYPALKREQQVTFTINFDFNLQNLQNQASLSFQALSESQEENKADNLVNLKIPLLYDAEIHLTRSTNINFYEISSDGNVPSIVHSFEDVGPKFIFSLKVTTGSVPVSMATVIIHIPQYTKEKNPLMYLTGVQTDKAGDISCNADINPLKIGQTSSSVSFKSENFRHTKELNCRTASCSNVTCWLKDVHMKGEYFVNVTTRIWNGTFASSTFQTVQLTAAAEINTYNPEIYVIEDNTVTIPLMIMKPDEKAEVPTGVIIGSIIAGILLLLALVAILWKLGFFKRKYEKMTKNPDEIDETTELSS
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
50PhosphorylationPSSEQFGYAVQQFIN
CCHHHHHHHHHHCCC		12.61-
82UbiquitinationNRMGDVYKCPVDLST
CCCCCEEECCCCCCH		31.7329901268
101PhosphorylationKLNLQTSTSIPNVTE
HCCCCCCCCCCCCHH		33.78-
105N-linked_GlycosylationQTSTSIPNVTEMKTN
CCCCCCCCCHHCCCC		52.2317660510
112N-linked_GlycosylationNVTEMKTNMSLGLIL
CCHHCCCCCEEEEEE		16.72UniProtKB CARBOHYD
216PhosphorylationTQVGLIQYANNPRVV
CCEEEEEECCCCEEE		12.3328152594
2612-HydroxyisobutyrylationGAIQYARKYAYSAAS
HHHHHHHHHHHHHHC		26.51-
262PhosphorylationAIQYARKYAYSAASG
HHHHHHHHHHHHHCC		12.76-
264PhosphorylationQYARKYAYSAASGGR
HHHHHHHHHHHCCCC		8.85-
273PhosphorylationAASGGRRSATKVMVV
HHCCCCCCCEEEEEE		38.6429083192
275PhosphorylationSGGRRSATKVMVVVT
CCCCCCCEEEEEEEE		25.9729083192
282PhosphorylationTKVMVVVTDGESHDG
EEEEEEEECCCCCCC		27.0329759185
286PhosphorylationVVVTDGESHDGSMLK
EEEECCCCCCCCHHH		32.1929083192
290PhosphorylationDGESHDGSMLKAVID
CCCCCCCCHHHHHHH		27.3129083192
3232-HydroxyisobutyrylationNRNALDTKNLIKEIK
CCCCCCHHHHHHHHH		49.80-
3302-HydroxyisobutyrylationKNLIKEIKAIASIPT
HHHHHHHHHHHCCCC		34.53-
343N-linked_GlycosylationPTERYFFNVSDEAAL
CCCEEECCCCCHHHH		23.6016263699
343N-linked_GlycosylationPTERYFFNVSDEAAL
CCCEEECCCCCHHHH		23.6016263699
412PhosphorylationSGTIVQKTSHGHLIF
CEEEEEECCCCEEEE		14.63-
432N-linked_GlycosylationDQILQDRNHSSYLGY
HHHHHCCCCCCCCCC		47.91UniProtKB CARBOHYD
460N-linked_GlycosylationVAGAPRANYTGQIVL
EECCCCCCCCCEEEE		35.86UniProtKB CARBOHYD
475N-linked_GlycosylationYSVNENGNITVIQAH
EEECCCCCEEEEEEE		38.04UniProtKB CARBOHYD
599UbiquitinationHQGTIRTKYSQKILG
CCCEEEEECCHHHHC		32.8123503661
601PhosphorylationGTIRTKYSQKILGSD
CEEEEECCHHHHCCC		26.93-
603UbiquitinationIRTKYSQKILGSDGA
EEEECCHHHHCCCCH		33.6823503661
612MethylationLGSDGAFRSHLQYFG
HCCCCHHHHHHHHHC		23.72115480673
613PhosphorylationGSDGAFRSHLQYFGR
CCCCHHHHHHHHHCC		23.30-
621PhosphorylationHLQYFGRSLDGYGDL
HHHHHCCCCCCCCCC		31.06-
671UbiquitinationEKITLVNKNAQIILK
HHEEEECCCHHHHHH		46.2929967540
699N-linked_GlycosylationNQVAIVYNITLDADG
CEEEEEEEEEECCCC		15.18UniProtKB CARBOHYD
712PhosphorylationDGFSSRVTSRGLFKE
CCCCCCCCCCCCCHH		16.1721406692
713PhosphorylationGFSSRVTSRGLFKEN
CCCCCCCCCCCCHHC		22.8421406692
768PhosphorylationSLENPGTSPALEAYS
EECCCCCCHHHHHHH		17.68-
774PhosphorylationTSPALEAYSETAKVF
CCHHHHHHHHCCEEE		9.54-
779UbiquitinationEAYSETAKVFSIPFH
HHHHHCCEEEEEECC		51.7623503661
821UbiquitinationFIVSNQNKRLTFSVT
EEEECCCCEEEEEEE		38.7322817900
830UbiquitinationLTFSVTLKNKRESAY
EEEEEEECCCCHHHC		51.57-
8842-HydroxyisobutyrylationDVGYPALKREQQVTF
ECCCCCCCCEEEEEE		56.87-
978PhosphorylationFIFSLKVTTGSVPVS
EEEEEEEECCCCCCE		24.69-
1005PhosphorylationKEKNPLMYLTGVQTD
CCCCCCEEEEECCCC		14.59-
1036PhosphorylationGQTSSSVSFKSENFR
CCCCCCEEECCCCCC		28.9824719451
1038UbiquitinationTSSSVSFKSENFRHT
CCCCEEECCCCCCCC		49.7223503661
1057N-linked_GlycosylationCRTASCSNVTCWLKD
CEECCCCCEEEEEEE		37.1317660510
1071PhosphorylationDVHMKGEYFVNVTTR
ECCCCCCEEEEEEEE		22.8423911959
1074N-linked_GlycosylationMKGEYFVNVTTRIWN
CCCCEEEEEEEEEEC		18.6019349973
1074N-linked_GlycosylationMKGEYFVNVTTRIWN
CCCCEEEEEEEEEEC		18.6016263699
1076PhosphorylationGEYFVNVTTRIWNGT
CCEEEEEEEEEECCC		12.7323911959
1081N-linked_GlycosylationNVTTRIWNGTFASST
EEEEEEECCCCCCCC		36.94UniProtKB CARBOHYD
1162UbiquitinationKLGFFKRKYEKMTKN
HHCHHHHHHHHHCCC		59.3523503661
1165UbiquitinationFFKRKYEKMTKNPDE
HHHHHHHHHCCCHHH		49.1022817900
1168UbiquitinationRKYEKMTKNPDEIDE
HHHHHHCCCHHHCCC		64.0821963094
1176PhosphorylationNPDEIDETTELSS--
CHHHCCCCCCCCC--		23.0923403867
1177PhosphorylationPDEIDETTELSS---
HHHCCCCCCCCC---		32.6423911959
1180PhosphorylationIDETTELSS------
CCCCCCCCC------		27.9825159151
1181PhosphorylationDETTELSS-------
CCCCCCCC-------		57.7925159151
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
1180SPhosphorylationKinaseSTK4Q13043
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITA2_HUMAN !!
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 ITA2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MCP_HUMANCD46physical
10741407
MMP1_HUMANMMP1physical
11359774
MSS4_HUMANRABIFphysical
10094488
SHRPN_HUMANSHARPINphysical
21947080
ITB1_HUMANITGB1physical
21947080
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 ITA2_HUMAN

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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-343, AND MASSSPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-343, AND MASSSPECTROMETRY.
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach.";
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
Mol. Cell. Proteomics 5:226-233(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-343, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1177, AND MASSSPECTROMETRY.

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