ITAV_HUMAN - dbPTM
ITAV_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITAV_HUMAN
UniProt AC P06756
Protein Name Integrin alpha-V
Gene Name ITGAV {ECO:0000312|HGNC:HGNC:6150}
Organism Homo sapiens (Human).
Sequence Length 1048
Subcellular Localization Membrane
Single-pass type I membrane protein. Cell junction, focal adhesion .
Protein Description The alpha-V (ITGAV) integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and vWF. They recognize the sequence R-G-D in a wide array of ligands. ITGAV:ITGB3 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. [PubMed: 23125415 ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling]
Protein Sequence MAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFVSGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQRASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSMPPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLKADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFMEYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYEAELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSSNLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWPYKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCLKIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAPMPVPVWVIILAVLAGLLLLAVLVFVMYRMGFFKRVRPPQEEQEREQLQPHENGEGNSET
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
21PhosphorylationRGLPLLLSGLLLPLC
CCHHHHHHHHHHHHH		27.62-
74N-linked_GlycosylationLVGAPKANTTQPGIV
EECCCCCCCCCCCEE		50.1928117447
74N-linked_GlycosylationLVGAPKANTTQPGIV
EECCCCCCCCCCCEE		50.1928117447
88UbiquitinationVEGGQVLKCDWSSTR
EECCEEEECCCCCCC		31.15-
112UbiquitinationTGNRDYAKDDPLEFK
CCCCCCCCCCCCCCC		57.33-
1122-HydroxyisobutyrylationTGNRDYAKDDPLEFK
CCCCCCCCCCCCCCC		57.33-
119UbiquitinationKDDPLEFKSHQWFGA
CCCCCCCCCCCCCCC		37.34-
149SumoylationYHWRTEMKQEREPVG
HHHHHHCCCCCCCCC		42.65-
149SumoylationYHWRTEMKQEREPVG
HHHHHHCCCCCCCCC		42.65-
165UbiquitinationCFLQDGTKTVEYAPC
EEEECCCEEEEEECC		56.98-
187UbiquitinationDGQGFCQGGFSIDFT
CCCCCCCCCEEEEEC		40.0521890473
197 (in isoform 2)Ubiquitination-42.6621890473
215PhosphorylationYWQGQLISDQVAEIV
CCCCEECHHHHHHHH		30.4928122231
225PhosphorylationVAEIVSKYDPNVYSI
HHHHHHCCCCCEEEE		29.1820068231
230PhosphorylationSKYDPNVYSIKYNNQ
HCCCCCEEEEEECCE		16.0020068231
231PhosphorylationKYDPNVYSIKYNNQL
CCCCCEEEEEECCEE		14.3424719451
233 (in isoform 1)Ubiquitination-35.6721890473
233UbiquitinationDPNVYSIKYNNQLAT
CCCEEEEEECCEEEC		35.6721890473
233UbiquitinationDPNVYSIKYNNQLAT
CCCEEEEEECCEEEC		35.6721890473
279PhosphorylationGVPRAARTLGMVYIY
CCCHHHHHCCEEEEE		23.9618669648
284PhosphorylationARTLGMVYIYDGKNM
HHHCCEEEEECCCCH		5.7218669648
286PhosphorylationTLGMVYIYDGKNMSS
HCCEEEEECCCCHHH		10.8528270605
290N-linked_GlycosylationVYIYDGKNMSSLYNF
EEEECCCCHHHHEEC		40.8928117447
296N-linked_GlycosylationKNMSSLYNFTGEQMA
CCHHHHEECCHHHHH		33.0428117447
314UbiquitinationGFSVAATDINGDDYA
CCEEEEECCCCCCCC		27.8521890473
324 (in isoform 2)Ubiquitination-4.3721890473
360UbiquitinationSGDFQTTKLNGFEVF
CCCCCCEEECCCHHH		43.2621890473
360 (in isoform 1)Ubiquitination-43.2621890473
360UbiquitinationSGDFQTTKLNGFEVF
CCCCCCEEECCCHHH		43.2621890473
363 (in isoform 2)Ubiquitination-30.4421890473
399UbiquitinationAPYGGEDKKGIVYIF
CCCCCCCCCCEEEEE		48.9021906983
399 (in isoform 1)Ubiquitination-48.9021890473
404PhosphorylationEDKKGIVYIFNGRST
CCCCCEEEEECCCCC		9.62-
410 (in isoform 2)Ubiquitination-28.3821890473
446UbiquitinationKGATDIDKNGYPDLI
CCCCCCCCCCCCCEE		53.2421906983
446 (in isoform 1)Ubiquitination-53.2421890473
488N-linked_GlycosylationPSILNQDNKTCSLPG
HHHHCCCCCCCCCCC		31.6028117447
490PhosphorylationILNQDNKTCSLPGTA
HHCCCCCCCCCCCCE		17.3721406692
492PhosphorylationNQDNKTCSLPGTALK
CCCCCCCCCCCCEEE		42.7121406692
496PhosphorylationKTCSLPGTALKVSCF
CCCCCCCCEEEEEEE		27.2021406692
514UbiquitinationFCLKADGKGVLPRKL
EEEEECCCCCCCCCC		46.52-
545 (in isoform 2)Ubiquitination-8.4921890473
546PhosphorylationRRALFLYSRSPSHSK
HHHHHHHCCCCCCCC		28.5624719451
548PhosphorylationALFLYSRSPSHSKNM
HHHHHCCCCCCCCCC		25.4730624053
550PhosphorylationFLYSRSPSHSKNMTI
HHHCCCCCCCCCCEE		41.4630624053
552PhosphorylationYSRSPSHSKNMTISR
HCCCCCCCCCCEECC		30.0230624053
554N-linked_GlycosylationRSPSHSKNMTISRGG
CCCCCCCCCEECCCC		35.5328117447
556PhosphorylationPSHSKNMTISRGGLM
CCCCCCCEECCCCHH		25.7930624053
581UbiquitinationDESEFRDKLTPITIF
CCHHHHHCCCCEEEE		50.4321906983
581 (in isoform 1)Ubiquitination-50.4321890473
586PhosphorylationRDKLTPITIFMEYRL
HHCCCCEEEEEEECC		14.9018669648
591PhosphorylationPITIFMEYRLDYRTA
CEEEEEEECCCCCCC		12.5118669648
609 (in isoform 2)Ubiquitination-35.3221890473
610 (in isoform 2)Ubiquitination-39.90-
615N-linked_GlycosylationLNQFTPANISRQAHI
HHCCCCCCHHCCEEE		33.6928117447
633UbiquitinationCGEDNVCKPKLEVSV
CCCCCCCCCCEEEEE		40.69-
645 (in isoform 1)Ubiquitination-46.2421890473
6452-HydroxyisobutyrylationVSVDSDQKKIYIGDD
EEECCCCCEEEECCC		46.24-
645UbiquitinationVSVDSDQKKIYIGDD
EEECCCCCEEEECCC		46.2421906983
646UbiquitinationSVDSDQKKIYIGDDN
EECCCCCEEEECCCC		34.80-
682 (in isoform 2)Ubiquitination-23.80-
701UbiquitinationARLSCAFKTENQTRQ
HHHHCEEECCCCEEE		36.08-
702PhosphorylationRLSCAFKTENQTRQV
HHHCEEECCCCEEEE		33.4429759185
704N-linked_GlycosylationSCAFKTENQTRQVVC
HCEEECCCCEEEEEE		54.4719159218
706PhosphorylationAFKTENQTRQVVCDL
EEECCCCEEEEEEEC		34.3529759185
718UbiquitinationCDLGNPMKAGTQLLA
EECCCCCCHHHHHHH		44.94-
719 (in isoform 2)Ubiquitination-21.73-
749PhosphorylationKFDLQIQSSNLFDKV
EEEEEEECCCCCCCC		23.8721712546
755UbiquitinationQSSNLFDKVSPVVSH
ECCCCCCCCCCCCCC		36.96-
798PhosphorylationEHKENPETEEDVGPV
CCCCCCCCCCCHHHH		46.03-
819PhosphorylationLRNNGPSSFSKAMLH
HHHCCCCCCCHHHHH		36.3524719451
835N-linked_GlycosylationQWPYKYNNNTLLYIL
ECCEEECCCEEEEEE		39.51UniProtKB CARBOHYD
837 (in isoform 2)Ubiquitination-21.9121890473
851N-linked_GlycosylationYDIDGPMNCTSDMEI
EECCCCCCCCCCCEE		29.11UniProtKB CARBOHYD
864UbiquitinationEINPLRIKISSLQTT
EECCEEEEEEECCCC		30.06-
866PhosphorylationNPLRIKISSLQTTEK
CCEEEEEEECCCCCC		21.72-
873UbiquitinationSSLQTTEKNDTVAGQ
EECCCCCCCCCCCCC		59.022190698
873 (in isoform 1)Ubiquitination-59.0221890473
874N-linked_GlycosylationSLQTTEKNDTVAGQG
ECCCCCCCCCCCCCC		43.9119349973
874N-linked_GlycosylationSLQTTEKNDTVAGQG
ECCCCCCCCCCCCCC		43.9117660510
889UbiquitinationERDHLITKRDLALSE
HHHEEEEHHHHCCCC		36.60-
923UbiquitinationVGRLDRGKSAILYVK
HCCCCCCCHHHHHHH		37.29-
945N-linked_GlycosylationFMNKENQNHSYSLKS
HCCCCCCCCCEECCC		37.34UniProtKB CARBOHYD
949PhosphorylationENQNHSYSLKSSASF
CCCCCCEECCCCCCE		32.1324719451
952PhosphorylationNHSYSLKSSASFNVI
CCCEECCCCCCEEEE		36.1121712546
953PhosphorylationHSYSLKSSASFNVIE
CCEECCCCCCEEEEE		26.7521712546
973N-linked_GlycosylationLPIEDITNSTLVTTN
CCHHHCCCCEEEEEE		33.07UniProtKB CARBOHYD
980N-linked_GlycosylationNSTLVTTNVTWGIQP
CCEEEEEEECCCCCC		21.61UniProtKB CARBOHYD
1046PhosphorylationHENGEGNSET-----
CCCCCCCCCC-----		54.1730266825
1048PhosphorylationNGEGNSET-------
CCCCCCCC-------		43.6730266825
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 ITAV_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITAV_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 ITAV_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ILK_HUMANILKphysical
8538749
CYR61_HUMANCYR61physical
11287419
MYPR_HUMANPLP1physical
12196561
MMP2_HUMANMMP2physical
22349830
CSF1R_HUMANCSF1Rphysical
16600665
CBL_HUMANCBLphysical
16600665
BCAR1_HUMANBCAR1physical
16600665
KPB2_HUMANPHKA2physical
16600665
PAXI_HUMANPXNphysical
16600665
K2C3_HUMANKRT3physical
22939629
TSP1_HUMANTHBS1physical
14963009
EPHA2_HUMANEPHA2physical
23874206
ITB1_HUMANITGB1physical
26344197
PSD12_HUMANPSMD12physical
26344197
LG3BP_HUMANLGALS3BPphysical
24362527
NCOR1_HUMANNCOR1physical
23640055
NCOR2_HUMANNCOR2physical
23640055
EP300_HUMANEP300physical
23640055
MK03_HUMANMAPK3physical
23640055
MK01_HUMANMAPK1physical
23640055
STAT1_HUMANSTAT1physical
23640055
SHC1_HUMANSHC1physical
19889638
FAK1_HUMANPTK2physical
19889638
ADAM9_HUMANADAM9physical
16373656
ERBB2_HUMANERBB2physical
26222911
ITA4_HUMANITGA4physical
25792870
ITAV_HUMANITGAVphysical
25792870
ITB1_HUMANITGB1physical
25792870
FAK1_HUMANPTK2physical
12844492
ITB5_HUMANITGB5physical
12844492
SPEB_HUMANAGMATphysical
27173435
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
D03497 Cilengitide (USAN/INN)
D09342 Etaracizumab (USAN/INN); Abegrin (TN)
D09631 Intetumumab (USAN/INN)
D09903 Fluciclatide F 18 (USAN/INN)
D09929 Maraciclatide (USAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ITAV_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-74 AND ASN-874, 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-74; ASN-615; ASN-704 ANDASN-874, AND MASS SPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-615.

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