ITA8_HUMAN - dbPTM
ITA8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITA8_HUMAN
UniProt AC P53708
Protein Name Integrin alpha-8
Gene Name ITGA8
Organism Homo sapiens (Human).
Sequence Length 1063
Subcellular Localization Membrane
Single-pass type I membrane protein . Cell membrane .
Protein Description Integrin alpha-8/beta-1 functions in the genesis of kidney and probably of other organs by regulating the recruitment of mesenchymal cells into epithelial structures. It recognizes the sequence R-G-D in a wide array of ligands including TNC, FN1, SPP1 TGFB1, TGFB3 and VTN. NPNT is probably its functional ligand in kidney genesis. Neuronal receptor for TNC it mediates cell-cell interactions and regulates neurite outgrowth of sensory and motor neurons..
Protein Sequence MSPGASRGPRGSQAPLIAPLCCAAAALGMLLWSPACQAFNLDVEKLTVYSGPKGSYFGYAVDFHIPDARTASVLVGAPKANTSQPDIVEGGAVYYCPWPAEGSAQCRQIPFDTTNNRKIRVNGTKEPIEFKSNQWFGATVKAHKGKVVACAPLYHWRTLKPTPEKDPVGTCYVAIQNFSAYAEFSPCRNSNADPEGQGYCQAGFSLDFYKNGDLIVGGPGSFYWQGQVITASVADIIANYSFKDILRKLAGEKQTEVAPASYDDSYLGYSVAAGEFTGDSQQELVAGIPRGAQNFGYVSIINSTDMTFIQNFTGEQMASYFGYTVVVSDVNSDGLDDVLVGAPLFMEREFESNPREVGQIYLYLQVSSLLFRDPQILTGTETFGRFGSAMAHLGDLNQDGYNDIAIGVPFAGKDQRGKVLIYNGNKDGLNTKPSQVLQGVWASHAVPSGFGFTLRGDSDIDKNDYPDLIVGAFGTGKVAVYRARPVVTVDAQLLLHPMIINLENKTCQVPDSMTSAACFSLRVCASVTGQSIANTIVLMAEVQLDSLKQKGAIKRTLFLDNHQAHRVFPLVIKRQKSHQCQDFIVYLRDETEFRDKLSPINISLNYSLDESTFKEGLEVKPILNYYRENIVSEQAHILVDCGEDNLCVPDLKLSARPDKHQVIIGDENHLMLIINARNEGEGAYEAELFVMIPEEADYVGIERNNKGFRPLSCEYKMENVTRMVVCDLGNPMVSGTNYSLGLRFAVPRLEKTNMSINFDLQIRSSNKDNPDSNFVSLQINITAVAQVEIRGVSHPPQIVLPIHNWEPEEEPHKEEEVGPLVEHIYELHNIGPSTISDTILEVGWPFSARDEFLLYIFHIQTLGPLQCQPNPNINPQDIKPAASPEDTPELSAFLRNSTIPHLVRKRDVHVVEFHRQSPAKILNCTNIECLQISCAVGRLEGGESAVLKVRSRLWAHTFLQRKNDPYALASLVSFEVKKMPYTDQPAKLPEGSIVIKTSVIWATPNVSFSIPLWVIILAILLGLLVLAILTLALWKCGFFDRARPPQEDMTDREQLTNDKTPEA
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
2Phosphorylation------MSPGASRGP
------CCCCCCCCC
43.2615302935
72PhosphorylationIPDARTASVLVGAPK
CCCCCCCEEEECCCC
18.5125884760
81N-linked_GlycosylationLVGAPKANTSQPDIV
EECCCCCCCCCCCCE
46.52UniProtKB CARBOHYD
122N-linked_GlycosylationNNRKIRVNGTKEPIE
CCCEEEECCCCCCEE
42.44UniProtKB CARBOHYD
177N-linked_GlycosylationTCYVAIQNFSAYAEF
EEEEEEECCEEEEEC
27.08UniProtKB CARBOHYD
239N-linked_GlycosylationSVADIIANYSFKDIL
EHHHHHHCCCHHHHH
23.67UniProtKB CARBOHYD
302N-linked_GlycosylationFGYVSIINSTDMTFI
CCEEEEEECCCCCEE
36.87UniProtKB CARBOHYD
311N-linked_GlycosylationTDMTFIQNFTGEQMA
CCCCEEECCCCHHHH
31.47UniProtKB CARBOHYD
367O-linked_GlycosylationIYLYLQVSSLLFRDP
HEEEHHHHHHHHCCC
11.4229351928
368O-linked_GlycosylationYLYLQVSSLLFRDPQ
EEEHHHHHHHHCCCC
30.1829351928
378PhosphorylationFRDPQILTGTETFGR
HCCCCCCCCCCCCHH
43.6222817900
418UbiquitinationAGKDQRGKVLIYNGN
CCCCCCCCEEEECCC
35.7421906983
422PhosphorylationQRGKVLIYNGNKDGL
CCCCEEEECCCCCCC
16.9229052541
453PhosphorylationVPSGFGFTLRGDSDI
CCCCCCEEEECCCCC
18.8724719451
481PhosphorylationGTGKVAVYRARPVVT
CCCCEEEEECCCEEE
6.71-
504N-linked_GlycosylationPMIINLENKTCQVPD
CEEEECCCCCCCCCC
48.37UniProtKB CARBOHYD
556PhosphorylationQKGAIKRTLFLDNHQ
HCCCCCEEEEECCCC
19.5024043423
573UbiquitinationRVFPLVIKRQKSHQC
HHHCEEEECCCCCCC
41.1021906983
601N-linked_GlycosylationRDKLSPINISLNYSL
HHHCCCEEEEECCCC
22.60UniProtKB CARBOHYD
605N-linked_GlycosylationSPINISLNYSLDEST
CCEEEEECCCCCCCC
19.98UniProtKB CARBOHYD
614AcetylationSLDESTFKEGLEVKP
CCCCCCCCCCCEEHH
51.4611794795
620AcetylationFKEGLEVKPILNYYR
CCCCCEEHHHHHHHH
19.5711792759
719N-linked_GlycosylationSCEYKMENVTRMVVC
CCEEECCCEEEEEEE
36.64UniProtKB CARBOHYD
737N-linked_GlycosylationNPMVSGTNYSLGLRF
CCCCCCCCCCCEEEE
28.11UniProtKB CARBOHYD
751UbiquitinationFAVPRLEKTNMSINF
EEEECEEECCCEEEE
50.20-
753N-linked_GlycosylationVPRLEKTNMSINFDL
EECEEECCCEEEEEE
33.02UniProtKB CARBOHYD
767UbiquitinationLQIRSSNKDNPDSNF
EEEECCCCCCCCCCC
61.91-
780N-linked_GlycosylationNFVSLQINITAVAQV
CCEEEEEEEEEEEEE
16.76UniProtKB CARBOHYD
896N-linked_GlycosylationELSAFLRNSTIPHLV
HHHHHHHCCCCCHHH
45.73UniProtKB CARBOHYD
923N-linked_GlycosylationQSPAKILNCTNIECL
CCCCHHHCCCCCEEE
33.76UniProtKB CARBOHYD
948UbiquitinationGGESAVLKVRSRLWA
CCCCCHHHHHHHHHH
29.0721906983
966PhosphorylationLQRKNDPYALASLVS
HHHCCCHHHHHHHEE
19.6722210691
970PhosphorylationNDPYALASLVSFEVK
CCHHHHHHHEEEEEE
30.1022210691
973PhosphorylationYALASLVSFEVKKMP
HHHHHHEEEEEEECC
22.4522210691
997O-linked_GlycosylationEGSIVIKTSVIWATP
CCCEEEEEEEEECCC
19.6629351928
998O-linked_GlycosylationGSIVIKTSVIWATPN
CCEEEEEEEEECCCC
13.4529351928
1005N-linked_GlycosylationSVIWATPNVSFSIPL
EEEECCCCCCCHHHH
37.40UniProtKB CARBOHYD
1056PhosphorylationMTDREQLTNDKTPEA
CCCHHHHHCCCCCCC
40.8526471730
1060PhosphorylationEQLTNDKTPEA----
HHHHCCCCCCC----
29.2626471730

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 ITA8_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITA8_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 ITA8_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NPNT_HUMANNPNTphysical
11470831

Drug and Disease Associations
Kegg Disease
OMIM Disease
191830Renal hypodysplasia/aplasia 1 (RHDA1)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ITA8_HUMAN

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Related Literatures of Post-Translational Modification

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