ITA11_HUMAN - dbPTM
ITA11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITA11_HUMAN
UniProt AC Q9UKX5
Protein Name Integrin alpha-11
Gene Name ITGA11
Organism Homo sapiens (Human).
Sequence Length 1188
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Integrin alpha-11/beta-1 is a receptor for collagen..
Protein Sequence MDLPRGLVVAWALSLWPGFTDTFNMDTRKPRVIPGSRTAFFGYTVQQHDISGNKWLVVGAPLETNGYQKTGDVYKCPVIHGNCTKLNLGRVTLSNVSERKDNMRLGLSLATNPKDNSFLACSPLWSHECGSSYYTTGMCSRVNSNFRFSKTVAPALQRCQTYMDIVIVLDGSNSIYPWVEVQHFLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTETRTAFGIEFARSEAFQKGGRKGAKKVMIVITDGESHDSPDLEKVIQQSERDNVTRYAVAVLGYYNRRGINPETFLNEIKYIASDPDDKHFFNVTDEAALKDIVDALGDRIFSLEGTNKNETSFGLEMSQTGFSSHVVEDGVLLGAVGAYDWNGAVLKETSAGKVIPLRESYLKEFPEELKNHGAYLGYTVTSVVSSRQGRVYVAGAPRFNHTGKVILFTMHNNRSLTIHQAMRGQQIGSYFGSEITSVDIDGDGVTDVLLVGAPMYFNEGRERGKVYVYELRQNLFVYNGTLKDSHSYQNARFGSSIASVRDLNQDSYNDVVVGAPLEDNHAGAIYIFHGFRGSILKTPKQRITASELATGLQYFGCSIHGQLDLNEDGLIDLAVGALGNAVILWSRPVVQINASLHFEPSKINIFHRDCKRSGRDATCLAAFLCFTPIFLAPHFQTTTVGIRYNATMDERRYTPRAHLDEGGDRFTNRAVLLSSGQELCERINFHVLDTADYVKPVTFSVEYSLEDPDHGPMLDDGWPTTLRVSVPFWNGCNEDEHCVPDLVLDARSDLPTAMEYCQRVLRKPAQDCSAYTLSFDTTVFIIESTRQRVAVEATLENRGENAYSTVLNISQSANLQFASLIQKEDSDGSIECVNEERRLQKQVCNVSYPFFRAKAKVAFRLDFEFSKSIFLHHLEIELAAGSDSNERDSTKEDNVAPLRFHLKYEADVLFTRSSSLSHYEVKPNSSLERYDGIGPPFSCIFRIQNLGLFPIHGMMMKITIPIATRSGNRLLKLRDFLTDEANTSCNIWGNSTEYRPTPVEEDLRRAPQLNHSNSDVVSINCNIRLVPNQEINFHLLGNLWLRSLKALKYKSMKIMVNAALQRQFHSPFIFREEDPSRQIVFEISKQEDWQVPIWIIVGSTLGGLLLLALLVLALWKLGFFRSARRRREPGLDPTPKVLE
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
82N-linked_GlycosylationKCPVIHGNCTKLNLG
ECCEEECCCCEEECC
19.00UniProtKB CARBOHYD
92PhosphorylationKLNLGRVTLSNVSER
EEECCEEEECCHHHC
24.1022210691
94PhosphorylationNLGRVTLSNVSERKD
ECCEEEECCHHHCCC
26.3129396449
95N-linked_GlycosylationLGRVTLSNVSERKDN
CCEEEECCHHHCCCC
44.43UniProtKB CARBOHYD
97PhosphorylationRVTLSNVSERKDNMR
EEEECCHHHCCCCEE
35.6129396449
150AcetylationNSNFRFSKTVAPALQ
CCCCCCCCCHHHHHH
44.287480079
291N-linked_GlycosylationIQQSERDNVTRYAVA
HHHHHHHCHHHHHHH
43.19UniProtKB CARBOHYD
331N-linked_GlycosylationPDDKHFFNVTDEAAL
CCCCCCCCCCCHHHH
34.5319159218
351PhosphorylationALGDRIFSLEGTNKN
HHHCEEEEEECCCCC
24.1223403867
358N-linked_GlycosylationSLEGTNKNETSFGLE
EEECCCCCCCCEEEE
60.90UniProtKB CARBOHYD
409PhosphorylationKVIPLRESYLKEFPE
CEEECCHHHHHHCCH
29.3624719451
430PhosphorylationAYLGYTVTSVVSSRQ
CCCCEEEEEEEECCC
14.1722210691
431PhosphorylationYLGYTVTSVVSSRQG
CCCEEEEEEEECCCC
19.04-
434PhosphorylationYTVTSVVSSRQGRVY
EEEEEEEECCCCCEE
20.0422210691
449N-linked_GlycosylationVAGAPRFNHTGKVIL
EEECCCCCCCCCEEE
32.84UniProtKB CARBOHYD
462N-linked_GlycosylationILFTMHNNRSLTIHQ
EEEEEECCCEEEEEH
21.90UniProtKB CARBOHYD
479PhosphorylationRGQQIGSYFGSEITS
CCCCCHHHCCCEEEE
13.5222210691
485PhosphorylationSYFGSEITSVDIDGD
HHCCCEEEEEECCCC
20.7423403867
486PhosphorylationYFGSEITSVDIDGDG
HCCCEEEEEECCCCC
24.3723403867
528N-linked_GlycosylationRQNLFVYNGTLKDSH
CCCEEEEECCCCCCC
31.50UniProtKB CARBOHYD
583PhosphorylationIFHGFRGSILKTPKQ
EEECCCCCCCCCHHH
22.0824719451
642N-linked_GlycosylationSRPVVQINASLHFEP
CCCEEEEEEEECCCH
13.34UniProtKB CARBOHYD
686PhosphorylationFLAPHFQTTTVGIRY
HHCCCCCCCEEEEEE
24.40-
693PhosphorylationTTTVGIRYNATMDER
CCEEEEEEECCCCCC
13.7625262027
694N-linked_GlycosylationTTVGIRYNATMDERR
CEEEEEEECCCCCCC
21.06UniProtKB CARBOHYD
696PhosphorylationVGIRYNATMDERRYT
EEEEEECCCCCCCCC
22.8625262027
703PhosphorylationTMDERRYTPRAHLDE
CCCCCCCCCCCCCCC
12.4230631047
769PhosphorylationMLDDGWPTTLRVSVP
CCCCCCCCEEEEEEE
31.7720363803
770PhosphorylationLDDGWPTTLRVSVPF
CCCCCCCEEEEEEEE
14.4220363803
857N-linked_GlycosylationNAYSTVLNISQSANL
CHHHHHEEHHHCCCC
27.77UniProtKB CARBOHYD
894N-linked_GlycosylationRLQKQVCNVSYPFFR
HHHHHHHCCCCHHHH
27.24UniProtKB CARBOHYD
953PhosphorylationPLRFHLKYEADVLFT
CCEEEEEEEEEEEEE
23.7824719451
960PhosphorylationYEADVLFTRSSSLSH
EEEEEEEECCCCCCC
26.0224719451
973N-linked_GlycosylationSHYEVKPNSSLERYD
CCCEECCCCCCCCCC
38.21UniProtKB CARBOHYD
1031N-linked_GlycosylationDFLTDEANTSCNIWG
HHHCCCCCCCCCCCC
30.40UniProtKB CARBOHYD
1039N-linked_GlycosylationTSCNIWGNSTEYRPT
CCCCCCCCCCCCCCC
30.66UniProtKB CARBOHYD
1059N-linked_GlycosylationLRRAPQLNHSNSDVV
HHHCCCCCCCCCCCE
31.15UniProtKB CARBOHYD
1098PhosphorylationRSLKALKYKSMKIMV
HHHHHHHHCHHHHHH
14.7818083107
1100PhosphorylationLKALKYKSMKIMVNA
HHHHHHCHHHHHHHH
23.40-
1183PhosphorylationREPGLDPTPKVLE--
CCCCCCCCCCCCC--
35.0930266825

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 ITA11_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITA11_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 ITA11_HUMAN !!

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

Oops, there are no PPI records of ITA11_HUMAN !!

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 ITA11_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-331, AND MASSSPECTROMETRY.

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