CD109_HUMAN - dbPTM
CD109_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD109_HUMAN
UniProt AC Q6YHK3
Protein Name CD109 antigen
Gene Name CD109
Organism Homo sapiens (Human).
Sequence Length 1445
Subcellular Localization Cell membrane
Lipid-anchor, GPI-anchor .
Protein Description Modulates negatively TGFB1 signaling in keratinocytes..
Protein Sequence MQGPPLLTAAHLLCVCTAALAVAPGPRFLVTAPGIIRPGGNVTIGVELLEHCPSQVTVKAELLKTASNLTVSVLEAEGVFEKGSFKTLTLPSLPLNSADEIYELRVTGRTQDEILFSNSTRLSFETKRISVFIQTDKALYKPKQEVKFRIVTLFSDFKPYKTSLNILIKDPKSNLIQQWLSQQSDLGVISKTFQLSSHPILGDWSIQVQVNDQTYYQSFQVSEYVLPKFEVTLQTPLYCSMNSKHLNGTITAKYTYGKPVKGDVTLTFLPLSFWGKKKNITKTFKINGSANFSFNDEEMKNVMDSSNGLSEYLDLSSPGPVEILTTVTESVTGISRNVSTNVFFKQHDYIIEFFDYTTVLKPSLNFTATVKVTRADGNQLTLEERRNNVVITVTQRNYTEYWSGSNSGNQKMEAVQKINYTVPQSGTFKIEFPILEDSSELQLKAYFLGSKSSMAVHSLFKSPSKTYIQLKTRDENIKVGSPFELVVSGNKRLKELSYMVVSRGQLVAVGKQNSTMFSLTPENSWTPKACVIVYYIEDDGEIISDVLKIPVQLVFKNKIKLYWSKVKAEPSEKVSLRISVTQPDSIVGIVAVDKSVNLMNASNDITMENVVHELELYNTGYYLGMFMNSFAVFQECGLWVLTDANLTKDYIDGVYDNAEYAERFMEENEGHIVDIHDFSLGSSPHVRKHFPETWIWLDTNMGYRIYQEFEVTVPDSITSWVATGFVISEDLGLGLTTTPVELQAFQPFFIFLNLPYSVIRGEEFALEITIFNYLKDATEVKVIIEKSDKFDILMTSNEINATGHQQTLLVPSEDGATVLFPIRPTHLGEIPITVTALSPTASDAVTQMILVKAEGIEKSYSQSILLDLTDNRLQSTLKTLSFSFPPNTVTGSERVQITAIGDVLGPSINGLASLIRMPYGCGEQNMINFAPNIYILDYLTKKKQLTDNLKEKALSFMRQGYQRELLYQREDGSFSAFGNYDPSGSTWLSAFVLRCFLEADPYIDIDQNVLHRTYTWLKGHQKSNGEFWDPGRVIHSELQGGNKSPVTLTAYIVTSLLGYRKYQPNIDVQESIHFLESEFSRGISDNYTLALITYALSSVGSPKAKEALNMLTWRAEQEGGMQFWVSSESKLSDSWQPRSLDIEVAAYALLSHFLQFQTSEGIPIMRWLSRQRNSLGGFASTQDTTVALKALSEFAALMNTERTNIQVTVTGPSSPSPVKFLIDTHNRLLLQTAELAVVQPTAVNISANGFGFAICQLNVVYNVKASGSSRRRRSIQNQEAFDLDVAVKENKDDLNHVDLNVCTSFSGPGRSGMALMEVNLLSGFMVPSEAISLSETVKKVEYDHGKLNLYLDSVNETQFCVNIPAVRNFKVSNTQDASVSIVDYYEPRRQAVRSYNSEVKLSSCDLCSDVQGCRPCEDGASGSHHHSSVIFIFCFKLLYFMELWL
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
31PhosphorylationPGPRFLVTAPGIIRP
CCCCEEEECCEEEEC		29.31-
68N-linked_GlycosylationELLKTASNLTVSVLE
HHHHHHCCCEEEEEE		36.9516335952
68N-linked_GlycosylationELLKTASNLTVSVLE
HHHHHHCCCEEEEEE		36.9516335952
102PhosphorylationLNSADEIYELRVTGR
CCCCCEEEEEEECCC		13.58-
118N-linked_GlycosylationQDEILFSNSTRLSFE
CCEEEECCCCEEEEE		39.8116335952
118N-linked_GlycosylationQDEILFSNSTRLSFE
CCEEEECCCCEEEEE		39.8116335952
143UbiquitinationDKALYKPKQEVKFRI
CHHHCCCCCEEEEEE		55.7429967540
155PhosphorylationFRIVTLFSDFKPYKT
EEEEEECCCCCCCCE		45.2925690035
160PhosphorylationLFSDFKPYKTSLNIL
ECCCCCCCCEEEEEE		27.7329978859
162PhosphorylationSDFKPYKTSLNILIK
CCCCCCCEEEEEEEC		32.3829978859
163PhosphorylationDFKPYKTSLNILIKD
CCCCCCEEEEEEECC		18.4429978859
169UbiquitinationTSLNILIKDPKSNLI
EEEEEEECCCCCCHH		65.6129967540
247N-linked_GlycosylationSMNSKHLNGTITAKY
ECCCCCCCCEEEEEE		45.3316263699
247N-linked_GlycosylationSMNSKHLNGTITAKY
ECCCCCCCCEEEEEE		45.3316335952
279N-linked_GlycosylationSFWGKKKNITKTFKI
EECCCCCCEEEEEEE		56.92UniProtKB CARBOHYD
283PhosphorylationKKKNITKTFKINGSA
CCCCEEEEEEECCEE		22.8528302921
289PhosphorylationKTFKINGSANFSFND
EEEEECCEEECCCCH		18.6228302921
293PhosphorylationINGSANFSFNDEEMK
ECCEEECCCCHHHHH		23.9728302921
305PhosphorylationEMKNVMDSSNGLSEY
HHHHHHHCCCCHHHH		13.9624043423
306PhosphorylationMKNVMDSSNGLSEYL
HHHHHHCCCCHHHHC		30.5624043423
310PhosphorylationMDSSNGLSEYLDLSS
HHCCCCHHHHCCCCC		26.1224043423
312PhosphorylationSSNGLSEYLDLSSPG
CCCCHHHHCCCCCCC		11.3524043423
316PhosphorylationLSEYLDLSSPGPVEI
HHHHCCCCCCCCEEE		33.8724043423
317PhosphorylationSEYLDLSSPGPVEIL
HHHCCCCCCCCEEEE		40.9724043423
325PhosphorylationPGPVEILTTVTESVT
CCCEEEEEEEEEHHH		25.5324043423
326PhosphorylationGPVEILTTVTESVTG
CCEEEEEEEEEHHHC		23.2224043423
328PhosphorylationVEILTTVTESVTGIS
EEEEEEEEEHHHCCC		22.0524043423
330PhosphorylationILTTVTESVTGISRN
EEEEEEEHHHCCCCC		18.6624043423
332PhosphorylationTTVTESVTGISRNVS
EEEEEHHHCCCCCCC		37.7724043423
335PhosphorylationTESVTGISRNVSTNV
EEHHHCCCCCCCCCE		21.1024043423
340UbiquitinationGISRNVSTNVFFKQH
CCCCCCCCCEEECCC		30.9929967540
365N-linked_GlycosylationTVLKPSLNFTATVKV
EEECCCCCEEEEEEE		36.24UniProtKB CARBOHYD
388UbiquitinationTLEERRNNVVITVTQ
EEHHHHCCEEEEEEE		27.8529967540
401UbiquitinationTQRNYTEYWSGSNSG
EECCCEEEECCCCCC		9.3229967540
414UbiquitinationSGNQKMEAVQKINYT
CCCHHHHEEEEEEEE		12.9229967540
417UbiquitinationQKMEAVQKINYTVPQ
HHHHEEEEEEEECCC		26.7329967540
419N-linked_GlycosylationMEAVQKINYTVPQSG
HHEEEEEEEECCCCC		33.2016335952
419N-linked_GlycosylationMEAVQKINYTVPQSG
HHEEEEEEEECCCCC		33.2019159218
446PhosphorylationSELQLKAYFLGSKSS
CCHHHHHHHHCCCHH		9.57-
450PhosphorylationLKAYFLGSKSSMAVH
HHHHHHCCCHHHHHH		31.35-
458PhosphorylationKSSMAVHSLFKSPSK
CHHHHHHHHHCCCCC		28.9824719451
465UbiquitinationSLFKSPSKTYIQLKT
HHHCCCCCEEEEEEE		49.0529967540
466PhosphorylationLFKSPSKTYIQLKTR
HHCCCCCEEEEEEEC		30.1420068231
467PhosphorylationFKSPSKTYIQLKTRD
HCCCCCEEEEEEECC		7.1520068231
478UbiquitinationKTRDENIKVGSPFEL
EECCCCCCCCCCEEE		52.7229967540
479UbiquitinationTRDENIKVGSPFELV
ECCCCCCCCCCEEEE		8.9833845483
491AcetylationELVVSGNKRLKELSY
EEEEECCHHHHEEEE		63.7330587545
491UbiquitinationELVVSGNKRLKELSY
EEEEECCHHHHEEEE		63.7329967540
497PhosphorylationNKRLKELSYMVVSRG
CHHHHEEEEEEEECC		16.5723403867
513N-linked_GlycosylationLVAVGKQNSTMFSLT
EEEECCCCCCCEECC		42.82UniProtKB CARBOHYD
556UbiquitinationIPVQLVFKNKIKLYW
CCHHEEECCCEEEEE		50.2633845483
579PhosphorylationEKVSLRISVTQPDSI
CCEEEEEEECCCCCE		16.8120068231
581PhosphorylationVSLRISVTQPDSIVG
EEEEEEECCCCCEEE		27.8220068231
585PhosphorylationISVTQPDSIVGIVAV
EEECCCCCEEEEEEE		26.3420068231
645N-linked_GlycosylationLWVLTDANLTKDYID
EEEEECCCCCHHHCC		51.56UniProtKB CARBOHYD
650 (in isoform 3)Phosphorylation-11.5026437602
650PhosphorylationDANLTKDYIDGVYDN
CCCCCHHHCCCCCCC		11.5030266825
655PhosphorylationKDYIDGVYDNAEYAE
HHHCCCCCCCHHHHH		14.7130266825
660PhosphorylationGVYDNAEYAERFMEE
CCCCCHHHHHHHHHH		16.0230266825
661 (in isoform 3)Phosphorylation-7.9326437602
716PhosphorylationFEVTVPDSITSWVAT
EEEECCHHHHHHEEE		22.9926074081
718PhosphorylationVTVPDSITSWVATGF
EECCHHHHHHEEECE		22.0826074081
719PhosphorylationTVPDSITSWVATGFV
ECCHHHHHHEEECEE		20.2026074081
723PhosphorylationSITSWVATGFVISED
HHHHHEEECEEEECC		22.8726074081
728PhosphorylationVATGFVISEDLGLGL
EEECEEEECCCCCCC		21.5426074081
736PhosphorylationEDLGLGLTTTPVELQ
CCCCCCCCCCCCHHH		27.1626074081
737PhosphorylationDLGLGLTTTPVELQA
CCCCCCCCCCCHHHH		33.8626074081
738PhosphorylationLGLGLTTTPVELQAF
CCCCCCCCCCHHHHC		21.8026074081
778PhosphorylationFNYLKDATEVKVIIE
EEHHCCCCEEEEEEE		51.9829083192
781UbiquitinationLKDATEVKVIIEKSD
HCCCCEEEEEEECCC		22.8329967540
833PhosphorylationHLGEIPITVTALSPT
CCCCCCEEEEEECCC		13.3719664995
840PhosphorylationTVTALSPTASDAVTQ
EEEEECCCCCHHHHH		35.1019664995
858UbiquitinationVKAEGIEKSYSQSIL
EEECCCCCCCCCEEE		53.4229967540
873UbiquitinationLDLTDNRLQSTLKTL
ECCCCHHHHHHHHHE		6.2229967540
945UbiquitinationYLTKKKQLTDNLKEK
HHHCCHHCCHHHHHH		9.9829967540
946PhosphorylationLTKKKQLTDNLKEKA
HHCCHHCCHHHHHHH		21.9822817900
950UbiquitinationKQLTDNLKEKALSFM
HHCCHHHHHHHHHHH		64.5229967540
1022UbiquitinationTWLKGHQKSNGEFWD
HHHCCCCCCCCCCCC		39.9729967540
1036PhosphorylationDPGRVIHSELQGGNK
CCCCEEECCCCCCCC		28.95-
1086N-linked_GlycosylationFSRGISDNYTLALIT
HHCCCCCHHHHHHHH		25.5416263699
1126PhosphorylationGGMQFWVSSESKLSD
CCEEEEECCCCCCCC		20.9829116813
1127PhosphorylationGMQFWVSSESKLSDS
CEEEEECCCCCCCCC		35.9529116813
1180PhosphorylationNSLGGFASTQDTTVA
CCCCCCCCCCHHHHH		25.0824719451
1214PhosphorylationVTVTGPSSPSPVKFL
EEEECCCCCCCCEEE		32.31-
1216PhosphorylationVTGPSSPSPVKFLID
EECCCCCCCCEEEEE		44.25-
1355N-linked_GlycosylationNLYLDSVNETQFCVN
EEEEECCCCCEEEEE		51.02UniProtKB CARBOHYD
1384PhosphorylationASVSIVDYYEPRRQA
CEEEEEECCHHHHHH		9.99-
1420GPI-anchorCRPCEDGASGSHHHS
CEECCCCCCCCCCCH		24.04-
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 CD109_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD109_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 CD109_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CD109_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 CD109_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-68 AND ASN-118, 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-419, 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-247, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-68; ASN-118; ASN-247 ANDASN-419, AND MASS SPECTROMETRY.

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