SH3R3_HUMAN - dbPTM
SH3R3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SH3R3_HUMAN
UniProt AC Q8TEJ3
Protein Name SH3 domain-containing RING finger protein 3
Gene Name SH3RF3
Organism Homo sapiens (Human).
Sequence Length 882
Subcellular Localization
Protein Description
Protein Sequence MLLGASWLCASKAAAAAAQSEGDEDRPGERRRRRAAATAAGAGEDMDESSLLDLLECSVCLERLDTTAKVLPCQHTFCRRCLESIVCSRHELRCPECRILVGCGVDELPANILLVRLLDGIRQRPRAGTSPGGSPPARPIPGQSAAPTLAGGGGGAAGSTPGSPVFLSAAAGSTAGSLRELATSRTAPAAKNPCLLPYGKALYSYEGKEPGDLKFNKGDIIVLRRKVDEQWYHGELHGTQGFLPASYIQCIQPLPHAPPQGKALYDFEMKDKDQDKDCLTFTKDEILTVLRRVDENWAEGMLGDKIGIFPLLYVELNDSAKQLIEMDKPCPAAASSCNASLPSDSGAVASVAPSPTLSSSGAVSAFQRRVDGKKNTKKRHSFTALSVTHRSSQAASHRHSMEISAPVLISSSDPRAAARIGDLAHLSCAAPTQDVSSSAGSTPTAVPRAASVSGEQGTPPKVQLPLNVYLALYAYKPQKSDELELHKGEMYRVLEKCQDGWFKGASLRTGVSGVFPGNYVTPVSRVPAGGAGPPRNNVVGGSPLAKGITTTMHPGSGSLSSLATATRPALPITTPQAHAQHPTASPPTGSCLRHSAQPTASQARSTISTAAHSAAQAQDRPTATVSPLRTQNSPSRLPATSLRPHSVVSPQHSHQPPVQMCPRPAIPLTSAASAITPPNVSAANLNGEAGGGPIGVLSTSSPTNTGCKLDEKKSEKKEKKSGLLKLLAGASTKKKSRSPPSVSPTHDPQVAVDALLQGAVGPEVSSLSIHGRAGSCPIESEMQGAMGMEPLHRKAGSLDLNFTSPSRQAPLSMAAIRPEPKLLPRERYRVVVSYPPQSEAEIELKEGDIVFVHKKREDGWYKGTLQRNGRTGLFPGSFVESF
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
50PhosphorylationGEDMDESSLLDLLEC
CCCCCHHHHHHHHHH		30.7929759185
66PhosphorylationVCLERLDTTAKVLPC
HHHHHHCCCCCEECC		32.99-
67PhosphorylationCLERLDTTAKVLPCQ
HHHHHCCCCCEECCC		24.93-
163PhosphorylationAAGSTPGSPVFLSAA
CCCCCCCCCCEEECC		21.06-
203PhosphorylationLPYGKALYSYEGKEP
ECCCEEECEECCCCC		17.6729496907
204PhosphorylationPYGKALYSYEGKEPG
CCCEEECEECCCCCC		19.9829496907
381PhosphorylationKNTKKRHSFTALSVT
CCCCCCCEEEEEEEE		28.4630576142
383PhosphorylationTKKRHSFTALSVTHR
CCCCCEEEEEEEEEC		29.6923927012
386PhosphorylationRHSFTALSVTHRSSQ
CCEEEEEEEEECCCH		23.6223927012
388PhosphorylationSFTALSVTHRSSQAA
EEEEEEEEECCCHHH		14.2722210691
391PhosphorylationALSVTHRSSQAASHR
EEEEEECCCHHHHCC		21.1423927012
392PhosphorylationLSVTHRSSQAASHRH
EEEEECCCHHHHCCC		24.6430576142
396PhosphorylationHRSSQAASHRHSMEI
ECCCHHHHCCCCEEE		24.8623927012
400PhosphorylationQAASHRHSMEISAPV
HHHHCCCCEEEECCE		20.3323927012
404PhosphorylationHRHSMEISAPVLISS
CCCCEEEECCEEECC		17.1423927012
412PhosphorylationAPVLISSSDPRAAAR
CCEEECCCCHHHHHH		44.86-
437PhosphorylationAPTQDVSSSAGSTPT
CCCCCCCCCCCCCCC		24.85-
438PhosphorylationPTQDVSSSAGSTPTA
CCCCCCCCCCCCCCC		29.19-
442PhosphorylationVSSSAGSTPTAVPRA
CCCCCCCCCCCCCCC		24.60-
451PhosphorylationTAVPRAASVSGEQGT
CCCCCCCCCCCCCCC		18.8129396449
458PhosphorylationSVSGEQGTPPKVQLP
CCCCCCCCCCCCCCC		35.7925159151
469PhosphorylationVQLPLNVYLALYAYK
CCCCHHHEEEHHEEC		5.79-
473PhosphorylationLNVYLALYAYKPQKS
HHHEEEHHEECCCCC		11.41-
529UbiquitinationPVSRVPAGGAGPPRN
CCCCCCCCCCCCCCC		22.0327667366
542PhosphorylationRNNVVGGSPLAKGIT
CCCCCCCCCCCCCCC		15.7118669648
549PhosphorylationSPLAKGITTTMHPGS
CCCCCCCCCEECCCC		25.5324719451
558PhosphorylationTMHPGSGSLSSLATA
EECCCCCCHHHHHHC		27.1227251275
560PhosphorylationHPGSGSLSSLATATR
CCCCCCHHHHHHCCC		25.6327251275
561PhosphorylationPGSGSLSSLATATRP
CCCCCHHHHHHCCCC		27.5827251275
564PhosphorylationGSLSSLATATRPALP
CCHHHHHHCCCCCCC		33.5827251275
566PhosphorylationLSSLATATRPALPIT
HHHHHHCCCCCCCCC		32.6024719451
573PhosphorylationTRPALPITTPQAHAQ
CCCCCCCCCCCHHCC		30.40-
613PhosphorylationTISTAAHSAAQAQDR
HHHHHHHHHHHHCCC		22.1529449344
622PhosphorylationAQAQDRPTATVSPLR
HHHCCCCCCEECCCC		35.5429449344
624PhosphorylationAQDRPTATVSPLRTQ
HCCCCCCEECCCCCC		24.8029449344
626PhosphorylationDRPTATVSPLRTQNS
CCCCCEECCCCCCCC		17.5424719451
731PhosphorylationLKLLAGASTKKKSRS
HHHHHCCCCCCCCCC		39.5818510355
732PhosphorylationKLLAGASTKKKSRSP
HHHHCCCCCCCCCCC		46.4818510355
736PhosphorylationGASTKKKSRSPPSVS
CCCCCCCCCCCCCCC		47.0418510355
738PhosphorylationSTKKKSRSPPSVSPT
CCCCCCCCCCCCCCC		48.5325627689
741PhosphorylationKKSRSPPSVSPTHDP
CCCCCCCCCCCCCCH		38.3125627689
743PhosphorylationSRSPPSVSPTHDPQV
CCCCCCCCCCCCHHH		28.5525627689
745PhosphorylationSPPSVSPTHDPQVAV
CCCCCCCCCCHHHHH		31.2525627689
775PhosphorylationSIHGRAGSCPIESEM
EEECCCCCCCCCHHH		18.7429978859
780PhosphorylationAGSCPIESEMQGAMG
CCCCCCCHHHCCCCC		38.8027732954
797PhosphorylationPLHRKAGSLDLNFTS
CCHHHCCCCCCCCCC		24.4623927012
803PhosphorylationGSLDLNFTSPSRQAP
CCCCCCCCCCCCCCC		38.3623403867
804PhosphorylationSLDLNFTSPSRQAPL
CCCCCCCCCCCCCCC		19.4221815630
806PhosphorylationDLNFTSPSRQAPLSM
CCCCCCCCCCCCCCH		36.4723403867
854UbiquitinationGDIVFVHKKREDGWY
CCEEEEEEECCCCCE		48.5027667366
881PhosphorylationFPGSFVESF------
CCCCHHCCC------		30.8427251275
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 SH3R3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SH3R3_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 SH3R3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAC1_HUMANRAC1physical
20696164
CDC42_HUMANCDC42physical
20696164
KCTD3_HUMANKCTD3physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
CING_HUMANCGNphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
LPIN3_HUMANLPIN3physical
27173435
LRFN1_HUMANLRFN1physical
27173435
RTKN_HUMANRTKNphysical
27173435
DEN4C_HUMANDENND4Cphysical
27173435
MAST3_HUMANMAST3physical
27173435
DEN1A_HUMANDENND1Aphysical
27173435
SPD2A_HUMANSH3PXD2Aphysical
27173435
SRGP2_HUMANSRGAP2physical
27173435
PPM1H_HUMANPPM1Hphysical
27173435
TANC2_HUMANTANC2physical
27173435
PTN13_HUMANPTPN13physical
27173435
RGPS2_HUMANRALGPS2physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
NF1_HUMANNF1physical
27173435
MPIP3_HUMANCDC25Cphysical
27173435
CBY1_HUMANCBY1physical
27173435
GGYF2_HUMANGIGYF2physical
27173435
LIMA1_HUMANLIMA1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
HDAC4_HUMANHDAC4physical
27173435
TESK2_HUMANTESK2physical
27173435
DCLK1_HUMANDCLK1physical
27173435
SIN1_HUMANMAPKAP1physical
27173435
INP5E_HUMANINPP5Ephysical
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
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SH3R3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-542 AND SER-797, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400 AND SER-797, ANDMASS SPECTROMETRY.

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