MOCOS_HUMAN - dbPTM
MOCOS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MOCOS_HUMAN
UniProt AC Q96EN8
Protein Name Molybdenum cofactor sulfurase {ECO:0000255|HAMAP-Rule:MF_03050}
Gene Name MOCOS {ECO:0000255|HAMAP-Rule:MF_03050}
Organism Homo sapiens (Human).
Sequence Length 888
Subcellular Localization
Protein Description Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form. In vitro, the C-terminal domain is able to reduce N-hydroxylated prodrugs, such as benzamidoxime..
Protein Sequence MAGAAAESGRELWTFAGSRDPSAPRLAYGYGPGSLRELRAREFSRLAGTVYLDHAGATLFSQSQLESFTSDLMENTYGNPHSQNISSKLTHDTVEQVRYRILAHFHTTAEDYTVIFTAGSTAALKLVAEAFPWVSQGPESSGSRFCYLTDSHTSVVGMRNVTMAINVISTPVRPEDLWSAEERSASASNPDCQLPHLFCYPAQSNFSGVRYPLSWIEEVKSGRLHPVSTPGKWFVLLDAASYVSTSPLDLSAHQADFVPISFYKIFGFPTGLGALLVHNRAAPLLRKTYFGGGTASAYLAGEDFYIPRQSVAQRFEDGTISFLDVIALKHGFDTLERLTGGMENIKQHTFTLAQYTYVALSSLQYPNGAPVVRIYSDSEFSSPEVQGPIINFNVLDDKGNIIGYSQVDKMASLYNIHLRTGCFCNTGACQRHLGISNEMVRKHFQAGHVCGDNMDLIDGQPTGSVRISFGYMSTLDDVQAFLRFIIDTRLHSSGDWPVPQAHADTGETGAPSADSQADVIPAVMGRRSLSPQEDALTGSRVWNNSSTVNAVPVAPPVCDVARTQPTPSEKAAGVLEGALGPHVVTNLYLYPIKSCAAFEVTRWPVGNQGLLYDRSWMVVNHNGVCLSQKQEPRLCLIQPFIDLRQRIMVIKAKGMEPIEVPLEENSERTQIRQSRVCADRVSTYDCGEKISSWLSTFFGRPCHLIKQSSNSQRNAKKKHGKDQLPGTMATLSLVNEAQYLLINTSSILELHRQLNTSDENGKEELFSLKDLSLRFRANIIINGKRAFEEEKWDEISIGSLRFQVLGPCHRCQMICIDQQTGQRNQHVFQKLSESRETKVNFGMYLMHASLDLSSPCFLSVGSQVLPVLKENVEGHDLPASEKHQDVTS
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
8PhosphorylationMAGAAAESGRELWTF
CCCCCCCCCCCCCEE		38.1222210691
18PhosphorylationELWTFAGSRDPSAPR
CCCEECCCCCCCCCC		30.0422210691
30PhosphorylationAPRLAYGYGPGSLRE
CCCCCCCCCCCCHHH		13.8922210691
34PhosphorylationAYGYGPGSLRELRAR
CCCCCCCCHHHHHHH		27.6428555341
147PhosphorylationSSGSRFCYLTDSHTS
CCCCCEEEECCCCCC		15.2123663014
149PhosphorylationGSRFCYLTDSHTSVV
CCCEEEECCCCCCEE		14.6923663014
151PhosphorylationRFCYLTDSHTSVVGM
CEEEECCCCCCEECC		24.3523663014
153PhosphorylationCYLTDSHTSVVGMRN
EEECCCCCCEECCEE		27.4523663014
154PhosphorylationYLTDSHTSVVGMRNV
EECCCCCCEECCEEE		14.9123663014
162PhosphorylationVVGMRNVTMAINVIS
EECCEEEEEEEEEEC		12.3930622161
169PhosphorylationTMAINVISTPVRPED
EEEEEEECCCCCHHH		23.5224275569
170PhosphorylationMAINVISTPVRPEDL
EEEEEECCCCCHHHH		18.0624275569
220UbiquitinationLSWIEEVKSGRLHPV
CHHHHHHHHCCCCCC		50.9321906983
264N6-(pyridoxal phosphate)lysineFVPISFYKIFGFPTG
CEEEEHHHHHCCCCC		29.55-
264OtherFVPISFYKIFGFPTG
CEEEEHHHHHCCCCC		29.55-
329UbiquitinationFLDVIALKHGFDTLE
HHHHHHHHCCCCHHH		32.4321906983
442UbiquitinationISNEMVRKHFQAGHV
CCHHHHHHHHHCCCC		37.0421963094
492PhosphorylationIIDTRLHSSGDWPVP
HHHCCCCCCCCCCCC		40.3820873877
493PhosphorylationIDTRLHSSGDWPVPQ
HHCCCCCCCCCCCCC		29.9820873877
505PhosphorylationVPQAHADTGETGAPS
CCCCCCCCCCCCCCC		37.3920873877
508PhosphorylationAHADTGETGAPSADS
CCCCCCCCCCCCCCC		39.7320873877
512PhosphorylationTGETGAPSADSQADV
CCCCCCCCCCCCCCH		44.1420873877
515PhosphorylationTGAPSADSQADVIPA
CCCCCCCCCCCHHHH		27.3020873877
528PhosphorylationPAVMGRRSLSPQEDA
HHHCCCCCCCCCCCC		31.6629255136
530PhosphorylationVMGRRSLSPQEDALT
HCCCCCCCCCCCCCC		26.2829255136
537PhosphorylationSPQEDALTGSRVWNN
CCCCCCCCCCCCCCC		34.5323927012
539PhosphorylationQEDALTGSRVWNNSS
CCCCCCCCCCCCCCC		20.5820873877
546PhosphorylationSRVWNNSSTVNAVPV
CCCCCCCCCCCEEEC		38.2028555341
547PhosphorylationRVWNNSSTVNAVPVA
CCCCCCCCCCEEECC		20.0128555341
570UbiquitinationTQPTPSEKAAGVLEG
CCCCCCHHHHCHHCC		48.1221963094
593UbiquitinationNLYLYPIKSCAAFEV
EEEEEECCCCEEEEE		34.6721963094
593AcetylationNLYLYPIKSCAAFEV
EEEEEECCCCEEEEE		34.6726051181
629MalonylationNGVCLSQKQEPRLCL
CCEECCCCCCCCEEE		53.9326320211
629AcetylationNGVCLSQKQEPRLCL
CCEECCCCCCCCEEE		53.9326051181
629UbiquitinationNGVCLSQKQEPRLCL
CCEECCCCCCCCEEE		53.9321963094
651UbiquitinationRQRIMVIKAKGMEPI
HHHEEEEEECCCCCC		32.4122817900
653UbiquitinationRIMVIKAKGMEPIEV
HEEEEEECCCCCCCC		54.5121906983
666PhosphorylationEVPLEENSERTQIRQ
CCCCCCCCCCHHHHH		31.5622210691
682PhosphorylationRVCADRVSTYDCGEK
HHCCCCCCCCCCHHH		23.3425159151
683PhosphorylationVCADRVSTYDCGEKI
HCCCCCCCCCCHHHH		22.1127251275
706UbiquitinationGRPCHLIKQSSNSQR
CCCHHHHHCCCCHHH		50.9529967540
709PhosphorylationCHLIKQSSNSQRNAK
HHHHHCCCCHHHHHH		37.7024425749
762UbiquitinationNTSDENGKEELFSLK
CCCCCCCCEEEEEHH		60.6429967540
767PhosphorylationNGKEELFSLKDLSLR
CCCEEEEEHHHHHHH		47.3224719451
772PhosphorylationLFSLKDLSLRFRANI
EEEHHHHHHHEEEEE		27.8624719451
799PhosphorylationWDEISIGSLRFQVLG
CCCCEECEEEEEEEC		18.0724719451
830UbiquitinationRNQHVFQKLSESRET
CCHHHHHHHHHCCCC		42.3821963094
882UbiquitinationHDLPASEKHQDVTS-
CCCCCHHHCCCCCC-		44.0329967540
882AcetylationHDLPASEKHQDVTS-
CCCCCHHHCCCCCC-		44.0326051181
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 MOCOS_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MOCOS_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 MOCOS_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PARVA_HUMANPARVAphysical
25416956
SERC_HUMANPSAT1physical
26344197
SEPT8_HUMANSEPT8physical
26344197
PARVA_HUMANPARVAphysical
21516116
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
603592Xanthinuria 2 (XU2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MOCOS_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-528 AND SER-530, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-530, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530, AND MASSSPECTROMETRY.

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