MOCS1_HUMAN - dbPTM
MOCS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MOCS1_HUMAN
UniProt AC Q9NZB8
Protein Name Molybdenum cofactor biosynthesis protein 1
Gene Name MOCS1
Organism Homo sapiens (Human).
Sequence Length 636
Subcellular Localization
Protein Description Isoform MOCS1A and isoform MOCS1B probably form a complex that catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP). MOCS1A catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate and MOCS1B catalyzes the subsequent conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cPMP..
Protein Sequence MAARPLSRMLRRLLRSSARSCSSGAPVTQPCPGESARAASEEVSRRRQFLREHAAPFSAFLTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNPVKVNCVVMRGLNEDELLDFAALTEGLPLDVRFIEYMPFDGNKWNFKKMVSYKEMLDTVRQQWPELEKVPEEESSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAGMFSISQMKNRPMILIELFLMFPNSPPANPSIFSWDPLHVQGLRPRMSFSSQVATLWKGCRVPQTPPLAQQRLGSGSFQRHYTSRADSDANSKCLSPGSWASAAPSGPQLTSEQLTHVDSEGRAAMVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALSHIQVQLELDSTRHAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQRGDFHRA
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
20PhosphorylationLLRSSARSCSSGAPV
HHHHHCHHCCCCCCC		20.3322468782
23PhosphorylationSSARSCSSGAPVTQP
HHCHHCCCCCCCCCC		43.2122468782
28PhosphorylationCSSGAPVTQPCPGES
CCCCCCCCCCCCCHH		26.2422468782
58PhosphorylationREHAAPFSAFLTDSF
HHHHCCHHHHHCCCC		19.6323186163
62PhosphorylationAPFSAFLTDSFGRQH
CCHHHHHCCCCCCCC		24.1223186163
64PhosphorylationFSAFLTDSFGRQHSY
HHHHHCCCCCCCCCE		25.1028857561
109PhosphorylationLTTEEILTLARLFVK
CCHHHHHHHHHHHHH		24.8424719451
150PhosphorylationQRLEGLRTIGVTTNG
HHHHCCCCEEECCCC		27.4222210691
155PhosphorylationLRTIGVTTNGINLAR
CCCEEECCCCHHHHH		29.10-
198AcetylationVRRKGFHKVMEGIHK
HHCCCHHHHHHHHHH		40.8019608861
263PhosphorylationWNFKKMVSYKEMLDT
CCHHHCCCHHHHHHH		27.3030631047
270PhosphorylationSYKEMLDTVRQQWPE
CHHHHHHHHHHHCHH		17.3930631047
334PhosphorylationKVCLFGNSEVSLRDH
EEEEECCCEEEHHHH		39.49-
342 (in isoform 3)Phosphorylation-4.74-
344 (in isoform 3)Phosphorylation-25.02-
371PhosphorylationRQHAGMFSISQMKNR
HCCCCCCCHHHHCCC		16.67-
373PhosphorylationHAGMFSISQMKNRPM
CCCCCCHHHHCCCCE		24.03-
415PhosphorylationQGLRPRMSFSSQVAT
CCCCCCCCCHHHHHH		24.2123403867
417PhosphorylationLRPRMSFSSQVATLW
CCCCCCCHHHHHHHH		16.7423403867
418PhosphorylationRPRMSFSSQVATLWK
CCCCCCHHHHHHHHC		27.0223403867
422PhosphorylationSFSSQVATLWKGCRV
CCHHHHHHHHCCCCC		34.0023403867
442PhosphorylationLAQQRLGSGSFQRHY
HHHHHHCCCCCHHHC		35.5429978859
444PhosphorylationQQRLGSGSFQRHYTS
HHHHCCCCCHHHCCC		21.6529978859
449PhosphorylationSGSFQRHYTSRADSD
CCCCHHHCCCCCCCC		14.4829978859
450PhosphorylationGSFQRHYTSRADSDA
CCCHHHCCCCCCCCC		12.9529978859
451PhosphorylationSFQRHYTSRADSDAN
CCHHHCCCCCCCCCC		20.5029978859
455PhosphorylationHYTSRADSDANSKCL
HCCCCCCCCCCCCCC		37.3229978859
459PhosphorylationRADSDANSKCLSPGS
CCCCCCCCCCCCCCC		26.8529978859
528AcetylationLVQQNQLKKGDALVV
HHHHCCCCCCCEEEH		44.9725953088
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 MOCS1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MOCS1_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 MOCS1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PIN1_HUMANPIN1physical
21988832
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
252150Molybdenum cofactor deficiency, complementation group A (MOCODA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MOCS1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-198, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory