MOC2B_HUMAN - dbPTM
MOC2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MOC2B_HUMAN
UniProt AC O96007
Protein Name Molybdopterin synthase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_03052}
Gene Name MOCS2 {ECO:0000255|HAMAP-Rule:MF_03052}
Organism Homo sapiens (Human).
Sequence Length 188
Subcellular Localization Cytoplasm, cytosol .
Protein Description Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group..
Protein Sequence MSSLEISSSCFSLETKLPLSPPLVEDSAFEPSRKDMDEVEEKSKDVINFTAEKLSVDEVSQLVISPLCGAISLFVGTTRNNFEGKKVISLEYEAYLPMAENEVRKICSDIRQKWPVKHIAVFHRLGLVPVSEASIIIAVSSAHRAASLEAVSYAIDTLKAKVPIWKKEIYEESSTWKGNKECFWASNS
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
2Phosphorylation------MSSLEISSS
------CCCCEECCC
43.5625159151
3Phosphorylation-----MSSLEISSSC
-----CCCCEECCCC
28.8225159151
7Phosphorylation-MSSLEISSSCFSLE
-CCCCEECCCCEECE
13.5628122231
8PhosphorylationMSSLEISSSCFSLET
CCCCEECCCCEECEE
36.4728122231
9PhosphorylationSSLEISSSCFSLETK
CCCEECCCCEECEEC
16.6428122231
12PhosphorylationEISSSCFSLETKLPL
EECCCCEECEECCCC
29.6228122231
15PhosphorylationSSCFSLETKLPLSPP
CCCEECEECCCCCCC
43.0826074081
20PhosphorylationLETKLPLSPPLVEDS
CEECCCCCCCCCCCC
23.6429255136
27PhosphorylationSPPLVEDSAFEPSRK
CCCCCCCCCCCCCCC
22.7329632367
32PhosphorylationEDSAFEPSRKDMDEV
CCCCCCCCCCCHHHH
44.7723927012
89PhosphorylationFEGKKVISLEYEAYL
CCCCEEEEEEEEECC
20.3825072903
92PhosphorylationKKVISLEYEAYLPMA
CEEEEEEEEECCHHC
15.9125072903
95PhosphorylationISLEYEAYLPMAENE
EEEEEEECCHHCHHH
10.2125072903
153PhosphorylationASLEAVSYAIDTLKA
HHHHHHHHHHHHHHH
10.8520068231
157PhosphorylationAVSYAIDTLKAKVPI
HHHHHHHHHHHCCCE
24.8520068231
170PhosphorylationPIWKKEIYEESSTWK
CEECHHHHCCCCCCC
18.09-
180UbiquitinationSSTWKGNKECFWASN
CCCCCCCCCCEEECC
65.61-
188PhosphorylationECFWASNS-------
CCEEECCC-------
38.8225159151

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 MOC2B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MOC2B_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 MOC2B_HUMAN !!

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

Oops, there are no PPI records of MOC2B_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
252160Molybdenum cofactor deficiency, complementation group B (MOCODB)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MOC2B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASSSPECTROMETRY.
"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-20, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASSSPECTROMETRY.
"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-20, AND MASSSPECTROMETRY.

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