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 | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSSLEISSS ------CCCCEECCC | 43.56 | 25159151 | |
3 | Phosphorylation | -----MSSLEISSSC -----CCCCEECCCC | 28.82 | 25159151 | |
7 | Phosphorylation | -MSSLEISSSCFSLE -CCCCEECCCCEECE | 13.56 | 28122231 | |
8 | Phosphorylation | MSSLEISSSCFSLET CCCCEECCCCEECEE | 36.47 | 28122231 | |
9 | Phosphorylation | SSLEISSSCFSLETK CCCEECCCCEECEEC | 16.64 | 28122231 | |
12 | Phosphorylation | EISSSCFSLETKLPL EECCCCEECEECCCC | 29.62 | 28122231 | |
15 | Phosphorylation | SSCFSLETKLPLSPP CCCEECEECCCCCCC | 43.08 | 26074081 | |
20 | Phosphorylation | LETKLPLSPPLVEDS CEECCCCCCCCCCCC | 23.64 | 29255136 | |
27 | Phosphorylation | SPPLVEDSAFEPSRK CCCCCCCCCCCCCCC | 22.73 | 29632367 | |
32 | Phosphorylation | EDSAFEPSRKDMDEV CCCCCCCCCCCHHHH | 44.77 | 23927012 | |
89 | Phosphorylation | FEGKKVISLEYEAYL CCCCEEEEEEEEECC | 20.38 | 25072903 | |
92 | Phosphorylation | KKVISLEYEAYLPMA CEEEEEEEEECCHHC | 15.91 | 25072903 | |
95 | Phosphorylation | ISLEYEAYLPMAENE EEEEEEECCHHCHHH | 10.21 | 25072903 | |
153 | Phosphorylation | ASLEAVSYAIDTLKA HHHHHHHHHHHHHHH | 10.85 | 20068231 | |
157 | Phosphorylation | AVSYAIDTLKAKVPI HHHHHHHHHHHCCCE | 24.85 | 20068231 | |
170 | Phosphorylation | PIWKKEIYEESSTWK CEECHHHHCCCCCCC | 18.09 | - | |
180 | Ubiquitination | SSTWKGNKECFWASN CCCCCCCCCCEEECC | 65.61 | - | |
188 | Phosphorylation | ECFWASNS------- CCEEECCC------- | 38.82 | 25159151 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MOC2B_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of MOC2B_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
252160 | Molybdenum 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. |
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Phosphorylation | |
Reference | PubMed |
"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. |