METE_SCHPO - dbPTM
METE_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID METE_SCHPO
UniProt AC Q9UT19
Protein Name Probable 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Gene Name met26
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 764
Subcellular Localization Nucleus . Cytoplasm .
Protein Description Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation..
Protein Sequence MVKSAVLGFPRIGKNRELKKATEAYWSGKTSAEELLATAKQLRLEHWKLQKAQGVDIIPSNDFSLYDQIMDHSFSFNVIPPRYRLSGLSSLDTYFAMGRGMQRAATADKAAVDVPAGEMVKWFDSNYHFLRPEVSEETDFKLSSTKALDEFLEAKEAGIITRPVLVGPVTYLFIAKAAKGSSIKPIELLPKLLPVYVELIKKLTEAGAEYIQIDEPILTLDLPQEILASYKEAYETLGKIGKLILTTYFGSLQSNADVLKGLPIAGVHVDVVRAPENLDRALAVLGENQIISVGVVSGRNIWKTDFQKATAIIEKAISAVGSERVQVASSSSILHIPHSLSGEDQINPEIKRWFAFAVEKCAELAILTKAANDGPASVRAELEANAADCKARAESPITNVEAVRERQSKVTPQMHERKSPFETRYAKQQASLKLPLFPTTTIGSFPQTKEIRVTRNRFAKGLISQEEYDAFIRKEISDVVKFQEEVGLDVLVHGEPERNDMVQYFGERMEGFVFTVNGWVQSYGSRCVRPPIIVGDVYRPAPMTVKESQYAQSITSKPMKGMLTAPITILRWSFPRDDVHDSVQAQQIALGLRDEVLDLEKAGIKVIQCDEPALREGLPLRRAEWDEYLKWAIDAFRLATAAVQDDTQIHSHFCYSDFNDIFDAIQRLDADVVSIENSKSDMKLLNVLSRYTSCIGPGLFDIHSPRVPPVSEFKERIDAIVKHVPKDHLWLNPDCGLKTRGWPETTADLKNMIAAAREAREQYA
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
4Phosphorylation----MVKSAVLGFPR
----CCCCHHHCCCC
16.5224763107
30PhosphorylationEAYWSGKTSAEELLA
HHHHCCCCCHHHHHH
36.3725720772
31PhosphorylationAYWSGKTSAEELLAT
HHHCCCCCHHHHHHH
36.8525720772
83PhosphorylationFNVIPPRYRLSGLSS
CCCCCCCCCCCCCCH
22.9825720772
86PhosphorylationIPPRYRLSGLSSLDT
CCCCCCCCCCCHHHH
28.7925720772
89PhosphorylationRYRLSGLSSLDTYFA
CCCCCCCCHHHHHHH
32.1725720772
90PhosphorylationYRLSGLSSLDTYFAM
CCCCCCCHHHHHHHH
34.9925720772
181PhosphorylationIAKAAKGSSIKPIEL
EHHHCCCCCCCCHHH
28.3424763107
182PhosphorylationAKAAKGSSIKPIELL
HHHCCCCCCCCHHHH
43.2128889911
395PhosphorylationDCKARAESPITNVEA
HHHHHCCCCCCCHHH
22.1828889911
419PhosphorylationPQMHERKSPFETRYA
CCHHCCCCHHHHHHH
40.8324763107
423PhosphorylationERKSPFETRYAKQQA
CCCCHHHHHHHHHHH
29.3821712547
439PhosphorylationLKLPLFPTTTIGSFP
CCCCCCCCCCCCCCC
29.2729996109
440PhosphorylationKLPLFPTTTIGSFPQ
CCCCCCCCCCCCCCC
19.3625720772
441PhosphorylationLPLFPTTTIGSFPQT
CCCCCCCCCCCCCCC
26.3128889911
444PhosphorylationFPTTTIGSFPQTKEI
CCCCCCCCCCCCCEE
29.8729996109
464PhosphorylationRFAKGLISQEEYDAF
HHHHHCCCHHHHHHH
36.2625720772
689PhosphorylationMKLLNVLSRYTSCIG
HHHHHHHHHHHCCCC
20.9625720772
693PhosphorylationNVLSRYTSCIGPGLF
HHHHHHHCCCCCCCC
8.5325720772
704PhosphorylationPGLFDIHSPRVPPVS
CCCCCCCCCCCCCHH
18.0928889911

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 METE_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of METE_SCHPO !!

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 METE_SCHPO !!

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

Oops, there are no PPI records of METE_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of METE_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND THR-441, ANDMASS SPECTROMETRY.

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