CNT6_SCHPO - dbPTM
CNT6_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNT6_SCHPO
UniProt AC Q10165
Protein Name Probable ribosylation factor GTPase-activating protein cnt6
Gene Name cnt6
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 923
Subcellular Localization Cytoplasm . Cell tip . Cell septum .
Protein Description GTPase-activating protein for the ADP ribosylation factor family..
Protein Sequence MDGSDSLLKSVDVSKLDNGSTISFRAREDGFLESISSSSGKLVDMVLDSTSKECLPKFSFQNKLDFYFLFSDRVLQLQKERKVLVLIHCESLQSFDSFFAQKLKYADLISSDNVHEIFLPDSNAANIRYHWEWSPPSGKLLEYECKNYSCIAVYSTEDCTLERISKFSYYTVSRCGDSMDDTFFSESQRVTSPLTTSQTVQTQPPQSPEAKTELSLINTKTVIFPENYEDGPSFRSMLHELEQKSSLMKYYCKKIMKRIVQLSDAYDASQVAVMKLSETLSEASNSTSMNMDILLDSYLTKAMDIHATFIQKLNYDLINLLYEPFHNIYSSFIKPIDDRRLEFDEQSKSFYGSLSRYLSAKKDKKGGDSKFFQKEKTFALQRYDYYCFMQDLHDGSIINDINGIFLQYFHRQYDHIALFSNLMNSVLPNLQQLNLKLEKTKWSTTRRDKGREMHRSQVIQTSGRPKSMAPPSPSPISPSFPLHEIQSPMPNRRMAASADDISQTSNFTTEIKGKCISNGGSASPDKIFKEGLLLVFGATELGTDLAMVSKAAWHKHWIVVENGSLWEYANWKDSVKSNVSSISLKHASADKVRKQGRRFCFEVVTPKLKRLYQATSAEEMDSWIEAICEAAKISSFQLSRVATPLSASVRRPSKVFPLFSTSFETTPISRKLSGSGIKKAFSRKGSWNLQQFFRSDNSGTMHMEQLERYHASANIFIQMLRKTDVSNSVCADCGSVKDVTWCSINIPVVLCIECSGIHRSLGTHISKTRSLLLDSLSQQSKVLLCKIGNAAVNRVYEKGLSNPSLKPKPEHNAQVKLAFAQKKYVEHAFIDFAGVDADATLLEGLEQNKISKILLGLAAKPNFEENGVVFLKAVTRDTSKLHLLELLFMNGLLLPDSEQLSEHVSPDMQSYLSQKQFTKYLKE
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
191PhosphorylationFSESQRVTSPLTTSQ
CCCCCCCCCCCCCCC
27.1525720772
192PhosphorylationSESQRVTSPLTTSQT
CCCCCCCCCCCCCCC
18.3028889911
195PhosphorylationQRVTSPLTTSQTVQT
CCCCCCCCCCCCEEC
27.9925720772
196PhosphorylationRVTSPLTTSQTVQTQ
CCCCCCCCCCCEECC
26.9029996109
207PhosphorylationVQTQPPQSPEAKTEL
EECCCCCCCCCCCEE
30.4028889911
467PhosphorylationQTSGRPKSMAPPSPS
ECCCCCCCCCCCCCC
23.9029996109
497PhosphorylationPNRRMAASADDISQT
CCCCCCCCHHHHHHC
23.7728889911
523PhosphorylationISNGGSASPDKIFKE
ECCCCCCCHHHHHHC
35.0227738172
639PhosphorylationKISSFQLSRVATPLS
CCCCEEHHCCCCCCC
17.5825720772
643PhosphorylationFQLSRVATPLSASVR
EEHHCCCCCCCCCCC
23.1629996109
646PhosphorylationSRVATPLSASVRRPS
HCCCCCCCCCCCCCH
21.5025720772
648PhosphorylationVATPLSASVRRPSKV
CCCCCCCCCCCCHHC
16.8725720772
653PhosphorylationSASVRRPSKVFPLFS
CCCCCCCHHCCCCCC
39.3725720772
660PhosphorylationSKVFPLFSTSFETTP
HHCCCCCCCCCCCCC
30.7225720772
661PhosphorylationKVFPLFSTSFETTPI
HCCCCCCCCCCCCCC
30.0521712547
662PhosphorylationVFPLFSTSFETTPIS
CCCCCCCCCCCCCCC
21.6421712547
665PhosphorylationLFSTSFETTPISRKL
CCCCCCCCCCCCCCC
35.5421712547
669PhosphorylationSFETTPISRKLSGSG
CCCCCCCCCCCCCCC
25.2721712547
673PhosphorylationTPISRKLSGSGIKKA
CCCCCCCCCCCCHHH
33.6724763107
675PhosphorylationISRKLSGSGIKKAFS
CCCCCCCCCCHHHHH
33.6929996109
686PhosphorylationKAFSRKGSWNLQQFF
HHHHCCCCCCHHHHH
18.8029996109

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 CNT6_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNT6_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 CNT6_SCHPO !!

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

Oops, there are no PPI records of CNT6_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CNT6_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-207, AND MASSSPECTROMETRY.

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