CAF1_SCHPO - dbPTM
CAF1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAF1_SCHPO
UniProt AC O74856
Protein Name Poly(A) ribonuclease pop2
Gene Name caf1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 335
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Acts as the catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. In vivo and in vitro, caf1 has 3'-exoribonuclease activity with a preference for poly(A) RNAs..
Protein Sequence MTAMNSNFSYPALGVDGISSQISPIRDVWSTNLQQEMNLIMSLIERYPVVSMDTEFPGVVARPLGVFKSSDDYHYQTLRANVDSLKIIQIGLALSDEEGNAPVEACTWQFNFTFNLQDDMYAPESIELLTKSGIDFKKHQEVGIEPADFAELLIGSGLVLQEEVTWITFHSGYDFAYLLKAMTQIPLPAEYEEFYKILCIYFPKNYDIKYIMKSVLNNSKGLQDIADDLQIHRIGPQHQAGSDALLTARIFFEIRSRYFDGSIDSRMLNQLYGLGSTGSVLWHNNSSTPQIQFRDLPGAHPSPTPSNAGIPTTLTNTSSAPNFANSTFRFPPRVV
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
277PhosphorylationQLYGLGSTGSVLWHN
HHHCCCCCCCEEEEC
31.5129996109
279PhosphorylationYGLGSTGSVLWHNNS
HCCCCCCCEEEECCC
17.7129996109
286PhosphorylationSVLWHNNSSTPQIQF
CEEEECCCCCCCEEE
40.6929996109
287PhosphorylationVLWHNNSSTPQIQFR
EEEECCCCCCCEEEE
46.3529996109
288PhosphorylationLWHNNSSTPQIQFRD
EEECCCCCCCEEEEC
21.0229996109
302PhosphorylationDLPGAHPSPTPSNAG
CCCCCCCCCCCCCCC
31.3828889911
304PhosphorylationPGAHPSPTPSNAGIP
CCCCCCCCCCCCCCC
43.6228889911
306PhosphorylationAHPSPTPSNAGIPTT
CCCCCCCCCCCCCCC
41.6228889911
312PhosphorylationPSNAGIPTTLTNTSS
CCCCCCCCCCCCCCC
32.3029996109
317PhosphorylationIPTTLTNTSSAPNFA
CCCCCCCCCCCCCCC
20.8729996109
318PhosphorylationPTTLTNTSSAPNFAN
CCCCCCCCCCCCCCC
26.9429996109
319PhosphorylationTTLTNTSSAPNFANS
CCCCCCCCCCCCCCC
45.7829996109

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 CAF1_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAF1_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 CAF1_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RIR2_SCHPOsuc22physical
17264117
RAD26_SCHPOrad26genetic
17264117
CDS1_SCHPOcds1genetic
17264117
NUP61_SCHPOnup61genetic
18818364
AGO1_SCHPOago1genetic
18818364
RNC1_SCHPOrnc1genetic
18818364
RAF2_SCHPOraf2genetic
18818364
CCR4_SCHPOccr4genetic
18818364
ELP2_SCHPOelp2genetic
18818364
NOT2_SCHPOnot2physical
27851962
RCD1_SCHPOrcd1physical
27851962
YAC4_SCHPOmot2physical
27851962
CCR4_SCHPOccr4physical
27851962
NOT3_SCHPOnot3physical
27851962
NOT1_SCHPOnot1physical
27851962
MMI1_SCHPOmmi1physical
27851962

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAF1_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-302; THR-304 ANDSER-306, AND MASS SPECTROMETRY.

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