YSH1_YEAST - dbPTM
YSH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YSH1_YEAST
UniProt AC Q06224
Protein Name Endoribonuclease YSH1
Gene Name YSH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 779
Subcellular Localization Nucleus .
Protein Description Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Has endonuclease activity..
Protein Sequence MERTNTTTFKFFSLGGSNEVGRSCHILQYKGKTVMLDAGIHPAYQGLASLPFYDEFDLSKVDILLISHFHLDHAASLPYVMQRTNFQGRVFMTHPTKAIYRWLLRDFVRVTSIGSSSSSMGTKDEGLFSDEDLVDSFDKIETVDYHSTVDVNGIKFTAFHAGHVLGAAMFQIEIAGLRVLFTGDYSREVDRHLNSAEVPPLSSNVLIVESTFGTATHEPRLNRERKLTQLIHSTVMRGGRVLLPVFALGRAQEIMLILDEYWSQHADELGGGQVPIFYASNLAKKCMSVFQTYVNMMNDDIRKKFRDSQTNPFIFKNISYLRNLEDFQDFGPSVMLASPGMLQSGLSRDLLERWCPEDKNLVLITGYSIEGTMAKFIMLEPDTIPSINNPEITIPRRCQVEEISFAAHVDFQENLEFIEKISAPNIILVHGEANPMGRLKSALLSNFASLKGTDNEVHVFNPRNCVEVDLEFQGVKVAKAVGNIVNEIYKEENVEIKEEIAAKIEPIKEENEDNLDSQAEKGLVDEEEHKDIVVSGILVSDDKNFELDFLSLSDLREHHPDLSTTILRERQSVRVNCKKELIYWHILQMFGEAEVLQDDDRVTNQEPKVKEESKDNLTNTGKLILQIMGDIKLTIVNTLAVVEWTQDLMNDTVADSIIAILMNVDSAPASVKLSSHSCDDHDHNNVQSNAQGKIDEVERVKQISRLFKEQFGDCFTLFLNKDEYASNKEETITGVVTIGKSTAKIDFNNMKILECNSNPLKGRVESLLNIGGNLVTPLC
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
365PhosphorylationDKNLVLITGYSIEGT
CCCEEEEEEEEEECC
26.3819795423
367PhosphorylationNLVLITGYSIEGTMA
CEEEEEEEEEECCEE
9.6019823750
368PhosphorylationLVLITGYSIEGTMAK
EEEEEEEEEECCEEE
18.6019823750
372PhosphorylationTGYSIEGTMAKFIML
EEEEEECCEEEEEEE
10.9319823750
517PhosphorylationENEDNLDSQAEKGLV
CCCCCCHHHHHHCCC
34.1622369663
521AcetylationNLDSQAEKGLVDEEE
CCHHHHHHCCCCHHH
61.6424489116
535PhosphorylationEHKDIVVSGILVSDD
HHHCEEEEEEEECCC
14.8227017623
540PhosphorylationVVSGILVSDDKNFEL
EEEEEEECCCCCEEE
36.3227017623
551PhosphorylationNFELDFLSLSDLREH
CEEEEEECHHHHHHH
26.3128132839
666PhosphorylationAILMNVDSAPASVKL
HHHHCCCCCCCCCCC
31.6928889911

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
517SPhosphorylationKinaseATMP38110
Uniprot
517SPhosphorylationKinaseATRP38111
Uniprot
517SPhosphorylationKinaseATM/ATR-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YSH1_YEAST !!

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 YSH1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CFT1_YEASTCFT1physical
11805826
CFT2_YEASTCFT2physical
11805826
FIP1_YEASTFIP1physical
11805826
PAP_YEASTPAP1physical
11805826
PFS2_YEASTPFS2physical
11805826
PTA1_YEASTPTA1physical
11805826
REF2_YEASTREF2physical
11805826
MPE1_YEASTMPE1physical
11805826
PP12_YEASTGLC7physical
11805826
YTH1_YEASTYTH1physical
11805826
CLP1_YEASTCLP1physical
12853609
TFC4_YEASTTFC4physical
12853609
CFT1_YEASTCFT1physical
16554755
FIP1_YEASTFIP1physical
16554755
PAP_YEASTPAP1physical
16554755
CORO_YEASTCRN1physical
16554755
YNU8_YEASTYNL208Wphysical
16554755
PFS2_YEASTPFS2physical
16554755
YTH1_YEASTYTH1physical
16554755
CFT1_YEASTCFT1physical
16429126
CFT2_YEASTCFT2physical
16429126
FIP1_YEASTFIP1physical
16429126
PP12_YEASTGLC7physical
16429126
MPE1_YEASTMPE1physical
16429126
PAP_YEASTPAP1physical
16429126
PFS2_YEASTPFS2physical
16429126
PTA1_YEASTPTA1physical
16429126
REF2_YEASTREF2physical
16429126
SWD2_YEASTSWD2physical
16429126
YTH1_YEASTYTH1physical
16429126
SYC1_YEASTSYC1genetic
16431986
CLP1_YEASTCLP1physical
22216186

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YSH1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517 AND SER-666, ANDMASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, AND MASSSPECTROMETRY.

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