YL032_YEAST - dbPTM
YL032_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YL032_YEAST
UniProt AC Q07834
Protein Name KH domain-containing protein YLL032C
Gene Name YLL032C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 825
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MDNFKIYSTVITTAFLQVPHLYTTNRLWKPIEAPFLVEFLQKRISSKELKNTKAICHIDPSWVNLNASFIRDDMISIKATTDDMDLDAICRISLPLPMNTNDLTAELEKMKRILLDLSEKFNLELIITKEPAYFTPEQTGESKELCIYVHALGFRSNLMECEPQLLAFVDLIKKNGMTLPPQHYIIEPMELNSYSVLPLYMGVDMENFKHISRAFKTSIYAPSLITLSRDLKANPQIFFSGAVHSLSLLARKTLRESISVNSKSFFYRRLTNITPGKLLFIRKYYQQKVNQLILKYQSLIRVTNEYIEFQSISTNLLEMVIKNFTIQVLHEIVEVQISLNENCAMSPELIIDSFFGHTGNQIVVITPKEDSFNQLIVVGNQSSTDEASDTSILHYLSDFIMGSNQVINPNLRQIKAIFEIHPDFEDFISGKKNGKLTRIMELSACLIQLEMEEEDDNLYLNLVSDSFPDFKESFKNVINEFPAEESFFIPEVCHRPIIGTGGSLIQATMRKHNVFIQFSNSFNLPQNKISMIRYDNVIIRCPRKNKANICLAKNDLKQIVQEYDSLQSKTLIRFSSGQYRHILHVNGQKNIIGQIEKNENVYIMIPLKEPLDGTSQLSIQGNDENASRAANELVNSAFGYEYEFKIDQEIDPNKEYEFYNLIVVPFLQIMNIIVTFEKDLITFTFEKDTNENTLTKAIELLSNYLETQKTKIIFKKIIKKFVLGSASSKSNTSNSNTNGNFRSMNNAKSRTTIDNTSQSGASPQRHKMPVITTVGGAQAIKGYIPNTYYNGYGYGYGYTYEYDYNYANSNKAQTNNRHKYQNGRK
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
570PhosphorylationYDSLQSKTLIRFSSG
HHHHCCCEEEEECCC		32.4421551504
576PhosphorylationKTLIRFSSGQYRHIL
CEEEEECCCCEEEEE		27.4921551504
751PhosphorylationMNNAKSRTTIDNTSQ
CCCCCCCEEECCCCC		34.8821126336
756PhosphorylationSRTTIDNTSQSGASP
CCEEECCCCCCCCCC		25.1328889911
757PhosphorylationRTTIDNTSQSGASPQ
CEEECCCCCCCCCCC		28.7122890988
759PhosphorylationTIDNTSQSGASPQRH
EECCCCCCCCCCCCC		35.7721440633
762PhosphorylationNTSQSGASPQRHKMP
CCCCCCCCCCCCCCC		25.7022369663
819AcetylationAQTNNRHKYQNGRK-
CCCCCCCCCCCCCC-		45.3425381059
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 YL032_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YL032_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 YL032_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LSM12_YEASTLSM12physical
16554755
RAD4_YEASTRAD4genetic
27708008
MPCP_YEASTMIR1genetic
27708008
PSB6_YEASTPRE7genetic
27708008
KPC1_YEASTPKC1genetic
27708008
TAF5_YEASTTAF5genetic
27708008
APC11_YEASTAPC11genetic
27708008
PRP9_YEASTPRP9genetic
27708008
LCB2_YEASTLCB2genetic
27708008
CDC20_YEASTCDC20genetic
27708008
CDC23_YEASTCDC23genetic
27708008
ATC7_YEASTNEO1genetic
27708008
KTHY_YEASTCDC8genetic
27708008
CDC11_YEASTCDC11genetic
27708008
NTR2_YEASTNTR2genetic
27708008
IML3_YEASTIML3genetic
27708008
SNF5_YEASTSNF5genetic
27708008
STE50_YEASTSTE50genetic
27708008
RL13A_YEASTRPL13Agenetic
27708008
ACL4_YEASTYDR161Wgenetic
27708008
RV167_YEASTRVS167genetic
27708008
ADH4_YEASTADH4genetic
27708008
RME1_YEASTRME1genetic
27708008
CHO2_YEASTCHO2genetic
27708008
TNA1_YEASTTNA1genetic
27708008
OPI1_YEASTOPI1genetic
27708008
KC11_YEASTYCK1genetic
27708008
NCE1_YEASTNCE101genetic
27708008
EFM7_YEASTNNT1genetic
27708008
ATP10_YEASTATP10genetic
27708008
SIN3_YEASTSIN3genetic
27708008
MDM12_YEASTMDM12genetic
27708008
SFG1_YEASTSFG1genetic
27708008
PDR10_YEASTPDR10genetic
27708008
LGE1_YEASTLGE1genetic
27708008
NIP80_YEASTNIP100genetic
27708008
MRN1_YEASTMRN1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YL032_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-757 AND SER-762, ANDMASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-762, AND MASSSPECTROMETRY.

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