REH1_YEAST - dbPTM
REH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID REH1_YEAST
UniProt AC Q06709
Protein Name Cytoplasmic 60S subunit biogenesis factor REH1
Gene Name REH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 432
Subcellular Localization Cytoplasm .
Protein Description Pre-60S-associated cytoplasmic factor involved in the cytoplasmic maturation of the 60S subunit. May act redundantly with REI1 to directly promote a stabilizing structural rearrangement in cytoplasmic 60S subunit maturation independent on the REI1-specific ARX1 recycling..
Protein Sequence MSSTFFTCNCCVIQFKTSDLQRYHMKTEWHRYNLKRRIANLPPIGAEQFAEKLQISEKEQAENQVDEFGFPVLKPVMNQSNALPQKQKKPIKSKRGRKVGTNLLKRKDRDIAKEKQNRSVSPSGSISSQLSNLTVGTENTNTDYGEDTVSEYGFTSDSNYEYATSDEELDIADKPSDKENEKITITECIYCGKDNKEVERNVKHMFSEHGLFIPERSYLIDLNGLLEFLIKMIVIDHNCLCCNFHGSGLESIRAHMASKRHCRLPYETKEERQLFAPFYDFTYDDHSISKNLQNDRAITSKLSSVYGAKNDEEDGEVDITLVSSENDINANYTTVSIDESGLELTLPTGARLGHRAGQRYYRQNLPSQPNPNESRRTITAADRRMVSGVTEKQYKKGMKKMQQLEKNAINTQIRREIKRVNFQTHYRDELLQ
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
98UbiquitinationIKSKRGRKVGTNLLK
CCCCCCCCCCHHHHH		48.0823749301
105UbiquitinationKVGTNLLKRKDRDIA
CCCHHHHHHCHHHHH		61.6423749301
107UbiquitinationGTNLLKRKDRDIAKE
CHHHHHHCHHHHHHH		56.3722817900
282PhosphorylationFAPFYDFTYDDHSIS
CCCCCCCCCCCCCHH		24.1222369663
283PhosphorylationAPFYDFTYDDHSISK
CCCCCCCCCCCCHHH		21.2622369663
287PhosphorylationDFTYDDHSISKNLQN
CCCCCCCCHHHHCCC		35.2422369663
289PhosphorylationTYDDHSISKNLQNDR
CCCCCCHHHHCCCHH		20.6420377248
301UbiquitinationNDRAITSKLSSVYGA
CHHHHHHHHHHHHCC		43.6823749301
301AcetylationNDRAITSKLSSVYGA
CHHHHHHHHHHHHCC		43.6825381059
303PhosphorylationRAITSKLSSVYGAKN
HHHHHHHHHHHCCCC		22.8421440633
304PhosphorylationAITSKLSSVYGAKND
HHHHHHHHHHCCCCC		29.7830377154
387PhosphorylationAADRRMVSGVTEKQY
HHHHHHHCCCCHHHH		20.4327017623
392UbiquitinationMVSGVTEKQYKKGMK
HHCCCCHHHHHHHHH		49.9523749301
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 REH1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of REH1_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 REH1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSK21_YEASTCKA1physical
16554755
LSG1_YEASTLSG1physical
19433447
REI1_YEASTREI1physical
19433447
NMD3_YEASTNMD3physical
19433447
IF6_YEASTTIF6physical
19433447
RLP24_YEASTRLP24physical
19433447
RL3_YEASTRPL3physical
19433447
REI1_YEASTREI1genetic
19433447
REI1_YEASTREI1genetic
20093466
YPR1_YEASTYPR1genetic
20093466
CAJ1_YEASTCAJ1genetic
20093466
MEH1_YEASTMEH1genetic
20093466
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
REI1_YEASTREI1genetic
27708008
YPR1_YEASTYPR1genetic
27708008
RL24A_YEASTRPL24Agenetic
27708008
IST3_YEASTIST3genetic
27708008
MEH1_YEASTMEH1genetic
27708008
MAC1_YEASTMAC1genetic
27708008
RL21B_YEASTRPL21Bgenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of REH1_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-287, AND MASSSPECTROMETRY.
"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-287, AND MASSSPECTROMETRY.

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