ZUO1_YEAST - dbPTM
ZUO1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZUO1_YEAST
UniProt AC P32527
Protein Name Zuotin
Gene Name ZUO1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 433
Subcellular Localization Cytoplasm .
Protein Description Component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain. ZUO1 can act as a J-protein for SSB1/SSB2 only when associated with SSZ1..
Protein Sequence MFSLPTLTSDITVEVNSSATKTPFVRRPVEPVGKFFLQHAQRTLRNHTWSEFERIEAEKNVKTVDESNVDPDELLFDTELADEDLLTHDARDWKTADLYAAMGLSKLRFRATESQIIKAHRKQVVKYHPDKQSAAGGSLDQDGFFKIIQKAFETLTDSNKRAQYDSCDFVADVPPPKKGTDYDFYEAWGPVFEAEARFSKKTPIPSLGNKDSSKKEVEQFYAFWHRFDSWRTFEFLDEDVPDDSSNRDHKRYIERKNKAARDKKKTADNARLVKLVERAVSEDPRIKMFKEEEKKEKERRKWEREAGARAEAEAKAKAEAEAKAKAESEAKANASAKADKKKAKEAAKAAKKKNKRAIRNSAKEADYFGDADKATTIDEQVGLIVDSLNDEELVSTADKIKANAAGAKEVLKESAKTIVDSGKLPSSLLSYFV
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
34AcetylationRPVEPVGKFFLQHAQ
CCCCCCHHHHHHHHH		32.9324489116
34UbiquitinationRPVEPVGKFFLQHAQ
CCCCCCHHHHHHHHH		32.9323749301
43PhosphorylationFLQHAQRTLRNHTWS
HHHHHHHHHHHCCHH		20.2819823750
48PhosphorylationQRTLRNHTWSEFERI
HHHHHHCCHHHHHHH		33.9522369663
50PhosphorylationTLRNHTWSEFERIEA
HHHHCCHHHHHHHHH		33.3022369663
59AcetylationFERIEAEKNVKTVDE
HHHHHHHHCCCCCCC		74.2724489116
592-HydroxyisobutyrylationFERIEAEKNVKTVDE
HHHHHHHHCCCCCCC		74.27-
63PhosphorylationEAEKNVKTVDESNVD
HHHHCCCCCCCCCCC		28.9822369663
67PhosphorylationNVKTVDESNVDPDEL
CCCCCCCCCCCHHHH		37.3821551504
78PhosphorylationPDELLFDTELADEDL
HHHHCCCCCCCCCCC		26.0921440633
95PhosphorylationHDARDWKTADLYAAM
CCCCCHHHHHHHHHH		22.5822369663
99PhosphorylationDWKTADLYAAMGLSK
CHHHHHHHHHHCCCH		7.8922369663
105PhosphorylationLYAAMGLSKLRFRAT
HHHHHCCCHHHCCCC		24.7422369663
106UbiquitinationYAAMGLSKLRFRATE
HHHHCCCHHHCCCCH		49.0423749301
106AcetylationYAAMGLSKLRFRATE
HHHHCCCHHHCCCCH		49.0424489116
112PhosphorylationSKLRFRATESQIIKA
CHHHCCCCHHHHHHH		31.7325752575
114PhosphorylationLRFRATESQIIKAHR
HHCCCCHHHHHHHHH		23.4822369663
118AcetylationATESQIIKAHRKQVV
CCHHHHHHHHHHHHH		39.5122865919
126AcetylationAHRKQVVKYHPDKQS
HHHHHHHHHCCCCCC		38.7024489116
131AcetylationVVKYHPDKQSAAGGS
HHHHCCCCCCCCCCC		51.0724489116
133PhosphorylationKYHPDKQSAAGGSLD
HHCCCCCCCCCCCCC		26.3128889911
138PhosphorylationKQSAAGGSLDQDGFF
CCCCCCCCCCCCCHH		28.0528889911
146AcetylationLDQDGFFKIIQKAFE
CCCCCHHHHHHHHHH		36.3224489116
150AcetylationGFFKIIQKAFETLTD
CHHHHHHHHHHHCCC		44.6324489116
150UbiquitinationGFFKIIQKAFETLTD
CHHHHHHHHHHHCCC		44.6324961812
160SuccinylationETLTDSNKRAQYDSC
HHCCCCCCCCCCCCC		53.7323954790
160UbiquitinationETLTDSNKRAQYDSC
HHCCCCCCCCCCCCC		53.7323749301
202PhosphorylationEARFSKKTPIPSLGN
HHHHCCCCCCCCCCC		30.1328889911
206PhosphorylationSKKTPIPSLGNKDSS
CCCCCCCCCCCCCCC		50.0221440633
214AcetylationLGNKDSSKKEVEQFY
CCCCCCCHHHHHHHH		57.8324489116
215AcetylationGNKDSSKKEVEQFYA
CCCCCCHHHHHHHHH		69.7824489116
229PhosphorylationAFWHRFDSWRTFEFL
HHHHHCCCCCHHHCC		18.7530377154
232PhosphorylationHRFDSWRTFEFLDED
HHCCCCCHHHCCCCC		22.6628889911
244PhosphorylationDEDVPDDSSNRDHKR
CCCCCCCCCCHHHHH		36.5728889911
245PhosphorylationEDVPDDSSNRDHKRY
CCCCCCCCCHHHHHH		42.7627214570
250AcetylationDSSNRDHKRYIERKN
CCCCHHHHHHHHHHH		51.7024489116
274AcetylationADNARLVKLVERAVS
HHHHHHHHHHHHHHC		51.9422865919
281PhosphorylationKLVERAVSEDPRIKM
HHHHHHHCCCHHHHC		34.9821440633
290AcetylationDPRIKMFKEEEKKEK
CHHHHCCHHHHHHHH		61.8025381059
328PhosphorylationEAKAKAESEAKANAS
HHHHHHHHHHHHHHH		47.9527017623
3312-HydroxyisobutyrylationAKAESEAKANASAKA
HHHHHHHHHHHHHHH		37.81-
363SuccinylationRAIRNSAKEADYFGD
HHHHHHHHHCHHCCC		53.9423954790
4012-HydroxyisobutyrylationVSTADKIKANAAGAK
HHHHHHHHHHHCCHH		41.13-
4082-HydroxyisobutyrylationKANAAGAKEVLKESA
HHHHCCHHHHHHHHH		47.65-
408UbiquitinationKANAAGAKEVLKESA
HHHHCCHHHHHHHHH		47.6523749301
408SuccinylationKANAAGAKEVLKESA
HHHHCCHHHHHHHHH		47.6523954790
412UbiquitinationAGAKEVLKESAKTIV
CCHHHHHHHHHHHHH		55.5922817900
412SuccinylationAGAKEVLKESAKTIV
CCHHHHHHHHHHHHH		55.5923954790
426PhosphorylationVDSGKLPSSLLSYFV
HHCCCCCHHHHHHCC		44.0128889911
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 ZUO1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZUO1_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 ZUO1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GBLP_YEASTASC1physical
11805826
C1TM_YEASTMIS1physical
11805826
SSZ1_YEASTSSZ1physical
11805826
SC160_YEASTSCP160physical
11805826
SKI3_YEASTSKI3physical
11805826
IF4F1_YEASTTIF4631physical
11805826
ARB1_YEASTARB1physical
16260602
RS4A_YEASTRPS4Aphysical
16429126
RS4B_YEASTRPS4Aphysical
16429126
RS5_YEASTRPS5physical
16429126
RS7A_YEASTRPS7Aphysical
16429126
SC160_YEASTSCP160physical
16429126
SSZ1_YEASTSSZ1physical
16429126
GBLP_YEASTASC1physical
16429126
C1TM_YEASTMIS1physical
16429126
RL25_YEASTRPL25physical
16429126
RL27A_YEASTRPL27Aphysical
16429126
RL3_YEASTRPL3physical
16429126
RL30_YEASTRPL30physical
16429126
RS11A_YEASTRPS11Aphysical
16429126
RS11B_YEASTRPS11Aphysical
16429126
RS13_YEASTRPS13physical
16429126
RS21A_YEASTRPS21Aphysical
16429126
RS3_YEASTRPS3physical
16429126
SKI3_YEASTSKI3physical
16429126
IF4F1_YEASTTIF4631physical
16429126
SSZ1_YEASTSSZ1physical
11929993
JJJ1_YEASTJJJ1genetic
17242366
SSZ1_YEASTSSZ1physical
17901048
RL31A_YEASTRPL31Aphysical
18829863
RL31B_YEASTRPL31Bphysical
18829863
SSZ1_YEASTSSZ1physical
18829863
SSZ1_YEASTSSZ1physical
19920147
SHE1_YEASTSHE1genetic
20093466
RLA1_YEASTRPP1Agenetic
20093466
MET28_YEASTMET28genetic
20093466
TRK2_YEASTTRK2genetic
20093466
XDJ1_YEASTXDJ1genetic
20093466
SST2_YEASTSST2genetic
20093466
MKT1_YEASTMKT1genetic
20093466
PP2A4_YEASTPPG1genetic
20093466
JJJ1_YEASTJJJ1genetic
20368619
RQC2_YEASTTAE2genetic
20691087
PDR1_YEASTPDR1genetic
22203981
PDR1_YEASTPDR1physical
23036859
SSZ1_YEASTSSZ1physical
20368619
SSB1_YEASTSSB1physical
20368619
RL24A_YEASTRPL24Aphysical
20368619
NMD3_YEASTNMD3physical
20368619
ECM1_YEASTECM1physical
20368619
CIC1_YEASTCIC1physical
20368619
RL8A_YEASTRPL8Aphysical
25380751
RL31A_YEASTRPL31Aphysical
27669034
RLA1_YEASTRPP1Agenetic
27708008
XDJ1_YEASTXDJ1genetic
27708008
RFC5_YEASTRFC5genetic
27708008
SPC19_YEASTSPC19genetic
27708008
CDC12_YEASTCDC12genetic
27708008
NDC80_YEASTNDC80genetic
27708008
XRN2_YEASTRAT1genetic
27708008
SGT1_YEASTSGT1genetic
27708008
TF2B_YEASTSUA7genetic
27708008
TRK2_YEASTTRK2genetic
27708008
JJJ1_YEASTJJJ1genetic
25639645
RL36A_YEASTRPL36Agenetic
29158977
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZUO1_YEAST

loading...

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-50; SER-114 AND SER-426,AND MASS 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-50 AND THR-63, AND MASSSPECTROMETRY.
"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-50, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASSSPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory