SSZ1_YEAST - dbPTM
SSZ1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SSZ1_YEAST
UniProt AC P38788
Protein Name Ribosome-associated complex subunit SSZ1
Gene Name SSZ1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 538
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. SSZ1 is required for ZUO1 to function efficiently as a J-protein for SSB1/SSB2. Also involved in pleiotropic drug resistance by post-translational activation of transcription factor PDR1..
Protein Sequence MSSPVIGITFGNTSSSIAYINPKNDVDVIANPDGERAIPSALSYVGEDEYHGGQALQQLIRNPKNTIINFRDFIGLPFDKCDVSKCANGAPAVEVDGKVGFVISRGEGKEEKLTVDEVVSRHLNRLKLAAEDYIGSAVKEAVLTVPTNFSEEQKTALKASAAKIGLQIVQFINEPSAALLAHAEQFPFEKDVNVVVADFGGIRSDAAVIAVRNGIFTILATAHDLSLGGDNLDTELVEYFASEFQKKYQANPRKNARSLAKLKANSSITKKTLSNATSATISIDSLADGFDYHASINRMRYELVANKVFAQFSSFVDSVIAKAELDPLDIDAVLLTGGVSFTPKLTTNLEYTLPESVEILGPQNKNASNNPNELAASGAALQARLISDYDADELAEALQPVIVNTPHLKKPIGLIGAKGEFHPVLLAETSFPVQKKLTLKQAKGDFLIGVYEGDHHIEEKTLEPIPKEENAEEDDESEWSDDEPEVVREKLYTLGTKLMELGIKNANGVEIIFNINKDGALRVTARDLKTGNAVKGEL
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
80AcetylationFIGLPFDKCDVSKCA
HCCCCCCCCCHHHCC		32.4824489116
85UbiquitinationFDKCDVSKCANGAPA
CCCCCHHHCCCCCCE		36.9023749301
85AcetylationFDKCDVSKCANGAPA
CCCCCHHHCCCCCCE		36.9025381059
109AcetylationVISRGEGKEEKLTVD
EEECCCCCCEECCHH		59.4024489116
112AcetylationRGEGKEEKLTVDEVV
CCCCCCEECCHHHHH		51.0224489116
136PhosphorylationAAEDYIGSAVKEAVL
HHHHHHHHHHHHHEE		21.9628889911
139AcetylationDYIGSAVKEAVLTVP
HHHHHHHHHHEEECC		39.4124489116
154AcetylationTNFSEEQKTALKASA
CCCCHHHHHHHHHHH		38.7624489116
1582-HydroxyisobutyrylationEEQKTALKASAAKIG
HHHHHHHHHHHHHHH		37.52-
204PhosphorylationADFGGIRSDAAVIAV
ECCCCCCCCCEEEEE		29.6727017623
263AcetylationARSLAKLKANSSITK
HHHHHHHHCCCCCCH		44.8325381059
267PhosphorylationAKLKANSSITKKTLS
HHHHCCCCCCHHHHC		33.8027214570
270SuccinylationKANSSITKKTLSNAT
HCCCCCCHHHHCCCC		41.9323954790
365UbiquitinationEILGPQNKNASNNPN
EECCCCCCCCCCCHH		48.9523749301
368PhosphorylationGPQNKNASNNPNELA
CCCCCCCCCCHHHHH		46.6728132839
377PhosphorylationNPNELAASGAALQAR
CHHHHHHCHHHHHHH		24.2928889911
405PhosphorylationLQPVIVNTPHLKKPI
HCCEEECCCCCCCCC		10.9422369663
410UbiquitinationVNTPHLKKPIGLIGA
ECCCCCCCCCEEECC		48.5023749301
418AcetylationPIGLIGAKGEFHPVL
CCEEECCCCCCCCEE		54.4824489116
429PhosphorylationHPVLLAETSFPVQKK
CCEEEEECCCCCCCC		30.0230377154
435SuccinylationETSFPVQKKLTLKQA
ECCCCCCCCEEEEEC		50.4023954790
435AcetylationETSFPVQKKLTLKQA
ECCCCCCCCEEEEEC		50.4024489116
443AcetylationKLTLKQAKGDFLIGV
CEEEEECCCCEEEEE		57.4224489116
460AcetylationGDHHIEEKTLEPIPK
CCCCCEEECCCCCCC		45.6924489116
461PhosphorylationDHHIEEKTLEPIPKE
CCCCEEECCCCCCCC		39.3722369663
477PhosphorylationNAEEDDESEWSDDEP
CCCCCCCCCCCCCCH		51.8925521595
480PhosphorylationEDDESEWSDDEPEVV
CCCCCCCCCCCHHHH		31.0022369663
490AcetylationEPEVVREKLYTLGTK
CHHHHHHHHHHHCHH		35.9122865919
490UbiquitinationEPEVVREKLYTLGTK
CHHHHHHHHHHHCHH		35.9123749301
4902-HydroxyisobutyrylationEPEVVREKLYTLGTK
CHHHHHHHHHHHCHH		35.91-
497AcetylationKLYTLGTKLMELGIK
HHHHHCHHHHHHCCC		44.0024489116
517AcetylationEIIFNINKDGALRVT
EEEEEECCCCCEEEE		54.4624489116
529SuccinylationRVTARDLKTGNAVKG
EEEEEECCCCCCCCC		59.6923954790
535UbiquitinationLKTGNAVKGEL----
CCCCCCCCCCC----		44.2323749301
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 SSZ1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SSZ1_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 SSZ1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZUO1_YEASTZUO1physical
11054575
ZUO1_YEASTZUO1physical
11274393
SSB1_YEASTSSB1genetic
11929994
ZUO1_YEASTZUO1genetic
11274393
TAT1_YEASTTAT1physical
16554755
ZUO1_YEASTZUO1physical
16554755
BEM2_YEASTBEM2physical
16429126
CDC25_YEASTCDC25physical
16429126
RL11A_YEASTRPL11Aphysical
16429126
RS10A_YEASTRPS10Aphysical
16429126
RS14B_YEASTRPS14Bphysical
16429126
RS20_YEASTRPS20physical
16429126
RS4A_YEASTRPS4Aphysical
16429126
RS4B_YEASTRPS4Aphysical
16429126
RS5_YEASTRPS5physical
16429126
RS7A_YEASTRPS7Aphysical
16429126
SC160_YEASTSCP160physical
16429126
RBG1_YEASTRBG1physical
16429126
ZUO1_YEASTZUO1physical
16429126
GBLP_YEASTASC1physical
16429126
C1TM_YEASTMIS1physical
16429126
DXO_YEASTRAI1physical
16429126
XRN2_YEASTRAT1physical
16429126
RL10_YEASTRPL10physical
16429126
RL27A_YEASTRPL27Aphysical
16429126
RL3_YEASTRPL3physical
16429126
RL8A_YEASTRPL8Aphysical
16429126
RS13_YEASTRPS13physical
16429126
RS17B_YEASTRPS17Bphysical
16429126
RS22A_YEASTRPS22Aphysical
16429126
RS3_YEASTRPS3physical
16429126
SKI3_YEASTSKI3physical
16429126
IF4F1_YEASTTIF4631physical
16429126
ZUO1_YEASTZUO1physical
17901048
ZUO1_YEASTZUO1genetic
11929994
RRP4_YEASTRRP4physical
19536198
INP51_YEASTINP51physical
19536198
PRR1_YEASTPRR1physical
19536198
KAE1_YEASTKAE1physical
19536198
SIR1_YEASTSIR1physical
19536198
RL15B_YEASTRPL15Bphysical
19536198
TMA46_YEASTTMA46physical
19536198
GDE1_YEASTGDE1physical
19536198
CCL1_YEASTCCL1physical
19536198
HSP82_YEASTHSP82physical
19536198
SSB1_YEASTSSB1physical
19536198
SSB2_YEASTSSB2physical
19536198
REI1_YEASTREI1genetic
20093466
ZUO1_YEASTZUO1physical
23202586
SA155_YEASTSAP155genetic
27708008
YJ24_YEASTKCH1genetic
27708008
NACB1_YEASTEGD1genetic
27708008
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SSZ1_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-136; SER-477 ANDSER-480, 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 THR-405; SER-477 ANDSER-480, AND MASS 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-477 AND SER-480, ANDMASS SPECTROMETRY.
"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-477 AND SER-480, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND MASSSPECTROMETRY.

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