Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Heat shock protein SSB1

Gene

SSB1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May aid in the passage of the nascent polypeptide chain through the ribosome channel into the cytosol. Such an interaction could be crucial for continuous transport of the polypeptide; could serve to prevent the nascent polypeptide from interfering with translation by clogging the ribosome channel.1 Publication

GO - Molecular functioni

  • ATPase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • calmodulin binding Source: SGD
  • unfolded protein binding Source: SGD

GO - Biological processi

  • 'de novo' cotranslational protein folding Source: SGD
  • cellular response to glucose starvation Source: SGD
  • cytoplasmic translation Source: SGD
  • regulation of translational fidelity Source: SGD
  • ribosomal subunit export from nucleus Source: SGD
  • rRNA processing Source: SGD
  • translational frameshifting Source: SGD
  • translational termination Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein biosynthesis, Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29608-MONOMER.
ReactomeiR-SCE-3371453. Regulation of HSF1-mediated heat shock response.
R-SCE-3371568. Attenuation phase.
R-SCE-3371571. HSF1-dependent transactivation.
R-SCE-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein SSB1
Alternative name(s):
Cold-inducible protein YG101
Gene namesi
Name:SSB1
Synonyms:YG101
Ordered Locus Names:YDL229W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL229W.
SGDiS000002388. SSB1.

Subcellular locationi

  • Cytoplasm

  • Note: Associated with translating ribosomes, may bind directly to the nascent polypeptide.

GO - Cellular componenti

  • cytoplasm Source: SGD
  • polysome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 613612Heat shock protein SSB1PRO_0000078389Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei47 – 471PhosphothreonineCombined sources
Modified residuei431 – 4311PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP11484.
PeptideAtlasiP11484.
PRIDEiP11484.
TopDownProteomicsiP11484.

2D gel databases

COMPLUYEAST-2DPAGEP11484.
SWISS-2DPAGEP11484.
UCD-2DPAGEP11484.

PTM databases

iPTMnetiP11484.

Interactioni

Subunit structurei

Interacts with NAP1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ADE16P541133EBI-8627,EBI-14213
ADE3P072453EBI-8627,EBI-3897
AHA1Q124493EBI-8627,EBI-37072
APE2P324544EBI-8627,EBI-2641
ARO1P085663EBI-8627,EBI-2883
ASF1P324473EBI-8627,EBI-3003
BET3P361493EBI-8627,EBI-3567
BLM10P435832EBI-8627,EBI-22761
BRR2P326393EBI-8627,EBI-861
BRX1Q082353EBI-8627,EBI-3775
BUD27P435735EBI-8627,EBI-22787
BZZ1P388223EBI-8627,EBI-3889
CAF40P538293EBI-8627,EBI-28306
CAM1P295473EBI-8627,EBI-6323
CCL1P373663EBI-8627,EBI-4385
CDC27P380423EBI-8627,EBI-4249
CDC28P005463EBI-8627,EBI-4253
CDC55Q003623EBI-8627,EBI-1942
CHD1P326573EBI-8627,EBI-4574
CHS5Q121143EBI-8627,EBI-4640
CKA1P157903EBI-8627,EBI-9533
CKA2P194543EBI-8627,EBI-9548
CTK2P469623EBI-8627,EBI-5236
CWC22P533333EBI-8627,EBI-565
DBP2P247833EBI-8627,EBI-5602
DBP6P537343EBI-8627,EBI-5625
DBP8P387193EBI-8627,EBI-5633
DCP2P535503EBI-8627,EBI-270
DIS3Q081623EBI-8627,EBI-1740
DNA2P388593EBI-8627,EBI-5973
DNM1P548613EBI-8627,EBI-6002
EAF3Q124323EBI-8627,EBI-6281
ECM16Q042173EBI-8627,EBI-1820
ECM29P387373EBI-8627,EBI-24359
EIS1Q050503EBI-8627,EBI-28061
EMW1P428423EBI-8627,EBI-28374
ENO1P009243EBI-8627,EBI-6468
FAR1P212683EBI-8627,EBI-6780
FIP1P459763EBI-8627,EBI-6940
GLC3P327753EBI-8627,EBI-7652
GLC7P325983EBI-8627,EBI-13715
GPT2P361483EBI-8627,EBI-26471
HAT1Q123413EBI-8627,EBI-8176
HHF2P023093EBI-8627,EBI-8113
HMO1Q039733EBI-8627,EBI-33047
HOS4P404803EBI-8627,EBI-8492
HSC82P151083EBI-8627,EBI-8666
HSP82P028293EBI-8627,EBI-8659
HTB2P022943EBI-8627,EBI-8094
IPI1P388033EBI-8627,EBI-24606
JSN1P471353EBI-8627,EBI-9422
KAP95Q061423EBI-8627,EBI-9145
KIN1P131853EBI-8627,EBI-9716
KRE33P539143EBI-8627,EBI-28914
LPD1P096243EBI-8627,EBI-5940
LSM4P400703EBI-8627,EBI-188
MAK21Q121763EBI-8627,EBI-10944
MAM3Q122963EBI-8627,EBI-33338
MAM33P405133EBI-8627,EBI-10316
MAS2P119143EBI-8627,EBI-11205
MCM2P294692EBI-8627,EBI-10533
MCM5P294963EBI-8627,EBI-10549
MDR1P532583EBI-8627,EBI-10889
MET18P404693EBI-8627,EBI-11492
MET5P471693EBI-8627,EBI-25702
MFT1P334413EBI-8627,EBI-10841
MRD1Q061063EBI-8627,EBI-34383
MRP1P106624EBI-8627,EBI-16234
MSH6Q038343EBI-8627,EBI-11383
NAM9P279293EBI-8627,EBI-11843
NEW1Q089723EBI-8627,EBI-32014
NOP13P538833EBI-8627,EBI-29032
NTH1P323563EBI-8627,EBI-19509
NUP1P206764EBI-8627,EBI-12392
NUP2P324993EBI-8627,EBI-12401
OCA5P387383EBI-8627,EBI-24355
ORC6P388263EBI-8627,EBI-12588
PFK26P404333EBI-8627,EBI-1956
PRT1P061033EBI-8627,EBI-8973
PTC2P399663EBI-8627,EBI-12795
PWP1P213044EBI-8627,EBI-14328
PXL1P361663EBI-8627,EBI-26535
RAD52P067783EBI-8627,EBI-14719
RCO1Q047793EBI-8627,EBI-28153
RET1P222763EBI-8627,EBI-15815
RFX1P487433EBI-8627,EBI-15036
RPA190P109643EBI-8627,EBI-15730
RPC34P329103EBI-8627,EBI-15835
RPC40P077033EBI-8627,EBI-15831
RPC82P323493EBI-8627,EBI-15821
RPF2P361603EBI-8627,EBI-15881
RPN7Q061033EBI-8627,EBI-15940
RRP5Q050223EBI-8627,EBI-16011
RSC2Q064883EBI-8627,EBI-16198
RSC8P436093EBI-8627,EBI-23005
RTN1Q049473EBI-8627,EBI-38020
SAM1P106593EBI-8627,EBI-10789
SEC7P110753EBI-8627,EBI-16882
SET2P469953EBI-8627,EBI-16985
SFB2P539534EBI-8627,EBI-17006
SIN3P225793EBI-8627,EBI-17160
SIW14P539653EBI-8627,EBI-28668
SKI2P352073EBI-8627,EBI-1851
SMC3P470373EBI-8627,EBI-17423
SMI1P325663EBI-8627,EBI-17452
SNF1P067823EBI-8627,EBI-17516
SNT2P531273EBI-8627,EBI-23958
SNX41Q040535EBI-8627,EBI-30464
SSA1P105913EBI-8627,EBI-8591
SSE1P325894EBI-8627,EBI-8648
STE20Q034973EBI-8627,EBI-18285
STH1P325973EBI-8627,EBI-18410
SVF1Q055153EBI-8627,EBI-38400
SWA2Q066773EBI-8627,EBI-30084
SXM1Q041753EBI-8627,EBI-35508
TEF2P029943EBI-8627,EBI-6314
TIF2P100813EBI-8627,EBI-9017
TOP2P067863EBI-8627,EBI-19352
TSC13Q991903EBI-8627,EBI-31149
TUB3P097343EBI-8627,EBI-18981
UBP1P250373EBI-8627,EBI-19819
UBP2Q014763EBI-8627,EBI-19826
UTP18P403624EBI-8627,EBI-4534
UTP21Q060783EBI-8627,EBI-359
UTP22P532543EBI-8627,EBI-1878
VIP1Q066853EBI-8627,EBI-35034
VPS16Q033083EBI-8627,EBI-20355
WTM1Q123633EBI-8627,EBI-20563
YCP4P253493EBI-8627,EBI-21840
YMR027WQ043713EBI-8627,EBI-28049
YMR099CQ031613EBI-8627,EBI-28203
YNR029CP537294EBI-8627,EBI-28492
YOL098CQ124963EBI-8627,EBI-29300
YPR089WO135853EBI-8627,EBI-33008
ZDS1P501113EBI-8627,EBI-29626
ZDS2P547863EBI-8627,EBI-29637

GO - Molecular functioni

  • calmodulin binding Source: SGD
  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi31882. 632 interactions.
DIPiDIP-2254N.
IntActiP11484. 3493 interactions.
MINTiMINT-1325604.

Structurei

Secondary structure

1
613
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 134Combined sources
Beta strandi16 – 3015Combined sources
Beta strandi38 – 414Combined sources
Beta strandi44 – 463Combined sources
Beta strandi51 – 544Combined sources
Helixi55 – 595Combined sources
Helixi61 – 633Combined sources
Helixi65 – 673Combined sources
Helixi72 – 743Combined sources
Turni75 – 773Combined sources
Helixi83 – 897Combined sources
Beta strandi93 – 997Combined sources
Beta strandi102 – 1098Combined sources
Beta strandi112 – 1165Combined sources
Helixi118 – 13720Combined sources
Beta strandi143 – 1486Combined sources
Helixi154 – 16613Combined sources
Beta strandi170 – 1767Combined sources
Helixi177 – 1848Combined sources
Turni185 – 1906Combined sources
Beta strandi196 – 2038Combined sources
Beta strandi208 – 2169Combined sources
Beta strandi219 – 22810Combined sources
Helixi233 – 25220Combined sources
Helixi260 – 27617Combined sources
Turni277 – 2793Combined sources
Beta strandi280 – 29112Combined sources
Beta strandi294 – 3018Combined sources
Helixi302 – 3087Combined sources
Helixi310 – 3156Combined sources
Helixi317 – 32711Combined sources
Helixi331 – 3333Combined sources
Beta strandi336 – 3416Combined sources
Helixi342 – 3454Combined sources
Helixi347 – 35610Combined sources
Turni357 – 3593Combined sources
Turni368 – 3703Combined sources
Helixi371 – 38313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GL1X-ray1.92A/B1-384[»]
ProteinModelPortaliP11484.
SMRiP11484. Positions 2-601.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11484.

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

GeneTreeiENSGT00830000129364.
HOGENOMiHOG000228135.
InParanoidiP11484.
OMAiFEEINST.
OrthoDBiEOG728916.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11484-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEGVFQGAI GIDLGTTYSC VATYESSVEI IANEQGNRVT PSFVAFTPEE
60 70 80 90 100
RLIGDAAKNQ AALNPRNTVF DAKRLIGRRF DDESVQKDMK TWPFKVIDVD
110 120 130 140 150
GNPVIEVQYL EETKTFSPQE ISAMVLTKMK EIAEAKIGKK VEKAVITVPA
160 170 180 190 200
YFNDAQRQAT KDAGAISGLN VLRIINEPTA AAIAYGLGAG KSEKERHVLI
210 220 230 240 250
FDLGGGTFDV SLLHIAGGVY TVKSTSGNTH LGGQDFDTNL LEHFKAEFKK
260 270 280 290 300
KTGLDISDDA RALRRLRTAA ERAKRTLSSV TQTTVEVDSL FDGEDFESSL
310 320 330 340 350
TRARFEDLNA ALFKSTLEPV EQVLKDAKIS KSQIDEVVLV GGSTRIPKVQ
360 370 380 390 400
KLLSDFFDGK QLEKSINPDE AVAYGAAVQG AILTGQSTSD ETKDLLLLDV
410 420 430 440 450
APLSLGVGMQ GDMFGIVVPR NTTVPTIKRR TFTTCADNQT TVQFPVYQGE
460 470 480 490 500
RVNCKENTLL GEFDLKNIPM MPAGEPVLEA IFEVDANGIL KVTAVEKSTG
510 520 530 540 550
KSSNITISNA VGRLSSEEIE KMVNQAEEFK AADEAFAKKH EARQRLESYV
560 570 580 590 600
ASIEQTVTDP VLSSKLKRGS KSKIEAALSD ALAALQIEDP SADELRKAEV
610
GLKRVVTKAM SSR
Length:613
Mass (Da):66,602
Last modified:January 23, 2007 - v3
Checksum:iF16FA7C25A40321A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti180 – 1845AAAIA → VVVIV in AAA34692 (PubMed:6761581).Curated
Sequence conflicti189 – 1891A → V in AAA34692 (PubMed:6761581).Curated
Sequence conflicti192 – 1921S → F in AAA34692 (PubMed:6761581).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13713 Genomic DNA. Translation: CAA31995.1.
M25395 mRNA. Translation: AAA35099.1.
Z74277 Genomic DNA. Translation: CAA98807.1.
M17585 Genomic DNA. Translation: AAA34692.1.
BK006938 Genomic DNA. Translation: DAA11637.1.
PIRiS20149.
RefSeqiNP_010052.1. NM_001180289.1.

Genome annotation databases

EnsemblFungiiYDL229W; YDL229W; YDL229W.
GeneIDi851369.
KEGGisce:YDL229W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13713 Genomic DNA. Translation: CAA31995.1.
M25395 mRNA. Translation: AAA35099.1.
Z74277 Genomic DNA. Translation: CAA98807.1.
M17585 Genomic DNA. Translation: AAA34692.1.
BK006938 Genomic DNA. Translation: DAA11637.1.
PIRiS20149.
RefSeqiNP_010052.1. NM_001180289.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GL1X-ray1.92A/B1-384[»]
ProteinModelPortaliP11484.
SMRiP11484. Positions 2-601.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31882. 632 interactions.
DIPiDIP-2254N.
IntActiP11484. 3493 interactions.
MINTiMINT-1325604.

PTM databases

iPTMnetiP11484.

2D gel databases

COMPLUYEAST-2DPAGEP11484.
SWISS-2DPAGEP11484.
UCD-2DPAGEP11484.

Proteomic databases

MaxQBiP11484.
PeptideAtlasiP11484.
PRIDEiP11484.
TopDownProteomicsiP11484.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL229W; YDL229W; YDL229W.
GeneIDi851369.
KEGGisce:YDL229W.

Organism-specific databases

EuPathDBiFungiDB:YDL229W.
SGDiS000002388. SSB1.

Phylogenomic databases

GeneTreeiENSGT00830000129364.
HOGENOMiHOG000228135.
InParanoidiP11484.
OMAiFEEINST.
OrthoDBiEOG728916.

Enzyme and pathway databases

BioCyciYEAST:G3O-29608-MONOMER.
ReactomeiR-SCE-3371453. Regulation of HSF1-mediated heat shock response.
R-SCE-3371568. Attenuation phase.
R-SCE-3371571. HSF1-dependent transactivation.
R-SCE-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.

Miscellaneous databases

EvolutionaryTraceiP11484.
NextBioi968489.
PROiP11484.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The SSB1 heat shock cognate gene of the yeast Saccharomyces cerevisiae."
    Slater M.R., Craig E.A.
    Nucleic Acids Res. 17:4891-4891(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP."
    Normington K., Kohno K., Kozutsumi Y., Gething M.J., Sambrook J.
    Cell 57:1223-1236(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides."
    Norbeck J., Blomberg A.
    Electrophoresis 16:149-156(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 39-49 AND 431-439.
    Strain: ATCC 38531 / Y41.
  6. Cited for: PROTEIN SEQUENCE OF 145-159.
    Strain: ATCC 204508 / S288c.
  7. "Saccharomyces cerevisiae contains a complex multigene family related to the major heat shock-inducible gene of Drosophila."
    Ingolia T.D., Slater M.R., Craig E.A.
    Mol. Cell. Biol. 2:1388-1398(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-403.
  8. "The translation machinery and 70 kd heat shock protein cooperate in protein synthesis."
    Nelson R.J., Ziegelhoffer T., Nicolet C., Werner-Washburne M., Craig E.A.
    Cell 71:97-105(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
    Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.
    Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT ALA-2.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  12. "Phosphorylation by casein kinase 2 regulates Nap1 localization and function."
    Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., Pemberton L.F.
    Mol. Cell. Biol. 28:1313-1325(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NAP1, IDENTIFICATION BY MASS SPECTROMETRY.
  13. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-431, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHSP75_YEAST
AccessioniPrimary (citable) accession number: P11484
Secondary accession number(s): D6VRC7, Q05834
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: April 13, 2016
This is version 163 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 170000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.