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P11484

- HSP75_YEAST

UniProt

P11484 - HSP75_YEAST

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Protein
Heat shock protein SSB1
Gene
SSB1, YG101, YDL229W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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

  1. ATP binding Source: UniProtKB-KW
  2. ATPase activity Source: SGD
  3. calmodulin binding Source: SGD
  4. protein binding Source: IntAct
  5. unfolded protein binding Source: SGD

GO - Biological processi

  1. 'de novo' cotranslational protein folding Source: SGD
  2. ATP catabolic process Source: GOC
  3. cellular response to glucose starvation Source: SGD
  4. cytoplasmic translation Source: SGD
  5. rRNA processing Source: SGD
  6. regulation of translational fidelity Source: SGD
  7. ribosomal subunit export from nucleus Source: SGD
  8. translational frameshifting Source: SGD
  9. 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.

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
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

SGDiS000002388. SSB1.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. polysome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 613612Heat shock protein SSB1
PRO_0000078389Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei47 – 471Phosphothreonine1 Publication
Modified residuei431 – 4311Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP11484.
PeptideAtlasiP11484.
PRIDEiP11484.

2D gel databases

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

Expressioni

Gene expression databases

GenevestigatoriP11484.

Interactioni

Subunit structurei

Interacts with NAP1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BUD27P435733EBI-8627,EBI-22787
PFK26P404332EBI-8627,EBI-1956
SSE1P325892EBI-8627,EBI-8648

Protein-protein interaction databases

BioGridi31882. 623 interactions.
DIPiDIP-2254N.
IntActiP11484. 741 interactions.
MINTiMINT-1325604.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GL1X-ray1.92A/B1-384[»]
ProteinModelPortaliP11484.
SMRiP11484. Positions 2-601.

Miscellaneous databases

EvolutionaryTraceiP11484.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00740000115745.
HOGENOMiHOG000228135.
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

MAEGVFQGAI GIDLGTTYSC VATYESSVEI IANEQGNRVT PSFVAFTPEE    50
RLIGDAAKNQ AALNPRNTVF DAKRLIGRRF DDESVQKDMK TWPFKVIDVD 100
GNPVIEVQYL EETKTFSPQE ISAMVLTKMK EIAEAKIGKK VEKAVITVPA 150
YFNDAQRQAT KDAGAISGLN VLRIINEPTA AAIAYGLGAG KSEKERHVLI 200
FDLGGGTFDV SLLHIAGGVY TVKSTSGNTH LGGQDFDTNL LEHFKAEFKK 250
KTGLDISDDA RALRRLRTAA ERAKRTLSSV TQTTVEVDSL FDGEDFESSL 300
TRARFEDLNA ALFKSTLEPV EQVLKDAKIS KSQIDEVVLV GGSTRIPKVQ 350
KLLSDFFDGK QLEKSINPDE AVAYGAAVQG AILTGQSTSD ETKDLLLLDV 400
APLSLGVGMQ GDMFGIVVPR NTTVPTIKRR TFTTCADNQT TVQFPVYQGE 450
RVNCKENTLL GEFDLKNIPM MPAGEPVLEA IFEVDANGIL KVTAVEKSTG 500
KSSNITISNA VGRLSSEEIE KMVNQAEEFK AADEAFAKKH EARQRLESYV 550
ASIEQTVTDP VLSSKLKRGS KSKIEAALSD ALAALQIEDP SADELRKAEV 600
GLKRVVTKAM SSR 613
Length:613
Mass (Da):66,602
Last modified:January 23, 2007 - v3
Checksum:iF16FA7C25A40321A
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti180 – 1845AAAIA → VVVIV in AAA34692. 1 Publication
Sequence conflicti189 – 1891A → V in AAA34692. 1 Publication
Sequence conflicti192 – 1921S → F in AAA34692. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S20149.
RefSeqi NP_010052.1. NM_001180289.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3GL1 X-ray 1.92 A/B 1-384 [» ]
ProteinModelPortali P11484.
SMRi P11484. Positions 2-601.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31882. 623 interactions.
DIPi DIP-2254N.
IntActi P11484. 741 interactions.
MINTi MINT-1325604.

2D gel databases

COMPLUYEAST-2DPAGE P11484.
SWISS-2DPAGE P11484.
UCD-2DPAGE P11484.

Proteomic databases

MaxQBi P11484.
PeptideAtlasi P11484.
PRIDEi P11484.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDL229W ; YDL229W ; YDL229W .
GeneIDi 851369.
KEGGi sce:YDL229W.

Organism-specific databases

SGDi S000002388. SSB1.

Phylogenomic databases

GeneTreei ENSGT00740000115745.
HOGENOMi HOG000228135.
OMAi FEEINST.
OrthoDBi EOG728916.

Enzyme and pathway databases

BioCyci YEAST:G3O-29608-MONOMER.

Miscellaneous databases

EvolutionaryTracei P11484.
NextBioi 968489.

Gene expression databases

Genevestigatori P11484.

Family and domain databases

Gene3Di 1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProi IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEi PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 146 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.

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

External Data

Dasty 3

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