P11484 (HSP75_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heat shock protein SSB1

Alternative name(s):
Cold-inducible protein YG101

Gene names

Name:	SSB1
Synonyms:	YG101
Ordered Locus Names:	YDL229W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	613 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8
Subunit structure	Interacts with NAP1. Ref.13
Subcellular location	Cytoplasm. Note: Associated with translating ribosomes, may bind directly to the nascent polypeptide.
Miscellaneous	Present with 170000 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Biological process	Protein biosynthesis Stress response
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' cotranslational protein folding Inferred from direct assay PubMed 9670014. Source: SGD cellular response to glucose starvation Inferred from genetic interaction PubMed 19723765. Source: SGD cytoplasmic translation Inferred from mutant phenotype Ref.8. Source: SGD rRNA processing Inferred from genetic interaction PubMed 20368619. Source: SGD regulation of translational fidelity Inferred from mutant phenotype PubMed 15456889. Source: SGD ribosomal subunit export from nucleus Inferred from genetic interaction PubMed 20368619. Source: SGD translational termination Inferred from mutant phenotype PubMed 17483428. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 19502427. Source: SGD plasma membrane Inferred from direct assay PubMed 16622836. Source: SGD polysome Inferred from direct assay Ref.8PubMed 16413483. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from direct assay PubMed 9860955. Source: SGD calmodulin binding Inferred from direct assay PubMed 17146552. Source: SGD unfolded protein binding Inferred from direct assay PubMed 9670014. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BUD27	P43573	2	EBI-8627,EBI-22787

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 613

612

Heat shock protein SSB1

PRO_0000078389

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.9

Modified residue

26

1

Phosphoserine Ref.14

Modified residue

27

1

Phosphoserine Ref.14

Modified residue

47

1

Phosphothreonine Ref.11 Ref.14

Modified residue

289

1

Phosphoserine Ref.14

Modified residue

332

1

Phosphoserine Ref.14

Modified residue

503

1

Phosphoserine Ref.14

Modified residue

506

1

Phosphothreonine Ref.14

Modified residue

515

1

Phosphoserine Ref.12 Ref.14

Modified residue

516

1

Phosphoserine Ref.11 Ref.14

Modified residue

548

1

Phosphoserine Ref.11 Ref.14

Modified residue

549

1

Phosphotyrosine Ref.14

Modified residue

591

1

Phosphoserine Ref.14

Experimental info

Sequence conflict

180 – 184

5

AAAIA → VVVIV in AAA34692. Ref.7

Sequence conflict

189

1

A → V in AAA34692. Ref.7

Sequence conflict

192

1

S → F in AAA34692. Ref.7

Secondary structure

1

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613

Helix Strand Turn

Details...

Beta strand

10 – 13

4

Beta strand

16 – 30

15

Beta strand

38 – 41

4

Beta strand

44 – 46

3

Beta strand

51 – 54

4

Helix

55 – 59

5

Helix

61 – 63

3

Helix

65 – 67

3

Helix

72 – 74

3

Turn

75 – 77

3

Helix

83 – 89

7

Beta strand

93 – 99

7

Beta strand

102 – 109

8

Beta strand

112 – 116

5

Helix

118 – 137

20

Beta strand

143 – 148

6

Helix

154 – 166

13

Beta strand

170 – 176

7

Helix

177 – 184

8

Turn

185 – 190

6

Beta strand

196 – 203

8

Beta strand

208 – 216

9

Beta strand

219 – 228

10

Helix

233 – 252

20

Helix

260 – 276

17

Turn

277 – 279

3

Beta strand

280 – 291

12

Beta strand

294 – 301

8

Helix

302 – 308

7

Helix

310 – 315

6

Helix

317 – 327

11

Helix

331 – 333

3

Beta strand

336 – 341

6

Helix

342 – 345

4

Helix

347 – 356

10

Turn

357 – 359

3

Turn

368 – 370

3

Helix

371 – 383

13

Sequences

	Sequence		Length	Mass (Da)
	P11484 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F16FA7C25A40321A	FASTA	613	66,602
	10 20 30 40 50 60 MAEGVFQGAI GIDLGTTYSC VATYESSVEI IANEQGNRVT PSFVAFTPEE RLIGDAAKNQ 70 80 90 100 110 120 AALNPRNTVF DAKRLIGRRF DDESVQKDMK TWPFKVIDVD GNPVIEVQYL EETKTFSPQE 130 140 150 160 170 180 ISAMVLTKMK EIAEAKIGKK VEKAVITVPA YFNDAQRQAT KDAGAISGLN VLRIINEPTA 190 200 210 220 230 240 AAIAYGLGAG KSEKERHVLI FDLGGGTFDV SLLHIAGGVY TVKSTSGNTH LGGQDFDTNL 250 260 270 280 290 300 LEHFKAEFKK KTGLDISDDA RALRRLRTAA ERAKRTLSSV TQTTVEVDSL FDGEDFESSL 310 320 330 340 350 360 TRARFEDLNA ALFKSTLEPV EQVLKDAKIS KSQIDEVVLV GGSTRIPKVQ KLLSDFFDGK 370 380 390 400 410 420 QLEKSINPDE AVAYGAAVQG AILTGQSTSD ETKDLLLLDV APLSLGVGMQ GDMFGIVVPR 430 440 450 460 470 480 NTTVPTIKRR TFTTCADNQT TVQFPVYQGE RVNCKENTLL GEFDLKNIPM MPAGEPVLEA 490 500 510 520 530 540 IFEVDANGIL KVTAVEKSTG KSSNITISNA VGRLSSEEIE KMVNQAEEFK AADEAFAKKH 550 560 570 580 590 600 EARQRLESYV ASIEQTVTDP VLSSKLKRGS KSKIEAALSD ALAALQIEDP SADELRKAEV 610 GLKRVVTKAM SSR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"Protein identifications for a Saccharomyces cerevisiae protein database." Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S. Electrophoresis 15:1466-1486(1994) [PubMed] [Europe PMC] [Abstract] 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]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47; SER-516 AND SER-548, MASS SPECTROMETRY. Strain: YAL6B.
[12]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, MASS SPECTROMETRY.
[13]	"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, MASS SPECTROMETRY.
[14]	"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 SER-26; SER-27; THR-47; SER-289; SER-332; SER-503; THR-506; SER-515; SER-516; SER-548; TYR-549 AND SER-591, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

S20149.

RefSeq

NP_010052.1. NM_001180289.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GL1	X-ray	1.92	A/B	1-384	[»]

ProteinModelPortal

P11484.

SMR

P11484. Positions 2-601.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2254N.

IntAct

P11484. 738 interactions.

MINT

MINT-1325604.

2D gel databases

COMPLUYEAST-2DPAGE

P11484.

SWISS-2DPAGE

P11484.

UCD-2DPAGE

P11484.

Proteomic databases

PeptideAtlas

P11484.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDL229W; YDL229W; YDL229W.

GeneID

851369.

KEGG

sce:YDL229W.

Organism-specific databases

SGD

S000002388. SSB1.

Phylogenomic databases

GeneTree

ENSGT00700000104565.

HOGENOM

HOG000228135.

OMA

EIDANGL.

OrthoDB

EOG43FM54.

Gene expression databases

ArrayExpress

P11484.

Genevestigator

P11484.

GermOnline

YDL229W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view]

Pfam

PF00012. HSP70. 1 hit.
[Graphical view]

PRINTS

PR00301. HEATSHOCK70.

PROSITE

PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P11484.

NextBio

968489.

Entry information

Entry name

HSP75_YEAST

Accession

Primary (citable) accession number: P11484
Secondary accession number(s): D6VRC7, Q05834

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 136 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program