UniProt Accession

 HSP75_YEAST; P11484; D6VRC7; Q05834 

Genbank Protein ID

 X13713; M25395; Z74277; M17585; BK006938 

Genbank Nucleotide ID

 CAA31995.1; AAA35099.1; CAA98807.1; AAA34692.1; DAA11637.1 

Protein Name

 Heat shock protein SSB1 

Protein Synonyms/Alias

 Cold-inducible protein YG101 

Gene Name

 SSB1 

Gene Synonyms/Alias

 YG101; YDL229W 

Created Date

 July 27, 2013 

Organism

 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 

NCBI Taxa ID

 559292 

Lysine Modification

Position	Peptide	Type	References
58	RLIGDAAKNQAALNP	acetylation	[1]
58	RLIGDAAKNQAALNP	ubiquitination	[2]
87	FDDESVQKDMKTWPF	acetylation	[1]
87	FDDESVQKDMKTWPF	ubiquitination	[2, 3]
90	ESVQKDMKTWPFKVI	acetylation	[1, 4]
95	DMKTWPFKVIDVDGN	acetylation	[4]
130	AMVLTKMKEIAEAKI	acetylation	[1]
130	AMVLTKMKEIAEAKI	ubiquitination	[2]
136	MKEIAEAKIGKKVEK	acetylation	[1]
161	DAQRQATKDAGAISG	acetylation	[1]
161	DAQRQATKDAGAISG	ubiquitination	[2]
191	AYGLGAGKSEKERHV	acetylation	[1]
251	FKAEFKKKTGLDISD	ubiquitination	[2]
314	DLNAALFKSTLEPVE	acetylation	[1]
314	DLNAALFKSTLEPVE	ubiquitination	[5]
325	EPVEQVLKDAKISKS	acetylation	[1]
325	EPVEQVLKDAKISKS	ubiquitination	[2]
331	LKDAKISKSQIDEVV	acetylation	[1]
331	LKDAKISKSQIDEVV	ubiquitination	[2]
351	TRIPKVQKLLSDFFD	acetylation	[1]
351	TRIPKVQKLLSDFFD	ubiquitination	[2]
360	LSDFFDGKQLEKSIN	acetylation	[1]
364	FDGKQLEKSINPDEA	acetylation	[1]
428	NTTVPTIKRRTFTTC	acetylation	[1]
428	NTTVPTIKRRTFTTC	ubiquitination	[2]
466	LLGEFDLKNIPMMPA	acetylation	[4]
497	LKVTAVEKSTGKSSN	acetylation	[1]
497	LKVTAVEKSTGKSSN	ubiquitination	[2]
501	AVEKSTGKSSNITIS	ubiquitination	[2]
521	LSSEEIEKMVNQAEE	acetylation	[1]
521	LSSEEIEKMVNQAEE	ubiquitination	[2, 3]
530	VNQAEEFKAADEAFA	acetylation	[1]
530	VNQAEEFKAADEAFA	ubiquitination	[2]
538	AADEAFAKKHEARQR	acetylation	[1, 4]
538	AADEAFAKKHEARQR	ubiquitination	[2]
539	ADEAFAKKHEARQRL	acetylation	[4]
565	TDPVLSSKLKRGSKS	acetylation	[1]
565	TDPVLSSKLKRGSKS	ubiquitination	[2, 3, 6]
571	SKLKRGSKSKIEAAL	acetylation	[4]
573	LKRGSKSKIEAALSD	acetylation	[4]
573	LKRGSKSKIEAALSD	ubiquitination	[3]
597	PSADELRKAEVGLKR	ubiquitination	[2]
603	RKAEVGLKRVVTKAM	acetylation	[4]
608	GLKRVVTKAMSSR**	ubiquitination	[2]

Reference

 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [3] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [4] mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
 Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Côté J, Figeys DA, Baetz K.
 Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. [PMID: 23572591]
 [5] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269]
 [6] Systematic approach for validating the ubiquitinated proteome.
 Seyfried NT, Xu P, Duong DM, Cheng D, Hanfelt J, Peng J.
 Anal Chem. 2008 Jun 1;80(11):4161-9. [PMID: 18433149] 

Functional Description

 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. 

Sequence Annotation

 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 47 47 Phosphothreonine.
 MOD_RES 431 431 Phosphothreonine.  

Keyword

 3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome; Stress response. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 613 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005886; C:plasma membrane; IDA:SGD.
 GO:0005844; C:polysome; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; IDA:SGD.
 GO:0005516; F:calmodulin binding; IDA:SGD.
 GO:0051082; F:unfolded protein binding; IDA:SGD.
 GO:0051083; P:'de novo' cotranslational protein folding; IDA:SGD.
 GO:0042149; P:cellular response to glucose starvation; IGI:SGD.
 GO:0002181; P:cytoplasmic translation; IMP:SGD.
 GO:0006450; P:regulation of translational fidelity; IMP:SGD.
 GO:0000054; P:ribosomal subunit export from nucleus; IGI:SGD.
 GO:0006364; P:rRNA processing; IGI:SGD.
 GO:0006415; P:translational termination; IMP:SGD. 

Interpro

 IPR018181; Heat_shock_70_CS.
 IPR013126; Hsp_70_fam. 

Pfam

 PF00012; HSP70 

SMART

  

PROSITE

 PS00297; HSP70_1
 PS00329; HSP70_2
 PS01036; HSP70_3 

PRINTS

 PR00301; HEATSHOCK70.