UniProt Accession

 HSP71_YEAST; P10591; D6VPL2 

Genbank Protein ID

 X12926; L22015; BK006935 

Genbank Nucleotide ID

 CAA31393.1; AAC04952.1; DAA06982.1 

Protein Name

 Heat shock protein SSA1 

Protein Synonyms/Alias

 Heat shock protein YG100 

Gene Name

 SSA1 

Gene Synonyms/Alias

 YAL005C 

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
54	RLIGDAAKNQAAMNP	acetylation	[1]
54	RLIGDAAKNQAAMNP	ubiquitination	[2, 3]
86	PEVQADMKHFPFKLI	acetylation	[1]
98	KLIDVDGKPQIQVEF	acetylation	[1]
98	KLIDVDGKPQIQVEF	ubiquitination	[3]
106	PQIQVEFKGETKNFT	acetylation	[1]
110	VEFKGETKNFTPEQI	acetylation	[1]
110	VEFKGETKNFTPEQI	ubiquitination	[3]
124	ISSMVLGKMKETAES	acetylation	[1]
126	SMVLGKMKETAESYL	ubiquitination	[3]
136	AESYLGAKVNDAVVT	acetylation	[1]
136	AESYLGAKVNDAVVT	ubiquitination	[3]
157	DSQRQATKDAGTIAG	acetylation	[1]
157	DSQRQATKDAGTIAG	ubiquitination	[2, 3]
243	NHFIQEFKRKNKKDL	acetylation	[1]
243	NHFIQEFKRKNKKDL	ubiquitination	[2, 3]
316	STLDPVEKVLRDAKL	acetylation	[1]
316	STLDPVEKVLRDAKL	ubiquitination	[3]
325	LRDAKLDKSQVDEIV	acetylation	[1]
345	TRIPKVQKLVTDYFN	acetylation	[1]
354	VTDYFNGKEPNRSIN	acetylation	[1]
354	VTDYFNGKEPNRSIN	ubiquitination	[3]
509	NDKGRLSKEDIEKMV	acetylation	[1]
509	NDKGRLSKEDIEKMV	ubiquitination	[3, 4]
514	LSKEDIEKMVAEAEK	acetylation	[1]
521	KMVAEAEKFKEEDEK	acetylation	[1]
521	KMVAEAEKFKEEDEK	ubiquitination	[3, 5, 6]
528	KFKEEDEKESQRIAS	acetylation	[1]
528	KFKEEDEKESQRIAS	ubiquitination	[2]
536	ESQRIASKNQLESIA	glycation	[7]
536	ESQRIASKNQLESIA	ubiquitination	[2, 3, 4, 5, 6]
547	ESIAYSLKNTISEAG	acetylation	[1]
556	TISEAGDKLEQADKD	acetylation	[1]
556	TISEAGDKLEQADKD	ubiquitination	[2, 3]
562	DKLEQADKDTVTKKA	acetylation	[1]
592	EEFDDKLKELQDIAN	acetylation	[1]

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] 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]
 [3] 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]
 [4] A perturbed ubiquitin landscape distinguishes between ubiquitin in trafficking and in proteolysis.
 Ziv I, Matiuhin Y, Kirkpatrick DS, Erpapazoglou Z, Leon S, Pantazopoulou M, Kim W, Gygi SP, Haguenauer-Tsapis R, Reis N, Glickman MH, Kleifeld O.
 Mol Cell Proteomics. 2011 May;10(5):M111.009753. [PMID: 21427232]
 [5] A proteomics approach to understanding protein ubiquitination.
 Peng J, Schwartz D, Elias JE, Thoreen CC, Cheng D, Marsischky G, Roelofs J, Finley D, Gygi SP.
 Nat Biotechnol. 2003 Aug;21(8):921-6. [PMID: 12872131]
 [6] 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]
 [7] Yeast protein glycation in vivo by methylglyoxal. Molecular modification of glycolytic enzymes and heat shock proteins.
 Gomes RA, Vicente Miranda H, Silva MS, Graça G, Coelho AV, Ferreira AE, Cordeiro C, Freire AP.
 FEBS J. 2006 Dec;273(23):5273-87. [PMID: 17064314] 

Functional Description

 May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A functional difference between SSA1 and SSA2 proteins is expected. SSA1 can participate in the ATP-dependent disassembly of clathrin-coated vesicles. 

Sequence Annotation

 MOD_RES 2 2 N-acetylserine.
 MOD_RES 35 35 Phosphothreonine (By similarity).
 MOD_RES 36 36 Phosphothreonine (By similarity).
 MOD_RES 62 62 Phosphoserine.
 MOD_RES 426 426 Phosphoserine (By similarity).
 MOD_RES 551 551 Phosphoserine.
 MOD_RES 603 603 Phosphoserine.
 CROSSLNK 521 521 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 536 536 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 3D-structure; Acetylation; ATP-binding; Cell wall; Complete proteome; Cytoplasm; Direct protein sequencing; Isopeptide bond; Nucleotide-binding; Phosphoprotein; Reference proteome; Secreted; Stress response; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 642 AA 

Protein Sequence

Gene Ontology

 GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
 GO:0009277; C:fungal-type cell wall; IDA:SGD.
 GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
 GO:0005634; C:nucleus; 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:0051082; F:unfolded protein binding; IDA:SGD.
 GO:0002181; P:cytoplasmic translation; IMP:SGD.
 GO:0000060; P:protein import into nucleus, translocation; IDA:SGD.
 GO:0042026; P:protein refolding; IDA:SGD.
 GO:0006626; P:protein targeting to mitochondrion; IMP:SGD.
 GO:0006950; P:response to stress; IEA:UniProtKB-KW.
 GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IDA: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.