CPLM-003808

Genbank Nucleotide ID

Heat shock protein SSA2

Protein Synonyms/Alias

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

Position	Peptide	Type	References
54	RLIGDAAKNQAAMNP	acetylation	[1]
54	RLIGDAAKNQAAMNP	ubiquitination	[2]
69	ANTVFDAKRLIGRNF	acetylation	[1]
86	PEVQGDMKHFPFKLI	acetylation	[1]
86	PEVQGDMKHFPFKLI	ubiquitination	[2]
421	NSTIPTKKSEVFSTY	ubiquitination	[2]
556	TISEAGDKLEQADKD	ubiquitination	[3, 4, 5, 6, 7]
562	DKLEQADKDAVTKKA	acetylation	[1]
592	EEFDDQLKELQEVAN	acetylation	[1]

[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] 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]
[4] Computational identification of ubiquitylation sites from protein sequences.
Tung CW, Ho SY.
BMC Bioinformatics. 2008 Jul 15;9:310. [PMID: 18625080]
[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] 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]
[7] 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]

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. SSA2 can participate in the ATP-dependent disassembly of clathrin-coated vesicles.

MOD_RES 2 2 N-acetylserine.
MOD_RES 20 20 Phosphoserine.
MOD_RES 35 35 Phosphothreonine.
MOD_RES 36 36 Phosphothreonine.
MOD_RES 426 426 Phosphoserine.
MOD_RES 551 551 Phosphoserine.
MOD_RES 603 603 Phosphoserine (By similarity).
CROSSLNK 556 556 Glycyl lysine isopeptide (Lys-Gly)

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

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; IDA:SGD.
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:0005739; C:mitochondrion; IDA:SGD.
GO:0005886; C:plasma membrane; IDA:SGD.
GO:0005844; C:polysome; IDA:SGD.
GO:0005524; F:ATP binding; IDA:SGD.
GO:0016887; F:ATPase activity; ISS:SGD.
GO:0051082; F:unfolded protein binding; IGI:SGD.
GO:0006457; P:protein folding; IDA:SGD.
GO:0006950; P:response to stress; IEA:UniProtKB-KW.
GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IMP:SGD.

IPR018181; Heat_shock_70_CS.
IPR013126; Hsp_70_fam.

PS00297; HSP70_1
PS00329; HSP70_2
PS01036; HSP70_3

PR00301; HEATSHOCK70.