UniProt Accession

 HSP71_RAT; Q07439; P42853; Q63256 

Genbank Protein ID

 L16764; X77208; X77207; X74271; X75357; BX883045; BX883045 

Genbank Nucleotide ID

 AAA17441.1; CAA54423.1; CAA54422.1; CAA52328.1; CAA53140.1; CAE83977.1; CAE83978.1 

Protein Name

 Heat shock 70 kDa protein 1A/1B 

Protein Synonyms/Alias

 Heat shock 70 kDa protein 1/2; HSP70-1/HSP70-2; HSP70.1/HSP70.2 

Gene Name

 Hspa1a; Hspa1b 

Gene Synonyms/Alias

 Hsp70-1; Hspa1; Hsp70-2; Hspa2 

Created Date

 July 27, 2013 

Organism

 Rattus norvegicus (Rat) 

NCBI Taxa ID

 10116 

Lysine Modification

Position	Peptide	Type	References
56	RLIGDAAKNQVALNP	acetylation	[1]
108	PKVQVNYKGENRSFY	acetylation	[1]
348	TRIPKVQKLLQDFFN	acetylation	[1]

Reference

 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 

Functional Description

 In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity). 

Sequence Annotation

 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 108 108 N6-acetyllysine (By similarity).
 MOD_RES 246 246 N6-acetyllysine (By similarity).
 MOD_RES 348 348 N6-acetyllysine (By similarity).
 MOD_RES 561 561 N6,N6,N6-trimethyllysine; by METTL21A; in
 MOD_RES 631 631 Phosphoserine (By similarity).
 MOD_RES 633 633 Phosphoserine (By similarity).
 MOD_RES 636 636 Phosphothreonine (By similarity).  

Keyword

 Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Methylation; Nucleotide-binding; Phosphoprotein; Reference proteome; Stress response. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 641 AA 

Protein Sequence

Gene Ontology

 GO:0016324; C:apical plasma membrane; IDA:RGD.
 GO:0016323; C:basolateral plasma membrane; IDA:RGD.
 GO:0005829; C:cytosol; IDA:RGD.
 GO:0016607; C:nuclear speck; ISS:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
 GO:0043234; C:protein complex; IDA:RGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0006952; P:defense response; IDA:RGD.
 GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
 GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
 GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:RGD.
 GO:0045906; P:negative regulation of vasoconstriction; IMP:RGD.
 GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:RGD.
 GO:0009612; P:response to mechanical stimulus; IEP:RGD.
 GO:0006986; P:response to unfolded protein; ISS:UniProtKB. 

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.