UniProt Accession

 HS74L_HUMAN; O95757; A2ICT2; Q4W5M5; Q8IWA2 

Genbank Protein ID

 AB023421; EF197155; AC093591; CH471056; BC040560 

Genbank Nucleotide ID

 BAA75063.1; ABM69040.1; AAY40975.1; EAX05198.1; AAH40560.1 

Protein Name

 Heat shock 70 kDa protein 4L 

Protein Synonyms/Alias

 Heat shock 70-related protein APG-1; Osmotic stress protein 94 

Gene Name

 HSPA4L 

Gene Synonyms/Alias

 APG1; OSP94 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
53	RAIGNAAKSQIVTNV	ubiquitination	[1, 2]
194	DLPPLDEKPRNVVFI	ubiquitination	[1, 3]
219	VCAFNKGKLKVLATT	acetylation	[4]
221	AFNKGKLKVLATTFD	acetylation	[4]
249	DYFCDEFKTKYKINV	ubiquitination	[1]
272	RLYQECEKLKKLMSA	acetylation	[5]
356	AVKEQITKFFLKDIS	ubiquitination	[6]
360	QITKFFLKDISTTLN	ubiquitination	[1, 2]
407	YSITLRWKTSFEDGS	ubiquitination	[3]
774	KVSEIVAKSKELDNF	ubiquitination	[2]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473] 

Functional Description

 Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase (By similarity). 

Sequence Annotation

 MOD_RES 74 74 Phosphoserine (By similarity).
 MOD_RES 761 761 Phosphothreonine.  

Keyword

 ATP-binding; Chaperone; Complete proteome; Cytoplasm; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Stress response. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 839 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0005524; F:ATP binding; ISS:UniProtKB.
 GO:0006457; P:protein folding; ISS:UniProtKB.
 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.