CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008943
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heat shock 70 kDa protein 1-like 
Protein Synonyms/Alias
 Heat shock 70 kDa protein 1L; Heat shock 70 kDa protein 3; HSP70.3 
Gene Name
 Hspa1l 
Gene Synonyms/Alias
 Hsp70-3 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
79AKRLIGRKFNDPVVQacetylation[1]
110PKVLVSYKGEKKAFYacetylation[1]
189AIAYGLDKGSHGERHacetylation[1]
248SHFVEEFKRKHKKDIacetylation[1]
350TRIPKVQKLLQDYFNacetylation[1]
502KSTGKANKITITNDKacetylation[1]
514NDKGRLSKEEIERMVacetylation[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
  
Keyword
 ATP-binding; Chaperone; Complete proteome; Nucleotide-binding; Reference proteome; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 641 AA 
Protein Sequence
MAANKGMAIG IDLGTTYSCV GVFQHGKVEI IANDQGNRTT PSYVAFTDTE RLIGDAAKNQ 60
VAMNPQNTVF DAKRLIGRKF NDPVVQSDMK LWPFQVINEA GKPKVLVSYK GEKKAFYPEE 120
ISSMVLTKMK ETAEAFLGHS VTNAVITVPA YFNDSQRQAT KDAGVIAGLN VLRIINEPTA 180
AAIAYGLDKG SHGERHVLIF DLGGGTFDVS ILTIDDGIFE VKATAGDTHL GGEDFDNRLV 240
SHFVEEFKRK HKKDISQNKR AVRRLRTACE RAKRTLSSST QANLEIDSLY EGIDFYTSIT 300
RARFEELCAD LFRGTLEPVE KSLRDAKMDK AKIHDIVLVG GSTRIPKVQK LLQDYFNGRD 360
LNKSINPDEA VAYGAAVQAA ILMGDKSEKV QDLLLLDVAP LSLGLETAGG VMTVLIKRNS 420
TIPTKQTQIF TTYSDNQPGV LIQVYEGERA MTRDNNLLGR FDLTGIPPAP RGVPQIEVTF 480
DIDANGILNV TAMDKSTGKA NKITITNDKG RLSKEEIERM VQEAERYKAE DEGQREKIAA 540
KNALESYAFN MKSAVGDEGL KDKISESDKK KILDKCSEVL SWLEANQLAE KEEFDHKRKE 600
LENMCNPIIT KLYQSGCTGP TCAPGYTPGR AATGPTIEEV D 641 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IDA:MGI.
 GO:0008180; C:signalosome; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0006950; P:response to stress; IEA:UniProtKB-KW. 
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.