CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004621
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heat shock 70 kDa protein 1B 
Protein Synonyms/Alias
 Heat shock 70 kDa protein 1; HSP70.1 
Gene Name
 Hspa1b 
Gene Synonyms/Alias
 Hcp70.1; Hsp70-1; Hsp70a1; Hspa1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
3*****MAKNTAIGIDubiquitination[1]
56RLIGDAAKNQVALNPacetylation[2]
56RLIGDAAKNQVALNPubiquitination[1]
71QNTVFDAKRLIGRKFubiquitination[1]
77AKRLIGRKFGDAVVQacetylation[3]
108PKVQVNYKGESRSFFubiquitination[1]
126ISSMVLTKMKEIAEAubiquitination[1]
190YGLDRTGKGERNVLIubiquitination[1]
348TRIPKVQKLLQDFFNubiquitination[1]
539QRDRVAAKNALESYAubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 
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 632 632 Phosphoserine (By similarity).
 MOD_RES 634 634 Phosphoserine (By similarity).
 MOD_RES 637 637 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
 642 AA 
Protein Sequence
MAKNTAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA 60
LNPQNTVFDA KRLIGRKFGD AVVQSDMKHW PFQVVNDGDK PKVQVNYKGE SRSFFPEEIS 120
SMVLTKMKEI AEAYLGHPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA 180
IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVSH 240
FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA 300
RFEELCSDLF RGTLEPVEKA LRDAKMDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN 360
KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI 420
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT RDNNLLGRFE LSGIPPAPRG VPQIEVTFDI 480
DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAERYKAEDE VQRDRVAAKN 540
ALESYAFNMK SAVEDEGLKG KLSEADKKKV LDKCQEVISW LDSNTLADKE EFVHKREELE 600
RVCSPIISGL YQGAGAPGAG GFGAQAPPKG ASGSGPTIEE VD 642 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 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.