CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004545
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heat shock-related 70 kDa protein 2 
Protein Synonyms/Alias
 Heat shock protein 70.2 
Gene Name
 Hspa2 
Gene Synonyms/Alias
 Hcp70.2; Hsp70-2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
78AKRLIGRKFEDATVQubiquitination[1]
160DSQRQATKDAGTITGubiquitination[1]
188AIAYGLDKKGCAGGEacetylation[2, 3, 4]
188AIAYGLDKKGCAGGEsuccinylation[4]
188AIAYGLDKKGCAGGEubiquitination[1]
328EKALRDAKLDKGQIQubiquitination[1]
351TRIPKIQKLLQDFFNacetylation[2, 3, 4, 5]
351TRIPKIQKLLQDFFNubiquitination[1]
360LQDFFNGKELNKSINacetylation[2, 4]
360LQDFFNGKELNKSINubiquitination[1]
454EGERAMTKDNNLLGKacetylation[4]
454EGERAMTKDNNLLGKsuccinylation[4]
454EGERAMTKDNNLLGKubiquitination[1]
500AADKSTGKENKITITubiquitination[1]
503KSTGKENKITITNDKubiquitination[1]
510KITITNDKGRLSKDDubiquitination[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] 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]
 [3] 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]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [5] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758] 
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. 
Sequence Annotation
 MOD_RES 403 403 Phosphoserine (By similarity).
 MOD_RES 408 408 Phosphothreonine (By similarity).
 MOD_RES 414 414 Phosphothreonine (By similarity).  
Keyword
 ATP-binding; Chaperone; Complete proteome; Nucleotide-binding; Phosphoprotein; Reference proteome; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 633 AA 
Protein Sequence
MSARGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER LIGDAAKNQV 60
AMNPTNTIFD AKRLIGRKFE DATVQSDMKH WPFRVVSEGG KPKVQVEYKG EMKTFFPEEI 120
SSMVLTKMKE IAEAYLGGKV QSAVITVPAY FNDSQRQATK DAGTITGLNV LRIINEPTAA 180
AIAYGLDKKG CAGGEKNVLI FDLGGGTFDV SILTIEDGIF EVKSTAGDTH LGGEDFDNRM 240
VSHLAEEFKR KHKKDIGPNK RAVRRLRTAC ERAKRTLSSS TQASIEIDSL YEGVDFYTSI 300
TRARFEELNA DLFRGTLEPV EKALRDAKLD KGQIQEIVLV GGSTRIPKIQ KLLQDFFNGK 360
ELNKSINPDE AVAYGAAVQA AILIGDKSEN VQDLLLLDVT PLSLGIETAG GVMTPLIKRN 420
TTIPTKQTQT FTTYSDNQSS VLVQVYEGER AMTKDNNLLG KFDLTGIPPA PRGVPQIEVT 480
FDIDANGILN VTAADKSTGK ENKITITNDK GRLSKDDIDR MVQEAERYKS EDEANRDRVA 540
AKNAVESYTY NIKQTVEDEK LRGKISEQDK NKILDKCQEV INWLDRNQMA EKDEYEHKQK 600
ELERVCNPII SKLYQGGPGG GGSSGGPTIE EVD 633 
Gene Ontology
 GO:0036128; C:CatSper complex; IDA:UniProtKB.
 GO:0009986; C:cell surface; IDA:MGI.
 GO:0001673; C:male germ cell nucleus; IDA:MGI.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0000795; C:synaptonemal complex; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0051861; F:glycolipid binding; IDA:MGI.
 GO:0007141; P:male meiosis I; IMP:MGI.
 GO:0031662; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G2/M transition of mitotic cell cycle; IMP:MGI.
 GO:0006950; P:response to stress; IEA:UniProtKB-KW.
 GO:0007286; P:spermatid development; IMP:MGI.
 GO:0070194; P:synaptonemal complex disassembly; IMP:MGI. 
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.