CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008877
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heat shock-related 70 kDa protein 2 
Protein Synonyms/Alias
 Heat shock 70 kDa protein 2 
Gene Name
 HSPA2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
109PKVQVEYKGETKTFFubiquitination[1]
188AIAYGLDKKGCAGGEubiquitination[2]
351TRIPKIQKLLQDFFNubiquitination[1]
454EGERAMTKDNNLLGKubiquitination[1]
500AADKSTGKENKITITubiquitination[1]
503KSTGKENKITITNDKubiquitination[1]
510KITITNDKGRLSKDDubiquitination[1]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865] 
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
 3D-structure; ATP-binding; Chaperone; Complete proteome; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 639 AA 
Protein Sequence
MSARGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER LIGDAAKNQV 60
AMNPTNTIFD AKRLIGRKFE DATVQSDMKH WPFRVVSEGG KPKVQVEYKG ETKTFFPEEI 120
SSMVLTKMKE IAEAYLGGKV HSAVITVPAY 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
AKNALESYTY NIKQTVEDEK LRGKISEQDK NKILDKCQEV INWLDRNQMA EKDEYEHKQK 600
ELERVCNPII SKLYQGGPGG GSGGGGSGAS GGPTIEEVD 639 
Gene Ontology
 GO:0036128; C:CatSper complex; ISS:UniProtKB.
 GO:0009986; C:cell surface; IDA:UniProtKB.
 GO:0001673; C:male germ cell nucleus; IEA:Compara.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0000795; C:synaptonemal complex; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0051861; F:glycolipid binding; IEA:Compara.
 GO:0051082; F:unfolded protein binding; TAS:ProtInc.
 GO:0007140; P:male meiosis; TAS:ProtInc.
 GO:0007141; P:male meiosis I; IEA:Compara.
 GO:0031662; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G2/M transition of mitotic cell cycle; IEA:Compara.
 GO:0006986; P:response to unfolded protein; TAS:ProtInc.
 GO:0007286; P:spermatid development; TAS:ProtInc.
 GO:0070194; P:synaptonemal complex disassembly; IEA:Compara. 
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.