CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-036899
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Heat shock 70 kDa protein 1A/1B 
Protein Synonyms/Alias
  
Gene Name
 HSPA1A 
Gene Synonyms/Alias
 HSPA1B 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
3*****MAKAAAIGIDacetylation[1]
3*****MAKAAAIGIDubiquitination[2, 3]
35ISSMVLTKMKEIAEAubiquitination[4]
37SMVLTKMKEIAEAYLubiquitination[4, 5]
68DSQRQATKDAGVIAGubiquitination[2, 3, 4, 5, 6, 7, 8, 9]
99YGLDRTGKGERNVLIubiquitination[4]
155NHFVEEFKRKHKKDIacetylation[1, 10]
155NHFVEEFKRKHKKDIubiquitination[2, 4, 5, 7, 8]
166KKDISQNKRAVRRLRubiquitination[2, 9]
228STLEPVEKALRDAKLacetylation[1, 10]
228STLEPVEKALRDAKLubiquitination[2, 3, 4, 7, 8]
234EKALRDAKLDKAQIHubiquitination[7]
237LRDAKLDKAQIHDLVubiquitination[2, 3, 4, 5, 8]
257TRIPKVQKLLQDFFNacetylation[1, 10]
257TRIPKVQKLLQDFFNubiquitination[2, 3, 4, 5, 6, 7, 8, 11, 12]
270FNGRDLNKSINPDEAubiquitination[2, 5, 7, 8]
324GVMTALIKRNSTIPTubiquitination[8]
332RNSTIPTKQTQIFTTubiquitination[2, 4, 5, 7, 8]
360EGERAMTKDNNLLGRubiquitination[2, 3, 5, 7, 8, 9, 12]
406ATDKSTGKANKITITubiquitination[2]
409KSTGKANKITITNDKacetylation[10]
409KSTGKANKITITNDKubiquitination[2, 3, 4, 7, 8, 12]
416KITITNDKGRLSKEEubiquitination[7]
421NDKGRLSKEEIERMVacetylation[12]
421NDKGRLSKEEIERMVubiquitination[2, 3, 4, 5, 6, 7, 8, 12]
433RMVQEAEKYKAEDEVacetylation[1]
433RMVQEAEKYKAEDEVubiquitination[2, 3, 5, 6, 7, 8, 9, 12]
435VQEAEKYKAEDEVQRacetylation[10, 12]
435VQEAEKYKAEDEVQRubiquitination[2, 4, 5, 7, 8, 12]
448QRERVSAKNALESYAubiquitination[2, 3, 4, 5, 7, 12]
459ESYAFNMKSAVEDEGacetylation[1]
459ESYAFNMKSAVEDEGubiquitination[2, 4, 5, 7, 8, 12]
468AVEDEGLKGKISEADubiquitination[2, 4, 5, 7, 8]
470EDEGLKGKISEADKKmethylation[13]
470EDEGLKGKISEADKKubiquitination[2, 7]
476GKISEADKKKVLDKCmethylation[13]
477KISEADKKKVLDKCQmethylation[13]
478ISEADKKKVLDKCQEubiquitination[5]
482DKKKVLDKCQEVISWubiquitination[7, 8]
498DANTLAEKDEFEHKRubiquitination[5]
504EKDEFEHKRKELEQVubiquitination[5]
506DEFEHKRKELEQVCNphosphoglycerylation[14]
506DEFEHKRKELEQVCNubiquitination[2, 3, 4, 5, 7, 8, 12]
537GFGAQGPKGGSGSGPubiquitination[2, 4, 5, 7, 9, 12]
Reference
 [1] 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]
 [2] 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]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] 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]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [7] 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]
 [8] 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]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [10] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [11] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [12] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [13] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
 Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
 Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837]
 [14] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 550 AA 
Protein Sequence
MAKAAAIGID LGTTYSCVGV FQHGKVQISS MVLTKMKEIA EAYLGYPVTN AVITVPAYFN 60
DSQRQATKDA GVIAGLNVLR IINEPTAAAI AYGLDRTGKG ERNVLIFDLG GGTFDVSILT 120
IDDGIFEVKA TAGDTHLGGE DFDNRLVNHF VEEFKRKHKK DISQNKRAVR RLRTACERAK 180
RTLSSSTQAS LEIDSLFEGI DFYTSITRAR FEELCSDLFR STLEPVEKAL RDAKLDKAQI 240
HDLVLVGGST RIPKVQKLLQ DFFNGRDLNK SINPDEAVAY GAAVQAAILM GDKSENVQDL 300
LLLDVAPLSL GLETAGGVMT ALIKRNSTIP TKQTQIFTTY SDNQPGVLIQ VYEGERAMTK 360
DNNLLGRFEL SGIPPAPRGV PQIEVTFDID ANGILNVTAT DKSTGKANKI TITNDKGRLS 420
KEEIERMVQE AEKYKAEDEV QRERVSAKNA LESYAFNMKS AVEDEGLKGK ISEADKKKVL 480
DKCQEVISWL DANTLAEKDE FEHKRKELEQ VCNPIISGLY QGAGGPGPGG FGAQGPKGGS 540
GSGPTIEEVD 550 
Gene Ontology
 GO:0005524; F:ATP binding; 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.