CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006963
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Stress-70 protein, mitochondrial 
Protein Synonyms/Alias
 75 kDa glucose-regulated protein; GRP-75; Heat shock 70 kDa protein 9; Mortalin; MOT; Peptide-binding protein 74; PBP74 
Gene Name
 HSPA9 
Gene Synonyms/Alias
 GRP75; HSPA9B; mt-HSP70 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
76VMEGKQAKVLENAEGubiquitination[1]
106RLVGMPAKRQAVTNPubiquitination[2]
121NNTFYATKRLIGRRYubiquitination[1, 2, 3, 4]
135YDDPEVQKDIKNVPFacetylation[5, 6]
135YDDPEVQKDIKNVPFubiquitination[1, 2]
138PEVQKDIKNVPFKIVacetylation[5]
138PEVQKDIKNVPFKIVubiquitination[1, 7, 8]
143DIKNVPFKIVRASNGacetylation[5]
143DIKNVPFKIVRASNGubiquitination[2]
159AWVEAHGKLYSPSQIacetylation[9]
175AFVLMKMKETAENYLubiquitination[1]
206DSQRQATKDAGQISGacetylation[9, 10]
206DSQRQATKDAGQISGmalonylation[11]
206DSQRQATKDAGQISGubiquitination[1, 2, 10]
234ALAYGLDKSEDKVIAacetylation[5, 9]
234ALAYGLDKSEDKVIAubiquitination[1, 12]
265QKGVFEVKSTNGDTFubiquitination[1]
288ALLRHIVKEFKRETGacetylation[5, 6, 10, 13]
300ETGVDLTKDNMALQRacetylation[5, 9, 10, 13]
300ETGVDLTKDNMALQRubiquitination[1, 2]
345GPKHLNMKLTRAQFEacetylation[5]
368RTIAPCQKAMQDAEVubiquitination[2, 7, 8]
377MQDAEVSKSDIGEVIubiquitination[1]
394GGMTRMPKVQQTVQDubiquitination[1, 2]
567NMVKNAEKYAEEDRRacetylation[5]
595IIHDTETKMEEFKDQacetylation[5]
600ETKMEEFKDQLPADEacetylation[9, 10]
612ADECNKLKEEISKMRacetylation[9, 10, 14]
612ADECNKLKEEISKMRubiquitination[2]
646SLQQASLKLFEMAYKacetylation[5, 9]
646SLQQASLKLFEMAYKubiquitination[7, 8]
653KLFEMAYKKMASEREubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [6] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [7] 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]
 [8] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [9] 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]
 [10] 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]
 [11] The first identification of lysine malonylation substrates and its regulatory enzyme.
 Peng C, Lu Z, Xie Z, Cheng Z, Chen Y, Tan M, Luo H, Zhang Y, He W, Yang K, Zwaans BM, Tishkoff D, Ho L, Lombard D, He TC, Dai J, Verdin E, Ye Y, Zhao Y.
 Mol Cell Proteomics. 2011 Dec;10(12):M111.012658. [PMID: 21908771]
 [12] 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]
 [13] 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]
 [14] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330
Functional Description
 Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone. 
Sequence Annotation
 MOD_RES 135 135 N6-acetyllysine.
 MOD_RES 138 138 N6-acetyllysine.
 MOD_RES 143 143 N6-acetyllysine.
 MOD_RES 206 206 N6-malonyllysine.
 MOD_RES 234 234 N6-acetyllysine.
 MOD_RES 288 288 N6-acetyllysine.
 MOD_RES 300 300 N6-acetyllysine.
 MOD_RES 567 567 N6-acetyllysine.
 MOD_RES 646 646 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Chaperone; Complete proteome; Direct protein sequencing; Mitochondrion; Nucleotide-binding; Nucleus; Polymorphism; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 679 AA 
Protein Sequence
MISASRAAAA RLVGAAASRG PTAARHQDSW NGLSHEAFRL VSRRDYASEA IKGAVVGIDL 60
GTTNSCVAVM EGKQAKVLEN AEGARTTPSV VAFTADGERL VGMPAKRQAV TNPNNTFYAT 120
KRLIGRRYDD PEVQKDIKNV PFKIVRASNG DAWVEAHGKL YSPSQIGAFV LMKMKETAEN 180
YLGHTAKNAV ITVPAYFNDS QRQATKDAGQ ISGLNVLRVI NEPTAAALAY GLDKSEDKVI 240
AVYDLGGGTF DISILEIQKG VFEVKSTNGD TFLGGEDFDQ ALLRHIVKEF KRETGVDLTK 300
DNMALQRVRE AAEKAKCELS SSVQTDINLP YLTMDSSGPK HLNMKLTRAQ FEGIVTDLIR 360
RTIAPCQKAM QDAEVSKSDI GEVILVGGMT RMPKVQQTVQ DLFGRAPSKA VNPDEAVAIG 420
AAIQGGVLAG DVTDVLLLDV TPLSLGIETL GGVFTKLINR NTTIPTKKSQ VFSTAADGQT 480
QVEIKVCQGE REMAGDNKLL GQFTLIGIPP APRGVPQIEV TFDIDANGIV HVSAKDKGTG 540
REQQIVIQSS GGLSKDDIEN MVKNAEKYAE EDRRKKERVE AVNMAEGIIH DTETKMEEFK 600
DQLPADECNK LKEEISKMRE LLARKDSETG ENIRQAASSL QQASLKLFEM AYKKMASERE 660
GSGSSGTGEQ KEDQKEEKQ 679 
Gene Ontology
 GO:0009986; C:cell surface; IDA:UniProtKB.
 GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0051082; F:unfolded protein binding; TAS:UniProtKB.
 GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
 GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
 GO:0006611; P:protein export from nucleus; IEA:Compara.
 GO:0006457; P:protein folding; IEA:InterPro.
 GO:0006626; P:protein targeting to mitochondrion; TAS:Reactome. 
Interpro
 IPR012725; Chaperone_DnaK.
 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.