CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000590
UniProt Accession
Genbank Protein ID
 U92313 
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 
Gene Name
 HSPA9 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) 
NCBI Taxa ID
 10029 
Lysine Modification
Position
Peptide
Type
References
121NNTFYATKRLIGRRYubiquitination[1]
300ETGVDLTKDNMALQRubiquitination[1]
360GIVTDLIKRTIAPCQubiquitination[1]
468NTTIPTKKSQVFSTAubiquitination[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] 
Functional Description
 Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone (By similarity). 
Sequence Annotation
 MOD_RES 135 135 N6-acetyllysine (By similarity).
 MOD_RES 138 138 N6-acetyllysine (By similarity).
 MOD_RES 143 143 N6-acetyllysine (By similarity).
 MOD_RES 206 206 N6-malonyllysine (By similarity).
 MOD_RES 234 234 N6-acetyllysine (By similarity).
 MOD_RES 288 288 N6-acetyllysine (By similarity).
 MOD_RES 300 300 N6-acetyllysine (By similarity).
 MOD_RES 360 360 N6-acetyllysine (By similarity).
 MOD_RES 567 567 N6-acetyllysine (By similarity).
 MOD_RES 646 646 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding; Nucleus; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 679 AA 
Protein Sequence
MISATRAAAA RLVGTAASRT PAAARHQDGW NGLSHEAFRF VSRRDYASET IKGAVVGIDL 60
GTTNSCVAVM EGKQAKVLEN AEGARTTPSV VAFTADGERL VGMPAKRQAV TNPNNTFYAT 120
KRLIGRRYDD PEVQKDTKNV PFKIVRASNG DAWVEAHGKL YSPSQIGAFV LMKMKETAEN 180
YLGHTAKNAV ITVPAYFNDS QRQATKDAGQ ISGLNVLRVI NEPTAAALAY GLDKSEDKII 240
AVYDLGGGTF DISILEIQKG VFEVKSTNGD TFLGGEDFDQ ALLRHIVKEF KRETGVDLTK 300
DNMALQRVRE AAEKAKCELS SSVQTDINLP YLTMDASGPK HLNMKLTRAQ FEGIVTDLIK 360
RTIAPCQKAM QDAEVSKSDI GEVILVGGMT RMPKVQQTVQ DLFGRAPSKA VNPDEAVAIG 420
AAIQGGVLAG DVTDVLLLDV TPLSLGIETL GGVFTKLINR NTTIPTKKSQ VFSTAADGQT 480
QVEIKVCQGE REMAGDNKLL GQFTLIGIPP APRGVPQIEV TFDLDANGIV HVSAKDKGTG 540
REQQIVIQSS GGLSKDDIEN MVKNAEKYAE EDRRKKERVE AVNMAEGIIH DTETKMEEFK 600
DQLPADECNK LKEEISKMRE LLARKDSETG ENIRQAASSL QQASLKLFEM AYKKMASERE 660
GSGSSGTGEQ KEDQKEEKQ 679 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0006457; P:protein folding; IEA:InterPro. 
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.