CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019957
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DnaJ homolog subfamily A member 3, mitochondrial 
Protein Synonyms/Alias
 DnaJ protein Tid-1; mTid-1; Tumorous imaginal discs protein Tid56 homolog 
Gene Name
 Dnaja3 
Gene Synonyms/Alias
 Tid1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
107VPRNASQKDIKKAYYacetylation[1]
118KAYYQLAKKYHPDTNacetylation[1, 2]
118KAYYQLAKKYHPDTNsuccinylation[2]
119AYYQLAKKYHPDTNKacetylation[1, 3]
126KYHPDTNKDDPKAKEacetylation[4]
130DTNKDDPKAKEKFSQacetylation[1]
134DDPKAKEKFSQLAEAacetylation[1, 3, 4]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] 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]
 [3] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654] 
Functional Description
 Modulates apoptotic signal transduction or effector structures within the mitochondrial matrix. Affect cytochrome C release from the mitochondria and caspase 3 activation, but not caspase 8 activation. Isoform 1 increases apoptosis triggered by both TNF and the DNA-damaging agent mytomycin C; in sharp contrast, isoform 2 suppresses apoptosis. Can modulate IFN-gamma- mediated transcriptional activity (By similarity). Isoform 2 may play a role in neuromuscular junction development as an effector of the MUSK signaling pathway. 
Sequence Annotation
 DOMAIN 93 158 J.
 REPEAT 236 243 CXXCXGXG motif.
 REPEAT 253 260 CXXCXGXG motif.
 REPEAT 275 282 CXXCXGXG motif.
 REPEAT 289 296 CXXCXGXG motif.
 ZN_FING 223 301 CR-type.
 METAL 236 236 Zinc 1 (By similarity).
 METAL 239 239 Zinc 1 (By similarity).
 METAL 253 253 Zinc 2 (By similarity).
 METAL 256 256 Zinc 2 (By similarity).
 METAL 275 275 Zinc 2 (By similarity).
 METAL 278 278 Zinc 2 (By similarity).
 METAL 289 289 Zinc 1 (By similarity).
 METAL 292 292 Zinc 1 (By similarity).
 MOD_RES 58 58 Omega-N-methylarginine; by CARM1 (By
 MOD_RES 238 238 Omega-N-methylarginine; by CARM1 (By
 MOD_RES 293 293 Omega-N-methylarginine; by CARM1 (By  
Keyword
 Alternative splicing; Apoptosis; Cell junction; Cell membrane; Chaperone; Complete proteome; Cytoplasm; Membrane; Metal-binding; Methylation; Mitochondrion; Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat; Synapse; Transit peptide; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 480 AA 
Protein Sequence
MAAWCSPRWL RVAVGTPRLP AAAGRGVQQP QGGVVATSLC RKLCVSAFGL SMGAHGPRAL 60
LTLRPGVRLT GTKSFPFVCT TSFHTSASLA KDDYYQILGV PRNASQKDIK KAYYQLAKKY 120
HPDTNKDDPK AKEKFSQLAE AYEVLSDEVK RKQYDAYGSA GFDPGTSSSG QGYWRGGPSV 180
DPEELFRKIF GEFSSSPFGD FQNVFDQPQE YIMELTFNQA AKGVNKEFTV NIMDTCERCD 240
GKGNEPGTKV QHCHYCGGSG METINTGPFV MRSTCRRCGG RGSIITNPCV VCRGAGQAKQ 300
KKRVTIPVPA GVEDGQTVRM PVGKREIFVT FRVQKSPVFR RDGADIHSDL FISIAQAILG 360
GTAKAQGLYE TINVTIPAGI QTDQKIRLTG KGIPRINSYG YGDHYIHIKI RVPKRLSSRQ 420
QNLILSYAED ETDVEGTVNG VTHTSTGGRT MDSSAGSKDR REAGEDNEGF LSKLKKIFTS 480 
Gene Ontology
 GO:0005884; C:actin filament; IEA:Compara.
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0019897; C:extrinsic to plasma membrane; IDA:UniProtKB.
 GO:0033256; C:I-kappaB/NF-kappaB complex; IEA:Compara.
 GO:0008385; C:IkappaB kinase complex; IEA:Compara.
 GO:0042645; C:mitochondrial nucleoid; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0005083; F:small GTPase regulator activity; IDA:MGI.
 GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Compara.
 GO:0006924; P:activation-induced cell death of T cells; IMP:MGI.
 GO:0007569; P:cell aging; IDA:MGI.
 GO:0009790; P:embryo development; IMP:MGI.
 GO:0006264; P:mitochondrial DNA replication; IMP:MGI.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0008285; P:negative regulation of cell proliferation; IEA:Compara.
 GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Compara.
 GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB cascade; IEA:Compara.
 GO:0060336; P:negative regulation of interferon-gamma-mediated signaling pathway; IEA:Compara.
 GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISA:MGI.
 GO:0006469; P:negative regulation of protein kinase activity; IEA:Compara.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0007528; P:neuromuscular junction development; IMP:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; IEA:Compara.
 GO:0031398; P:positive regulation of protein ubiquitination; IEA:Compara.
 GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
 GO:0006457; P:protein folding; IEA:InterPro.
 GO:0050821; P:protein stabilization; IEA:Compara.
 GO:0009408; P:response to heat; IEA:InterPro.
 GO:0034341; P:response to interferon-gamma; IEA:Compara.
 GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; IMP:UniProtKB.
 GO:0007264; P:small GTPase mediated signal transduction; IDA:MGI.
 GO:0033077; P:T cell differentiation in thymus; IMP:MGI. 
Interpro
 IPR012724; DnaJ.
 IPR002939; DnaJ_C.
 IPR001623; DnaJ_domain.
 IPR018253; DnaJ_domain_CS.
 IPR008971; HSP40/DnaJ_pept-bd.
 IPR001305; HSP_DnaJ_Cys-rich_dom. 
Pfam
 PF00226; DnaJ
 PF01556; DnaJ_C
 PF00684; DnaJ_CXXCXGXG 
SMART
 SM00271; DnaJ 
PROSITE
 PS00636; DNAJ_1
 PS50076; DNAJ_2
 PS51188; ZF_CR 
PRINTS
 PR00625; JDOMAIN.