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Q99M87

- DNJA3_MOUSE

UniProt

Q99M87 - DNJA3_MOUSE

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Protein
DnaJ homolog subfamily A member 3, mitochondrial
Gene
Dnaja3, Tid1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi236 – 2361Zinc 1 By similarity
Metal bindingi239 – 2391Zinc 1 By similarity
Metal bindingi253 – 2531Zinc 2 By similarity
Metal bindingi256 – 2561Zinc 2 By similarity
Metal bindingi275 – 2751Zinc 2 By similarity
Metal bindingi278 – 2781Zinc 2 By similarity
Metal bindingi289 – 2891Zinc 1 By similarity
Metal bindingi292 – 2921Zinc 1 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri223 – 30179CR-typeUniRule annotation
Add
BLAST

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: MGI
  4. receptor tyrosine kinase binding Source: UniProtKB
  5. small GTPase regulator activity Source: MGI
  6. unfolded protein binding Source: MGI

GO - Biological processi

  1. T cell differentiation in thymus Source: MGI
  2. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  3. activation-induced cell death of T cells Source: MGI
  4. apoptotic process Source: MGI
  5. cell aging Source: MGI
  6. mitochondrial DNA replication Source: MGI
  7. mitochondrion organization Source: MGI
  8. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  9. negative regulation of NF-kappaB transcription factor activity Source: MGI
  10. negative regulation of apoptotic process Source: Ensembl
  11. negative regulation of cell proliferation Source: Ensembl
  12. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  13. negative regulation of interferon-gamma-mediated signaling pathway Source: Ensembl
  14. negative regulation of programmed cell death Source: MGI
  15. negative regulation of protein kinase activity Source: Ensembl
  16. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  17. neuromuscular junction development Source: UniProtKB
  18. positive regulation of T cell proliferation Source: MGI
  19. positive regulation of apoptotic process Source: Ensembl
  20. positive regulation of protein ubiquitination Source: Ensembl
  21. protein folding Source: InterPro
  22. protein stabilization Source: Ensembl
  23. response to heat Source: InterPro
  24. response to interferon-gamma Source: Ensembl
  25. skeletal muscle acetylcholine-gated channel clustering Source: UniProtKB
  26. small GTPase mediated signal transduction Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
DnaJ homolog subfamily A member 3, mitochondrial
Alternative name(s):
DnaJ protein Tid-1
Short name:
mTid-1
Tumorous imaginal discs protein Tid56 homolog
Gene namesi
Name:Dnaja3
Synonyms:Tid1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:1933786. Dnaja3.

Subcellular locationi

Mitochondrion matrix By similarity. Cytoplasmcytosol. Cell junctionsynapsepostsynaptic cell membrane; Peripheral membrane protein
Note: Recruited to the postsynaptic cell membrane of the neuromuscular junction through interaction with MUSK.1 Publication

GO - Cellular componenti

  1. I-kappaB/NF-kappaB complex Source: Ensembl
  2. IkappaB kinase complex Source: Ensembl
  3. actin filament Source: Ensembl
  4. cell junction Source: UniProtKB-KW
  5. cytosol Source: UniProtKB
  6. extrinsic component of plasma membrane Source: UniProtKB
  7. mitochondrial nucleoid Source: Ensembl
  8. mitochondrion Source: MGI
  9. neuromuscular junction Source: UniProtKB
  10. nucleus Source: MGI
  11. postsynaptic membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Mitochondrion, Postsynaptic cell membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 480DnaJ homolog subfamily A member 3, mitochondrialUniRule annotationPRO_0000007257
Transit peptidei1 – ?Mitochondrion Reviewed prediction

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581Omega-N-methylarginine; by CARM1 By similarity
Modified residuei134 – 1341N6-acetyllysine1 Publication
Modified residuei238 – 2381Omega-N-methylarginine; by CARM1 By similarity
Modified residuei293 – 2931Omega-N-methylarginine; by CARM1 By similarity

Post-translational modificationi

Tyrosine phosphorylated.UniRule annotation

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ99M87.
PaxDbiQ99M87.
PRIDEiQ99M87.

PTM databases

PhosphoSiteiQ99M87.

Expressioni

Gene expression databases

ArrayExpressiQ99M87.
BgeeiQ99M87.
CleanExiMM_DNAJA3.
GenevestigatoriQ99M87.

Interactioni

Subunit structurei

Interacts with JAK2, HSPA9B and IFN-gammaR2 chain. Interacts with Ras GTPase-activating protein 1 (RASA1). Isoform 2 interacts with MUSK (via the cytoplasmic domain).2 Publications

Protein-protein interaction databases

BioGridi219986. 4 interactions.
IntActiQ99M87. 4 interactions.
MINTiMINT-1847235.
STRINGi10090.ENSMUSP00000053842.

Structurei

3D structure databases

ProteinModelPortaliQ99M87.
SMRiQ99M87. Positions 87-160, 213-429.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini93 – 15866J
Add
BLAST
Repeati236 – 2438CXXCXGXG motifUniRule annotation
Repeati253 – 2608CXXCXGXG motifUniRule annotation
Repeati275 – 2828CXXCXGXG motifUniRule annotation
Repeati289 – 2968CXXCXGXG motifUniRule annotation

Domaini

Modulation of apoptosis, i.e. proapoptotic activity of isoform 1 and antiapoptotic activity of isoform 2, is J domain-dependent By similarity.UniRule annotation

Sequence similaritiesi

Contains 1 J domain.

Keywords - Domaini

Repeat, Transit peptide, Zinc-finger

Phylogenomic databases

eggNOGiCOG0484.
GeneTreeiENSGT00730000111013.
HOVERGENiHBG051371.
InParanoidiQ99M87.
KOiK09504.
OMAiDTCERCN.
OrthoDBiEOG7B31N2.
PhylomeDBiQ99M87.
TreeFamiTF105152.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
HAMAPiMF_01152. DnaJ.
InterProiIPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamiPF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
SSF57938. SSF57938. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99M87-1) [UniParc]FASTAAdd to Basket

Also known as: Tid-1L, TID1L

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAAWCSPRWL RVAVGTPRLP AAAGRGVQQP QGGVVATSLC RKLCVSAFGL    50
SMGAHGPRAL LTLRPGVRLT GTKSFPFVCT TSFHTSASLA KDDYYQILGV 100
PRNASQKDIK KAYYQLAKKY HPDTNKDDPK AKEKFSQLAE AYEVLSDEVK 150
RKQYDAYGSA GFDPGTSSSG QGYWRGGPSV DPEELFRKIF GEFSSSPFGD 200
FQNVFDQPQE YIMELTFNQA AKGVNKEFTV NIMDTCERCD GKGNEPGTKV 250
QHCHYCGGSG METINTGPFV MRSTCRRCGG RGSIITNPCV VCRGAGQAKQ 300
KKRVTIPVPA GVEDGQTVRM PVGKREIFVT FRVQKSPVFR RDGADIHSDL 350
FISIAQAILG GTAKAQGLYE TINVTIPAGI QTDQKIRLTG KGIPRINSYG 400
YGDHYIHIKI RVPKRLSSRQ QNLILSYAED ETDVEGTVNG VTHTSTGGRT 450
MDSSAGSKDR REAGEDNEGF LSKLKKIFTS 480
Length:480
Mass (Da):52,443
Last modified:June 1, 2001 - v1
Checksum:i30AA5557C18665A8
GO
Isoform 2 (identifier: Q99M87-2) [UniParc]FASTAAdd to Basket

Also known as: Tid-1S, TID1S

The sequence of this isoform differs from the canonical sequence as follows:
     448-453: GRTMDS → KRSTGN
     454-480: Missing.

Show »
Length:453
Mass (Da):49,486
Checksum:iA5798CD5C8071EA7
GO
Isoform 3 (identifier: Q99M87-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     211-261: Missing.

Show »
Length:429
Mass (Da):46,847
Checksum:iF549A184D4EFD96F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei211 – 26151Missing in isoform 3.
VSP_007440Add
BLAST
Alternative sequencei448 – 4536GRTMDS → KRSTGN in isoform 2.
VSP_007427
Alternative sequencei454 – 48027Missing in isoform 2.
VSP_007428Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti403 – 4031D → H in BAB23661. 1 Publication
Sequence conflicti456 – 4561G → E in BAB23384. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY009320 mRNA. Translation: AAG37303.1.
AF325535 mRNA. Translation: AAK11222.1.
AF326358 mRNA. Translation: AAK11223.1.
AK004575 mRNA. Translation: BAB23384.1.
AK004910 mRNA. Translation: BAB23661.1.
AK011535 mRNA. Translation: BAB27682.2.
AK031250 mRNA. Translation: BAC27321.1.
BC003920 mRNA. Translation: AAH03920.1.
BC027240 mRNA. Translation: AAH27240.1.
CCDSiCCDS27922.1. [Q99M87-1]
CCDS49748.1. [Q99M87-2]
RefSeqiNP_001128584.1. NM_001135112.1. [Q99M87-2]
NP_076135.3. NM_023646.4. [Q99M87-1]
UniGeneiMm.248337.

Genome annotation databases

EnsembliENSMUST00000060067; ENSMUSP00000053842; ENSMUSG00000004069. [Q99M87-1]
ENSMUST00000115854; ENSMUSP00000111520; ENSMUSG00000004069. [Q99M87-2]
GeneIDi83945.
KEGGimmu:83945.
UCSCiuc007yac.2. mouse. [Q99M87-1]
uc012aat.1. mouse. [Q99M87-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY009320 mRNA. Translation: AAG37303.1 .
AF325535 mRNA. Translation: AAK11222.1 .
AF326358 mRNA. Translation: AAK11223.1 .
AK004575 mRNA. Translation: BAB23384.1 .
AK004910 mRNA. Translation: BAB23661.1 .
AK011535 mRNA. Translation: BAB27682.2 .
AK031250 mRNA. Translation: BAC27321.1 .
BC003920 mRNA. Translation: AAH03920.1 .
BC027240 mRNA. Translation: AAH27240.1 .
CCDSi CCDS27922.1. [Q99M87-1 ]
CCDS49748.1. [Q99M87-2 ]
RefSeqi NP_001128584.1. NM_001135112.1. [Q99M87-2 ]
NP_076135.3. NM_023646.4. [Q99M87-1 ]
UniGenei Mm.248337.

3D structure databases

ProteinModelPortali Q99M87.
SMRi Q99M87. Positions 87-160, 213-429.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 219986. 4 interactions.
IntActi Q99M87. 4 interactions.
MINTi MINT-1847235.
STRINGi 10090.ENSMUSP00000053842.

PTM databases

PhosphoSitei Q99M87.

Proteomic databases

MaxQBi Q99M87.
PaxDbi Q99M87.
PRIDEi Q99M87.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000060067 ; ENSMUSP00000053842 ; ENSMUSG00000004069 . [Q99M87-1 ]
ENSMUST00000115854 ; ENSMUSP00000111520 ; ENSMUSG00000004069 . [Q99M87-2 ]
GeneIDi 83945.
KEGGi mmu:83945.
UCSCi uc007yac.2. mouse. [Q99M87-1 ]
uc012aat.1. mouse. [Q99M87-3 ]

Organism-specific databases

CTDi 9093.
MGIi MGI:1933786. Dnaja3.

Phylogenomic databases

eggNOGi COG0484.
GeneTreei ENSGT00730000111013.
HOVERGENi HBG051371.
InParanoidi Q99M87.
KOi K09504.
OMAi DTCERCN.
OrthoDBi EOG7B31N2.
PhylomeDBi Q99M87.
TreeFami TF105152.

Miscellaneous databases

ChiTaRSi DNAJA3. mouse.
NextBioi 350822.
PROi Q99M87.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q99M87.
Bgeei Q99M87.
CleanExi MM_DNAJA3.
Genevestigatori Q99M87.

Family and domain databases

Gene3Di 1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
HAMAPi MF_01152. DnaJ.
InterProi IPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view ]
Pfami PF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view ]
PRINTSi PR00625. JDOMAIN.
SMARTi SM00271. DnaJ. 1 hit.
[Graphical view ]
SUPFAMi SSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
SSF57938. SSF57938. 1 hit.
PROSITEi PS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A mouse homologue of the Drosophila tumor suppressor l(2)tid gene defines a novel Ras GTPase-activating protein (RasGAP)-binding protein."
    Trentin G.A., Yin X., Tahir S., Lhotak S., Farhang-Fallah J., Li Y., Rozakis-Adcock M.
    J. Biol. Chem. 276:13087-13095(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), INTERACTION WITH RASA1.
    Strain: C57BL/6 X CBA.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Embryo, Forelimb and Lung.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  4. "A mammalian homolog of Drosophila tumorous imaginal discs, Tid1, mediates agrin signaling at the neuromuscular junction."
    Linnoila J., Wang Y., Yao Y., Wang Z.Z.
    Neuron 60:625-641(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEUROMUSCULAR JUNCTION DEVELOPMENT, INTERACTION WITH MUSK, SUBCELLULAR LOCATION.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-134, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDNJA3_MOUSE
AccessioniPrimary (citable) accession number: Q99M87
Secondary accession number(s): Q8BSM0
, Q99L09, Q99P71, Q99P76, Q9CT11, Q9DBJ7, Q9DC44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi