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Q96EY1 (DNJA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DnaJ homolog subfamily A member 3, mitochondrial
Alternative name(s):
DnaJ protein Tid-1
Short name=hTid-1
Hepatocellular carcinoma-associated antigen 57
Tumorous imaginal discs protein Tid56 homolog
Gene names
Name:DNAJA3
Synonyms:HCA57, TID1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Isoform 2 may play a role in neuromuscular junction development as an effector of the MUSK signaling pathway. HAMAP-Rule MF_01152

Subunit structure

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) By similarity. Ref.2

Subcellular location

Mitochondrion matrix. Cytoplasmcytosol By similarity. Cell junctionsynapsepostsynaptic cell membrane; Peripheral membrane protein By similarity. Note: Recruited to the postsynaptic cell membrane of the neuromuscular junction through interaction with MUSK By similarity. HAMAP-Rule MF_01152

Tissue specificity

Widely expressed with highest levels in heart, liver, lung and skeletal muscles. Also expressed in keratinocytes. Ref.1

Domain

Modulation of apoptosis, i.e. proapoptotic activity of isoform 1 and antiapoptotic activity of isoform 2, is J domain-dependent. HAMAP-Rule MF_01152

Post-translational modification

Tyrosine phosphorylated By similarity. HAMAP-Rule MF_01152

Sequence similarities

Contains 1 CR-type zinc finger.

Contains 1 J domain.

Sequence caution

The sequence AAF66245.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAF66245.1 differs from that shown. Reason: Frameshift at positions 408 and 411.

The sequence AAH12343.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCell junction
Cell membrane
Cytoplasm
Membrane
Mitochondrion
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Transit peptide
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChaperone
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell differentiation in thymus

Inferred from electronic annotation. Source: Ensembl

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay Ref.7. Source: UniProtKB

activation-induced cell death of T cells

Inferred from electronic annotation. Source: Ensembl

cell aging

Inferred from electronic annotation. Source: Ensembl

embryo development

Inferred from electronic annotation. Source: Ensembl

mitochondrial DNA replication

Inferred from electronic annotation. Source: Ensembl

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay PubMed 11927590. Source: UniProtKB

negative regulation of NF-kappaB transcription factor activity

Inferred from direct assay PubMed 11927590. Source: UniProtKB

negative regulation of apoptotic process

Inferred from direct assay Ref.7. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay PubMed 11719219. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay Ref.7. Source: UniProtKB

negative regulation of interferon-gamma-mediated signaling pathway

Inferred from direct assay Ref.2. Source: UniProtKB

negative regulation of protein kinase activity

Inferred from direct assay PubMed 15601829PubMed 15601829. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 21106534. Source: UniProtKB

neuromuscular junction development

Inferred from direct assay PubMed 19038220. Source: UniProtKB

positive regulation of T cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from direct assay Ref.7. Source: UniProtKB

positive regulation of protein ubiquitination

Inferred from direct assay PubMed 15520177. Source: UniProtKB

protein folding

Inferred from direct assay PubMed 16531398PubMed 16531398. Source: UniProtKB

protein stabilization

Inferred from direct assay PubMed 11927590. Source: UniProtKB

response to heat

Inferred from electronic annotation. Source: InterPro

response to interferon-gamma

Inferred from direct assay Ref.2. Source: UniProtKB

skeletal muscle acetylcholine-gated channel clustering

Inferred from sequence or structural similarity. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay Ref.2. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

extrinsic component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

mitochondrial matrix

Inferred from direct assay PubMed 11719219Ref.7. Source: UniProtKB

mitochondrial nucleoid

Inferred from direct assay PubMed 16531398PubMed 16531398. Source: UniProtKB

mitochondrion

Inferred from direct assay. Source: HPA

neuromuscular junction

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.2. Source: UniProtKB

postsynaptic membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

NF-kappaB binding

Inferred from physical interaction PubMed 15601829PubMed 15601829. Source: UniProtKB

interferon-gamma receptor binding

Inferred from direct assay Ref.2. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase binding

Inferred from physical interaction Ref.2PubMed 15601829PubMed 15601829. Source: UniProtKB

small GTPase regulator activity

Inferred from electronic annotation. Source: Ensembl

transcription factor binding

Inferred from physical interaction PubMed 16531398PubMed 21106534. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96EY1-1)

Also known as: Tid-1(L);

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.
Isoform 2 (identifier: Q96EY1-2)

Also known as: Tid-1(S);

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 480DnaJ homolog subfamily A member 3, mitochondrial HAMAP-Rule MF_01152PRO_0000007256

Regions

Domain93 – 15866J
Repeat236 – 2438CXXCXGXG motif HAMAP-Rule MF_01152
Repeat253 – 2608CXXCXGXG motif HAMAP-Rule MF_01152
Repeat275 – 2828CXXCXGXG motif HAMAP-Rule MF_01152
Repeat289 – 2968CXXCXGXG motif HAMAP-Rule MF_01152
Zinc finger223 – 30179CR-type HAMAP-Rule MF_01152

Sites

Metal binding2361Zinc 1 By similarity
Metal binding2391Zinc 1 By similarity
Metal binding2531Zinc 2 By similarity
Metal binding2561Zinc 2 By similarity
Metal binding2751Zinc 2 By similarity
Metal binding2781Zinc 2 By similarity
Metal binding2891Zinc 1 By similarity
Metal binding2921Zinc 1 By similarity

Amino acid modifications

Modified residue581Omega-N-methylarginine; by CARM1 Ref.9
Modified residue1341N6-acetyllysine By similarity
Modified residue2381Omega-N-methylarginine; by CARM1 Ref.9
Modified residue2931Omega-N-methylarginine; by CARM1 Ref.9

Natural variations

Alternative sequence448 – 4536GSTMDS → KRSTGN in isoform 2.
VSP_007425
Alternative sequence454 – 48027Missing in isoform 2.
VSP_007426
Natural variant751N → Y. Ref.2 Ref.3 Ref.5 Ref.6
Corresponds to variant rs4785963 [ dbSNP | Ensembl ].
VAR_027965

Experimental info

Mutagenesis1211H → Q: Loss of modulation of apoptosis. Ref.7
Sequence conflict3201M → W in AAF66245. Ref.6

Secondary structure

........................... 480
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Tid-1(L)) [UniParc].

Last modified November 2, 2010. Version 2.
Checksum: 5A57B9020992CF59

FASTA48052,489
        10         20         30         40         50         60 
MAARCSTRWL LVVVGTPRLP AISGRGARPP REGVVGAWLS RKLSVPAFAS SLTSCGPRAL 

        70         80         90        100        110        120 
LTLRPGVSLT GTKHNPFICT ASFHTSAPLA KEDYYQILGV PRNASQKEIK KAYYQLAKKY 

       130        140        150        160        170        180 
HPDTNKDDPK AKEKFSQLAE AYEVLSDEVK RKQYDAYGSA GFDPGASGSQ HSYWKGGPTV 

       190        200        210        220        230        240 
DPEELFRKIF GEFSSSSFGD FQTVFDQPQE YFMELTFNQA AKGVNKEFTV NIMDTCERCN 

       250        260        270        280        290        300 
GKGNEPGTKV QHCHYCGGSG METINTGPFV MRSTCRRCGG RGSIIISPCV VCRGAGQAKQ 

       310        320        330        340        350        360 
KKRVMIPVPA GVEDGQTVRM PVGKREIFIT FRVQKSPVFR RDGADIHSDL FISIAQALLG 

       370        380        390        400        410        420 
GTARAQGLYE TINVTIPPGT QTDQKIRMGG KGIPRINSYG YGDHYIHIKI RVPKRLTSRQ 

       430        440        450        460        470        480 
QSLILSYAED ETDVEGTVNG VTLTSSGGST MDSSAGSKAR REAGEDEEGF LSKLKKMFTS 

« Hide

Isoform 2 (Tid-1(S)) [UniParc].

Checksum: E235B8DC1DB99FBC
Show »

FASTA45349,611

References

« Hide 'large scale' references
[1]"A novel human DnaJ protein, hTid-1, a homolog of the Drosophila tumor suppressor protein Tid56, can interact with the human papillomavirus type 16 E7 oncoprotein."
Schilling B., De-Medina T., Syken J., Vidal M., Munger K.
Virology 247:74-85(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"hTid-1, a human DnaJ protein, modulates the interferon signaling pathway."
Sarkar S., Pollack B.P., Lin K.-T., Kotenko S.V., Cook J.R., Lewis A., Pestka S.
J. Biol. Chem. 276:49034-49042(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH JAK2; HSP70 AND IFN-GAMMAR2, VARIANT TYR-75.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT TYR-75.
Tissue: Urinary bladder.
[4]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1 AND 2), VARIANT TYR-75.
Tissue: Brain, Colon, Lung, Muscle and Placenta.
[6]"Large scale identification of human hepatocellular carcinoma-associated antigens by autoantibodies."
Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y., Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W., Chen W.-F.
J. Immunol. 169:1102-1109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-480 (ISOFORM 2), VARIANT TYR-75.
Tissue: Hepatoma.
[7]"TID1, a human homolog of the Drosophila tumor suppressor l(2)tid, encodes two mitochondrial modulators of apoptosis with opposing functions."
Syken J., De-Medina T., Muenger K.
Proc. Natl. Acad. Sci. U.S.A. 96:8499-8504(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF HIS-121.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"A Y2H-seq approach defines the human protein methyltransferase interactome."
Weimann M., Grossmann A., Woodsmith J., Ozkan Z., Birth P., Meierhofer D., Benlasfer N., Valovka T., Timmermann B., Wanker E.E., Sauer S., Stelzl U.
Nat. Methods 10:339-342(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-58; ARG-238 AND ARG-293 BY CARM1, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Solution structure of J-domain and of zinc finger domain from human DnaJ subfamily A member 3."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 93-303.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF061749 mRNA. Translation: AAC29066.1.
AF411044 mRNA. Translation: AAL35323.1.
AK314218 mRNA. Translation: BAG36892.1.
AC012676 Genomic DNA. No translation available.
BC007225 mRNA. Translation: AAH07225.1.
BC011855 mRNA. Translation: AAH11855.1.
BC012343 mRNA. Translation: AAH12343.1. Different initiation.
BC014062 mRNA. Translation: AAH14062.1.
BC020248 mRNA. Translation: AAH20248.1.
BC030145 mRNA. Translation: AAH30145.1.
BC032100 mRNA. Translation: AAH32100.1.
AF244136 mRNA. Translation: AAF66245.1. Sequence problems.
RefSeqNP_001128582.1. NM_001135110.2.
NP_001273445.1. NM_001286516.1.
NP_005138.3. NM_005147.5.
UniGeneHs.459779.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CTTNMR-A213-303[»]
2DN9NMR-A93-158[»]
ProteinModelPortalQ96EY1.
SMRQ96EY1. Positions 90-431.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114547. 48 interactions.
DIPDIP-33870N.
IntActQ96EY1. 29 interactions.
MINTMINT-1151431.
STRING9606.ENSP00000262375.

PTM databases

PhosphoSiteQ96EY1.

Polymorphism databases

DMDM311033374.

Proteomic databases

PaxDbQ96EY1.
PRIDEQ96EY1.

Protocols and materials databases

DNASU9093.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262375; ENSP00000262375; ENSG00000103423. [Q96EY1-1]
ENST00000355296; ENSP00000347445; ENSG00000103423. [Q96EY1-2]
GeneID9093.
KEGGhsa:9093.
UCSCuc002cwk.3. human. [Q96EY1-1]
uc002cwl.3. human. [Q96EY1-2]

Organism-specific databases

CTD9093.
GeneCardsGC16P004475.
H-InvDBHIX0012782.
HGNCHGNC:11808. DNAJA3.
HPACAB016095.
HPA040875.
HPA044229.
MIM608382. gene.
neXtProtNX_Q96EY1.
PharmGKBPA27410.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0484.
HOVERGENHBG051371.
InParanoidQ96EY1.
KOK09504.
OMAFVTFRVE.
OrthoDBEOG7B31N2.
PhylomeDBQ96EY1.
TreeFamTF105152.

Gene expression databases

ArrayExpressQ96EY1.
BgeeQ96EY1.
CleanExHS_DNAJA3.
GenevestigatorQ96EY1.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
HAMAPMF_01152. DnaJ.
InterProIPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamPF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 1 hit.
SSF57938. SSF57938. 1 hit.
PROSITEPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ96EY1.
GeneWikiDNAJA3.
GenomeRNAi9093.
NextBio34071.
PROQ96EY1.
SOURCESearch...

Entry information

Entry nameDNJA3_HUMAN
AccessionPrimary (citable) accession number: Q96EY1
Secondary accession number(s): B2RAJ5 expand/collapse secondary AC list , O75472, Q8WUJ6, Q8WXJ3, Q96D76, Q96IV1, Q9NYH8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: November 2, 2010
Last modified: April 16, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM