Q96EY1 (DNJA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	480 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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. Cytoplasm › cytosol By similarity. Cell junction › synapse › postsynaptic cell membrane; Peripheral membrane protein By similarity. Note: Recruited to the postsynaptic cell membrane of the neuromuscular junction through interaction with MUSK By similarity.
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.
Post-translational modification	Tyrosine phosphorylated By similarity. Ref.8 Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.8
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 process	Apoptosis
Cellular component	Cell junction Cell membrane Cytoplasm Membrane Mitochondrion Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Transit peptide Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chaperone
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from direct assay Ref.7. Source: UniProtKB negative regulation of I-kappaB kinase/NF-kappaB cascade 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 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 electronic annotation. Source: InterPro 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
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial matrix Inferred from direct assay PubMed 11719219. Source: UniProtKB mitochondrial nucleoid Inferred from direct assay PubMed 16531398PubMed 16531398. Source: UniProtKB 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 function	ATP binding Inferred from electronic annotation. Source: InterPro NF-kappaB binding Inferred from physical interaction PubMed 15601829PubMed 15601829. Source: UniProtKB heat shock protein binding Inferred from electronic annotation. Source: InterPro 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MET	P08581	2	EBI-3952284,EBI-1039152
STAT5B	P51692	2	EBI-356767,EBI-1186119
Stat5b	P42232	2	EBI-3952284,EBI-617454	From a different organism.

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Mitochondrion Potential

Chain

? – 480

DnaJ homolog subfamily A member 3, mitochondrial

PRO_0000007256

Regions

Domain

93 – 158

66

J

Repeat

236 – 243

8

CXXCXGXG motif

Repeat

253 – 260

8

CXXCXGXG motif

Repeat

275 – 282

8

CXXCXGXG motif

Repeat

289 – 296

8

CXXCXGXG motif

Zinc finger

223 – 301

79

CR-type

Sites

Metal binding

236

1

Zinc 1 By similarity

Metal binding

239

1

Zinc 1 By similarity

Metal binding

253

1

Zinc 2 By similarity

Metal binding

256

1

Zinc 2 By similarity

Metal binding

275

1

Zinc 2 By similarity

Metal binding

278

1

Zinc 2 By similarity

Metal binding

289

1

Zinc 1 By similarity

Metal binding

292

1

Zinc 1 By similarity

Amino acid modifications

Modified residue

169

1

Phosphoserine Ref.8

Natural variations

Alternative sequence

448 – 453

6

GSTMDS → KRSTGN in isoform 2.

VSP_007425

Alternative sequence

454 – 480

27

Missing in isoform 2.

VSP_007426

Natural variant

75

1

N → Y. Ref.2 Ref.3 Ref.5 Ref.6
Corresponds to variant rs4785963 [ dbSNP | Ensembl ].

VAR_027965

Experimental info

Mutagenesis

121

1

H → Q: Loss of modulation of apoptosis. Ref.7

Sequence conflict

320

1

M → W in AAF66245. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

480

Helix Strand Turn

Details...

Helix

94 – 98

5

Helix

106 – 119

14

Turn

122 – 124

3

Helix

131 – 146

16

Helix

148 – 156

9

Beta strand

222 – 224

3

Beta strand

237 – 244

8

Beta strand

254 – 259

6

Beta strand

261 – 266

6

Beta strand

269 – 274

6

Beta strand

276 – 284

9

Beta strand

290 – 294

5

Beta strand

296 – 298

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Tid-1(L)) [UniParc]. Last modified November 2, 2010. Version 2. Checksum: 5A57B9020992CF59	FASTA	480	52,489
	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
	Isoform 2 (Tid-1(S)) [UniParc]. Checksum: E235B8DC1DB99FBC	FASTA	453	49,611
	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 QSLILSYAED ETDVEGTVNG VTLTSSGKRS TGN

References

	« Hide 'large scale' referencesShow '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: 9683573] [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: 11679576] [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. , 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: 14702039] [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. , 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: 15616553] [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: 15489334] [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: 12097419] [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: 10411904] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS OF HIS-121.
[8]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.

IPI

IPI00179187.
IPI00294610.

RefSeq

NP_001128582.1. NM_001135110.2.
NP_005138.3. NM_005147.5.

UniGene

Hs.688238.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CTT	NMR	-	A	213-303	[»]
2DN9	NMR	-	A	93-158	[»]

ProteinModelPortal

Q96EY1.

SMR

Q96EY1. Positions 93-160, 203-414.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96EY1. 15 interactions.

MINT

MINT-1151431.

STRING

Q96EY1.

PTM databases

PhosphoSite

Q96EY1.

Polymorphism databases

DMDM

311033374.

Proteomic databases

PRIDE

Q96EY1.

Protocols and materials databases

DNASU

9093.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262375; ENSP00000262375; ENSG00000103423.

GeneID

9093.

KEGG

hsa:9093.

UCSC

uc002cwk.3. human.
uc002cwl.3. human.

Organism-specific databases

CTD

9093.

GeneCards

GC16P004475.

H-InvDB

HIX0012782.

HGNC

HGNC:11808. DNAJA3.

MIM

608382. gene.

neXtProt

NX_Q96EY1.

PharmGKB

PA27410.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0484.

GeneTree

ENSGT00650000093209.

HOVERGEN

HBG051371.

InParanoid

Q96EY1.

KO

K09504.

OMA

CNGKGNE.

OrthoDB

EOG4CVG73.

PhylomeDB

Q96EY1.

Enzyme and pathway databases

Pathway_Interaction_DB

trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.

Gene expression databases

ArrayExpress

Q96EY1.

Bgee

Q96EY1.

CleanEx

HS_DNAJA3.

Genevestigator

Q96EY1.

GermOnline

ENSG00000103423. Homo sapiens.

Family and domain databases

Gene3D

G3DSA:1.10.287.110. DnaJ_N. 1 hit.
G3DSA:2.10.230.10. HSP_DnaJ_cys-rich. 1 hit.

InterPro

IPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_N.
IPR018253. Heat_shock_DnaJ_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR003095. Hsp_DnaJ.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]

PANTHER

PTHR24076:SF80. PTHR24076:SF80. 1 hit.

Pfam

PF00226. DnaJ. 1 hit.
PF01556. DnaJ_C. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]

PRINTS

PR00625. JDOMAIN.

SMART

SM00271. DnaJ. 1 hit.
[Graphical view]

SUPFAM

SSF46565. DnaJ_N. 1 hit.
SSF49493. HSP40_DnaJ_pep. 2 hits.
SSF57938. HSP_DnaJ_cys-rich. 1 hit.

PROSITE

PS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q96EY1.

NextBio

34071.

SOURCE

Search...

Entry information

Entry name

DNJA3_HUMAN

Accession

Primary (citable) accession number: Q96EY1
Secondary accession number(s): B2RAJ5 , 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 18, 2012
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.