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Protein

DnaJ homolog subfamily A member 3, mitochondrial

Gene

DNAJA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Isoform 2 may play a role in neuromuscular junction development as an effector of the MUSK signaling pathway.

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri223 – 30179CR-typeAdd
BLAST

GO - Molecular functioni

  • ATP binding Source: InterPro
  • chaperone binding Source: GO_Central
  • GTPase regulator activity Source: Ensembl
  • interferon-gamma receptor binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • NF-kappaB binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • unfolded protein binding Source: GO_Central

GO - Biological processi

  • activation-induced cell death of T cells Source: Ensembl
  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • cell aging Source: Ensembl
  • mitochondrial DNA replication Source: Ensembl
  • mitochondrion organization Source: GO_Central
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • negative regulation of interferon-gamma-mediated signaling pathway Source: UniProtKB
  • negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • negative regulation of programmed cell death Source: Ensembl
  • negative regulation of protein kinase activity Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • neuromuscular junction development Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of protein ubiquitination Source: UniProtKB
  • positive regulation of T cell proliferation Source: Ensembl
  • protein folding Source: UniProtKB
  • protein refolding Source: GO_Central
  • protein stabilization Source: UniProtKB
  • response to heat Source: InterPro
  • response to interferon-gamma Source: UniProtKB
  • skeletal muscle acetylcholine-gated channel clustering Source: UniProtKB
  • small GTPase mediated signal transduction Source: Ensembl
  • T cell differentiation in thymus Source: Ensembl
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:
hTid-1
Hepatocellular carcinoma-associated antigen 57
Tumorous imaginal discs protein Tid56 homolog
Gene namesi
Name:DNAJA3
Synonyms:HCA57, TID1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:11808. DNAJA3.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • extrinsic component of plasma membrane Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • mitochondrial matrix Source: UniProtKB
  • mitochondrial nucleoid Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • neuromuscular junction Source: UniProtKB
  • nucleus Source: UniProtKB
  • postsynaptic membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi121 – 1211H → Q: Loss of modulation of apoptosis. 1 Publication

Organism-specific databases

PharmGKBiPA27410.

Polymorphism and mutation databases

BioMutaiDNAJA3.
DMDMi311033374.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 480DnaJ homolog subfamily A member 3, mitochondrialPRO_0000007256
Transit peptidei1 – ?MitochondrionSequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581Omega-N-methylarginine; by CARM11 Publication
Modified residuei134 – 1341N6-acetyllysineBy similarity
Modified residuei238 – 2381Omega-N-methylarginine; by CARM11 Publication
Modified residuei293 – 2931Omega-N-methylarginine; by CARM11 Publication

Post-translational modificationi

Tyrosine phosphorylated.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ96EY1.
PaxDbiQ96EY1.
PRIDEiQ96EY1.

PTM databases

PhosphoSiteiQ96EY1.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ96EY1.
CleanExiHS_DNAJA3.
ExpressionAtlasiQ96EY1. baseline and differential.
GenevisibleiQ96EY1. HS.

Organism-specific databases

HPAiCAB016095.
HPA040875.
HPA044229.

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) (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9H6143EBI-3952284,EBI-10249899
ALS2CR11Q53TS83EBI-3952284,EBI-739879
CARM1Q86X552EBI-356767,EBI-2339854
FAM214BQ7L5A33EBI-3952284,EBI-745689
FOSL2P154083EBI-3952284,EBI-3893419
FRMD6Q96NE93EBI-3952284,EBI-741729
GCC1Q96CN93EBI-3952284,EBI-746252
INPP5JQ157353EBI-3952284,EBI-10236940
KDM1AO603412EBI-356767,EBI-710124
METP085812EBI-3952284,EBI-1039152
NOC4LQ9BVI43EBI-3952284,EBI-395927
OSGIN1Q9UJX03EBI-3952284,EBI-9057006
PRMT6Q96LA82EBI-356767,EBI-912440
STAT5BP516922EBI-356767,EBI-1186119
Stat5bP422323EBI-356767,EBI-617454From a different organism.
STK16O757163EBI-3952284,EBI-749295
TCF19D2IYK53EBI-3952284,EBI-10176552

Protein-protein interaction databases

BioGridi114547. 63 interactions.
DIPiDIP-33870N.
IntActiQ96EY1. 45 interactions.
MINTiMINT-1151431.
STRINGi9606.ENSP00000262375.

Structurei

Secondary structure

1
480
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi94 – 985Combined sources
Helixi106 – 11914Combined sources
Turni122 – 1243Combined sources
Helixi131 – 14616Combined sources
Helixi148 – 1569Combined sources
Beta strandi222 – 2243Combined sources
Beta strandi237 – 2448Combined sources
Beta strandi254 – 2596Combined sources
Beta strandi261 – 2666Combined sources
Beta strandi269 – 2746Combined sources
Beta strandi276 – 2849Combined sources
Beta strandi290 – 2945Combined sources
Beta strandi296 – 2983Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CTTNMR-A213-303[»]
2DN9NMR-A93-158[»]
ProteinModelPortaliQ96EY1.
SMRiQ96EY1. Positions 90-191, 213-429.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96EY1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini93 – 15866JAdd
BLAST
Repeati236 – 2438CXXCXGXG motif
Repeati253 – 2608CXXCXGXG motif
Repeati275 – 2828CXXCXGXG motif
Repeati289 – 2968CXXCXGXG motif

Domaini

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

Sequence similaritiesi

Contains 1 CR-type zinc finger.Curated
Contains 1 J domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri223 – 30179CR-typeAdd
BLAST

Keywords - Domaini

Repeat, Transit peptide, Zinc-finger

Phylogenomic databases

eggNOGiCOG0484.
GeneTreeiENSGT00730000111013.
HOGENOMiHOG000203530.
HOVERGENiHBG051371.
InParanoidiQ96EY1.
KOiK09504.
OMAiDQPQEYF.
OrthoDBiEOG7B31N2.
PhylomeDBiQ96EY1.
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. 1 hit.
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. AlignAdd to basket

Isoform 1 (identifier: Q96EY1-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAARCSTRWL LVVVGTPRLP AISGRGARPP REGVVGAWLS RKLSVPAFAS
60 70 80 90 100
SLTSCGPRAL LTLRPGVSLT GTKHNPFICT ASFHTSAPLA KEDYYQILGV
110 120 130 140 150
PRNASQKEIK KAYYQLAKKY HPDTNKDDPK AKEKFSQLAE AYEVLSDEVK
160 170 180 190 200
RKQYDAYGSA GFDPGASGSQ HSYWKGGPTV DPEELFRKIF GEFSSSSFGD
210 220 230 240 250
FQTVFDQPQE YFMELTFNQA AKGVNKEFTV NIMDTCERCN GKGNEPGTKV
260 270 280 290 300
QHCHYCGGSG METINTGPFV MRSTCRRCGG RGSIIISPCV VCRGAGQAKQ
310 320 330 340 350
KKRVMIPVPA GVEDGQTVRM PVGKREIFIT FRVQKSPVFR RDGADIHSDL
360 370 380 390 400
FISIAQALLG GTARAQGLYE TINVTIPPGT QTDQKIRMGG KGIPRINSYG
410 420 430 440 450
YGDHYIHIKI RVPKRLTSRQ QSLILSYAED ETDVEGTVNG VTLTSSGGST
460 470 480
MDSSAGSKAR REAGEDEEGF LSKLKKMFTS
Length:480
Mass (Da):52,489
Last modified:November 2, 2010 - v2
Checksum:i5A57B9020992CF59
GO
Isoform 2 (identifier: Q96EY1-2) [UniParc]FASTAAdd to basket

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.

Show »
Length:453
Mass (Da):49,611
Checksum:iE235B8DC1DB99FBC
GO
Isoform 3 (identifier: Q96EY1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     3-186: ARCSTRWLLV...GPTVDPEELF → EPQAERPRLCVFPDLLRPPSAADIETWCQPY
     448-453: GSTMDS → KRSTGN
     454-480: Missing.

Show »
Length:300
Mass (Da):33,082
Checksum:i36D883E568E8ECC8
GO

Sequence cautioni

The sequence AAF66245.1 differs from that shown. Reason: Frameshift at positions 408 and 411. Curated
The sequence AAF66245.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH12343.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti320 – 3201M → W in AAF66245 (PubMed:12097419).Curated
Isoform 3 (identifier: Q96EY1-3)
Sequence conflicti33 – 331Y → H in BAG58345 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti75 – 751N → Y.4 Publications
Corresponds to variant rs4785963 [ dbSNP | Ensembl ].
VAR_027965

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei3 – 186184ARCST…PEELF → EPQAERPRLCVFPDLLRPPS AADIETWCQPY in isoform 3. 1 PublicationVSP_055728Add
BLAST
Alternative sequencei448 – 4536GSTMDS → KRSTGN in isoform 2 and isoform 3. 4 PublicationsVSP_007425
Alternative sequencei454 – 48027Missing in isoform 2 and isoform 3. 4 PublicationsVSP_007426Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061749 mRNA. Translation: AAC29066.1.
AF411044 mRNA. Translation: AAL35323.1.
AK295391 mRNA. Translation: BAG58345.1.
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.
CCDSiCCDS10515.1. [Q96EY1-1]
CCDS45400.1. [Q96EY1-2]
CCDS66930.1. [Q96EY1-3]
RefSeqiNP_001128582.1. NM_001135110.2. [Q96EY1-2]
NP_001273445.1. NM_001286516.1. [Q96EY1-3]
NP_005138.3. NM_005147.5. [Q96EY1-1]
UniGeneiHs.459779.

Genome annotation databases

EnsembliENST00000262375; ENSP00000262375; ENSG00000103423.
ENST00000355296; ENSP00000347445; ENSG00000103423. [Q96EY1-2]
ENST00000431375; ENSP00000393970; ENSG00000103423. [Q96EY1-3]
ENST00000612103; ENSP00000477570; ENSG00000276726.
ENST00000614397; ENSP00000479815; ENSG00000276726. [Q96EY1-2]
ENST00000615114; ENSP00000480419; ENSG00000276726. [Q96EY1-3]
GeneIDi9093.
KEGGihsa:9093.
UCSCiuc002cwk.3. human. [Q96EY1-1]
uc002cwl.3. human. [Q96EY1-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061749 mRNA. Translation: AAC29066.1.
AF411044 mRNA. Translation: AAL35323.1.
AK295391 mRNA. Translation: BAG58345.1.
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.
CCDSiCCDS10515.1. [Q96EY1-1]
CCDS45400.1. [Q96EY1-2]
CCDS66930.1. [Q96EY1-3]
RefSeqiNP_001128582.1. NM_001135110.2. [Q96EY1-2]
NP_001273445.1. NM_001286516.1. [Q96EY1-3]
NP_005138.3. NM_005147.5. [Q96EY1-1]
UniGeneiHs.459779.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CTTNMR-A213-303[»]
2DN9NMR-A93-158[»]
ProteinModelPortaliQ96EY1.
SMRiQ96EY1. Positions 90-191, 213-429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114547. 63 interactions.
DIPiDIP-33870N.
IntActiQ96EY1. 45 interactions.
MINTiMINT-1151431.
STRINGi9606.ENSP00000262375.

PTM databases

PhosphoSiteiQ96EY1.

Polymorphism and mutation databases

BioMutaiDNAJA3.
DMDMi311033374.

Proteomic databases

MaxQBiQ96EY1.
PaxDbiQ96EY1.
PRIDEiQ96EY1.

Protocols and materials databases

DNASUi9093.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262375; ENSP00000262375; ENSG00000103423.
ENST00000355296; ENSP00000347445; ENSG00000103423. [Q96EY1-2]
ENST00000431375; ENSP00000393970; ENSG00000103423. [Q96EY1-3]
ENST00000612103; ENSP00000477570; ENSG00000276726.
ENST00000614397; ENSP00000479815; ENSG00000276726. [Q96EY1-2]
ENST00000615114; ENSP00000480419; ENSG00000276726. [Q96EY1-3]
GeneIDi9093.
KEGGihsa:9093.
UCSCiuc002cwk.3. human. [Q96EY1-1]
uc002cwl.3. human. [Q96EY1-2]

Organism-specific databases

CTDi9093.
GeneCardsiGC16P004475.
H-InvDBHIX0012782.
HGNCiHGNC:11808. DNAJA3.
HPAiCAB016095.
HPA040875.
HPA044229.
MIMi608382. gene.
neXtProtiNX_Q96EY1.
PharmGKBiPA27410.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0484.
GeneTreeiENSGT00730000111013.
HOGENOMiHOG000203530.
HOVERGENiHBG051371.
InParanoidiQ96EY1.
KOiK09504.
OMAiDQPQEYF.
OrthoDBiEOG7B31N2.
PhylomeDBiQ96EY1.
TreeFamiTF105152.

Miscellaneous databases

ChiTaRSiDNAJA3. human.
EvolutionaryTraceiQ96EY1.
GeneWikiiDNAJA3.
GenomeRNAii9093.
NextBioi34071.
PROiQ96EY1.
SOURCEiSearch...

Gene expression databases

BgeeiQ96EY1.
CleanExiHS_DNAJA3.
ExpressionAtlasiQ96EY1. baseline and differential.
GenevisibleiQ96EY1. HS.

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. 1 hit.
SSF57938. SSF57938. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] (ISOFORMS 1 AND 3), VARIANT TYR-75.
    Tissue: Corpus callosum and 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] [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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. 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.

Entry informationi

Entry nameiDNJA3_HUMAN
AccessioniPrimary (citable) accession number: Q96EY1
Secondary accession number(s): B2RAJ5
, B4DI33, E7ES32, O75472, Q8WUJ6, Q8WXJ3, Q96D76, Q96IV1, Q9NYH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: November 2, 2010
Last modified: July 22, 2015
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.