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O60884

- DNJA2_HUMAN

UniProt

O60884 - DNJA2_HUMAN

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Protein

DnaJ homolog subfamily A member 2

Gene

DNAJA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Co-chaperone of Hsc70.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi143 – 1431Zinc 1By similarity
Metal bindingi146 – 1461Zinc 1By similarity
Metal bindingi159 – 1591Zinc 2By similarity
Metal bindingi162 – 1621Zinc 2By similarity
Metal bindingi186 – 1861Zinc 2By similarity
Metal bindingi189 – 1891Zinc 2By similarity
Metal bindingi202 – 2021Zinc 1By similarity
Metal bindingi205 – 2051Zinc 1By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri130 – 21485CR-typeAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. chaperone binding Source: UniProt
  3. metal ion binding Source: UniProtKB-KW
  4. unfolded protein binding Source: UniProt

GO - Biological processi

  1. positive regulation of cell proliferation Source: ProtInc
  2. protein refolding Source: UniProt
  3. response to heat Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
DnaJ homolog subfamily A member 2
Alternative name(s):
Cell cycle progression restoration gene 3 protein
Dnj3
Short name:
Dj3
HIRA-interacting protein 4
Renal carcinoma antigen NY-REN-14
Gene namesi
Name:DNAJA2
Synonyms:CPR3, HIRIP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:14884. DNAJA2.

Subcellular locationi

Membrane Curated; Lipid-anchor Curated

GO - Cellular componenti

  1. cytosol Source: UniProt
  2. extracellular vesicular exosome Source: UniProt
  3. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27409.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 409409DnaJ homolog subfamily A member 2PRO_0000071011Add
BLAST
Propeptidei410 – 4123Removed in mature formCuratedPRO_0000393942

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391N6-acetyllysineBy similarity
Modified residuei78 – 781Phosphoserine3 Publications
Modified residuei152 – 1521N6-acetyllysineBy similarity
Modified residuei409 – 4091Cysteine methyl esterCurated
Lipidationi409 – 4091S-farnesyl cysteine1 Publication

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiO60884.
PaxDbiO60884.
PeptideAtlasiO60884.
PRIDEiO60884.

PTM databases

PhosphoSiteiO60884.

Expressioni

Gene expression databases

BgeeiO60884.
CleanExiHS_DNAJA2.
ExpressionAtlasiO60884. baseline and differential.
GenevestigatoriO60884.

Organism-specific databases

HPAiHPA049789.
HPA060538.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
AICDAQ9GZX73EBI-352957,EBI-3834328
DNAJA4Q8WW222EBI-352957,EBI-2555157
NUDCQ9Y2662EBI-352957,EBI-357298

Protein-protein interaction databases

BioGridi115582. 39 interactions.
IntActiO60884. 31 interactions.
MINTiMINT-5005885.
STRINGi9606.ENSP00000314030.

Structurei

3D structure databases

ProteinModelPortaliO60884.
SMRiO60884. Positions 4-377.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 7063JAdd
BLAST
Repeati143 – 1508CXXCXGXG motif
Repeati159 – 1668CXXCXGXG motif
Repeati186 – 1938CXXCXGXG motif
Repeati202 – 2098CXXCXGXG motif

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri130 – 21485CR-typeAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0484.
GeneTreeiENSGT00490000043321.
HOGENOMiHOG000226718.
HOVERGENiHBG066727.
InParanoidiO60884.
KOiK09503.
OMAiKEHETYR.
OrthoDBiEOG7XM2XK.
PhylomeDBiO60884.
TreeFamiTF105141.

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]

Sequencei

Sequence statusi: Complete.

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

O60884-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MANVADTKLY DILGVPPGAS ENELKKAYRK LAKEYHPDKN PNAGDKFKEI
60 70 80 90 100
SFAYEVLSNP EKRELYDRYG EQGLREGSGG GGGMDDIFSH IFGGGLFGFM
110 120 130 140 150
GNQSRSRNGR RRGEDMMHPL KVSLEDLYNG KTTKLQLSKN VLCSACSGQG
160 170 180 190 200
GKSGAVQKCS ACRGRGVRIM IRQLAPGMVQ QMQSVCSDCN GEGEVINEKD
210 220 230 240 250
RCKKCEGKKV IKEVKILEVH VDKGMKHGQR ITFTGEADQA PGVEPGDIVL
260 270 280 290 300
LLQEKEHEVF QRDGNDLHMT YKIGLVEALC GFQFTFKHLD GRQIVVKYPP
310 320 330 340 350
GKVIEPGCVR VVRGEGMPQY RNPFEKGDLY IKFDVQFPEN NWINPDKLSE
360 370 380 390 400
LEDLLPSRPE VPNIIGETEE VELQEFDSTR GSGGGQRREA YNDSSDEESS
410
SHHGPGVQCA HQ
Length:412
Mass (Da):45,746
Last modified:August 1, 1998 - v1
Checksum:i8F1BC367425CB428
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171P → A in AAB69313. (PubMed:9383053)Curated
Sequence conflicti42 – 465NAGDK → QMQETN in AAB69313. (PubMed:9383053)Curated
Sequence conflicti83 – 9311GMDDIFSHIFG → WHGLIFSLTVFC in AAB69313. (PubMed:9383053)CuratedAdd
BLAST
Sequence conflicti242 – 25716GVEPG…QEKEH → EWNPETLFFLLPGEKNM in AAB69313. (PubMed:9383053)CuratedAdd
BLAST
Sequence conflicti286 – 2872FK → LS in AAB69313. (PubMed:9383053)Curated
Sequence conflicti328 – 3281D → G in AAB69313. (PubMed:9383053)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001309 mRNA. Translation: CAA04669.1.
Y13350 mRNA. Translation: CAA73791.1.
AF011793 mRNA. Translation: AAB69313.1.
AK313031 mRNA. Translation: BAG35864.1.
CH471092 Genomic DNA. Translation: EAW82693.1.
BC013044 mRNA. Translation: AAH13044.1.
BC015809 mRNA. Translation: AAH15809.1.
CCDSiCCDS10726.1.
RefSeqiNP_005871.1. NM_005880.3.
UniGeneiHs.368078.

Genome annotation databases

EnsembliENST00000317089; ENSP00000314030; ENSG00000069345.
GeneIDi10294.
KEGGihsa:10294.
UCSCiuc002eeo.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001309 mRNA. Translation: CAA04669.1 .
Y13350 mRNA. Translation: CAA73791.1 .
AF011793 mRNA. Translation: AAB69313.1 .
AK313031 mRNA. Translation: BAG35864.1 .
CH471092 Genomic DNA. Translation: EAW82693.1 .
BC013044 mRNA. Translation: AAH13044.1 .
BC015809 mRNA. Translation: AAH15809.1 .
CCDSi CCDS10726.1.
RefSeqi NP_005871.1. NM_005880.3.
UniGenei Hs.368078.

3D structure databases

ProteinModelPortali O60884.
SMRi O60884. Positions 4-377.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115582. 39 interactions.
IntActi O60884. 31 interactions.
MINTi MINT-5005885.
STRINGi 9606.ENSP00000314030.

PTM databases

PhosphoSitei O60884.

Proteomic databases

MaxQBi O60884.
PaxDbi O60884.
PeptideAtlasi O60884.
PRIDEi O60884.

Protocols and materials databases

DNASUi 10294.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000317089 ; ENSP00000314030 ; ENSG00000069345 .
GeneIDi 10294.
KEGGi hsa:10294.
UCSCi uc002eeo.2. human.

Organism-specific databases

CTDi 10294.
GeneCardsi GC16M046931.
H-InvDB HIX0173287.
HGNCi HGNC:14884. DNAJA2.
HPAi HPA049789.
HPA060538.
MIMi 611322. gene.
neXtProti NX_O60884.
PharmGKBi PA27409.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0484.
GeneTreei ENSGT00490000043321.
HOGENOMi HOG000226718.
HOVERGENi HBG066727.
InParanoidi O60884.
KOi K09503.
OMAi KEHETYR.
OrthoDBi EOG7XM2XK.
PhylomeDBi O60884.
TreeFami TF105141.

Miscellaneous databases

ChiTaRSi DNAJA2. human.
GeneWikii DNAJA2.
GenomeRNAii 10294.
NextBioi 39010.
PROi O60884.
SOURCEi Search...

Gene expression databases

Bgeei O60884.
CleanExi HS_DNAJA2.
ExpressionAtlasi O60884. baseline and differential.
Genevestigatori O60884.

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. "HIRIP4, a new human DnaJ, is a nuclear protein that interacts with the product of the DiGeorge syndrome gene candidate HIRA."
    Lorain S., Brendel C., Scamps C., Lecluse Y., Lipinski M.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Human CPR (cell cycle progression restoration) genes impart a Far-phenotype on yeast cells."
    Edwards M.C., Liegeois N., Horecka J., DePinho R.A., Sprague G.F. Jr., Tyers M., Elledge S.J.
    Genetics 147:1063-1076(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
    Tissue: Amygdala.
  4. 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].
    Tissue: Placenta and Skin.
  6. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  7. "Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70."
    Terada K., Mori M.
    J. Biol. Chem. 275:24728-24734(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "A tagging-via-substrate technology for detection and proteomics of farnesylated proteins."
    Kho Y., Kim S.C., Jiang C., Barma D., Kwon S.W., Cheng J., Jaunbergs J., Weinbaum C., Tamanoi F., Falck J., Zhao Y.
    Proc. Natl. Acad. Sci. U.S.A. 101:12479-12484(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-409.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDNJA2_HUMAN
AccessioniPrimary (citable) accession number: O60884
Secondary accession number(s): B2R7L7, O14711
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: August 1, 1998
Last modified: October 29, 2014
This is version 145 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3