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O60884 (DNJA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DNAJA2
Synonyms:CPR3, HIRIP4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Co-chaperone of Hsc70. HAMAP-Rule MF_01152

Subcellular location

Membrane; Lipid-anchor Potential HAMAP-Rule MF_01152.

Sequence similarities

Contains 1 CR-type zinc finger.

Contains 1 J domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AICDAQ9GZX73EBI-352957,EBI-3834328

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 409409DnaJ homolog subfamily A member 2 HAMAP-Rule MF_01152
PRO_0000071011
Propeptide410 – 4123Removed in mature form Probable
PRO_0000393942

Regions

Domain8 – 7063J
Repeat143 – 1508CXXCXGXG motif HAMAP-Rule MF_01152
Repeat159 – 1668CXXCXGXG motif HAMAP-Rule MF_01152
Repeat186 – 1938CXXCXGXG motif HAMAP-Rule MF_01152
Repeat202 – 2098CXXCXGXG motif HAMAP-Rule MF_01152
Zinc finger130 – 21485CR-type HAMAP-Rule MF_01152

Sites

Metal binding1431Zinc 1 By similarity
Metal binding1461Zinc 1 By similarity
Metal binding1591Zinc 2 By similarity
Metal binding1621Zinc 2 By similarity
Metal binding1861Zinc 2 By similarity
Metal binding1891Zinc 2 By similarity
Metal binding2021Zinc 1 By similarity
Metal binding2051Zinc 1 By similarity

Amino acid modifications

Modified residue391N6-acetyllysine By similarity
Modified residue781Phosphoserine Ref.9 Ref.10 Ref.11
Modified residue1521N6-acetyllysine By similarity
Modified residue4091Cysteine methyl ester Probable
Lipidation4091S-farnesyl cysteine Ref.8

Experimental info

Sequence conflict171P → A in AAB69313. Ref.2
Sequence conflict42 – 465NAGDK → QMQETN in AAB69313. Ref.2
Sequence conflict83 – 9311GMDDIFSHIFG → WHGLIFSLTVFC in AAB69313. Ref.2
Sequence conflict242 – 25716GVEPG…QEKEH → EWNPETLFFLLPGEKNM in AAB69313. Ref.2
Sequence conflict286 – 2872FK → LS in AAB69313. Ref.2
Sequence conflict3281D → G in AAB69313. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O60884 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 8F1BC367425CB428

FASTA41245,746
        10         20         30         40         50         60 
MANVADTKLY DILGVPPGAS ENELKKAYRK LAKEYHPDKN PNAGDKFKEI SFAYEVLSNP 

        70         80         90        100        110        120 
EKRELYDRYG EQGLREGSGG GGGMDDIFSH IFGGGLFGFM GNQSRSRNGR RRGEDMMHPL 

       130        140        150        160        170        180 
KVSLEDLYNG KTTKLQLSKN VLCSACSGQG GKSGAVQKCS ACRGRGVRIM IRQLAPGMVQ 

       190        200        210        220        230        240 
QMQSVCSDCN GEGEVINEKD RCKKCEGKKV IKEVKILEVH VDKGMKHGQR ITFTGEADQA 

       250        260        270        280        290        300 
PGVEPGDIVL LLQEKEHEVF QRDGNDLHMT YKIGLVEALC GFQFTFKHLD GRQIVVKYPP 

       310        320        330        340        350        360 
GKVIEPGCVR VVRGEGMPQY RNPFEKGDLY IKFDVQFPEN NWINPDKLSE LEDLLPSRPE 

       370        380        390        400        410 
VPNIIGETEE VELQEFDSTR GSGGGQRREA YNDSSDEESS SHHGPGVQCA HQ 

« Hide

References

« Hide 'large scale' references
[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. 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].
Tissue: Amygdala.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
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]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10726.1.
RefSeqNP_005871.1. NM_005880.3.
UniGeneHs.368078.

3D structure databases

ProteinModelPortalO60884.
SMRO60884. Positions 4-377.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115582. 47 interactions.
IntActO60884. 27 interactions.
MINTMINT-5005885.
STRING9606.ENSP00000314030.

PTM databases

PhosphoSiteO60884.

Proteomic databases

MaxQBO60884.
PaxDbO60884.
PeptideAtlasO60884.
PRIDEO60884.

Protocols and materials databases

DNASU10294.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000317089; ENSP00000314030; ENSG00000069345.
GeneID10294.
KEGGhsa:10294.
UCSCuc002eeo.2. human.

Organism-specific databases

CTD10294.
GeneCardsGC16M046931.
H-InvDBHIX0173287.
HGNCHGNC:14884. DNAJA2.
HPAHPA049789.
HPA060538.
MIM611322. gene.
neXtProtNX_O60884.
PharmGKBPA27409.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0484.
HOGENOMHOG000226718.
HOVERGENHBG066727.
InParanoidO60884.
KOK09503.
OMAKEHETYR.
OrthoDBEOG7XM2XK.
PhylomeDBO60884.
TreeFamTF105141.

Gene expression databases

ArrayExpressO60884.
BgeeO60884.
CleanExHS_DNAJA2.
GenevestigatorO60884.

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. 3 hits.
SSF57938. SSF57938. 1 hit.
PROSITEPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDNAJA2. human.
GeneWikiDNAJA2.
GenomeRNAi10294.
NextBio39010.
PROO60884.
SOURCESearch...

Entry information

Entry nameDNJA2_HUMAN
AccessionPrimary (citable) accession number: O60884
Secondary accession number(s): B2R7L7, O14711
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 142 of the entry and version 1 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

MIM cross-references

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

Human chromosome 16

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