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UniProtKB/Swiss-Prot entry O60884


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DNJA2_HUMAN
Primary accession number O60884
Secondary accession number O14711
Integrated into Swiss-Prot on July 11, 2001
Sequence was last modified on August 1, 1998 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 87)
Name and origin of the protein
Protein name DnaJ homolog subfamily A member 2
Synonyms HIRA-interacting protein 4
Cell cycle progression restoration gene 3 protein
Dnj3
Dj3
Renal carcinoma antigen NY-REN-14
Gene name
Name: DNAJA2
Synonyms: CPR3, HIRIP4
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Lorain S., Brendel C., Scamps C., Lecluse Y., Lipinski M.;
"HIRIP4, a new human DnaJ, is a nuclear protein that interacts with the product of the DiGeorge syndrome gene candidate HIRA.";
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9383053 [NCBI, ExPASy, EBI, Israel, Japan]
Edwards M.C., Liegeois N., Horecka J., DePinho R.A., Sprague G.F. Jr., Tyers M., Elledge S.J.;
"Human CPR (cell cycle progression restoration) genes impart a Far-phenotype on yeast cells.";
Genetics 147:1063-1076(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5; PubMed=10508479 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Antigens recognized by autologous antibody in patients with renal-cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[5]
CHARACTERIZATION.
DOI=10.1074/jbc.M002021200; PubMed=10816573 [NCBI, ExPASy, EBI, Israel, Japan]
Terada K., Mori M.;
"Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70.";
J. Biol. Chem. 275:24728-24734(2000).
[6]
ISOPRENYLATION AT CYS-409.
DOI=10.1073/pnas.0403413101; PubMed=15308774 [NCBI, ExPASy, EBI, Israel, Japan]
Kho Y., Kim S.C., Jiang C., Barma D., Kwon S.W., Cheng J., Jaunbergs J., Weinbaum C., Tamanoi F., Falck J., Zhao Y.;
"A tagging-via-substrate technology for detection and proteomics of farnesylated proteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12479-12484(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[8]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ001309; CAA04669.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y13350; CAA73791.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011793; AAB69313.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013044; AAH13044.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015809; AAH15809.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00032406; -.
RefSeq NP_005871.1; -.
UniGene Hs.368078
3D structure databases
HSSP P25685; 1HDJ. [HSSP ENTRY / PDB]
ModBase O60884.
Protein-protein interaction databases
IntAct O60884; 6.
PTM databases
PhosphoSite O60884; -.
Organism-specific databases
GeneCards GC16M045547; -.
H-InvDB HIX0005215; -.
HIX0013004; -.
HIX0038923; -.
HGNC HGNC:14884; DNAJA2.
GenAtlas DNAJA2.
MIM 611322; gene. [NCBI / EBI]
PharmGKB PA27409; -.
Gene expression databases
ArrayExpress O60884; -.
Bgee O60884; -.
CleanEx HS_DNAJA2; -.
GermOnline ENSG00000069345; Homo sapiens.
Ontologies
GO
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0031072; Molecular function: heat shock protein binding (inferred from electronic annotation from InterPro).
GO:0051082; Molecular function: unfolded protein binding (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008284; Biological process: positive regulation of cell proliferation (traceable author statement from ProtInc).
GO:0006457; Biological process: protein folding (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR002939; DnaJ_C.
IPR001623; DnaJ_N.
IPR018253; Heat_shock_DnaJ_CS.
IPR015609; Hsp40/DnaJ_Rel.
IPR003095; Hsp_DnaJ.
IPR001305; HSP_DnaJ_cys-rich.
Graphical view of domain structure.
Gene3D G3DSA:1.10.287.110; DnaJ_N; 1.
PANTHER PTHR11821; Hsp40/DnaJ_Rel; 1.
Pfam PF00226; DnaJ; 1.
PF01556; DnaJ_C; 1.
PF00684; DnaJ_CXXCXGXG; 1.
Pfam graphical view of domain structure.
PRINTS PR00625; DNAJPROTEIN.
SMART SM00271; DnaJ; 1.
SMART graphical view of domain structure.
PROSITE PS00636; DNAJ_1; 1.
PS50076; DNAJ_2; 1.
PS51188; ZF_CR; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas O60884; -.
PRIDE O60884; -.
Genome annotation databases
Ensembl ENSG00000069345; Homo sapiens. [Contig view]
GeneID 10294; -.
KEGG hsa:10294; -.
Phylogenomic databases
HOGENOM O60884; -.
HOVERGEN O60884; -.
OMA O60884; VDLQEFD.
Other
NextBio 39010; -.
SOURCE DNAJA2; Homo sapiens.
ProtoNet O60884.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chaperone; Lipoprotein; Membrane; Metal-binding; Phosphoprotein; Prenylation; Repeat; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   412  412     DnaJ homolog subfamily A member 2. PRO_0000071011
DOMAIN   8    70  63     J. 
REPEAT   143   150  8     CXXCXGXG motif. 
REPEAT   159   166  8     CXXCXGXG motif. 
REPEAT   186   193  8     CXXCXGXG motif. 
REPEAT   202   209  8     CXXCXGXG motif. 
ZN_FING   130   214  85     CR-type. 
METAL   143   143        Zinc 1 (By similarity). 
METAL   146   146        Zinc 1 (By similarity). 
METAL   159   159        Zinc 2 (By similarity). 
METAL   162   162        Zinc 2 (By similarity). 
METAL   186   186        Zinc 2 (By similarity). 
METAL   189   189        Zinc 2 (By similarity). 
METAL   202   202        Zinc 1 (By similarity). 
METAL   205   205        Zinc 1 (By similarity). 
MOD_RES   78    78        Phosphoserine. 
LIPID   409   409        S-farnesyl cysteine. 
CONFLICT   17    17        P -> A (in Ref. 2; AAB69313). 
CONFLICT   42    46        NAGDK -> QMQETN (in Ref. 2; AAB69313). 
CONFLICT   83    93        GMDDIFSHIFG -> WHGLIFSLTVFC (in Ref. 2; AAB69313). 
CONFLICT   242   257        GVEPGDIVLLLQEKEH -> EWNPETLFFLLPGEKNM (in Ref. 2; AAB69313). 
CONFLICT   286   287        FK -> LS (in Ref. 2; AAB69313). 
CONFLICT   328   328        D -> G (in Ref. 2; AAB69313). 
Sequence information
Length: 412 AA [This is the length of the unprocessed precursor] Molecular weight: 45746 Da [This is the MW of the unprocessed precursor] CRC64: 8F1BC367425CB428 [This is a checksum on the sequence]
        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 

O60884 in FASTA format

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