Full text data of DNAJA2
DNAJA2
(CPR3, HIRIP4)
[Confidence: low (only semi-automatic identification from reviews)]
DnaJ homolog subfamily A member 2 (Cell cycle progression restoration gene 3 protein; Dnj3; Dj3; HIRA-interacting protein 4; Renal carcinoma antigen NY-REN-14; Flags: Precursor)
DnaJ homolog subfamily A member 2 (Cell cycle progression restoration gene 3 protein; Dnj3; Dj3; HIRA-interacting protein 4; Renal carcinoma antigen NY-REN-14; Flags: Precursor)
UniProt
O60884
ID DNJA2_HUMAN Reviewed; 412 AA.
AC O60884; B2R7L7; O14711;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1998, sequence version 1.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=DnaJ homolog subfamily A member 2;
DE AltName: Full=Cell cycle progression restoration gene 3 protein;
DE AltName: Full=Dnj3;
DE Short=Dj3;
DE AltName: Full=HIRA-interacting protein 4;
DE AltName: Full=Renal carcinoma antigen NY-REN-14;
DE Flags: Precursor;
GN Name=DNAJA2; Synonyms=CPR3, HIRIP4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lorain S., Brendel C., Scamps C., Lecluse Y., Lipinski M.;
RT "HIRIP4, a new human DnaJ, is a nuclear protein that interacts with
RT the product of the DiGeorge syndrome gene candidate HIRA.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9383053;
RA Edwards M.C., Liegeois N., Horecka J., DePinho R.A., Sprague G.F. Jr.,
RA Tyers M., Elledge S.J.;
RT "Human CPR (cell cycle progression restoration) genes impart a Far-
RT phenotype on yeast cells.";
RL Genetics 147:1063-1076(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-
RT cell carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [7]
RP CHARACTERIZATION.
RX PubMed=10816573; DOI=10.1074/jbc.M002021200;
RA Terada K., Mori M.;
RT "Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones
RT of hsc70.";
RL J. Biol. Chem. 275:24728-24734(2000).
RN [8]
RP ISOPRENYLATION AT CYS-409.
RX PubMed=15308774; DOI=10.1073/pnas.0403413101;
RA Kho Y., Kim S.C., Jiang C., Barma D., Kwon S.W., Cheng J.,
RA Jaunbergs J., Weinbaum C., Tamanoi F., Falck J., Zhao Y.;
RT "A tagging-via-substrate technology for detection and proteomics of
RT farnesylated proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12479-12484(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Co-chaperone of Hsc70.
CC -!- INTERACTION:
CC Q9GZX7:AICDA; NbExp=3; IntAct=EBI-352957, EBI-3834328;
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor (Potential).
CC -!- SIMILARITY: Contains 1 CR-type zinc finger.
CC -!- SIMILARITY: Contains 1 J domain.
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DR EMBL; AJ001309; CAA04669.1; -; mRNA.
DR EMBL; Y13350; CAA73791.1; -; mRNA.
DR EMBL; AF011793; AAB69313.1; -; mRNA.
DR EMBL; AK313031; BAG35864.1; -; mRNA.
DR EMBL; CH471092; EAW82693.1; -; Genomic_DNA.
DR EMBL; BC013044; AAH13044.1; -; mRNA.
DR EMBL; BC015809; AAH15809.1; -; mRNA.
DR RefSeq; NP_005871.1; NM_005880.3.
DR UniGene; Hs.368078; -.
DR ProteinModelPortal; O60884; -.
DR SMR; O60884; 4-72, 111-377.
DR IntAct; O60884; 24.
DR MINT; MINT-5005885; -.
DR STRING; 9606.ENSP00000314030; -.
DR PhosphoSite; O60884; -.
DR PaxDb; O60884; -.
DR PeptideAtlas; O60884; -.
DR PRIDE; O60884; -.
DR DNASU; 10294; -.
DR Ensembl; ENST00000317089; ENSP00000314030; ENSG00000069345.
DR GeneID; 10294; -.
DR KEGG; hsa:10294; -.
DR UCSC; uc002eeo.2; human.
DR CTD; 10294; -.
DR GeneCards; GC16M046931; -.
DR H-InvDB; HIX0173287; -.
DR HGNC; HGNC:14884; DNAJA2.
DR MIM; 611322; gene.
DR neXtProt; NX_O60884; -.
DR PharmGKB; PA27409; -.
DR eggNOG; COG0484; -.
DR HOGENOM; HOG000226718; -.
DR HOVERGEN; HBG066727; -.
DR InParanoid; O60884; -.
DR KO; K09503; -.
DR OMA; LFSFMGN; -.
DR OrthoDB; EOG7XM2XK; -.
DR PhylomeDB; O60884; -.
DR ChiTaRS; DNAJA2; human.
DR GeneWiki; DNAJA2; -.
DR GenomeRNAi; 10294; -.
DR NextBio; 39010; -.
DR PRO; PR:O60884; -.
DR ArrayExpress; O60884; -.
DR Bgee; O60884; -.
DR CleanEx; HS_DNAJA2; -.
DR Genevestigator; O60884; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 2.10.230.10; -; 1.
DR InterPro; IPR012724; DnaJ.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR Pfam; PF01556; CTDII; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 3.
DR SUPFAM; SSF57938; SSF57938; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 1: Evidence at protein level;
KW Chaperone; Complete proteome; Lipoprotein; Membrane; Metal-binding;
KW Methylation; Phosphoprotein; Prenylation; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1 409 DnaJ homolog subfamily A member 2.
FT /FTId=PRO_0000071011.
FT PROPEP 410 412 Removed in mature form (Probable).
FT /FTId=PRO_0000393942.
FT DOMAIN 8 70 J.
FT REPEAT 143 150 CXXCXGXG motif.
FT REPEAT 159 166 CXXCXGXG motif.
FT REPEAT 186 193 CXXCXGXG motif.
FT REPEAT 202 209 CXXCXGXG motif.
FT ZN_FING 130 214 CR-type.
FT METAL 143 143 Zinc 1 (By similarity).
FT METAL 146 146 Zinc 1 (By similarity).
FT METAL 159 159 Zinc 2 (By similarity).
FT METAL 162 162 Zinc 2 (By similarity).
FT METAL 186 186 Zinc 2 (By similarity).
FT METAL 189 189 Zinc 2 (By similarity).
FT METAL 202 202 Zinc 1 (By similarity).
FT METAL 205 205 Zinc 1 (By similarity).
FT MOD_RES 78 78 Phosphoserine.
FT MOD_RES 409 409 Cysteine methyl ester (Probable).
FT LIPID 409 409 S-farnesyl cysteine.
FT CONFLICT 17 17 P -> A (in Ref. 2; AAB69313).
FT CONFLICT 42 46 NAGDK -> QMQETN (in Ref. 2; AAB69313).
FT CONFLICT 83 93 GMDDIFSHIFG -> WHGLIFSLTVFC (in Ref. 2;
FT AAB69313).
FT CONFLICT 242 257 GVEPGDIVLLLQEKEH -> EWNPETLFFLLPGEKNM (in
FT Ref. 2; AAB69313).
FT CONFLICT 286 287 FK -> LS (in Ref. 2; AAB69313).
FT CONFLICT 328 328 D -> G (in Ref. 2; AAB69313).
SQ SEQUENCE 412 AA; 45746 MW; 8F1BC367425CB428 CRC64;
MANVADTKLY DILGVPPGAS ENELKKAYRK LAKEYHPDKN PNAGDKFKEI SFAYEVLSNP
EKRELYDRYG EQGLREGSGG GGGMDDIFSH IFGGGLFGFM GNQSRSRNGR RRGEDMMHPL
KVSLEDLYNG KTTKLQLSKN VLCSACSGQG GKSGAVQKCS ACRGRGVRIM IRQLAPGMVQ
QMQSVCSDCN GEGEVINEKD RCKKCEGKKV IKEVKILEVH VDKGMKHGQR ITFTGEADQA
PGVEPGDIVL LLQEKEHEVF QRDGNDLHMT YKIGLVEALC GFQFTFKHLD GRQIVVKYPP
GKVIEPGCVR VVRGEGMPQY RNPFEKGDLY IKFDVQFPEN NWINPDKLSE LEDLLPSRPE
VPNIIGETEE VELQEFDSTR GSGGGQRREA YNDSSDEESS SHHGPGVQCA HQ
//
ID DNJA2_HUMAN Reviewed; 412 AA.
AC O60884; B2R7L7; O14711;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1998, sequence version 1.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=DnaJ homolog subfamily A member 2;
DE AltName: Full=Cell cycle progression restoration gene 3 protein;
DE AltName: Full=Dnj3;
DE Short=Dj3;
DE AltName: Full=HIRA-interacting protein 4;
DE AltName: Full=Renal carcinoma antigen NY-REN-14;
DE Flags: Precursor;
GN Name=DNAJA2; Synonyms=CPR3, HIRIP4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lorain S., Brendel C., Scamps C., Lecluse Y., Lipinski M.;
RT "HIRIP4, a new human DnaJ, is a nuclear protein that interacts with
RT the product of the DiGeorge syndrome gene candidate HIRA.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9383053;
RA Edwards M.C., Liegeois N., Horecka J., DePinho R.A., Sprague G.F. Jr.,
RA Tyers M., Elledge S.J.;
RT "Human CPR (cell cycle progression restoration) genes impart a Far-
RT phenotype on yeast cells.";
RL Genetics 147:1063-1076(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-
RT cell carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [7]
RP CHARACTERIZATION.
RX PubMed=10816573; DOI=10.1074/jbc.M002021200;
RA Terada K., Mori M.;
RT "Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones
RT of hsc70.";
RL J. Biol. Chem. 275:24728-24734(2000).
RN [8]
RP ISOPRENYLATION AT CYS-409.
RX PubMed=15308774; DOI=10.1073/pnas.0403413101;
RA Kho Y., Kim S.C., Jiang C., Barma D., Kwon S.W., Cheng J.,
RA Jaunbergs J., Weinbaum C., Tamanoi F., Falck J., Zhao Y.;
RT "A tagging-via-substrate technology for detection and proteomics of
RT farnesylated proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12479-12484(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Co-chaperone of Hsc70.
CC -!- INTERACTION:
CC Q9GZX7:AICDA; NbExp=3; IntAct=EBI-352957, EBI-3834328;
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor (Potential).
CC -!- SIMILARITY: Contains 1 CR-type zinc finger.
CC -!- SIMILARITY: Contains 1 J domain.
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DR EMBL; AJ001309; CAA04669.1; -; mRNA.
DR EMBL; Y13350; CAA73791.1; -; mRNA.
DR EMBL; AF011793; AAB69313.1; -; mRNA.
DR EMBL; AK313031; BAG35864.1; -; mRNA.
DR EMBL; CH471092; EAW82693.1; -; Genomic_DNA.
DR EMBL; BC013044; AAH13044.1; -; mRNA.
DR EMBL; BC015809; AAH15809.1; -; mRNA.
DR RefSeq; NP_005871.1; NM_005880.3.
DR UniGene; Hs.368078; -.
DR ProteinModelPortal; O60884; -.
DR SMR; O60884; 4-72, 111-377.
DR IntAct; O60884; 24.
DR MINT; MINT-5005885; -.
DR STRING; 9606.ENSP00000314030; -.
DR PhosphoSite; O60884; -.
DR PaxDb; O60884; -.
DR PeptideAtlas; O60884; -.
DR PRIDE; O60884; -.
DR DNASU; 10294; -.
DR Ensembl; ENST00000317089; ENSP00000314030; ENSG00000069345.
DR GeneID; 10294; -.
DR KEGG; hsa:10294; -.
DR UCSC; uc002eeo.2; human.
DR CTD; 10294; -.
DR GeneCards; GC16M046931; -.
DR H-InvDB; HIX0173287; -.
DR HGNC; HGNC:14884; DNAJA2.
DR MIM; 611322; gene.
DR neXtProt; NX_O60884; -.
DR PharmGKB; PA27409; -.
DR eggNOG; COG0484; -.
DR HOGENOM; HOG000226718; -.
DR HOVERGEN; HBG066727; -.
DR InParanoid; O60884; -.
DR KO; K09503; -.
DR OMA; LFSFMGN; -.
DR OrthoDB; EOG7XM2XK; -.
DR PhylomeDB; O60884; -.
DR ChiTaRS; DNAJA2; human.
DR GeneWiki; DNAJA2; -.
DR GenomeRNAi; 10294; -.
DR NextBio; 39010; -.
DR PRO; PR:O60884; -.
DR ArrayExpress; O60884; -.
DR Bgee; O60884; -.
DR CleanEx; HS_DNAJA2; -.
DR Genevestigator; O60884; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 2.10.230.10; -; 1.
DR InterPro; IPR012724; DnaJ.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR Pfam; PF01556; CTDII; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 3.
DR SUPFAM; SSF57938; SSF57938; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 1: Evidence at protein level;
KW Chaperone; Complete proteome; Lipoprotein; Membrane; Metal-binding;
KW Methylation; Phosphoprotein; Prenylation; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1 409 DnaJ homolog subfamily A member 2.
FT /FTId=PRO_0000071011.
FT PROPEP 410 412 Removed in mature form (Probable).
FT /FTId=PRO_0000393942.
FT DOMAIN 8 70 J.
FT REPEAT 143 150 CXXCXGXG motif.
FT REPEAT 159 166 CXXCXGXG motif.
FT REPEAT 186 193 CXXCXGXG motif.
FT REPEAT 202 209 CXXCXGXG motif.
FT ZN_FING 130 214 CR-type.
FT METAL 143 143 Zinc 1 (By similarity).
FT METAL 146 146 Zinc 1 (By similarity).
FT METAL 159 159 Zinc 2 (By similarity).
FT METAL 162 162 Zinc 2 (By similarity).
FT METAL 186 186 Zinc 2 (By similarity).
FT METAL 189 189 Zinc 2 (By similarity).
FT METAL 202 202 Zinc 1 (By similarity).
FT METAL 205 205 Zinc 1 (By similarity).
FT MOD_RES 78 78 Phosphoserine.
FT MOD_RES 409 409 Cysteine methyl ester (Probable).
FT LIPID 409 409 S-farnesyl cysteine.
FT CONFLICT 17 17 P -> A (in Ref. 2; AAB69313).
FT CONFLICT 42 46 NAGDK -> QMQETN (in Ref. 2; AAB69313).
FT CONFLICT 83 93 GMDDIFSHIFG -> WHGLIFSLTVFC (in Ref. 2;
FT AAB69313).
FT CONFLICT 242 257 GVEPGDIVLLLQEKEH -> EWNPETLFFLLPGEKNM (in
FT Ref. 2; AAB69313).
FT CONFLICT 286 287 FK -> LS (in Ref. 2; AAB69313).
FT CONFLICT 328 328 D -> G (in Ref. 2; AAB69313).
SQ SEQUENCE 412 AA; 45746 MW; 8F1BC367425CB428 CRC64;
MANVADTKLY DILGVPPGAS ENELKKAYRK LAKEYHPDKN PNAGDKFKEI SFAYEVLSNP
EKRELYDRYG EQGLREGSGG GGGMDDIFSH IFGGGLFGFM GNQSRSRNGR RRGEDMMHPL
KVSLEDLYNG KTTKLQLSKN VLCSACSGQG GKSGAVQKCS ACRGRGVRIM IRQLAPGMVQ
QMQSVCSDCN GEGEVINEKD RCKKCEGKKV IKEVKILEVH VDKGMKHGQR ITFTGEADQA
PGVEPGDIVL LLQEKEHEVF QRDGNDLHMT YKIGLVEALC GFQFTFKHLD GRQIVVKYPP
GKVIEPGCVR VVRGEGMPQY RNPFEKGDLY IKFDVQFPEN NWINPDKLSE LEDLLPSRPE
VPNIIGETEE VELQEFDSTR GSGGGQRREA YNDSSDEESS SHHGPGVQCA HQ
//
MIM
611322
*RECORD*
*FIELD* NO
611322
*FIELD* TI
*611322 DNAJ/HSP40 HOMOLOG, SUBFAMILY A, MEMBER 2; DNAJA2
;;DJ3;;
CELL CYCLE PROGRESSION RESTORATION 3; CPR3
read more*FIELD* TX
DESCRIPTION
DNAJA2 belongs to the evolutionarily conserved DNAJ/HSP40 family of
proteins, which regulate molecular chaperone activity by stimulating
ATPase activity. DNAJ proteins may have up to 3 distinct domains: a
conserved 70-amino acid J domain, usually at the N terminus; a
glycine/phenylalanine (G/F)-rich region; and a cysteine-rich domain
containing 4 motifs resembling a zinc finger domain (Ohtsuka and Hata,
2000).
CLONING
By screening a human hepatoma cDNA expression library for clones that
could block mating pheromone-induced G1 arrest in yeast, Edwards et al.
(1997) cloned DNAJA2, which they called CPR3. The deduced 417-amino acid
protein shares 42% overall sequence identity with its yeast homolog
Ydj1.
By searching EST databases for J domain-containing proteins, Ohtsuka and
Hata (2000) identified 10 mouse and human DNAJ homologs, including mouse
Dnaja2. The predicted type I transmembrane protein contains 412 amino
acids with an N-terminal J domain and a C-terminal CaaX prenylation
motif. By immunohistochemical analysis and Western blot analysis, Terada
et al. (2005) found that Dnaja2 was expressed in mouse testis,
predominantly in pachytene stage spermatocytes.
GENE FUNCTION
Edwards et al. (1997) found that DNAJA2 required cyclin-3 to induce
resistance to pheromone-induced G1 arrest in yeast. DNAJA2 could also
rescue the temperature-sensitive lethality of yeast harboring a deletion
of Ydj1.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DNAJA2
gene to chromosome 16 (TMAP RH70485).
*FIELD* RF
1. 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.
2. Ohtsuka, K.; Hata, M.: Mammalian HSP40/DNAJ homologs: cloning
of novel cDNAs and a proposal for their classification and nomenclature. Cell
Stress Chaperones 5: 98-112, 2000.
3. Terada, K.; Yomogida, K.; Imai, T.; Kiyonari, H.; Takeda, N.; Kadomatsu,
T.; Yano, M.; Aizawa, S.; Mori, M.: A type I DnaJ homolog, DjA1,
regulates androgen receptor signaling and spermatogenesis. EMBO J. 24:
611-622, 2005.
*FIELD* CD
Patricia A. Hartz: 8/15/2007
*FIELD* ED
carol: 08/16/2007
carol: 8/15/2007
*RECORD*
*FIELD* NO
611322
*FIELD* TI
*611322 DNAJ/HSP40 HOMOLOG, SUBFAMILY A, MEMBER 2; DNAJA2
;;DJ3;;
CELL CYCLE PROGRESSION RESTORATION 3; CPR3
read more*FIELD* TX
DESCRIPTION
DNAJA2 belongs to the evolutionarily conserved DNAJ/HSP40 family of
proteins, which regulate molecular chaperone activity by stimulating
ATPase activity. DNAJ proteins may have up to 3 distinct domains: a
conserved 70-amino acid J domain, usually at the N terminus; a
glycine/phenylalanine (G/F)-rich region; and a cysteine-rich domain
containing 4 motifs resembling a zinc finger domain (Ohtsuka and Hata,
2000).
CLONING
By screening a human hepatoma cDNA expression library for clones that
could block mating pheromone-induced G1 arrest in yeast, Edwards et al.
(1997) cloned DNAJA2, which they called CPR3. The deduced 417-amino acid
protein shares 42% overall sequence identity with its yeast homolog
Ydj1.
By searching EST databases for J domain-containing proteins, Ohtsuka and
Hata (2000) identified 10 mouse and human DNAJ homologs, including mouse
Dnaja2. The predicted type I transmembrane protein contains 412 amino
acids with an N-terminal J domain and a C-terminal CaaX prenylation
motif. By immunohistochemical analysis and Western blot analysis, Terada
et al. (2005) found that Dnaja2 was expressed in mouse testis,
predominantly in pachytene stage spermatocytes.
GENE FUNCTION
Edwards et al. (1997) found that DNAJA2 required cyclin-3 to induce
resistance to pheromone-induced G1 arrest in yeast. DNAJA2 could also
rescue the temperature-sensitive lethality of yeast harboring a deletion
of Ydj1.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DNAJA2
gene to chromosome 16 (TMAP RH70485).
*FIELD* RF
1. 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.
2. Ohtsuka, K.; Hata, M.: Mammalian HSP40/DNAJ homologs: cloning
of novel cDNAs and a proposal for their classification and nomenclature. Cell
Stress Chaperones 5: 98-112, 2000.
3. Terada, K.; Yomogida, K.; Imai, T.; Kiyonari, H.; Takeda, N.; Kadomatsu,
T.; Yano, M.; Aizawa, S.; Mori, M.: A type I DnaJ homolog, DjA1,
regulates androgen receptor signaling and spermatogenesis. EMBO J. 24:
611-622, 2005.
*FIELD* CD
Patricia A. Hartz: 8/15/2007
*FIELD* ED
carol: 08/16/2007
carol: 8/15/2007