DNJA4_HUMAN
ID DNJA4_HUMAN Reviewed; 397 AA.
AC Q8WW22; E9PDM9; Q6AW87; Q8N5Z4; Q8N7P2;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=DnaJ homolog subfamily A member 4;
DE Flags: Precursor;
GN Name=DNAJA4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Trachea;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Endometrial tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP ARG-226.
RC TISSUE=Brain, and Testis;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- INTERACTION:
CC Q8WW22; O60884: DNAJA2; NbExp=2; IntAct=EBI-2555157, EBI-352957;
CC Q8WW22; Q14249: ENDOG; NbExp=2; IntAct=EBI-2555157, EBI-9369928;
CC Q8WW22-2; Q8N9N5: BANP; NbExp=3; IntAct=EBI-10277181, EBI-744695;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WW22-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WW22-2; Sequence=VSP_038965;
CC Name=3;
CC IsoId=Q8WW22-3; Sequence=VSP_045696;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21720.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH31044.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK096616; BAC04828.1; -; mRNA.
DR EMBL; AK098079; BAC05229.1; -; mRNA.
DR EMBL; BX648710; CAH10558.1; -; mRNA.
DR EMBL; AC092755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471136; EAW99177.1; -; Genomic_DNA.
DR EMBL; BC021720; AAH21720.1; ALT_INIT; mRNA.
DR EMBL; BC031044; AAH31044.2; ALT_INIT; mRNA.
DR CCDS; CCDS10299.2; -. [Q8WW22-2]
DR CCDS; CCDS45316.1; -. [Q8WW22-1]
DR CCDS; CCDS45317.1; -. [Q8WW22-3]
DR RefSeq; NP_001123654.1; NM_001130182.1. [Q8WW22-1]
DR RefSeq; NP_001123655.1; NM_001130183.1. [Q8WW22-3]
DR RefSeq; NP_061072.3; NM_018602.3. [Q8WW22-2]
DR RefSeq; XP_005254592.1; XM_005254535.3. [Q8WW22-1]
DR RefSeq; XP_006720664.1; XM_006720601.1. [Q8WW22-1]
DR AlphaFoldDB; Q8WW22; -.
DR SMR; Q8WW22; -.
DR BioGRID; 120675; 82.
DR IntAct; Q8WW22; 28.
DR MINT; Q8WW22; -.
DR STRING; 9606.ENSP00000378324; -.
DR iPTMnet; Q8WW22; -.
DR PhosphoSitePlus; Q8WW22; -.
DR BioMuta; DNAJA4; -.
DR DMDM; 27805462; -.
DR EPD; Q8WW22; -.
DR jPOST; Q8WW22; -.
DR MassIVE; Q8WW22; -.
DR MaxQB; Q8WW22; -.
DR PaxDb; Q8WW22; -.
DR PeptideAtlas; Q8WW22; -.
DR PRIDE; Q8WW22; -.
DR ProteomicsDB; 19707; -.
DR ProteomicsDB; 74849; -. [Q8WW22-1]
DR ProteomicsDB; 74850; -. [Q8WW22-2]
DR Antibodypedia; 27578; 144 antibodies from 25 providers.
DR DNASU; 55466; -.
DR Ensembl; ENST00000343789.7; ENSP00000339581.3; ENSG00000140403.13. [Q8WW22-1]
DR Ensembl; ENST00000394852.8; ENSP00000378321.3; ENSG00000140403.13. [Q8WW22-1]
DR Ensembl; ENST00000394855.7; ENSP00000378324.3; ENSG00000140403.13. [Q8WW22-2]
DR Ensembl; ENST00000446172.2; ENSP00000413499.2; ENSG00000140403.13. [Q8WW22-3]
DR GeneID; 55466; -.
DR KEGG; hsa:55466; -.
DR MANE-Select; ENST00000394852.8; ENSP00000378321.3; NM_001130182.2; NP_001123654.1.
DR UCSC; uc002bdi.4; human. [Q8WW22-1]
DR CTD; 55466; -.
DR DisGeNET; 55466; -.
DR GeneCards; DNAJA4; -.
DR HGNC; HGNC:14885; DNAJA4.
DR HPA; ENSG00000140403; Tissue enhanced (tongue).
DR neXtProt; NX_Q8WW22; -.
DR OpenTargets; ENSG00000140403; -.
DR PharmGKB; PA27411; -.
DR VEuPathDB; HostDB:ENSG00000140403; -.
DR eggNOG; KOG0712; Eukaryota.
DR GeneTree; ENSGT00940000155707; -.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; Q8WW22; -.
DR PhylomeDB; Q8WW22; -.
DR TreeFam; TF105141; -.
DR PathwayCommons; Q8WW22; -.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR SignaLink; Q8WW22; -.
DR BioGRID-ORCS; 55466; 23 hits in 1068 CRISPR screens.
DR ChiTaRS; DNAJA4; human.
DR GenomeRNAi; 55466; -.
DR Pharos; Q8WW22; Tbio.
DR PRO; PR:Q8WW22; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8WW22; protein.
DR Bgee; ENSG00000140403; Expressed in bronchial epithelial cell and 183 other tissues.
DR ExpressionAtlas; Q8WW22; baseline and differential.
DR Genevisible; Q8WW22; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IMP:ARUK-UCL.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0042026; P:protein refolding; IDA:UniProtKB.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR HAMAP; MF_01152; DnaJ; 1.
DR InterPro; IPR012724; DnaJ.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR044713; DNJA1/2-like.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR43888; PTHR43888; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 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; 2.
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 Alternative splicing; Chaperone; Lipoprotein; Membrane; Metal-binding;
KW Methylation; Phosphoprotein; Prenylation; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..394
FT /note="DnaJ homolog subfamily A member 4"
FT /id="PRO_0000071014"
FT PROPEP 395..397
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396760"
FT DOMAIN 4..70
FT /note="J"
FT REPEAT 135..142
FT /note="CXXCXGXG motif"
FT REPEAT 151..158
FT /note="CXXCXGXG motif"
FT REPEAT 178..185
FT /note="CXXCXGXG motif"
FT REPEAT 194..201
FT /note="CXXCXGXG motif"
FT ZN_FING 122..206
FT /note="CR-type"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 394
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 394
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..44
FT /note="MVKETQYYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEGEK -> MWES
FT LTLDSGQISALTR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045696"
FT VAR_SEQ 1
FT /note="M -> MARGGSQSWSSGESDGQPKEQTPEKPRHKM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_038965"
FT VARIANT 226
FT /note="H -> R (in dbSNP:rs17852881)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_069064"
FT CONFLICT 33
FT /note="Y -> C (in Ref. 1; BAC05229)"
FT /evidence="ECO:0000305"
FT CONFLICT Q8WW22-3:1
FT /note="M -> T (in Ref. 5; AAH31044)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 44798 MW; 60D6AAD12C9B2529 CRC64;
MVKETQYYDI LGVKPSASPE EIKKAYRKLA LKYHPDKNPD EGEKFKLISQ AYEVLSDPKK
RDVYDQGGEQ AIKEGGSGSP SFSSPMDIFD MFFGGGGRMA RERRGKNVVH QLSVTLEDLY
NGVTKKLALQ KNVICEKCEG VGGKKGSVEK CPLCKGRGMQ IHIQQIGPGM VQQIQTVCIE
CKGQGERINP KDRCESCSGA KVIREKKIIE VHVEKGMKDG QKILFHGEGD QEPELEPGDV
IIVLDQKDHS VFQRRGHDLI MKMKIQLSEA LCGFKKTIKT LDNRILVITS KAGEVIKHGD
LRCVRDEGMP IYKAPLEKGI LIIQFLVIFP EKHWLSLEKL PQLEALLPPR QKVRITDDMD
QVELKEFCPN EQNWRQHREA YEEDEDGPQA GVQCQTA
