ID DNJB4_HUMAN Reviewed; 337 AA. AC Q9UDY4; B2R824; Q13431; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 02-NOV-2016, entry version 139. DE RecName: Full=DnaJ homolog subfamily B member 4; DE AltName: Full=Heat shock 40 kDa protein 1 homolog; DE Short=HSP40 homolog; DE Short=Heat shock protein 40 homolog; DE AltName: Full=Human liver DnaJ-like protein; GN Name=DNAJB4; Synonyms=DNAJW, HLJ1; 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], INDUCTION, AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=9546042; DOI=10.1016/S0167-4838(97)00207-0; RA Hoe K.L., Won M., Chung K.S., Jang Y.J., Lee S.B., Kim D.U., Lee J.W., RA Yun J.H., Yoo H.S.; RT "Isolation of a new member of DnaJ-like heat shock protein 40 (Hsp40) RT from human liver."; RL Biochim. Biophys. Acta 1383:4-8(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [3] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lymph; 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 [5] RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RA Won M., Moon K.-M., Lee C.-E., Yoo H.-S.; RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases. RN [6] RP PROTEIN SEQUENCE OF 2-13; 45-59; 166-177; 219-236; 260-275 AND RP 293-302, CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Embryonic kidney; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [7] RP HOMODIMERIZATION. RX PubMed=15661747; DOI=10.1074/jbc.M408349200; RA Borges J.C., Fischer H., Craievich A.F., Ramos C.H.I.; RT "Low resolution structural study of two human HSP40 chaperones in RT solution. DJA1 from subfamily A and DJB4 from subfamily B have RT different quaternary structures."; RL J. Biol. Chem. 280:13671-13681(2005). RN [8] RP SUBCELLULAR LOCATION, AND INTERACTION WITH OPRM1. RX PubMed=16542645; DOI=10.1016/j.brainres.2006.01.125; RA Ancevska-Taneva N., Onoprishvili I., Andria M.L., Hiller J.M., RA Simon E.J.; RT "A member of the heat shock protein 40 family, hlj1, binds to the RT carboxyl tail of the human mu opioid receptor."; RL Brain Res. 1081:28-33(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=18837411; RA Lin X., Ma L., Wang J., Tan Y., Wen Q., Luo W., Su J., Lin Y., RA Wang X.; RT "Preparation of the anti-HLJ1 monoclonal antibodies and establishment RT of method for detection of the antigen."; RL Sheng Wu Gong Cheng Xue Bao 24:1293-1299(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-148, AND 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., 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). RN [13] RP INTERACTION WITH SDIM1. RX PubMed=21255413; DOI=10.1186/1750-1326-6-9; RA Lei J.X., Cassone C.G., Luebbert C., Liu Q.Y.; RT "A novel neuron-enriched protein SDIM1 is down regulated in RT Alzheimer's brains and attenuates cell death induced by DNAJB4 over- RT expression in neuro-progenitor cells."; RL Mol. Neurodegener. 6:9-9(2011). CC -!- FUNCTION: Probable chaperone. CC -!- SUBUNIT: Homodimer. The C-terminal section interacts with the C- CC terminal tail of OPRM1. Interacts also with SDIM1. CC {ECO:0000269|PubMed:16542645, ECO:0000269|PubMed:21255413}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18837411}. CC Cell membrane {ECO:0000269|PubMed:16542645}. Note=Cytoplasmic CC according to PubMed:18837411 and membrane-associated according to CC PubMed:16542645. CC -!- TISSUE SPECIFICITY: Expressed in heart, pancreas and skeletal CC muscle, and to a lesser extent in brain, placenta and liver. CC {ECO:0000269|PubMed:9546042}. CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:9546042}. CC -!- SIMILARITY: Contains 1 J domain. {ECO:0000255|PROSITE- CC ProRule:PRU00286}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U40992; AAC14483.2; -; mRNA. DR EMBL; AK313205; BAG36021.1; -; mRNA. DR EMBL; CH471059; EAX06354.1; -; Genomic_DNA. DR EMBL; BC034721; AAH34721.1; -; mRNA. DR EMBL; U41290; AAB07346.1; ALT_FRAME; Genomic_DNA. DR CCDS; CCDS684.1; -. DR PIR; G02272; G02272. DR RefSeq; NP_001304028.1; NM_001317099.1. DR RefSeq; NP_001304029.1; NM_001317100.1. DR RefSeq; NP_001304030.1; NM_001317101.1. DR RefSeq; NP_001304031.1; NM_001317102.1. DR RefSeq; NP_001304032.1; NM_001317103.1. DR RefSeq; NP_008965.2; NM_007034.4. DR UniGene; Hs.13852; -. DR UniGene; Hs.690049; -. DR ProteinModelPortal; Q9UDY4; -. DR SMR; Q9UDY4; -. DR BioGrid; 116263; 57. DR IntAct; Q9UDY4; 24. DR MINT; MINT-1142940; -. DR STRING; 9606.ENSP00000359799; -. DR iPTMnet; Q9UDY4; -. DR PhosphoSitePlus; Q9UDY4; -. DR BioMuta; DNAJB4; -. DR DMDM; 8928155; -. DR EPD; Q9UDY4; -. DR MaxQB; Q9UDY4; -. DR PaxDb; Q9UDY4; -. DR PeptideAtlas; Q9UDY4; -. DR PRIDE; Q9UDY4; -. DR DNASU; 11080; -. DR Ensembl; ENST00000370763; ENSP00000359799; ENSG00000162616. DR GeneID; 11080; -. DR KEGG; hsa:11080; -. DR UCSC; uc001dij.4; human. DR CTD; 11080; -. DR DisGeNET; 11080; -. DR GeneCards; DNAJB4; -. DR HGNC; HGNC:14886; DNAJB4. DR HPA; CAB004995; -. DR HPA; HPA028383; -. DR HPA; HPA028385; -. DR MIM; 611327; gene. DR neXtProt; NX_Q9UDY4; -. DR OpenTargets; ENSG00000162616; -. DR PharmGKB; PA27416; -. DR eggNOG; KOG0714; Eukaryota. DR eggNOG; COG0484; LUCA. DR GeneTree; ENSGT00760000118947; -. DR HOVERGEN; HBG066727; -. DR InParanoid; Q9UDY4; -. DR KO; K09510; -. DR OMA; MDGRTIP; -. DR OrthoDB; EOG091G0DLS; -. DR PhylomeDB; Q9UDY4; -. DR TreeFam; TF105141; -. DR BioCyc; ZFISH:ENSG00000162616-MONOMER; -. DR GeneWiki; DNAJB4; -. DR GenomeRNAi; 11080; -. DR PRO; PR:Q9UDY4; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000162616; -. DR CleanEx; HS_DNAJB4; -. DR ExpressionAtlas; Q9UDY4; baseline and differential. DR Genevisible; Q9UDY4; HS. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0051087; F:chaperone binding; IPI:UniProtKB. DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR GO; GO:0009408; P:response to heat; TAS:ProtInc. DR GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc. DR CDD; cd06257; DnaJ; 1. DR Gene3D; 1.10.287.110; -; 1. DR InterPro; IPR002939; DnaJ_C. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR018253; DnaJ_domain_CS. DR InterPro; IPR008971; HSP40/DnaJ_pept-bd. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF01556; DnaJ_C; 1. DR PRINTS; PR00625; JDOMAIN. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF46565; SSF46565; 1. DR SUPFAM; SSF49493; SSF49493; 2. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. PE 1: Evidence at protein level; KW Cell membrane; Chaperone; Complete proteome; Cytoplasm; KW Direct protein sequencing; Membrane; Phosphoprotein; KW Reference proteome; Stress response. FT INIT_MET 1 1 Removed. {ECO:0000269|Ref.6}. FT CHAIN 2 337 DnaJ homolog subfamily B member 4. FT /FTId=PRO_0000071021. FT DOMAIN 2 70 J. {ECO:0000255|PROSITE- FT ProRule:PRU00286}. FT MOD_RES 122 122 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 148 148 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. SQ SEQUENCE 337 AA; 37807 MW; C7A9C613F73BCDAC CRC64; MGKDYYCILG IEKGASDEDI KKAYRKQALK FHPDKNKSPQ AEEKFKEVAE AYEVLSDPKK REIYDQFGEE GLKGGAGGTD GQGGTFRYTF HGDPHATFAA FFGGSNPFEI FFGRRMGGGR DSEEMEIDGD PFSAFGFSMN GYPRDRNSVG PSRLKQDPPV IHELRVSLEE IYSGCTKRMK ISRKRLNADG RSYRSEDKIL TIEIKKGWKE GTKITFPREG DETPNSIPAD IVFIIKDKDH PKFKRDGSNI IYTAKISLRE ALCGCSINVP TLDGRNIPMS VNDIVKPGMR RRIIGYGLPF PKNPDQRGDL LIEFEVSFPD TISSSSKEVL RKHLPAS //