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DnaJ homolog subfamily B member 4 (Heat shock 40 kDa protein 1 homolog) (HSP40 homolog) (Heat shock protein 40 homolog) (Human liver DnaJ-like protein)

 DNJB4_HUMAN             Reviewed;         337 AA.
Q9UDY4; B2R824; Q13431;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
12-SEP-2018, entry version 152.
RecName: Full=DnaJ homolog subfamily B member 4;
AltName: Full=Heat shock 40 kDa protein 1 homolog;
Short=HSP40 homolog;
Short=Heat shock protein 40 homolog;
AltName: Full=Human liver DnaJ-like protein;
Name=DNAJB4; Synonyms=DNAJW, HLJ1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=9546042; DOI=10.1016/S0167-4838(97)00207-0;
Hoe K.L., Won M., Chung K.S., Jang Y.J., Lee S.B., Kim D.U., Lee J.W.,
Yun J.H., Yoo H.S.;
"Isolation of a new member of DnaJ-like heat shock protein 40 (Hsp40)
from human liver.";
Biochim. Biophys. Acta 1383:4-8(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[5]
PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
Won M., Moon K.-M., Lee C.-E., Yoo H.-S.;
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 2-13; 45-59; 166-177; 219-236; 260-275 AND
293-302, CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Embryonic kidney;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[7]
HOMODIMERIZATION.
PubMed=15661747; DOI=10.1074/jbc.M408349200;
Borges J.C., Fischer H., Craievich A.F., Ramos C.H.I.;
"Low resolution structural study of two human HSP40 chaperones in
solution. DJA1 from subfamily A and DJB4 from subfamily B have
different quaternary structures.";
J. Biol. Chem. 280:13671-13681(2005).
[8]
SUBCELLULAR LOCATION, AND INTERACTION WITH OPRM1.
PubMed=16542645; DOI=10.1016/j.brainres.2006.01.125;
Ancevska-Taneva N., Onoprishvili I., Andria M.L., Hiller J.M.,
Simon E.J.;
"A member of the heat shock protein 40 family, hlj1, binds to the
carboxyl tail of the human mu opioid receptor.";
Brain Res. 1081:28-33(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
SUBCELLULAR LOCATION.
PubMed=18837411;
Lin X., Ma L., Wang J., Tan Y., Wen Q., Luo W., Su J., Lin Y.,
Wang X.;
"Preparation of the anti-HLJ1 monoclonal antibodies and establishment
of method for detection of the antigen.";
Sheng Wu Gong Cheng Xue Bao 24:1293-1299(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-148, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
INTERACTION WITH SDIM1.
PubMed=21255413; DOI=10.1186/1750-1326-6-9;
Lei J.X., Cassone C.G., Luebbert C., Liu Q.Y.;
"A novel neuron-enriched protein SDIM1 is down regulated in
Alzheimer's brains and attenuates cell death induced by DNAJB4 over-
expression in neuro-progenitor cells.";
Mol. Neurodegener. 6:9-9(2011).
[14]
FUNCTION.
PubMed=24318877; DOI=10.1074/jbc.M113.521997;
Rauch J.N., Gestwicki J.E.;
"Binding of human nucleotide exchange factors to heat shock protein 70
(Hsp70) generates functionally distinct complexes in vitro.";
J. Biol. Chem. 289:1402-1414(2014).
-!- FUNCTION: Probable chaperone. Stimulates ATP hydrolysis and the
folding of unfolded proteins mediated by HSPA1A/B (in vitro)
(PubMed:24318877). {ECO:0000269|PubMed:24318877}.
-!- SUBUNIT: Homodimer. The C-terminal section interacts with the C-
terminal tail of OPRM1. Interacts also with SDIM1.
{ECO:0000269|PubMed:16542645, ECO:0000269|PubMed:21255413}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18837411}.
Cell membrane {ECO:0000269|PubMed:16542645}. Note=Cytoplasmic
according to PubMed:18837411 and membrane-associated according to
PubMed:16542645.
-!- TISSUE SPECIFICITY: Expressed in heart, pancreas and skeletal
muscle, and to a lesser extent in brain, placenta and liver.
{ECO:0000269|PubMed:9546042}.
-!- INDUCTION: By heat shock. {ECO:0000269|PubMed:9546042}.
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EMBL; U40992; AAC14483.2; -; mRNA.
EMBL; AK313205; BAG36021.1; -; mRNA.
EMBL; CH471059; EAX06354.1; -; Genomic_DNA.
EMBL; BC034721; AAH34721.1; -; mRNA.
EMBL; U41290; AAB07346.1; ALT_FRAME; Genomic_DNA.
CCDS; CCDS684.1; -.
PIR; G02272; G02272.
RefSeq; NP_001304028.1; NM_001317099.1.
RefSeq; NP_001304029.1; NM_001317100.1.
RefSeq; NP_001304030.1; NM_001317101.1.
RefSeq; NP_001304031.1; NM_001317102.1.
RefSeq; NP_001304032.1; NM_001317103.1.
RefSeq; NP_008965.2; NM_007034.4.
UniGene; Hs.13852; -.
UniGene; Hs.690049; -.
ProteinModelPortal; Q9UDY4; -.
SMR; Q9UDY4; -.
BioGrid; 116263; 67.
IntAct; Q9UDY4; 31.
MINT; Q9UDY4; -.
STRING; 9606.ENSP00000359799; -.
iPTMnet; Q9UDY4; -.
PhosphoSitePlus; Q9UDY4; -.
BioMuta; DNAJB4; -.
DMDM; 8928155; -.
EPD; Q9UDY4; -.
MaxQB; Q9UDY4; -.
PaxDb; Q9UDY4; -.
PeptideAtlas; Q9UDY4; -.
PRIDE; Q9UDY4; -.
ProteomicsDB; 84132; -.
DNASU; 11080; -.
Ensembl; ENST00000370763; ENSP00000359799; ENSG00000162616.
GeneID; 11080; -.
KEGG; hsa:11080; -.
UCSC; uc001dij.4; human.
CTD; 11080; -.
DisGeNET; 11080; -.
EuPathDB; HostDB:ENSG00000162616.8; -.
GeneCards; DNAJB4; -.
HGNC; HGNC:14886; DNAJB4.
HPA; CAB004995; -.
HPA; HPA028383; -.
HPA; HPA028385; -.
MIM; 611327; gene.
neXtProt; NX_Q9UDY4; -.
OpenTargets; ENSG00000162616; -.
PharmGKB; PA27416; -.
eggNOG; KOG0714; Eukaryota.
eggNOG; COG0484; LUCA.
GeneTree; ENSGT00760000118947; -.
HOVERGEN; HBG066727; -.
InParanoid; Q9UDY4; -.
KO; K09510; -.
OMA; MDGRTIP; -.
OrthoDB; EOG091G0DLS; -.
PhylomeDB; Q9UDY4; -.
TreeFam; TF105141; -.
ChiTaRS; DNAJB4; human.
GeneWiki; DNAJB4; -.
GenomeRNAi; 11080; -.
PRO; PR:Q9UDY4; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000162616; Expressed in 231 organ(s), highest expression level in skeletal muscle tissue of rectus abdominis.
CleanEx; HS_DNAJB4; -.
ExpressionAtlas; Q9UDY4; baseline and differential.
Genevisible; Q9UDY4; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0009408; P:response to heat; TAS:ProtInc.
GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
CDD; cd06257; DnaJ; 1.
Gene3D; 1.10.287.110; -; 1.
InterPro; IPR002939; DnaJ_C.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR018253; DnaJ_domain_CS.
InterPro; IPR008971; HSP40/DnaJ_pept-bd.
InterPro; IPR036869; J_dom_sf.
Pfam; PF00226; DnaJ; 1.
Pfam; PF01556; DnaJ_C; 1.
PRINTS; PR00625; JDOMAIN.
SMART; SM00271; DnaJ; 1.
SUPFAM; SSF46565; SSF46565; 1.
SUPFAM; SSF49493; SSF49493; 2.
PROSITE; PS00636; DNAJ_1; 1.
PROSITE; PS50076; DNAJ_2; 1.
1: Evidence at protein level;
Cell membrane; Chaperone; Complete proteome; Cytoplasm;
Direct protein sequencing; Membrane; Phosphoprotein;
Reference proteome; Stress response.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.6}.
CHAIN 2 337 DnaJ homolog subfamily B member 4.
/FTId=PRO_0000071021.
DOMAIN 2 70 J. {ECO:0000255|PROSITE-
ProRule:PRU00286}.
MOD_RES 122 122 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 148 148 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
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


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