ID   DNJB5_HUMAN             Reviewed;         348 AA.
AC   O75953; B3KN14; B4DSA6; J3KQM9; J3KR08; Q5T656; Q8TDR7; Q96EM4;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   28-JAN-2026, entry version 184.
DE   RecName: Full=DnaJ homolog subfamily B member 5;
DE   AltName: Full=Heat shock protein Hsp40-2;
DE   AltName: Full=Heat shock protein Hsp40-3;
DE   AltName: Full=Heat shock protein cognate 40;
DE            Short=Hsc40;
GN   Name=DNAJB5; Synonyms=HSC40;
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 [MRNA] (ISOFORM 1).
RC   TISSUE=Colon;
RX   PubMed=10570961; DOI=10.1016/s0378-1119(99)00333-9;
RA   Chen M.-S., Roti J.R., Laszlo A.;
RT   "Hsc40, a new member of the hsp40 family, exhibits similar expression
RT   profile to that of hsc70 in mammalian cells.";
RL   Gene 238:333-341(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Fu Q., Yu L., Yue P., Zhou Y., Jiang J.X., Zhao S.Y.;
RT   "Cloning and expression of a new human cDNA homology to human heat-shock
RT   protein 40 mRNA.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- INTERACTION:
CC       O75953; O00555: CACNA1A; NbExp=2; IntAct=EBI-5655937, EBI-766279;
CC       O75953; Q8WZ42: TTN; NbExp=4; IntAct=EBI-5655937, EBI-681210;
CC       O75953; Q8AZK7: EBNA-LP; Xeno; NbExp=3; IntAct=EBI-5655937, EBI-1185167;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O75953-3; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O75953-4; Sequence=VSP_046223;
CC       Name=3;
CC         IsoId=O75953-5; Sequence=VSP_047250;
CC   -!- INDUCTION: Expressed under normal conditions, its expression can
CC       further be increased after various stress treatments.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH12115.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
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DR   EMBL; AF088982; AAC35860.1; -; mRNA.
DR   EMBL; AF087870; AAM10498.1; -; mRNA.
DR   EMBL; AK023253; BAG51176.1; -; mRNA.
DR   EMBL; AK299647; BAG61568.1; -; mRNA.
DR   EMBL; AL355377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471071; EAW58407.1; -; Genomic_DNA.
DR   EMBL; BC012115; AAH12115.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS35007.1; -. [O75953-3]
DR   CCDS; CCDS47959.1; -. [O75953-4]
DR   RefSeq; NP_001128476.3; NM_001135004.3.
DR   RefSeq; NP_001128477.1; NM_001135005.3. [O75953-4]
DR   RefSeq; NP_001336652.1; NM_001349723.3. [O75953-4]
DR   RefSeq; NP_001336653.1; NM_001349724.2. [O75953-3]
DR   RefSeq; NP_036398.3; NM_012266.5. [O75953-3]
DR   AlphaFoldDB; O75953; -.
DR   SMR; O75953; -.
DR   BioGRID; 117350; 120.
DR   FunCoup; O75953; 1246.
DR   IntAct; O75953; 72.
DR   MINT; O75953; -.
DR   STRING; 9606.ENSP00000404079; -.
DR   iPTMnet; O75953; -.
DR   PhosphoSitePlus; O75953; -.
DR   BioMuta; DNAJB5; -.
DR   jPOST; O75953; -.
DR   MassIVE; O75953; -.
DR   PaxDb; 9606-ENSP00000404079; -.
DR   PeptideAtlas; O75953; -.
DR   ProteomicsDB; 50319; -. [O75953-3]
DR   Pumba; O75953; -.
DR   Antibodypedia; 11397; 186 antibodies from 27 providers.
DR   DNASU; 25822; -.
DR   Ensembl; ENST00000312316.9; ENSP00000312517.5; ENSG00000137094.16. [O75953-3]
DR   Ensembl; ENST00000454002.6; ENSP00000413684.2; ENSG00000137094.16. [O75953-4]
DR   Ensembl; ENST00000545841.5; ENSP00000441999.1; ENSG00000137094.16. [O75953-3]
DR   Ensembl; ENST00000682809.1; ENSP00000507741.1; ENSG00000137094.16. [O75953-4]
DR   Ensembl; ENST00000684748.1; ENSP00000506753.1; ENSG00000137094.16. [O75953-3]
DR   GeneID; 25822; -.
DR   KEGG; hsa:25822; -.
DR   MANE-Select; ENST00000682809.1; ENSP00000507741.1; NM_001349723.3; NP_001336652.1. [O75953-4]
DR   UCSC; uc003zvs.5; human. [O75953-3]
DR   AGR; HGNC:14887; -.
DR   ClinPGx; PA27417; -.
DR   CTD; 25822; -.
DR   DisGeNET; 25822; -.
DR   GeneCards; DNAJB5; -.
DR   HGNC; HGNC:14887; DNAJB5.
DR   HPA; ENSG00000137094; Tissue enhanced (skeletal muscle, tongue).
DR   MIM; 611328; gene.
DR   OpenTargets; ENSG00000137094; -.
DR   VEuPathDB; HostDB:ENSG00000137094; -.
DR   eggNOG; KOG0714; Eukaryota.
DR   GeneTree; ENSGT00940000156090; -.
DR   HOGENOM; CLU_017633_0_0_1; -.
DR   InParanoid; O75953; -.
DR   OMA; IVFHIVE; -.
DR   OrthoDB; 550424at2759; -.
DR   PAN-GO; O75953; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; O75953; -.
DR   PathwayCommons; O75953; -.
DR   SignaLink; O75953; -.
DR   Agora; ENSG00000137094; -.
DR   BioGRID-ORCS; 25822; 11 hits in 1147 CRISPR screens.
DR   CD-CODE; 91857CE7; Nucleolus.
DR   ChiTaRS; DNAJB5; human.
DR   GenomeRNAi; 25822; -.
DR   Pharos; O75953; Tbio.
DR   PRO; PR:O75953; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; O75953; protein.
DR   Bgee; ENSG00000137094; Expressed in hindlimb stylopod muscle and 167 other cell types or tissues.
DR   ExpressionAtlas; O75953; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IPI:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0006986; P:response to unfolded protein; IEP:UniProtKB.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd10747; DnaJ_C; 1.
DR   FunFam; 1.10.287.110:FF:000005; DnaJ (Hsp40) homolog, subfamily B, member 4; 1.
DR   FunFam; 2.60.260.20:FF:000002; Dnaj homolog subfamily b member; 1.
DR   FunFam; 2.60.260.20:FF:000007; dnaJ homolog subfamily B member 5; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR051339; DnaJ_subfamily_B.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR24078:SF553; DNAJ HOMOLOG SUBFAMILY B MEMBER 5; 1.
DR   PANTHER; PTHR24078; DNAJ HOMOLOG SUBFAMILY C MEMBER; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chaperone; Proteomics identification;
KW   Reference proteome.
FT   CHAIN           1..348
FT                   /note="DnaJ homolog subfamily B member 5"
FT                   /id="PRO_0000071023"
FT   DOMAIN          4..68
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   VAR_SEQ         1
FT                   /note="M -> MFKRTVLSCPPPAAPPLQARGAFRSFPHSWGEDFLASLMFKIQLEPL
FT                   KLRAWTLNGFVKFRNKETSAGPVAVM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046223"
FT   VAR_SEQ         1
FT                   /note="M -> MGGAEAEPWGRAPGPAIGGRRAGDSCPGWRRRSRSRGRGQRLSHGPR
FT                   RRPQLLTAAPPLQARGAFRSFPHSWGEDFLASLMFKIQLEPLKLRAWTLNGFVKFRNKE
FT                   TSAGPVAVM (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_047250"
FT   CONFLICT        190..196
FT                   /note="MKITRRR -> IEDHKAS (in Ref. 2; AAM10498)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        234..235
FT                   /note="TP -> HL (in Ref. 2; AAM10498)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   348 AA;  39133 MW;  DC9FE45DE4FD8CFC CRC64;
     MGKDYYKILG IPSGANEDEI KKAYRKMALK YHPDKNKEPN AEEKFKEIAE AYDVLSDPKK
     RGLYDQYGEE GLKTGGGTSG GSSGSFHYTF HGDPHATFAS FFGGSNPFDI FFASSRSTRP
     FSGFDPDDMD VDEDEDPFGA FGRFGFNGLS RGPRRAPEPL YPRRKVQDPP VVHELRVSLE
     EIYHGSTKRM KITRRRLNPD GRTVRTEDKI LHIVIKRGWK EGTKITFPKE GDATPDNIPA
     DIVFVLKDKP HAHFRRDGTN VLYSALISLK EALCGCTVNI PTIDGRVIPL PCNDVIKPGT
     VKRLRGEGLP FPKVPTQRGD LIVEFKVRFP DRLTPQTRQI LKQHLPCS
//