DJC12_HUMAN
ID DJC12_HUMAN Reviewed; 198 AA.
AC Q9UKB3; Q5JVQ1; Q9UKB2;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=DnaJ homolog subfamily C member 12;
DE AltName: Full=J domain-containing protein 1;
GN Name=DNAJC12; Synonyms=JDP1;
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] (ISOFORMS A AND B).
RX PubMed=10760603; DOI=10.1016/s0167-4781(00)00047-6;
RA Lee J., Hahn Y., Yun J.H., Mita K., Chung J.H.;
RT "Characterization of JDP genes, an evolutionarily conserved J domain-only
RT protein family, from human and moths.";
RL Biochim. Biophys. Acta 1491:355-363(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Lung;
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 [5]
RP IDENTIFICATION 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 [6]
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., Buerckstuemmer T.,
RA 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
RN [9]
RP SUBCELLULAR LOCATION, INDUCTION BY ER STRESS, AND INTERACTION WITH HSPA8.
RX PubMed=24122553; DOI=10.1007/s12192-013-0471-6;
RA Choi J., Djebbar S., Fournier A., Labrie C.;
RT "The co-chaperone DNAJC12 binds to Hsc70 and is upregulated by endoplasmic
RT reticulum stress.";
RL Cell Stress Chaperones 19:439-446(2014).
RN [10]
RP INVOLVEMENT IN HPANBH4, VARIANT HPANBH4 PRO-72, AND CHARACTERIZATION OF
RP VARIANT HPANBH4 PRO-72.
RX PubMed=28132689; DOI=10.1016/j.ajhg.2017.01.002;
RA Anikster Y., Haack T.B., Vilboux T., Pode-Shakked B., Thoeny B., Shen N.,
RA Guarani V., Meissner T., Mayatepek E., Trefz F.K., Marek-Yagel D.,
RA Martinez A., Huttlin E.L., Paulo J.A., Berutti R., Benoist J.F., Imbard A.,
RA Dorboz I., Heimer G., Landau Y., Ziv-Strasser L., Malicdan M.C.,
RA Gemperle-Britschgi C., Cremer K., Engels H., Meili D., Keller I.,
RA Bruggmann R., Strom T.M., Meitinger T., Mullikin J.C., Schwartz G.,
RA Ben-Zeev B., Gahl W.A., Harper J.W., Blau N., Hoffmann G.F., Prokisch H.,
RA Opladen T., Schiff M.;
RT "Biallelic mutations in DNAJC12 cause hyperphenylalaninemia, dystonia, and
RT intellectual disability.";
RL Am. J. Hum. Genet. 100:257-266(2017).
RN [11]
RP STRUCTURE BY NMR OF 1-100.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of J-domain from human DnaJ subfamily C member 12.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- SUBUNIT: Interacts with HSPA8. {ECO:0000269|PubMed:24122553}.
CC -!- SUBCELLULAR LOCATION: [Isoform a]: Cytoplasm
CC {ECO:0000269|PubMed:24122553}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a; Synonyms=JDP1a;
CC IsoId=Q9UKB3-1; Sequence=Displayed;
CC Name=B; Synonyms=JDP1b;
CC IsoId=Q9UKB3-2; Sequence=VSP_001295, VSP_001296;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, heart, and
CC testis, and at reduced levels in kidney and stomach.
CC -!- INDUCTION: Up-regulated by ER stress. {ECO:0000269|PubMed:24122553}.
CC -!- DISEASE: Hyperphenylalaninemia, mild, non-BH4-deficient (HPANBH4)
CC [MIM:617384]: An autosomal recessive disorder characterized by
CC increased serum phenylalanine, normal BH4 metabolism, and highly
CC variable neurologic defects, including movement abnormalities and
CC intellectual disability. {ECO:0000269|PubMed:28132689}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; AF176012; AAD52650.1; -; mRNA.
DR EMBL; AF176013; AAD52651.1; -; mRNA.
DR EMBL; AL133551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54257.1; -; Genomic_DNA.
DR EMBL; BC017018; AAH17018.1; -; mRNA.
DR CCDS; CCDS7271.1; -. [Q9UKB3-1]
DR CCDS; CCDS7272.1; -. [Q9UKB3-2]
DR RefSeq; NP_068572.1; NM_021800.2. [Q9UKB3-1]
DR RefSeq; NP_957714.1; NM_201262.1. [Q9UKB3-2]
DR PDB; 2CTQ; NMR; -; A=1-99.
DR PDBsum; 2CTQ; -.
DR AlphaFoldDB; Q9UKB3; -.
DR SMR; Q9UKB3; -.
DR BioGRID; 121150; 55.
DR IntAct; Q9UKB3; 15.
DR STRING; 9606.ENSP00000225171; -.
DR GlyGen; Q9UKB3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UKB3; -.
DR PhosphoSitePlus; Q9UKB3; -.
DR BioMuta; DNAJC12; -.
DR DMDM; 28201819; -.
DR EPD; Q9UKB3; -.
DR jPOST; Q9UKB3; -.
DR MassIVE; Q9UKB3; -.
DR MaxQB; Q9UKB3; -.
DR PaxDb; Q9UKB3; -.
DR PeptideAtlas; Q9UKB3; -.
DR PRIDE; Q9UKB3; -.
DR ProteomicsDB; 84763; -. [Q9UKB3-1]
DR ProteomicsDB; 84764; -. [Q9UKB3-2]
DR Antibodypedia; 28382; 86 antibodies from 20 providers.
DR DNASU; 56521; -.
DR Ensembl; ENST00000225171.7; ENSP00000225171.2; ENSG00000108176.15. [Q9UKB3-1]
DR Ensembl; ENST00000339758.7; ENSP00000343575.6; ENSG00000108176.15. [Q9UKB3-2]
DR GeneID; 56521; -.
DR KEGG; hsa:56521; -.
DR MANE-Select; ENST00000225171.7; ENSP00000225171.2; NM_021800.3; NP_068572.1.
DR UCSC; uc001jnb.4; human. [Q9UKB3-1]
DR CTD; 56521; -.
DR DisGeNET; 56521; -.
DR GeneCards; DNAJC12; -.
DR HGNC; HGNC:28908; DNAJC12.
DR HPA; ENSG00000108176; Tissue enhanced (adrenal gland, liver).
DR MalaCards; DNAJC12; -.
DR MIM; 606060; gene.
DR MIM; 617384; phenotype.
DR neXtProt; NX_Q9UKB3; -.
DR OpenTargets; ENSG00000108176; -.
DR Orphanet; 508523; Hyperphenylalaninemia due to DNAJC12 deficiency.
DR PharmGKB; PA134931354; -.
DR VEuPathDB; HostDB:ENSG00000108176; -.
DR eggNOG; KOG0691; Eukaryota.
DR GeneTree; ENSGT00940000159378; -.
DR HOGENOM; CLU_2313030_0_0_1; -.
DR InParanoid; Q9UKB3; -.
DR OrthoDB; 1499433at2759; -.
DR PhylomeDB; Q9UKB3; -.
DR TreeFam; TF105171; -.
DR PathwayCommons; Q9UKB3; -.
DR SignaLink; Q9UKB3; -.
DR BioGRID-ORCS; 56521; 9 hits in 1077 CRISPR screens.
DR ChiTaRS; DNAJC12; human.
DR EvolutionaryTrace; Q9UKB3; -.
DR GenomeRNAi; 56521; -.
DR Pharos; Q9UKB3; Tbio.
DR PRO; PR:Q9UKB3; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9UKB3; protein.
DR Bgee; ENSG00000108176; Expressed in islet of Langerhans and 165 other tissues.
DR ExpressionAtlas; Q9UKB3; baseline and differential.
DR Genevisible; Q9UKB3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR029827; JDP1-like.
DR PANTHER; PTHR44500; PTHR44500; 1.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone; Cytoplasm;
KW Disease variant; Phosphoprotein; Reference proteome.
FT CHAIN 1..198
FT /note="DnaJ homolog subfamily C member 12"
FT /id="PRO_0000071066"
FT DOMAIN 14..79
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 114..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R022"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R022"
FT VAR_SEQ 100..107
FT /note="SMHWVVRG -> VGFSLGAT (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10760603"
FT /id="VSP_001295"
FT VAR_SEQ 108..198
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10760603"
FT /id="VSP_001296"
FT VARIANT 72
FT /note="R -> P (in HPANBH4; decreased protein levels in
FT patient cells; dbSNP:rs1035794099)"
FT /evidence="ECO:0000269|PubMed:28132689"
FT /id="VAR_078797"
FT VARIANT 124
FT /note="M -> I (in dbSNP:rs35690028)"
FT /id="VAR_048913"
FT VARIANT 129
FT /note="C -> W (in dbSNP:rs36099123)"
FT /id="VAR_048914"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:2CTQ"
FT HELIX 27..39
FT /evidence="ECO:0007829|PDB:2CTQ"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2CTQ"
FT HELIX 52..67
FT /evidence="ECO:0007829|PDB:2CTQ"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:2CTQ"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:2CTQ"
SQ SEQUENCE 198 AA; 23415 MW; 03429472C61413EB CRC64;
MDAILNYRSE DTEDYYTLLG CDELSSVEQI LAEFKVRALE CHPDKHPENP KAVETFQKLQ
KAKEILTNEE SRARYDHWRR SQMSMPFQQW EALNDSVKTS MHWVVRGKKD LMLEESDKTH
TTKMENEECN EQRERKKEEL ASTAEKTEQK EPKPLEKSVS PQNSDSSGFA DVNGWHLRFR
WSKDAPSELL RKFRNYEI
