DJC24_HUMAN
ID DJC24_HUMAN Reviewed; 149 AA.
AC Q6P3W2; A8K0V0; B1ALC1; I6L9B4;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=DnaJ homolog subfamily C member 24 {ECO:0000305};
DE AltName: Full=CSL-type zinc finger-containing protein 3;
DE AltName: Full=Diphthamide biosynthesis protein 4;
GN Name=DNAJC24 {ECO:0000312|HGNC:HGNC:26979}; Synonyms=DPH4, ZCSL3;
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] (ISOFORM 1).
RC TISSUE=Amygdala;
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 GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Uterus;
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 FUNCTION IN DIPHTHAMIDE BIOSYNTHESIS.
RX PubMed=22509046; DOI=10.1073/pnas.1204523109;
RA Wei H., Xiang L., Wayne A.S., Chertov O., FitzGerald D.J., Bera T.K.,
RA Pastan I.;
RT "Immunotoxin resistance via reversible methylation of the DPH4 promoter is
RT a unique survival strategy.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:6898-6903(2012).
RN [6]
RP STRUCTURE BY NMR IN COMPLEX WITH ZINC ION, PARTIAL PROTEIN SEQUENCE,
RP FUNCTION AS HSP70-TYPE CO-CHAPERONE, SUBUNIT, IRON-BINDING, AND MUTAGENESIS
RP OF CYS-139.
RX PubMed=22367199; DOI=10.1074/jbc.m112.339655;
RA Thakur A., Chitoor B., Goswami A.V., Pareek G., Atreya H.S., D'Silva P.;
RT "Structure and mechanistic insights into novel iron-mediated moonlighting
RT functions of human J-protein cochaperone, Dph4.";
RL J. Biol. Chem. 287:13194-13205(2012).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-23.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Stimulates the ATPase activity of several Hsp70-type
CC chaperones. This ability is enhanced by iron-binding. The iron-bound
CC form is redox-active and can function as electron carrier. Plays a role
CC in the diphthamide biosynthesis, a post-translational modification of
CC histidine which occurs in translation elongation factor 2 (EEF2) which
CC can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin
CC A (Eta). {ECO:0000269|PubMed:22367199, ECO:0000269|PubMed:22509046}.
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC -!- SUBUNIT: Monomer and homooligomer. Iron binding promotes
CC oligomerization. {ECO:0000269|PubMed:22367199}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P3W2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P3W2-2; Sequence=VSP_056274;
CC -!- DOMAIN: The DPH-type metal-binding (MB) domain can bind either zinc or
CC iron ions. {ECO:0000255|PROSITE-ProRule:PRU00456,
CC ECO:0000269|PubMed:22367199}.
CC -!- SIMILARITY: Belongs to the DPH4 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH36571.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH63804.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF82354.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK289665; BAF82354.1; ALT_INIT; mRNA.
DR EMBL; AC108456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68245.1; -; Genomic_DNA.
DR EMBL; BC036571; AAH36571.1; ALT_INIT; mRNA.
DR EMBL; BC063804; AAH63804.1; ALT_INIT; mRNA.
DR CCDS; CCDS7873.2; -. [Q6P3W2-1]
DR RefSeq; NP_859057.4; NM_181706.4. [Q6P3W2-1]
DR PDB; 2L6L; NMR; -; A=2-149.
DR PDBsum; 2L6L; -.
DR AlphaFoldDB; Q6P3W2; -.
DR BMRB; Q6P3W2; -.
DR SMR; Q6P3W2; -.
DR BioGRID; 125688; 6.
DR STRING; 9606.ENSP00000417548; -.
DR iPTMnet; Q6P3W2; -.
DR PhosphoSitePlus; Q6P3W2; -.
DR BioMuta; DNAJC24; -.
DR DMDM; 66773991; -.
DR EPD; Q6P3W2; -.
DR MassIVE; Q6P3W2; -.
DR MaxQB; Q6P3W2; -.
DR PaxDb; Q6P3W2; -.
DR PeptideAtlas; Q6P3W2; -.
DR PRIDE; Q6P3W2; -.
DR ProteomicsDB; 66934; -. [Q6P3W2-1]
DR Antibodypedia; 12795; 112 antibodies from 23 providers.
DR DNASU; 120526; -.
DR Ensembl; ENST00000465995.6; ENSP00000417548.1; ENSG00000170946.15. [Q6P3W2-1]
DR Ensembl; ENST00000526042.5; ENSP00000435771.1; ENSG00000170946.15. [Q6P3W2-2]
DR GeneID; 120526; -.
DR KEGG; hsa:120526; -.
DR MANE-Select; ENST00000465995.6; ENSP00000417548.1; NM_181706.5; NP_859057.4.
DR CTD; 120526; -.
DR DisGeNET; 120526; -.
DR GeneCards; DNAJC24; -.
DR HGNC; HGNC:26979; DNAJC24.
DR HPA; ENSG00000170946; Low tissue specificity.
DR MIM; 611072; gene.
DR neXtProt; NX_Q6P3W2; -.
DR OpenTargets; ENSG00000170946; -.
DR PharmGKB; PA162383906; -.
DR VEuPathDB; HostDB:ENSG00000170946; -.
DR eggNOG; KOG0715; Eukaryota.
DR GeneTree; ENSGT00390000005430; -.
DR InParanoid; Q6P3W2; -.
DR OMA; SWPVDAC; -.
DR OrthoDB; 1580122at2759; -.
DR PhylomeDB; Q6P3W2; -.
DR TreeFam; TF326955; -.
DR PathwayCommons; Q6P3W2; -.
DR Reactome; R-HSA-5358493; Synthesis of diphthamide-EEF2.
DR UniPathway; UPA00559; -.
DR BioGRID-ORCS; 120526; 36 hits in 1052 CRISPR screens.
DR ChiTaRS; DNAJC24; human.
DR GenomeRNAi; 120526; -.
DR Pharos; Q6P3W2; Tbio.
DR PRO; PR:Q6P3W2; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6P3W2; protein.
DR Bgee; ENSG00000170946; Expressed in heart right ventricle and 203 other tissues.
DR ExpressionAtlas; Q6P3W2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; TAS:UniProtKB.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IEA:UniProtKB-UniPathway.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:UniProtKB.
DR CDD; cd06257; DnaJ; 1.
DR DisProt; DP00865; -.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 3.10.660.10; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR042978; DNAJC24.
DR InterPro; IPR007872; DPH_MB_dom.
DR InterPro; IPR036671; DPH_MB_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR45255; PTHR45255; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF05207; zf-CSL; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF144217; SSF144217; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51074; DPH_MB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Electron transport; Iron; Metal-binding;
KW Reference proteome; Transport; Zinc.
FT CHAIN 1..149
FT /note="DnaJ homolog subfamily C member 24"
FT /id="PRO_0000082622"
FT DOMAIN 11..82
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 93..148
FT /note="DPH-type MB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456,
FT ECO:0000269|PubMed:22367199"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456,
FT ECO:0000269|PubMed:22367199, ECO:0007744|PDB:2L6L"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456,
FT ECO:0000269|PubMed:22367199"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456,
FT ECO:0000269|PubMed:22367199, ECO:0007744|PDB:2L6L"
FT VAR_SEQ 84..149
FT /note="EDDLRNVGPVDAQVYLEEMSWNEGDHSFYLSCRCGGKYSVSKDEAEEVSLIS
FT CDTCSLIIELLHYN -> GS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056274"
FT VARIANT 23
FT /note="N -> D (in a breast cancer sample; somatic mutation;
FT dbSNP:rs111299050)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036397"
FT MUTAGEN 139
FT /note="C->S: Loss of iron-binding."
FT /evidence="ECO:0000269|PubMed:22367199"
FT HELIX 11..16
FT /evidence="ECO:0007829|PDB:2L6L"
FT HELIX 24..38
FT /evidence="ECO:0007829|PDB:2L6L"
FT HELIX 50..68
FT /evidence="ECO:0007829|PDB:2L6L"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2L6L"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:2L6L"
FT HELIX 77..88
FT /evidence="ECO:0007829|PDB:2L6L"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:2L6L"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:2L6L"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:2L6L"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:2L6L"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:2L6L"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:2L6L"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:2L6L"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:2L6L"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:2L6L"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:2L6L"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:2L6L"
SQ SEQUENCE 149 AA; 17139 MW; 84A4BC5F6D2A3F4C CRC64;
MMAVEQMPKK DWYSILGADP SANISDLKQK YQKLILMYHP DKQSTDVPAG TVEECVQKFI
EIDQAWKILG NEETKREYDL QRCEDDLRNV GPVDAQVYLE EMSWNEGDHS FYLSCRCGGK
YSVSKDEAEE VSLISCDTCS LIIELLHYN
