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DnaJ homolog subfamily C member 24 (CSL-type zinc finger-containing protein 3) (Diphthamide biosynthesis protein 4)

 DJC24_HUMAN             Reviewed;         148 AA.
Q6P3W2; A8K0V0; B1ALC1; I6L9B4;
24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 116.
RecName: Full=DnaJ homolog subfamily C member 24;
AltName: Full=CSL-type zinc finger-containing protein 3;
AltName: Full=Diphthamide biosynthesis protein 4;
Name=DNAJC24; Synonyms=DPH4, ZCSL3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Amygdala;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[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] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Uterus;
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]
FUNCTION IN DIPHTHAMIDE BIOSYNTHESIS.
PubMed=22509046; DOI=10.1073/pnas.1204523109;
Wei H., Xiang L., Wayne A.S., Chertov O., FitzGerald D.J., Bera T.K.,
Pastan I.;
"Immunotoxin resistance via reversible methylation of the DPH4
promoter is a unique survival strategy.";
Proc. Natl. Acad. Sci. U.S.A. 109:6898-6903(2012).
[6]
STRUCTURE BY NMR IN COMPLEX WITH ZINC ION, PARTIAL PROTEIN SEQUENCE,
FUNCTION AS HSP70-TYPE CO-CHAPERONE, SUBUNIT, IRON-BINDING, AND
MUTAGENESIS OF CYS-138.
PubMed=22367199; DOI=10.1074/jbc.M112.339655;
Thakur A., Chitoor B., Goswami A.V., Pareek G., Atreya H.S.,
D'Silva P.;
"Structure and mechanistic insights into novel iron-mediated
moonlighting functions of human J-protein cochaperone, Dph4.";
J. Biol. Chem. 287:13194-13205(2012).
[7]
VARIANT [LARGE SCALE ANALYSIS] ASP-22.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Stimulates the ATPase activity of several Hsp70-type
chaperones. This ability is enhanced by iron-binding. The iron-
bound form is redox-active and can function as electron carrier.
Plays a role in the diphthamide biosynthesis, a post-translational
modification of histidine which occurs in translation elongation
factor 2 (EEF2) which can be ADP-ribosylated by diphtheria toxin
and by Pseudomonas exotoxin A (Eta). {ECO:0000269|PubMed:22367199,
ECO:0000269|PubMed:22509046}.
-!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
-!- SUBUNIT: Monomer and homooligomer. Iron binding promotes
oligomerization. {ECO:0000269|PubMed:22367199}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6P3W2-1; Sequence=Displayed;
Name=2;
IsoId=Q6P3W2-2; Sequence=VSP_056274;
Note=No experimental confirmation available.;
-!- DOMAIN: The DPH-type zinc finger can also bind iron ions instead
of the expected zinc ions. {ECO:0000269|PubMed:22367199}.
-!- SIMILARITY: Belongs to the DPH4 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=EAW68245.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK289665; BAF82354.1; -; mRNA.
EMBL; AC108456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL137804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471064; EAW68245.1; ALT_INIT; Genomic_DNA.
EMBL; BC036571; AAH36571.1; -; mRNA.
EMBL; BC063804; AAH63804.1; -; mRNA.
RefSeq; NP_859057.4; NM_181706.4.
UniGene; Hs.187269; -.
UniGene; Hs.741895; -.
PDB; 2L6L; NMR; -; A=1-148.
PDBsum; 2L6L; -.
DisProt; DP00865; -.
ProteinModelPortal; Q6P3W2; -.
SMR; Q6P3W2; -.
BioGrid; 125688; 2.
IntAct; Q6P3W2; 1.
STRING; 9606.ENSP00000417548; -.
iPTMnet; Q6P3W2; -.
PhosphoSitePlus; Q6P3W2; -.
BioMuta; DNAJC24; -.
DMDM; 66773991; -.
EPD; Q6P3W2; -.
MaxQB; Q6P3W2; -.
PaxDb; Q6P3W2; -.
PeptideAtlas; Q6P3W2; -.
PRIDE; Q6P3W2; -.
Ensembl; ENST00000536040; ENSP00000444967; ENSG00000170946.
GeneID; 120526; -.
KEGG; hsa:120526; -.
CTD; 120526; -.
GeneCards; DNAJC24; -.
HGNC; HGNC:26979; DNAJC24.
HPA; HPA020025; -.
HPA; HPA025237; -.
MIM; 611072; gene.
neXtProt; NX_Q6P3W2; -.
PharmGKB; PA162383906; -.
eggNOG; KOG0715; Eukaryota.
eggNOG; COG0484; LUCA.
HOGENOM; HOG000189813; -.
HOVERGEN; HBG066253; -.
InParanoid; Q6P3W2; -.
KO; K17867; -.
OMA; NTLKDPI; -.
PhylomeDB; Q6P3W2; -.
TreeFam; TF326955; -.
Reactome; R-HSA-5358493; Synthesis of diphthamide-EEF2.
UniPathway; UPA00559; -.
ChiTaRS; DNAJC24; human.
GenomeRNAi; 120526; -.
PRO; PR:Q6P3W2; -.
Proteomes; UP000005640; Unplaced.
CleanEx; HS_DNAJC24; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0061077; P:chaperone-mediated protein folding; TAS:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IEA:UniProtKB-UniPathway.
GO; GO:0032781; P:positive regulation of ATPase activity; IDA:UniProtKB.
CDD; cd06257; DnaJ; 1.
Gene3D; 1.10.287.110; -; 1.
Gene3D; 3.10.660.10; -; 1.
InterPro; IPR036869; DnaJ_dom_sf.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR007872; Znf_DHP.
InterPro; IPR036671; Znf_DHP_sf.
Pfam; PF00226; DnaJ; 1.
Pfam; PF05207; zf-CSL; 1.
PRINTS; PR00625; JDOMAIN.
SMART; SM00271; DnaJ; 1.
SUPFAM; SSF144217; SSF144217; 1.
SUPFAM; SSF46565; SSF46565; 1.
PROSITE; PS50076; DNAJ_2; 1.
PROSITE; PS51074; ZF_DPH; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Electron transport; Iron;
Metal-binding; Polymorphism; Reference proteome; Transport; Zinc;
Zinc-finger.
CHAIN 1 148 DnaJ homolog subfamily C member 24.
/FTId=PRO_0000082622.
DOMAIN 10 81 J. {ECO:0000255|PROSITE-
ProRule:PRU00286}.
ZN_FING 92 147 DPH-type. {ECO:0000255|PROSITE-
ProRule:PRU00456}.
VAR_SEQ 83 148 EDDLRNVGPVDAQVYLEEMSWNEGDHSFYLSCRCGGKYSVS
KDEAEEVSLISCDTCSLIIELLHYN -> GS (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056274.
VARIANT 22 22 N -> D (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036397.
MUTAGEN 138 138 C->S: Loss of iron-binding.
{ECO:0000269|PubMed:22367199}.
HELIX 10 15 {ECO:0000244|PDB:2L6L}.
HELIX 23 37 {ECO:0000244|PDB:2L6L}.
HELIX 49 67 {ECO:0000244|PDB:2L6L}.
STRAND 68 70 {ECO:0000244|PDB:2L6L}.
TURN 71 74 {ECO:0000244|PDB:2L6L}.
HELIX 76 87 {ECO:0000244|PDB:2L6L}.
STRAND 91 97 {ECO:0000244|PDB:2L6L}.
TURN 98 100 {ECO:0000244|PDB:2L6L}.
STRAND 101 104 {ECO:0000244|PDB:2L6L}.
TURN 105 108 {ECO:0000244|PDB:2L6L}.
STRAND 109 113 {ECO:0000244|PDB:2L6L}.
STRAND 115 117 {ECO:0000244|PDB:2L6L}.
STRAND 119 123 {ECO:0000244|PDB:2L6L}.
HELIX 126 129 {ECO:0000244|PDB:2L6L}.
STRAND 132 134 {ECO:0000244|PDB:2L6L}.
STRAND 136 139 {ECO:0000244|PDB:2L6L}.
STRAND 141 145 {ECO:0000244|PDB:2L6L}.
SEQUENCE 148 AA; 17008 MW; A9A4F58BC74FECFD CRC64;
MAVEQMPKKD WYSILGADPS ANISDLKQKY QKLILMYHPD KQSTDVPAGT VEECVQKFIE
IDQAWKILGN EETKREYDLQ RCEDDLRNVG PVDAQVYLEE MSWNEGDHSF YLSCRCGGKY
SVSKDEAEEV SLISCDTCSL IIELLHYN


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