Full text data of CIAO1
CIAO1
(WDR39)
[Confidence: low (only semi-automatic identification from reviews)]
Probable cytosolic iron-sulfur protein assembly protein CIAO1 (WD repeat-containing protein 39)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Probable cytosolic iron-sulfur protein assembly protein CIAO1 (WD repeat-containing protein 39)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O76071
ID CIAO1_HUMAN Reviewed; 339 AA.
AC O76071; A0MNN9; Q53FM5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1998, sequence version 1.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Probable cytosolic iron-sulfur protein assembly protein CIAO1;
DE AltName: Full=WD repeat-containing protein 39;
GN Name=CIAO1; Synonyms=WDR39;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH WT1.
RX PubMed=9556563; DOI=10.1074/jbc.273.18.10880;
RA Johnstone R.W., Wang J., Tommerup N., Vissing H., Roberts T., Shi Y.;
RT "Ciao 1 is a novel WD40 protein that interacts with the tumor
RT suppressor protein WT1.";
RL J. Biol. Chem. 273:10880-10887(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=17041588; DOI=10.1038/ncb1490;
RA Higa L.A., Wu M., Ye T., Kobayashi R., Sun H., Zhang H.;
RT "CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat
RT proteins and regulates histone methylation.";
RL Nat. Cell Biol. 8:1277-1283(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R.,
RA Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L.,
RA Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E.,
RA Harris P.C., Venter J.C., Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from
RT human chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastric mucosa;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, and 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP CHARACTERIZATION.
RX PubMed=10438340; DOI=10.1007/s002510050571;
RA Johnstone R.W., Tommerup N., Hansen C., Vissing H., Shi Y.;
RT "Structural organization, tissue expression, and chromosomal
RT localization of Ciao 1, a functional modulator of the Wilms' tumor
RT suppressor, WT1.";
RL Immunogenetics 49:900-905(1999).
RN [8]
RP FUNCTION.
RX PubMed=17937914; DOI=10.1016/j.str.2007.08.009;
RA Srinivasan V., Netz D.J.A., Webert H., Mascarenhas J., Pierik A.J.,
RA Michel H., Lill R.;
RT "Structure of the yeast WD40 domain protein Cia1, a component acting
RT late in iron-sulfur protein biogenesis.";
RL Structure 15:1246-1257(2007).
RN [9]
RP FUNCTION, AND IDENTIFICATION IN MMXD COMPLEX.
RX PubMed=20797633; DOI=10.1016/j.molcel.2010.07.029;
RA Ito S., Tan L.J., Andoh D., Narita T., Seki M., Hirano Y., Narita K.,
RA Kuraoka I., Hiraoka Y., Tanaka K.;
RT "MMXD, a TFIIH-independent XPD-MMS19 protein complex involved in
RT chromosome segregation.";
RL Mol. Cell 39:632-640(2010).
RN [10]
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.,
RA Buerckstuemmer T., 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 [11]
RP INTERACTION WITH FAM96A.
RX PubMed=22683786; DOI=10.1107/S0907444912006592;
RA Chen K.E., Richards A.A., Ariffin J.K., Ross I.L., Sweet M.J.,
RA Kellie S., Kobe B., Martin J.L.;
RT "The mammalian DUF59 protein Fam96a forms two distinct types of
RT domain-swapped dimer.";
RL Acta Crystallogr. D 68:637-648(2012).
RN [12]
RP IDENTIFICATION BY MASS 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP IDENTIFICATION IN THE CIA COMPLEX.
RX PubMed=22678362; DOI=10.1126/science.1219723;
RA Stehling O., Vashisht A.A., Mascarenhas J., Jonsson Z.O., Sharma T.,
RA Netz D.J., Pierik A.J., Wohlschlegel J.A., Lill R.;
RT "MMS19 assembles iron-sulfur proteins required for DNA metabolism and
RT genomic integrity.";
RL Science 337:195-199(2012).
RN [14]
RP IDENTIFICATION IN THE CIA COMPLEX.
RX PubMed=22678361; DOI=10.1126/science.1219664;
RA Gari K., Leon Ortiz A.M., Borel V., Flynn H., Skehel J.M.,
RA Boulton S.J.;
RT "MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA
RT metabolism.";
RL Science 337:243-245(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=21468892; DOI=10.1007/s13238-011-1018-1;
RA Xu C., Min J.;
RT "Structure and function of WD40 domain proteins.";
RL Protein Cell 2:202-214(2011).
CC -!- FUNCTION: Key component of the cytosolic iron-sulfur protein
CC assembly (CIA) complex, a multiprotein complex that mediates the
CC incorporation of iron-sulfur cluster into extramitochondrial Fe/S
CC proteins. Seems to specifically modulate the transactivation
CC activity of WT1. As part of the mitotic spindle-associated MMXD
CC complex it may play a role in chromosome segregation.
CC -!- SUBUNIT: Component of the CIA complex. Component of the MMXD
CC complex, which includes CIAO1, ERCC2, FAM96B, MMS19 and SLC25A5.
CC Interacts with WT1. Interacts with FAM96A.
CC -!- MISCELLANEOUS: 'Ciao' means 'bridge' in Chinese.
CC -!- SIMILARITY: Belongs to the WD repeat CIA1 family.
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U63810; AAC24948.1; -; mRNA.
DR EMBL; EF011618; ABK41108.1; -; mRNA.
DR EMBL; AC004020; AAC23493.1; -; Genomic_DNA.
DR EMBL; CR456802; CAG33083.1; -; mRNA.
DR EMBL; AK223257; BAD96977.1; -; mRNA.
DR EMBL; BC001395; AAH01395.1; -; mRNA.
DR EMBL; BC032812; AAH32812.1; -; mRNA.
DR RefSeq; NP_004795.1; NM_004804.2.
DR UniGene; Hs.12109; -.
DR PDB; 3FM0; X-ray; 1.70 A; A=1-339.
DR PDBsum; 3FM0; -.
DR ProteinModelPortal; O76071; -.
DR SMR; O76071; 4-335.
DR IntAct; O76071; 9.
DR MINT; MINT-1416717; -.
DR STRING; 9606.ENSP00000418287; -.
DR PhosphoSite; O76071; -.
DR PaxDb; O76071; -.
DR PeptideAtlas; O76071; -.
DR PRIDE; O76071; -.
DR DNASU; 9391; -.
DR Ensembl; ENST00000488633; ENSP00000418287; ENSG00000144021.
DR GeneID; 9391; -.
DR KEGG; hsa:9391; -.
DR UCSC; uc002svs.3; human.
DR CTD; 9391; -.
DR GeneCards; GC02P096931; -.
DR HGNC; HGNC:14280; CIAO1.
DR HPA; HPA017882; -.
DR MIM; 604333; gene.
DR neXtProt; NX_O76071; -.
DR PharmGKB; PA162382269; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000208901; -.
DR HOVERGEN; HBG056532; -.
DR InParanoid; O76071; -.
DR OMA; VWKCVCT; -.
DR OrthoDB; EOG7XH6Q1; -.
DR PhylomeDB; O76071; -.
DR Reactome; REACT_111217; Metabolism.
DR SignaLink; O76071; -.
DR ChiTaRS; CIAO1; human.
DR EvolutionaryTrace; O76071; -.
DR GeneWiki; CIAO1; -.
DR GenomeRNAi; 9391; -.
DR NextBio; 35187; -.
DR PRO; PR:O76071; -.
DR Bgee; O76071; -.
DR CleanEx; HS_CIAO1; -.
DR Genevestigator; O76071; -.
DR GO; GO:0097361; C:CIA complex; IDA:UniProtKB.
DR GO; GO:0071817; C:MMXD complex; IDA:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IGI:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03037; ciao1; 1; -.
DR InterPro; IPR028608; CIAO1/Cia1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 7.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome partition; Complete proteome;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1 339 Probable cytosolic iron-sulfur protein
FT assembly protein CIAO1.
FT /FTId=PRO_0000051389.
FT REPEAT 14 53 WD 1.
FT REPEAT 59 98 WD 2.
FT REPEAT 103 142 WD 3.
FT REPEAT 148 187 WD 4.
FT REPEAT 192 231 WD 5.
FT REPEAT 250 289 WD 6.
FT REPEAT 301 339 WD 7.
FT CONFLICT 243 243 C -> G (in Ref. 5; BAD96977).
FT STRAND 5 11
FT STRAND 19 24
FT STRAND 31 35
FT STRAND 40 46
FT STRAND 49 56
FT STRAND 64 69
FT STRAND 73 80
FT STRAND 85 90
FT STRAND 95 101
FT STRAND 108 113
FT STRAND 117 124
FT STRAND 129 134
FT STRAND 140 146
FT STRAND 153 158
FT STRAND 160 163
FT STRAND 165 169
FT STRAND 174 180
FT STRAND 183 190
FT STRAND 197 202
FT STRAND 206 213
FT STRAND 218 224
FT STRAND 240 247
FT STRAND 255 260
FT TURN 262 264
FT STRAND 267 271
FT STRAND 276 281
FT STRAND 292 298
FT STRAND 301 304
FT STRAND 306 311
FT STRAND 313 315
FT STRAND 318 323
FT STRAND 328 333
SQ SEQUENCE 339 AA; 37840 MW; 63A8D8257A204FC8 CRC64;
MKDSLVLLGR VPAHPDSRCW FLAWNPAGTL LASCGGDRRI RIWGTEGDSW ICKSVLSEGH
QRTVRKVAWS PCGNYLASAS FDATTCIWKK NQDDFECVTT LEGHENEVKS VAWAPSGNLL
ATCSRDKSVW VWEVDEEDEY ECVSVLNSHT QDVKHVVWHP SQELLASASY DDTVKLYREE
EDDWVCCATL EGHESTVWSL AFDPSGQRLA SCSDDRTVRI WRQYLPGNEQ GVACSGSDPS
WKCICTLSGF HSRTIYDIAW CQLTGALATA CGDDAIRVFQ EDPNSDPQQP TFSLTAHLHQ
AHSQDVNCVA WNPKEPGLLA SCSDDGEVAF WKYQRPEGL
//
ID CIAO1_HUMAN Reviewed; 339 AA.
AC O76071; A0MNN9; Q53FM5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1998, sequence version 1.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Probable cytosolic iron-sulfur protein assembly protein CIAO1;
DE AltName: Full=WD repeat-containing protein 39;
GN Name=CIAO1; Synonyms=WDR39;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH WT1.
RX PubMed=9556563; DOI=10.1074/jbc.273.18.10880;
RA Johnstone R.W., Wang J., Tommerup N., Vissing H., Roberts T., Shi Y.;
RT "Ciao 1 is a novel WD40 protein that interacts with the tumor
RT suppressor protein WT1.";
RL J. Biol. Chem. 273:10880-10887(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=17041588; DOI=10.1038/ncb1490;
RA Higa L.A., Wu M., Ye T., Kobayashi R., Sun H., Zhang H.;
RT "CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat
RT proteins and regulates histone methylation.";
RL Nat. Cell Biol. 8:1277-1283(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R.,
RA Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L.,
RA Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E.,
RA Harris P.C., Venter J.C., Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from
RT human chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastric mucosa;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, and 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP CHARACTERIZATION.
RX PubMed=10438340; DOI=10.1007/s002510050571;
RA Johnstone R.W., Tommerup N., Hansen C., Vissing H., Shi Y.;
RT "Structural organization, tissue expression, and chromosomal
RT localization of Ciao 1, a functional modulator of the Wilms' tumor
RT suppressor, WT1.";
RL Immunogenetics 49:900-905(1999).
RN [8]
RP FUNCTION.
RX PubMed=17937914; DOI=10.1016/j.str.2007.08.009;
RA Srinivasan V., Netz D.J.A., Webert H., Mascarenhas J., Pierik A.J.,
RA Michel H., Lill R.;
RT "Structure of the yeast WD40 domain protein Cia1, a component acting
RT late in iron-sulfur protein biogenesis.";
RL Structure 15:1246-1257(2007).
RN [9]
RP FUNCTION, AND IDENTIFICATION IN MMXD COMPLEX.
RX PubMed=20797633; DOI=10.1016/j.molcel.2010.07.029;
RA Ito S., Tan L.J., Andoh D., Narita T., Seki M., Hirano Y., Narita K.,
RA Kuraoka I., Hiraoka Y., Tanaka K.;
RT "MMXD, a TFIIH-independent XPD-MMS19 protein complex involved in
RT chromosome segregation.";
RL Mol. Cell 39:632-640(2010).
RN [10]
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.,
RA Buerckstuemmer T., 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 [11]
RP INTERACTION WITH FAM96A.
RX PubMed=22683786; DOI=10.1107/S0907444912006592;
RA Chen K.E., Richards A.A., Ariffin J.K., Ross I.L., Sweet M.J.,
RA Kellie S., Kobe B., Martin J.L.;
RT "The mammalian DUF59 protein Fam96a forms two distinct types of
RT domain-swapped dimer.";
RL Acta Crystallogr. D 68:637-648(2012).
RN [12]
RP IDENTIFICATION BY MASS 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP IDENTIFICATION IN THE CIA COMPLEX.
RX PubMed=22678362; DOI=10.1126/science.1219723;
RA Stehling O., Vashisht A.A., Mascarenhas J., Jonsson Z.O., Sharma T.,
RA Netz D.J., Pierik A.J., Wohlschlegel J.A., Lill R.;
RT "MMS19 assembles iron-sulfur proteins required for DNA metabolism and
RT genomic integrity.";
RL Science 337:195-199(2012).
RN [14]
RP IDENTIFICATION IN THE CIA COMPLEX.
RX PubMed=22678361; DOI=10.1126/science.1219664;
RA Gari K., Leon Ortiz A.M., Borel V., Flynn H., Skehel J.M.,
RA Boulton S.J.;
RT "MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA
RT metabolism.";
RL Science 337:243-245(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=21468892; DOI=10.1007/s13238-011-1018-1;
RA Xu C., Min J.;
RT "Structure and function of WD40 domain proteins.";
RL Protein Cell 2:202-214(2011).
CC -!- FUNCTION: Key component of the cytosolic iron-sulfur protein
CC assembly (CIA) complex, a multiprotein complex that mediates the
CC incorporation of iron-sulfur cluster into extramitochondrial Fe/S
CC proteins. Seems to specifically modulate the transactivation
CC activity of WT1. As part of the mitotic spindle-associated MMXD
CC complex it may play a role in chromosome segregation.
CC -!- SUBUNIT: Component of the CIA complex. Component of the MMXD
CC complex, which includes CIAO1, ERCC2, FAM96B, MMS19 and SLC25A5.
CC Interacts with WT1. Interacts with FAM96A.
CC -!- MISCELLANEOUS: 'Ciao' means 'bridge' in Chinese.
CC -!- SIMILARITY: Belongs to the WD repeat CIA1 family.
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U63810; AAC24948.1; -; mRNA.
DR EMBL; EF011618; ABK41108.1; -; mRNA.
DR EMBL; AC004020; AAC23493.1; -; Genomic_DNA.
DR EMBL; CR456802; CAG33083.1; -; mRNA.
DR EMBL; AK223257; BAD96977.1; -; mRNA.
DR EMBL; BC001395; AAH01395.1; -; mRNA.
DR EMBL; BC032812; AAH32812.1; -; mRNA.
DR RefSeq; NP_004795.1; NM_004804.2.
DR UniGene; Hs.12109; -.
DR PDB; 3FM0; X-ray; 1.70 A; A=1-339.
DR PDBsum; 3FM0; -.
DR ProteinModelPortal; O76071; -.
DR SMR; O76071; 4-335.
DR IntAct; O76071; 9.
DR MINT; MINT-1416717; -.
DR STRING; 9606.ENSP00000418287; -.
DR PhosphoSite; O76071; -.
DR PaxDb; O76071; -.
DR PeptideAtlas; O76071; -.
DR PRIDE; O76071; -.
DR DNASU; 9391; -.
DR Ensembl; ENST00000488633; ENSP00000418287; ENSG00000144021.
DR GeneID; 9391; -.
DR KEGG; hsa:9391; -.
DR UCSC; uc002svs.3; human.
DR CTD; 9391; -.
DR GeneCards; GC02P096931; -.
DR HGNC; HGNC:14280; CIAO1.
DR HPA; HPA017882; -.
DR MIM; 604333; gene.
DR neXtProt; NX_O76071; -.
DR PharmGKB; PA162382269; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000208901; -.
DR HOVERGEN; HBG056532; -.
DR InParanoid; O76071; -.
DR OMA; VWKCVCT; -.
DR OrthoDB; EOG7XH6Q1; -.
DR PhylomeDB; O76071; -.
DR Reactome; REACT_111217; Metabolism.
DR SignaLink; O76071; -.
DR ChiTaRS; CIAO1; human.
DR EvolutionaryTrace; O76071; -.
DR GeneWiki; CIAO1; -.
DR GenomeRNAi; 9391; -.
DR NextBio; 35187; -.
DR PRO; PR:O76071; -.
DR Bgee; O76071; -.
DR CleanEx; HS_CIAO1; -.
DR Genevestigator; O76071; -.
DR GO; GO:0097361; C:CIA complex; IDA:UniProtKB.
DR GO; GO:0071817; C:MMXD complex; IDA:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IGI:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03037; ciao1; 1; -.
DR InterPro; IPR028608; CIAO1/Cia1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 7.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome partition; Complete proteome;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1 339 Probable cytosolic iron-sulfur protein
FT assembly protein CIAO1.
FT /FTId=PRO_0000051389.
FT REPEAT 14 53 WD 1.
FT REPEAT 59 98 WD 2.
FT REPEAT 103 142 WD 3.
FT REPEAT 148 187 WD 4.
FT REPEAT 192 231 WD 5.
FT REPEAT 250 289 WD 6.
FT REPEAT 301 339 WD 7.
FT CONFLICT 243 243 C -> G (in Ref. 5; BAD96977).
FT STRAND 5 11
FT STRAND 19 24
FT STRAND 31 35
FT STRAND 40 46
FT STRAND 49 56
FT STRAND 64 69
FT STRAND 73 80
FT STRAND 85 90
FT STRAND 95 101
FT STRAND 108 113
FT STRAND 117 124
FT STRAND 129 134
FT STRAND 140 146
FT STRAND 153 158
FT STRAND 160 163
FT STRAND 165 169
FT STRAND 174 180
FT STRAND 183 190
FT STRAND 197 202
FT STRAND 206 213
FT STRAND 218 224
FT STRAND 240 247
FT STRAND 255 260
FT TURN 262 264
FT STRAND 267 271
FT STRAND 276 281
FT STRAND 292 298
FT STRAND 301 304
FT STRAND 306 311
FT STRAND 313 315
FT STRAND 318 323
FT STRAND 328 333
SQ SEQUENCE 339 AA; 37840 MW; 63A8D8257A204FC8 CRC64;
MKDSLVLLGR VPAHPDSRCW FLAWNPAGTL LASCGGDRRI RIWGTEGDSW ICKSVLSEGH
QRTVRKVAWS PCGNYLASAS FDATTCIWKK NQDDFECVTT LEGHENEVKS VAWAPSGNLL
ATCSRDKSVW VWEVDEEDEY ECVSVLNSHT QDVKHVVWHP SQELLASASY DDTVKLYREE
EDDWVCCATL EGHESTVWSL AFDPSGQRLA SCSDDRTVRI WRQYLPGNEQ GVACSGSDPS
WKCICTLSGF HSRTIYDIAW CQLTGALATA CGDDAIRVFQ EDPNSDPQQP TFSLTAHLHQ
AHSQDVNCVA WNPKEPGLLA SCSDDGEVAF WKYQRPEGL
//
MIM
604333
*RECORD*
*FIELD* NO
604333
*FIELD* TI
*604333 WD40 REPEAT-CONTAINING PROTEIN CIAO1; CIAO1
;;WD REPEAT-CONTAINING PROTEIN 39; WDR39
read more*FIELD* TX
DESCRIPTION
CIAO1 is a subunit of a protein complex involved in the biosynthesis of
Fe-S proteins. Other subunits of this complex are MMS19 (614777), FAM96B
(614778), and NARFL (611118) (Stehling et al., 2012; Gari et al., 2012).
CLONING
The Wilms tumor gene (WT1; 607102) on 11p13 is involved in regulating
cell cycle progression and apoptosis. In an attempt to dissect the
molecular mechanisms of transcriptional activation and repression by
WT1, and to identify other proteins that may be involved in kidney and
hematopoietic cell tumorigenesis, several groups have studied
WT1-interacting proteins. WT1 binds in vivo and in vitro to p53
(191170), resulting in WT1 functioning as a transcriptional repressor.
Mutations in p53 increase the aggressiveness of Wilms tumors, resulting
in poorer patient prognosis, but are not thought to be a primary genetic
cause of Wilms tumor formation. WT1 also interacts with and regulates
the transcriptional activity of steroidogenic factor-1 (184757), a key
molecule in gonadal development. Johnstone et al. (1996) identified a
protein called PAWR (601936), the gene for which maps to 12q21, that is
capable of modulating the transcriptional activities of WT1. Johnstone
et al. (1998) identified a second protein, which they named CIAO1 after
the Chinese word for 'bridge,' that is also capable of modulating the
transcriptional activities of WT1. CIAO1 is a 339-amino acid polypeptide
containing 7 WD40 or beta-transducin repeats. It can inhibit the
transcriptional activation function of WT1, but does not affect
WT1-mediated transcriptional repression. Johnstone et al. (1998)
demonstrated that the yeast Ciao1 homolog is an essential protein that
appears to be highly evolutionarily conserved.
GENE STRUCTURE
Johnstone et al. (1999) described the structural organization of the
CIAO1 gene, with the intron/exon boundaries closely matching the
consensus 5-prime donor/3-prime acceptor splice site sequences. The gene
contains 7 exons.
GENE FUNCTION
Ito et al. (2010) showed that CIAO1 coprecipitated with ANT2 (SLC25A5;
300150), XPD (ERCC2; 126340), MIP18 (FAM96B), and MMS19 in a protein
complex that was required for chromosome segregation in human cell
lines.
In HEK293 cells, Stehling et al. (2012) identified and confirmed a
protein complex made up of several known or putative proteins involved
in the biosynthesis of Fe-S proteins: MMS19, CIAO1, and IOP1 (NARFL).
Inactivation of MMS19, FAM96B, or IOP1 reduced HEK293 cell survival
following UV irradiation or methyl methanesulfonate treatment. Stehling
et al. (2012) hypothesized that the complex acts late in Fe-S protein
biogenesis to facilitate Fe-S cluster transfer from the CIA scaffold
complex CFD1 (NUBP2; 610779)-NBP35 (NUBP1; 600280) to Fe-S target
proteins.
Using coimmunoprecipitation and gel filtration studies, Gari et al.
(2012) independently identified a stable complex that involved MMS19,
CIAO1, IOP1, and FAM96B.
MAPPING
By FISH and radiation hybrid analysis, Johnstone et al. (1999) mapped
the WDR39 gene to the pericentric region of chromosome 2. They stated
that the probable location is 2q11.2 based on the gene's inclusion
within a previously mapped BAC clone (GenBank GENBANK AC004020).
*FIELD* RF
1. Gari, K.; Ortiz, A. M. L.; Borel, V.; Flynn, H.; Skehel, J. M.;
Boulton, S. J.: MMS19 links cytoplasmic iron-sulfur cluster assembly
to DNA metabolism. Science 337: 243-245, 2012.
2. Ito, S.; Tan, L. J.; Andoh, D.; Narita, T.; Seki, M.; Hirano, Y.;
Narita, K.; Kuraoka, I.; Hiraoka, Y.; Tanaka, K.: MMXD, a TFIIH-independent
XPD-MMS19 protein complex involved in chromosome segregation. Molec.
Cell 39: 632-640, 2010.
3. Johnstone, R. W.; See, R. H.; Sells, S. F.; Wang, J.; Muthukkumar,
S.; Englert, C.; Haber, D. A.; Licht, J. D.; Sugrue, S. P.; Roberts,
T.; Rangnekar, V. M.; Shi, Y.: A novel repressor, par-4, modulates
transcription and growth suppression functions of the Wilms' tumor
suppressor WT1. Molec. Cell. Biol. 16: 6945-6956, 1996.
4. Johnstone, R. W.; Tommerup, N.; Hansen, C.; Vissing, H.; Shi, Y.
: Structural organization, tissue expression, and chromosomal localization
of Ciao 1, a functional modulator of the Wilms' tumor suppressor,
WT1. Immunogenetics 49: 900-905, 1999.
5. Johnstone, R. W.; Wang, J.; Tommerup, N.; Vissing, H.; Roberts,
T.; Shi, Y.: Ciao 1 is a novel WD40 protein that interacts with the
tumor suppressor protein WT1. J. Biol. Chem. 273: 10880-10887, 1998.
6. Stehling, O.; Vashisht, A. A.; Mascarenhas, J.; Jonsson, Z. O.;
Sharma, T.; Netz, D. J. A.; Pierik, A. J.; Wohlschlegel, J. A.; Lill,
R.: MMS19 assembles iron-sulfur proteins required for DNA metabolism
and genomic integrity. Science 337: 195-199, 2012.
*FIELD* CN
Patricia A. Hartz - updated: 8/15/2012
*FIELD* CD
Victor A. McKusick: 12/3/1999
*FIELD* ED
carol: 08/20/2012
carol: 8/20/2012
terry: 8/15/2012
alopez: 10/19/2005
ckniffin: 8/26/2002
mgross: 12/3/1999
*RECORD*
*FIELD* NO
604333
*FIELD* TI
*604333 WD40 REPEAT-CONTAINING PROTEIN CIAO1; CIAO1
;;WD REPEAT-CONTAINING PROTEIN 39; WDR39
read more*FIELD* TX
DESCRIPTION
CIAO1 is a subunit of a protein complex involved in the biosynthesis of
Fe-S proteins. Other subunits of this complex are MMS19 (614777), FAM96B
(614778), and NARFL (611118) (Stehling et al., 2012; Gari et al., 2012).
CLONING
The Wilms tumor gene (WT1; 607102) on 11p13 is involved in regulating
cell cycle progression and apoptosis. In an attempt to dissect the
molecular mechanisms of transcriptional activation and repression by
WT1, and to identify other proteins that may be involved in kidney and
hematopoietic cell tumorigenesis, several groups have studied
WT1-interacting proteins. WT1 binds in vivo and in vitro to p53
(191170), resulting in WT1 functioning as a transcriptional repressor.
Mutations in p53 increase the aggressiveness of Wilms tumors, resulting
in poorer patient prognosis, but are not thought to be a primary genetic
cause of Wilms tumor formation. WT1 also interacts with and regulates
the transcriptional activity of steroidogenic factor-1 (184757), a key
molecule in gonadal development. Johnstone et al. (1996) identified a
protein called PAWR (601936), the gene for which maps to 12q21, that is
capable of modulating the transcriptional activities of WT1. Johnstone
et al. (1998) identified a second protein, which they named CIAO1 after
the Chinese word for 'bridge,' that is also capable of modulating the
transcriptional activities of WT1. CIAO1 is a 339-amino acid polypeptide
containing 7 WD40 or beta-transducin repeats. It can inhibit the
transcriptional activation function of WT1, but does not affect
WT1-mediated transcriptional repression. Johnstone et al. (1998)
demonstrated that the yeast Ciao1 homolog is an essential protein that
appears to be highly evolutionarily conserved.
GENE STRUCTURE
Johnstone et al. (1999) described the structural organization of the
CIAO1 gene, with the intron/exon boundaries closely matching the
consensus 5-prime donor/3-prime acceptor splice site sequences. The gene
contains 7 exons.
GENE FUNCTION
Ito et al. (2010) showed that CIAO1 coprecipitated with ANT2 (SLC25A5;
300150), XPD (ERCC2; 126340), MIP18 (FAM96B), and MMS19 in a protein
complex that was required for chromosome segregation in human cell
lines.
In HEK293 cells, Stehling et al. (2012) identified and confirmed a
protein complex made up of several known or putative proteins involved
in the biosynthesis of Fe-S proteins: MMS19, CIAO1, and IOP1 (NARFL).
Inactivation of MMS19, FAM96B, or IOP1 reduced HEK293 cell survival
following UV irradiation or methyl methanesulfonate treatment. Stehling
et al. (2012) hypothesized that the complex acts late in Fe-S protein
biogenesis to facilitate Fe-S cluster transfer from the CIA scaffold
complex CFD1 (NUBP2; 610779)-NBP35 (NUBP1; 600280) to Fe-S target
proteins.
Using coimmunoprecipitation and gel filtration studies, Gari et al.
(2012) independently identified a stable complex that involved MMS19,
CIAO1, IOP1, and FAM96B.
MAPPING
By FISH and radiation hybrid analysis, Johnstone et al. (1999) mapped
the WDR39 gene to the pericentric region of chromosome 2. They stated
that the probable location is 2q11.2 based on the gene's inclusion
within a previously mapped BAC clone (GenBank GENBANK AC004020).
*FIELD* RF
1. Gari, K.; Ortiz, A. M. L.; Borel, V.; Flynn, H.; Skehel, J. M.;
Boulton, S. J.: MMS19 links cytoplasmic iron-sulfur cluster assembly
to DNA metabolism. Science 337: 243-245, 2012.
2. Ito, S.; Tan, L. J.; Andoh, D.; Narita, T.; Seki, M.; Hirano, Y.;
Narita, K.; Kuraoka, I.; Hiraoka, Y.; Tanaka, K.: MMXD, a TFIIH-independent
XPD-MMS19 protein complex involved in chromosome segregation. Molec.
Cell 39: 632-640, 2010.
3. Johnstone, R. W.; See, R. H.; Sells, S. F.; Wang, J.; Muthukkumar,
S.; Englert, C.; Haber, D. A.; Licht, J. D.; Sugrue, S. P.; Roberts,
T.; Rangnekar, V. M.; Shi, Y.: A novel repressor, par-4, modulates
transcription and growth suppression functions of the Wilms' tumor
suppressor WT1. Molec. Cell. Biol. 16: 6945-6956, 1996.
4. Johnstone, R. W.; Tommerup, N.; Hansen, C.; Vissing, H.; Shi, Y.
: Structural organization, tissue expression, and chromosomal localization
of Ciao 1, a functional modulator of the Wilms' tumor suppressor,
WT1. Immunogenetics 49: 900-905, 1999.
5. Johnstone, R. W.; Wang, J.; Tommerup, N.; Vissing, H.; Roberts,
T.; Shi, Y.: Ciao 1 is a novel WD40 protein that interacts with the
tumor suppressor protein WT1. J. Biol. Chem. 273: 10880-10887, 1998.
6. Stehling, O.; Vashisht, A. A.; Mascarenhas, J.; Jonsson, Z. O.;
Sharma, T.; Netz, D. J. A.; Pierik, A. J.; Wohlschlegel, J. A.; Lill,
R.: MMS19 assembles iron-sulfur proteins required for DNA metabolism
and genomic integrity. Science 337: 195-199, 2012.
*FIELD* CN
Patricia A. Hartz - updated: 8/15/2012
*FIELD* CD
Victor A. McKusick: 12/3/1999
*FIELD* ED
carol: 08/20/2012
carol: 8/20/2012
terry: 8/15/2012
alopez: 10/19/2005
ckniffin: 8/26/2002
mgross: 12/3/1999