Full text data of DCAF7
DCAF7
(HAN11, WDR68)
[Confidence: low (only semi-automatic identification from reviews)]
DDB1- and CUL4-associated factor 7 (WD repeat-containing protein 68; WD repeat-containing protein An11 homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
DDB1- and CUL4-associated factor 7 (WD repeat-containing protein 68; WD repeat-containing protein An11 homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P61962
ID DCAF7_HUMAN Reviewed; 342 AA.
AC P61962; D3DU14; O15491; Q9DAE4;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-JUN-2004, sequence version 1.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=DDB1- and CUL4-associated factor 7;
DE AltName: Full=WD repeat-containing protein 68;
DE AltName: Full=WD repeat-containing protein An11 homolog;
GN Name=DCAF7; Synonyms=HAN11, WDR68;
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].
RC TISSUE=Liver;
RX PubMed=9192870;
RA de Vetten N., Quattrocchio F., Mol J., Koes R.;
RT "The an11 locus controlling flower pigmentation in petunia encodes a
RT novel WD-repeat protein conserved in yeast, plants, and animals.";
RL Genes Dev. 11:1422-1434(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [4]
RP INTERACTION WITH DYRK1A AND DYRK1B.
RX PubMed=14593110; DOI=10.1074/jbc.M301769200;
RA Skurat A.V., Dietrich A.D.;
RT "Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family
RT protein kinases.";
RL J. Biol. Chem. 279:2490-2498(2004).
RN [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH DIAPH1 AND DYRK1A, AND
RP FUNCTION.
RX PubMed=16887337; DOI=10.1016/j.jdermsci.2006.06.001;
RA Morita K., Lo Celso C., Spencer-Dene B., Zouboulis C.C., Watt F.M.;
RT "HAN11 binds mDia1 and controls GLI1 transcriptional activity.";
RL J. Dermatol. Sci. 44:11-20(2006).
RN [6]
RP FUNCTION, INTERACTION WITH DDB1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16949367; DOI=10.1016/j.molcel.2006.08.010;
RA Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.;
RT "A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
RT which is required for S phase destruction of the replication factor
RT Cdt1.";
RL Mol. Cell 23:709-721(2006).
RN [7]
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 [8]
RP INTERACTION WITH ZNF703, AND SUBCELLULAR LOCATION.
RX PubMed=21328542; DOI=10.1002/emmm.201100121;
RA Sircoulomb F., Nicolas N., Ferrari A., Finetti P., Bekhouche I.,
RA Rousselet E., Lonigro A., Adelaide J., Baudelet E., Esteyries S.,
RA Wicinski J., Audebert S., Charafe-Jauffret E., Jacquemier J.,
RA Lopez M., Borg J.P., Sotiriou C., Popovici C., Bertucci F.,
RA Birnbaum D., Chaffanet M., Ginestier C.;
RT "ZNF703 gene amplification at 8p12 specifies luminal B breast
RT cancer.";
RL EMBO Mol. Med. 3:153-166(2011).
CC -!- FUNCTION: Involved in craniofacial development. Acts upstream of
CC the EDN1 pathway and is required for formation of the upper jaw
CC equivalent, the palatoquadrate. The activity required for EDN1
CC pathway function differs between the first and second arches (By
CC similarity). Associates with DIAPH1 and controls GLI1
CC transcriptional activity. Could be involved in normal and disease
CC skin development. May function as a substrate receptor for CUL4-
CC DDB1 E3 ubiquitin-protein ligase complex.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DYRK1A, DYRK1B and DIAPH1. Interacts with
CC DDB1. Interacts with ZNF703.
CC -!- INTERACTION:
CC Q13627:DYRK1A; NbExp=3; IntAct=EBI-359808, EBI-1053596;
CC Q9Y463:DYRK1B; NbExp=2; IntAct=EBI-359808, EBI-634187;
CC Q9H2X6:HIPK2; NbExp=10; IntAct=EBI-359808, EBI-348345;
CC Q13233:MAP3K1; NbExp=6; IntAct=EBI-359808, EBI-49776;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Overexpression of
CC DIAHP1 or active RHOA causes translocation from the nucleus to
CC cytoplasm.
CC -!- SIMILARITY: Belongs to the WD repeat DCAF7 family.
CC -!- SIMILARITY: Contains 4 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; U94747; AAC18913.1; -; mRNA.
DR EMBL; CH471109; EAW94305.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94306.1; -; Genomic_DNA.
DR EMBL; BC001264; AAH01264.1; -; mRNA.
DR RefSeq; NP_005819.3; NM_005828.4.
DR UniGene; Hs.410596; -.
DR ProteinModelPortal; P61962; -.
DR DIP; DIP-40363N; -.
DR IntAct; P61962; 22.
DR MINT; MINT-1141032; -.
DR STRING; 9606.ENSP00000308344; -.
DR PhosphoSite; P61962; -.
DR DMDM; 48428729; -.
DR PaxDb; P61962; -.
DR PRIDE; P61962; -.
DR DNASU; 10238; -.
DR Ensembl; ENST00000310827; ENSP00000308344; ENSG00000136485.
DR GeneID; 10238; -.
DR KEGG; hsa:10238; -.
DR UCSC; uc002jbc.4; human.
DR CTD; 10238; -.
DR GeneCards; GC17P061627; -.
DR HGNC; HGNC:30915; DCAF7.
DR HPA; HPA022948; -.
DR HPA; HPA022962; -.
DR MIM; 605973; gene.
DR neXtProt; NX_P61962; -.
DR PharmGKB; PA165431770; -.
DR eggNOG; NOG314410; -.
DR HOGENOM; HOG000260968; -.
DR HOVERGEN; HBG050497; -.
DR InParanoid; P61962; -.
DR KO; K11805; -.
DR OMA; NKVQIVS; -.
DR SignaLink; P61962; -.
DR UniPathway; UPA00143; -.
DR GeneWiki; WDR68; -.
DR GenomeRNAi; 10238; -.
DR NextBio; 38784; -.
DR PRO; PR:P61962; -.
DR ArrayExpress; P61962; -.
DR Bgee; P61962; -.
DR CleanEx; HS_WDR68; -.
DR Genevestigator; P61962; -.
DR GO; GO:0080008; C:Cul4-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IC:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
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; 2.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Developmental protein; Nucleus;
KW Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1 342 DDB1- and CUL4-associated factor 7.
FT /FTId=PRO_0000051425.
FT REPEAT 66 108 WD 1.
FT REPEAT 118 160 WD 2.
FT REPEAT 172 214 WD 3.
FT REPEAT 264 304 WD 4.
SQ SEQUENCE 342 AA; 38926 MW; 794CC69A45D0CC7C CRC64;
MSLHGKRKEI YKYEAPWTVY AMNWSVRPDK RFRLALGSFV EEYNNKVQLV GLDEESSEFI
CRNTFDHPYP TTKLMWIPDT KGVYPDLLAT SGDYLRVWRV GETETRLECL LNNNKNSDFC
APLTSFDWNE VDPYLLGTSS IDTTCTIWGL ETGQVLGRVN LVSGHVKTQL IAHDKEVYDI
AFSRAGGGRD MFASVGADGS VRMFDLRHLE HSTIIYEDPQ HHPLLRLCWN KQDPNYLATM
AMDGMEVVIL DVRVPCTPVA RLNNHRACVN GIAWAPHSSC HICTAADDHQ ALIWDIQQMP
RAIEDPILAY TAEGEINNVQ WASTQPDWIA ICYNNCLEIL RV
//
ID DCAF7_HUMAN Reviewed; 342 AA.
AC P61962; D3DU14; O15491; Q9DAE4;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-JUN-2004, sequence version 1.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=DDB1- and CUL4-associated factor 7;
DE AltName: Full=WD repeat-containing protein 68;
DE AltName: Full=WD repeat-containing protein An11 homolog;
GN Name=DCAF7; Synonyms=HAN11, WDR68;
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].
RC TISSUE=Liver;
RX PubMed=9192870;
RA de Vetten N., Quattrocchio F., Mol J., Koes R.;
RT "The an11 locus controlling flower pigmentation in petunia encodes a
RT novel WD-repeat protein conserved in yeast, plants, and animals.";
RL Genes Dev. 11:1422-1434(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [4]
RP INTERACTION WITH DYRK1A AND DYRK1B.
RX PubMed=14593110; DOI=10.1074/jbc.M301769200;
RA Skurat A.V., Dietrich A.D.;
RT "Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family
RT protein kinases.";
RL J. Biol. Chem. 279:2490-2498(2004).
RN [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH DIAPH1 AND DYRK1A, AND
RP FUNCTION.
RX PubMed=16887337; DOI=10.1016/j.jdermsci.2006.06.001;
RA Morita K., Lo Celso C., Spencer-Dene B., Zouboulis C.C., Watt F.M.;
RT "HAN11 binds mDia1 and controls GLI1 transcriptional activity.";
RL J. Dermatol. Sci. 44:11-20(2006).
RN [6]
RP FUNCTION, INTERACTION WITH DDB1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16949367; DOI=10.1016/j.molcel.2006.08.010;
RA Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.;
RT "A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
RT which is required for S phase destruction of the replication factor
RT Cdt1.";
RL Mol. Cell 23:709-721(2006).
RN [7]
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 [8]
RP INTERACTION WITH ZNF703, AND SUBCELLULAR LOCATION.
RX PubMed=21328542; DOI=10.1002/emmm.201100121;
RA Sircoulomb F., Nicolas N., Ferrari A., Finetti P., Bekhouche I.,
RA Rousselet E., Lonigro A., Adelaide J., Baudelet E., Esteyries S.,
RA Wicinski J., Audebert S., Charafe-Jauffret E., Jacquemier J.,
RA Lopez M., Borg J.P., Sotiriou C., Popovici C., Bertucci F.,
RA Birnbaum D., Chaffanet M., Ginestier C.;
RT "ZNF703 gene amplification at 8p12 specifies luminal B breast
RT cancer.";
RL EMBO Mol. Med. 3:153-166(2011).
CC -!- FUNCTION: Involved in craniofacial development. Acts upstream of
CC the EDN1 pathway and is required for formation of the upper jaw
CC equivalent, the palatoquadrate. The activity required for EDN1
CC pathway function differs between the first and second arches (By
CC similarity). Associates with DIAPH1 and controls GLI1
CC transcriptional activity. Could be involved in normal and disease
CC skin development. May function as a substrate receptor for CUL4-
CC DDB1 E3 ubiquitin-protein ligase complex.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DYRK1A, DYRK1B and DIAPH1. Interacts with
CC DDB1. Interacts with ZNF703.
CC -!- INTERACTION:
CC Q13627:DYRK1A; NbExp=3; IntAct=EBI-359808, EBI-1053596;
CC Q9Y463:DYRK1B; NbExp=2; IntAct=EBI-359808, EBI-634187;
CC Q9H2X6:HIPK2; NbExp=10; IntAct=EBI-359808, EBI-348345;
CC Q13233:MAP3K1; NbExp=6; IntAct=EBI-359808, EBI-49776;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Overexpression of
CC DIAHP1 or active RHOA causes translocation from the nucleus to
CC cytoplasm.
CC -!- SIMILARITY: Belongs to the WD repeat DCAF7 family.
CC -!- SIMILARITY: Contains 4 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; U94747; AAC18913.1; -; mRNA.
DR EMBL; CH471109; EAW94305.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94306.1; -; Genomic_DNA.
DR EMBL; BC001264; AAH01264.1; -; mRNA.
DR RefSeq; NP_005819.3; NM_005828.4.
DR UniGene; Hs.410596; -.
DR ProteinModelPortal; P61962; -.
DR DIP; DIP-40363N; -.
DR IntAct; P61962; 22.
DR MINT; MINT-1141032; -.
DR STRING; 9606.ENSP00000308344; -.
DR PhosphoSite; P61962; -.
DR DMDM; 48428729; -.
DR PaxDb; P61962; -.
DR PRIDE; P61962; -.
DR DNASU; 10238; -.
DR Ensembl; ENST00000310827; ENSP00000308344; ENSG00000136485.
DR GeneID; 10238; -.
DR KEGG; hsa:10238; -.
DR UCSC; uc002jbc.4; human.
DR CTD; 10238; -.
DR GeneCards; GC17P061627; -.
DR HGNC; HGNC:30915; DCAF7.
DR HPA; HPA022948; -.
DR HPA; HPA022962; -.
DR MIM; 605973; gene.
DR neXtProt; NX_P61962; -.
DR PharmGKB; PA165431770; -.
DR eggNOG; NOG314410; -.
DR HOGENOM; HOG000260968; -.
DR HOVERGEN; HBG050497; -.
DR InParanoid; P61962; -.
DR KO; K11805; -.
DR OMA; NKVQIVS; -.
DR SignaLink; P61962; -.
DR UniPathway; UPA00143; -.
DR GeneWiki; WDR68; -.
DR GenomeRNAi; 10238; -.
DR NextBio; 38784; -.
DR PRO; PR:P61962; -.
DR ArrayExpress; P61962; -.
DR Bgee; P61962; -.
DR CleanEx; HS_WDR68; -.
DR Genevestigator; P61962; -.
DR GO; GO:0080008; C:Cul4-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IC:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
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; 2.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Developmental protein; Nucleus;
KW Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1 342 DDB1- and CUL4-associated factor 7.
FT /FTId=PRO_0000051425.
FT REPEAT 66 108 WD 1.
FT REPEAT 118 160 WD 2.
FT REPEAT 172 214 WD 3.
FT REPEAT 264 304 WD 4.
SQ SEQUENCE 342 AA; 38926 MW; 794CC69A45D0CC7C CRC64;
MSLHGKRKEI YKYEAPWTVY AMNWSVRPDK RFRLALGSFV EEYNNKVQLV GLDEESSEFI
CRNTFDHPYP TTKLMWIPDT KGVYPDLLAT SGDYLRVWRV GETETRLECL LNNNKNSDFC
APLTSFDWNE VDPYLLGTSS IDTTCTIWGL ETGQVLGRVN LVSGHVKTQL IAHDKEVYDI
AFSRAGGGRD MFASVGADGS VRMFDLRHLE HSTIIYEDPQ HHPLLRLCWN KQDPNYLATM
AMDGMEVVIL DVRVPCTPVA RLNNHRACVN GIAWAPHSSC HICTAADDHQ ALIWDIQQMP
RAIEDPILAY TAEGEINNVQ WASTQPDWIA ICYNNCLEIL RV
//
MIM
605973
*RECORD*
*FIELD* NO
605973
*FIELD* TI
*605973 DDB1- AND CUL4-ASSOCIATED FACTOR 7; DCAF7
;;AN11, PETUNIA, HOMOLOG OF; AN11
read more*FIELD* TX
CLONING
The An1, An2, and An11 loci control the pigmentation of petunias by
stimulating transcription of anthocyanin genes. By Southern blot
analysis with a petunia An11 probe, followed by EST database searching
and PCR, de Vetten et al. (1997) obtained a cDNA encoding human AN11.
The deduced 342-amino acid, WD repeat-containing protein is 53%
identical to the petunia An11 protein and is conserved in worms and
yeast, which do not produce anthocyanins. Functional analysis showed
that human AN11 could partially complement a petunia An11 mutant. De
Vetten et al. (1997) concluded that An11 is involved in signal
transduction in petunias.
*FIELD* RF
1. de Vetten, N.; Quattrocchio, F.; Mol, J.; Koes, R.: The an11 locus
controlling flower pigmentation in petunia encodes a novel WD-repeat
protein conserved in yeast, plants, and animals. Genes Dev. 11:
1422-1434, 1997.
*FIELD* CD
Paul J. Converse: 5/25/2001
*FIELD* ED
alopez: 03/27/2012
mgross: 5/25/2001
*RECORD*
*FIELD* NO
605973
*FIELD* TI
*605973 DDB1- AND CUL4-ASSOCIATED FACTOR 7; DCAF7
;;AN11, PETUNIA, HOMOLOG OF; AN11
read more*FIELD* TX
CLONING
The An1, An2, and An11 loci control the pigmentation of petunias by
stimulating transcription of anthocyanin genes. By Southern blot
analysis with a petunia An11 probe, followed by EST database searching
and PCR, de Vetten et al. (1997) obtained a cDNA encoding human AN11.
The deduced 342-amino acid, WD repeat-containing protein is 53%
identical to the petunia An11 protein and is conserved in worms and
yeast, which do not produce anthocyanins. Functional analysis showed
that human AN11 could partially complement a petunia An11 mutant. De
Vetten et al. (1997) concluded that An11 is involved in signal
transduction in petunias.
*FIELD* RF
1. de Vetten, N.; Quattrocchio, F.; Mol, J.; Koes, R.: The an11 locus
controlling flower pigmentation in petunia encodes a novel WD-repeat
protein conserved in yeast, plants, and animals. Genes Dev. 11:
1422-1434, 1997.
*FIELD* CD
Paul J. Converse: 5/25/2001
*FIELD* ED
alopez: 03/27/2012
mgross: 5/25/2001