ZN423_HUMAN
ID ZN423_HUMAN Reviewed; 1284 AA.
AC Q2M1K9; O94860; Q76N04; Q9NZ13;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Zinc finger protein 423;
DE AltName: Full=Olf1/EBF-associated zinc finger protein;
DE Short=hOAZ;
DE AltName: Full=Smad- and Olf-interacting zinc finger protein;
GN Name=ZNF423; Synonyms=KIAA0760, NPHP14, OAZ;
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).
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 61-1284, FUNCTION, DNA-BINDING, SUBCELLULAR
RP LOCATION, DOMAIN, TISSUE SPECIFICITY, INTERACTION WITH SMAD1 AND SMAD4, AND
RP MUTAGENESIS OF ASN-420; GLU-426; THR-452; GLU-458; ASP-491; GLU-497;
RP THR-528; GLU-534; PHE-574 AND THR-581.
RX PubMed=10660046; DOI=10.1016/s0092-8674(00)81561-5;
RA Hata A., Seoane J., Lagna G., Montalvo E., Hemmati-Brivanlou A.,
RA Massague J.;
RT "OAZ uses distinct DNA- and protein-binding zinc fingers in separate BMP-
RT Smad and Olf signaling pathways.";
RL Cell 100:229-240(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-1284.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-50; SER-604 AND
RP SER-1054, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [6]
RP INTERACTION WITH PARP1 AND CEP290, VARIANT NPHP14 LEU-913, AND VARIANT
RP JBTS19 TYR-1277.
RX PubMed=22863007; DOI=10.1016/j.cell.2012.06.028;
RA Chaki M., Airik R., Ghosh A.K., Giles R.H., Chen R., Slaats G.G., Wang H.,
RA Hurd T.W., Zhou W., Cluckey A., Gee H.Y., Ramaswami G., Hong C.J.,
RA Hamilton B.A., Cervenka I., Ganji R.S., Bryja V., Arts H.H.,
RA van Reeuwijk J., Oud M.M., Letteboer S.J., Roepman R., Husson H.,
RA Ibraghimov-Beskrovnaya O., Yasunaga T., Walz G., Eley L., Sayer J.A.,
RA Schermer B., Liebau M.C., Benzing T., Le Corre S., Drummond I., Janssen S.,
RA Allen S.J., Natarajan S., O'Toole J.F., Attanasio M., Saunier S.,
RA Antignac C., Koenekoop R.K., Ren H., Lopez I., Nayir A., Stoetzel C.,
RA Dollfus H., Massoudi R., Gleeson J.G., Andreoli S.P., Doherty D.G.,
RA Lindstrad A., Golzio C., Katsanis N., Pape L., Abboud E.B., Al-Rajhi A.A.,
RA Lewis R.A., Omran H., Lee E.Y., Wang S., Sekiguchi J.M., Saunders R.,
RA Johnson C.A., Garner E., Vanselow K., Andersen J.S., Shlomai J.,
RA Nurnberg G., Nurnberg P., Levy S., Smogorzewska A., Otto E.A.,
RA Hildebrandt F.;
RT "Exome capture reveals ZNF423 and CEP164 mutations, linking renal
RT ciliopathies to DNA damage response signaling.";
RL Cell 150:533-548(2012).
CC -!- FUNCTION: Transcription factor that can both act as an activator or a
CC repressor depending on the context. Plays a central role in BMP
CC signaling and olfactory neurogenesis. Associates with SMADs in response
CC to BMP2 leading to activate transcription of BMP target genes. Acts as
CC a transcriptional repressor via its interaction with EBF1, a
CC transcription factor involved in terminal olfactory receptor neurons
CC differentiation; this interaction preventing EBF1 to bind DNA and
CC activate olfactory-specific genes. Involved in olfactory neurogenesis
CC by participating in a developmental switch that regulates the
CC transition from differentiation to maturation in olfactory receptor
CC neurons. Controls proliferation and differentiation of neural
CC precursors in cerebellar vermis formation.
CC {ECO:0000269|PubMed:10660046}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with EBF1 (By
CC similarity). Interacts with SMAD1 and SMAD4. Interacts with PARP1.
CC Interacts with CEP290. {ECO:0000250, ECO:0000269|PubMed:10660046,
CC ECO:0000269|PubMed:22863007}.
CC -!- INTERACTION:
CC Q2M1K9; O15078: CEP290; NbExp=3; IntAct=EBI-950016, EBI-1811944;
CC Q2M1K9; P09874: PARP1; NbExp=2; IntAct=EBI-950016, EBI-355676;
CC Q2M1K9; P10276: RARA; NbExp=2; IntAct=EBI-950016, EBI-413374;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10660046}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2M1K9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2M1K9-2; Sequence=VSP_057595;
CC -!- TISSUE SPECIFICITY: Expressed in brain, lung, skeletal muscle, heart,
CC pancreas and kidney but not liver or placenta. Also expressed in aorta,
CC ovary, pituitary, small intestine, fetal brain, fetal kidney and,
CC within the adult brain, in the substantia nigra, medulla, amygdala,
CC thalamus and cerebellum. {ECO:0000269|PubMed:10660046}.
CC -!- DOMAIN: Uses different DNA- and protein-binding zinc fingers to
CC regulate the distinct BMP-Smad and Olf signaling pathways. C2H2-type
CC zinc fingers 14-19 mediate the interaction with SMAD1 and SMAD4, while
CC zinc fingers 28-30 mediate the interaction with EBF1. zinc fingers 2-8
CC bind the 5'-CCGCCC-3' DNA sequence in concert with EBF1, while zinc
CC fingers 9-13 bind BMP target gene promoters in concert with SMADs.
CC {ECO:0000269|PubMed:10660046}.
CC -!- DISEASE: Nephronophthisis 14 (NPHP14) [MIM:614844]: An autosomal
CC recessive disorder manifesting as infantile-onset kidney disease,
CC cerebellar vermis hypoplasia, and situs inversus. Nephronophthisis is a
CC progressive tubulo-interstitial kidney disorder histologically
CC characterized by modifications of the tubules with thickening of the
CC basement membrane, interstitial fibrosis and, in the advanced stages,
CC medullary cysts. {ECO:0000269|PubMed:22863007}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Joubert syndrome 19 (JBTS19) [MIM:614844]: A form of Joubert
CC syndrome, a disorder presenting with cerebellar ataxia, oculomotor
CC apraxia, hypotonia, neonatal breathing abnormalities and psychomotor
CC delay. Neuroradiologically, it is characterized by cerebellar vermian
CC hypoplasia/aplasia, thickened and reoriented superior cerebellar
CC peduncles, and an abnormally large interpeduncular fossa, giving the
CC appearance of a molar tooth on transaxial slices (molar tooth sign).
CC JBTS19 patients have polycystic kidney disease, Leber congenital
CC amaurosis, cerebellar vermis hypoplasia, and breathing abnormality.
CC {ECO:0000269|PubMed:22863007}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; BC112315; AAI12316.1; -; mRNA.
DR EMBL; BC112317; AAI12318.1; -; mRNA.
DR EMBL; AF221712; AAF28354.1; -; mRNA.
DR EMBL; AB018303; BAA34480.2; -; mRNA.
DR CCDS; CCDS32445.1; -. [Q2M1K9-1]
DR CCDS; CCDS61930.1; -. [Q2M1K9-2]
DR RefSeq; NP_001258549.1; NM_001271620.2. [Q2M1K9-2]
DR RefSeq; NP_055884.2; NM_015069.4. [Q2M1K9-1]
DR RefSeq; XP_005255913.1; XM_005255856.4. [Q2M1K9-2]
DR RefSeq; XP_016878566.1; XM_017023077.1. [Q2M1K9-2]
DR RefSeq; XP_016878567.1; XM_017023078.1. [Q2M1K9-2]
DR PDB; 2MDG; NMR; -; A=928-981.
DR PDBsum; 2MDG; -.
DR AlphaFoldDB; Q2M1K9; -.
DR BMRB; Q2M1K9; -.
DR SMR; Q2M1K9; -.
DR BioGRID; 116718; 29.
DR IntAct; Q2M1K9; 19.
DR MINT; Q2M1K9; -.
DR STRING; 9606.ENSP00000455426; -.
DR GlyGen; Q2M1K9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q2M1K9; -.
DR PhosphoSitePlus; Q2M1K9; -.
DR BioMuta; ZNF423; -.
DR DMDM; 121941357; -.
DR EPD; Q2M1K9; -.
DR jPOST; Q2M1K9; -.
DR MassIVE; Q2M1K9; -.
DR PaxDb; Q2M1K9; -.
DR PeptideAtlas; Q2M1K9; -.
DR PRIDE; Q2M1K9; -.
DR ProteomicsDB; 61340; -.
DR ABCD; Q2M1K9; 1 sequenced antibody.
DR Antibodypedia; 28187; 108 antibodies from 26 providers.
DR DNASU; 23090; -.
DR Ensembl; ENST00000561648.5; ENSP00000455426.1; ENSG00000102935.12. [Q2M1K9-1]
DR Ensembl; ENST00000562520.1; ENSP00000457664.1; ENSG00000102935.12. [Q2M1K9-2]
DR Ensembl; ENST00000562871.5; ENSP00000457928.1; ENSG00000102935.12. [Q2M1K9-2]
DR GeneID; 23090; -.
DR KEGG; hsa:23090; -.
DR UCSC; uc031qwd.2; human. [Q2M1K9-1]
DR CTD; 23090; -.
DR DisGeNET; 23090; -.
DR GeneCards; ZNF423; -.
DR GeneReviews; ZNF423; -.
DR HGNC; HGNC:16762; ZNF423.
DR HPA; ENSG00000102935; Tissue enhanced (brain, skeletal muscle).
DR MalaCards; ZNF423; -.
DR MIM; 604557; gene.
DR MIM; 614844; phenotype.
DR neXtProt; NX_Q2M1K9; -.
DR OpenTargets; ENSG00000102935; -.
DR Orphanet; 93591; Infantile nephronophthisis.
DR Orphanet; 2318; Joubert syndrome with oculorenal defect.
DR PharmGKB; PA134903681; -.
DR VEuPathDB; HostDB:ENSG00000102935; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158492; -.
DR InParanoid; Q2M1K9; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q2M1K9; -.
DR TreeFam; TF331504; -.
DR PathwayCommons; Q2M1K9; -.
DR SignaLink; Q2M1K9; -.
DR SIGNOR; Q2M1K9; -.
DR BioGRID-ORCS; 23090; 14 hits in 1097 CRISPR screens.
DR ChiTaRS; ZNF423; human.
DR GeneWiki; ZNF423; -.
DR GenomeRNAi; 23090; -.
DR Pharos; Q2M1K9; Tbio.
DR PRO; PR:Q2M1K9; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q2M1K9; protein.
DR Bgee; ENSG00000102935; Expressed in skeletal muscle tissue of biceps brachii and 173 other tissues.
DR ExpressionAtlas; Q2M1K9; baseline and differential.
DR Genevisible; Q2M1K9; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0007219; P:Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0061512; P:protein localization to cilium; IMP:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00355; ZnF_C2H2; 30.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 27.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 23.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Ciliopathy;
KW Developmental protein; Differentiation; Disease variant; DNA-binding;
KW Joubert syndrome; Metal-binding; Nephronophthisis; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1284
FT /note="Zinc finger protein 423"
FT /id="PRO_0000308595"
FT ZN_FING 67..93
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 138..160
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 166..188
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 194..216
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 222..244
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 263..286
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 295..318
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 323..345
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 409..433
FT /note="C2H2-type 9; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 441..464
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 480..503
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 517..540
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 563..588
FT /note="C2H2-type 13; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 632..654
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 662..684
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 692..715
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 720..743
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 750..773
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 781..803
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 807..830
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 886..908
FT /note="C2H2-type 21; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 930..952
FT /note="C2H2-type 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 959..981
FT /note="C2H2-type 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1020..1042
FT /note="C2H2-type 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1064..1082
FT /note="C2H2-type 25; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1120..1143
FT /note="C2H2-type 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1168..1190
FT /note="C2H2-type 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1198..1220
FT /note="C2H2-type 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1229..1252
FT /note="C2H2-type 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1259..1282
FT /note="C2H2-type 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1054
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 2)"
FT /id="VSP_057595"
FT VARIANT 629
FT /note="N -> S (in dbSNP:rs34214571)"
FT /id="VAR_036844"
FT VARIANT 913
FT /note="P -> L (in NPHP14; found at homozygosity in two
FT siblings with nephronophthisis, cerebellar vermis
FT hypoplasia and situs inversus; dbSNP:rs200585917)"
FT /evidence="ECO:0000269|PubMed:22863007"
FT /id="VAR_068501"
FT VARIANT 1277
FT /note="H -> Y (in JBTS19; dbSNP:rs1596988259)"
FT /evidence="ECO:0000269|PubMed:22863007"
FT /id="VAR_068502"
FT MUTAGEN 420
FT /note="N->A: Abolishes the ability to bind promoter of BMP
FT target genes; when associated with A-426; A-452; A-458; A-
FT 491; A-497; A-528; A-534; A-574 and A-581."
FT /evidence="ECO:0000269|PubMed:10660046"
FT MUTAGEN 426
FT /note="E->A: Abolishes the ability to bind promoter of BMP
FT target genes; when associated with A-420; A-452; A-458; A-
FT 491; A-497; A-528; A-534; A-574 and A-581."
FT /evidence="ECO:0000269|PubMed:10660046"
FT MUTAGEN 452
FT /note="T->A: Abolishes the ability to bind promoter of BMP
FT target genes; when associated with A-420; A-426; A-458; A-
FT 491; A-497; A-528; A-534; A-574 and A-581."
FT /evidence="ECO:0000269|PubMed:10660046"
FT MUTAGEN 458
FT /note="E->A: Abolishes the ability to bind promoter of BMP
FT target genes; when associated with A-420; A-426; A-452; A-
FT 491; A-497; A-528; A-534; A-574 and A-581."
FT /evidence="ECO:0000269|PubMed:10660046"
FT MUTAGEN 491
FT /note="D->A: Abolishes the ability to bind promoter of BMP
FT target genes; when associated with A-420; A-426; A-452; A-
FT 458; A-497; A-528; A-534; A-574 and A-581."
FT /evidence="ECO:0000269|PubMed:10660046"
FT MUTAGEN 497
FT /note="E->A: Abolishes the ability to bind promoter of BMP
FT target genes; when associated with A-420; A-426; A-452; A-
FT 458; A-491; A-528; A-534; A-574 and A-581."
FT /evidence="ECO:0000269|PubMed:10660046"
FT MUTAGEN 528
FT /note="T->A: Abolishes the ability to bind promoter of BMP
FT target genes; when associated with A-420; A-426; A-452; A-
FT 458; A-491; A-497; A-534; A-574 and A-581."
FT /evidence="ECO:0000269|PubMed:10660046"
FT MUTAGEN 534
FT /note="E->A: Abolishes the ability to bind promoter of BMP
FT target genes; when associated with A-420; A-426; A-452; A-
FT 458; A-491; A-497; A-528; A-574 and A-581."
FT /evidence="ECO:0000269|PubMed:10660046"
FT MUTAGEN 574
FT /note="F->A: Abolishes the ability to bind promoter of BMP
FT target genes; when associated with A-420; A-426; A-452; A-
FT 458; A-491; A-497; A-528; A-534 and A-581."
FT /evidence="ECO:0000269|PubMed:10660046"
FT MUTAGEN 581
FT /note="T->A: Abolishes the ability to bind promoter of BMP
FT target genes; when associated with A-420; A-426; A-452; A-
FT 458; A-491; A-497; A-528; A-534 and A-574."
FT /evidence="ECO:0000269|PubMed:10660046"
FT STRAND 933..937
FT /evidence="ECO:0007829|PDB:2MDG"
FT HELIX 942..949
FT /evidence="ECO:0007829|PDB:2MDG"
FT HELIX 950..952
FT /evidence="ECO:0007829|PDB:2MDG"
FT STRAND 958..960
FT /evidence="ECO:0007829|PDB:2MDG"
FT STRAND 962..964
FT /evidence="ECO:0007829|PDB:2MDG"
FT STRAND 967..970
FT /evidence="ECO:0007829|PDB:2MDG"
FT HELIX 973..979
FT /evidence="ECO:0007829|PDB:2MDG"
SQ SEQUENCE 1284 AA; 144605 MW; F34CB87161738321 CRC64;
MHKKRVEEGE ASDFSLAWDS SVTAAGGLEG EPECDQKTSR ALEDRNSVTS QEERNEDDED
MEDESIYTCD HCQQDFESLA DLTDHRAHRC PGDGDDDPQL SWVASSPSSK DVASPTQMIG
DGCDLGLGEE EGGTGLPYPC QFCDKSFIRL SYLKRHEQIH SDKLPFKCTY CSRLFKHKRS
RDRHIKLHTG DKKYHCHECE AAFSRSDHLK IHLKTHSSSK PFKCTVCKRG FSSTSSLQSH
MQAHKKNKEH LAKSEKEAKK DDFMCDYCED TFSQTEELEK HVLTRHPQLS EKADLQCIHC
PEVFVDENTL LAHIHQAHAN QKHKCPMCPE QFSSVEGVYC HLDSHRQPDS SNHSVSPDPV
LGSVASMSSA TPDSSASVER GSTPDSTLKP LRGQKKMRDD GQGWTKVVYS CPYCSKRDFN
SLAVLEIHLK TIHADKPQQS HTCQICLDSM PTLYNLNEHV RKLHKNHAYP VMQFGNISAF
HCNYCPEMFA DINSLQEHIR VSHCGPNANP SDGNNAFFCN QCSMGFLTES SLTEHIQQAH
CSVGSAKLES PVVQPTQSFM EVYSCPYCTN SPIFGSILKL TKHIKENHKN IPLAHSKKSK
AEQSPVSSDV EVSSPKRQRL SASANSISNG EYPCNQCDLK FSNFESFQTH LKLHLELLLR
KQACPQCKED FDSQESLLQH LTVHYMTTST HYVCESCDKQ FSSVDDLQKH LLDMHTFVLY
HCTLCQEVFD SKVSIQVHLA VKHSNEKKMY RCTACNWDFR KEADLQVHVK HSHLGNPAKA
HKCIFCGETF STEVELQCHI TTHSKKYNCK FCSKAFHAII LLEKHLREKH CVFDAATENG
TANGVPPMAT KKAEPADLQG MLLKNPEAPN SHEASEDDVD ASEPMYGCDI CGAAYTMEVL
LQNHRLRDHN IRPGEDDGSR KKAEFIKGSH KCNVCSRTFF SENGLREHLQ THRGPAKHYM
CPICGERFPS LLTLTEHKVT HSKSLDTGTC RICKMPLQSE EEFIEHCQMH PDLRNSLTGF
RCVVCMQTVT STLELKIHGT FHMQKLAGSS AASSPNGQGL QKLYKCALCL KEFRSKQDLV
KLDVNGLPYG LCAGCMARSA NGQVGGLAPP EPADRPCAGL RCPECSVKFE SAEDLESHMQ
VDHRDLTPET SGPRKGTQTS PVPRKKTYQC IKCQMTFENE REIQIHVANH MIEEGINHEC
KLCNQMFDSP AKLLCHLIEH SFEGMGGTFK CPVCFTVFVQ ANKLQQHIFA VHGQEDKIYD
CSQCPQKFFF QTELQNHTMS QHAQ
