ID   ZN431_HUMAN             Reviewed;         576 AA.
AC   Q8TF32; A8KAK7; Q8IWC4;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Zinc finger protein 431;
GN   Name=ZNF431; Synonyms=KIAA1969;
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].
RC   TISSUE=Brain;
RX   PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA   Nagase T., Kikuno R., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XXII. The
RT   complete sequences of 50 new cDNA clones which code for large proteins.";
RL   DNA Res. 8:319-327(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
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   [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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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).
CC   -!- FUNCTION: Sequence-specific DNA binding transcriptional repressor.
CC       Represses target gene transcription by recruiting HDAC1 and HDAC2
CC       histone deacetylases. Acts as a specific transcriptional repressor for
CC       PTCH1 during embryonic development. Required for osteoblast
CC       differentiation and sonic hedgehog/SHH signaling response. Binds to the
CC       consensus site 5'-GCGCCC-3' in the promoter of PTCH1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via KRAB domain) with HDAC2; the interaction is
CC       direct. Interacts (via KRAB domain) with HDAC1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The KRAB domain is necessary for its repressive activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB85555.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB075849; BAB85555.1; ALT_INIT; mRNA.
DR   EMBL; AK293072; BAF85761.1; -; mRNA.
DR   EMBL; CH471106; EAW84889.1; -; Genomic_DNA.
DR   EMBL; BC040506; AAH40506.1; -; mRNA.
DR   CCDS; CCDS32979.1; -.
DR   RefSeq; NP_001306053.1; NM_001319124.1.
DR   RefSeq; NP_001306055.1; NM_001319126.1.
DR   RefSeq; NP_001306056.1; NM_001319127.1.
DR   RefSeq; NP_597730.2; NM_133473.3.
DR   AlphaFoldDB; Q8TF32; -.
DR   SMR; Q8TF32; -.
DR   BioGRID; 128094; 22.
DR   IntAct; Q8TF32; 12.
DR   MINT; Q8TF32; -.
DR   STRING; 9606.ENSP00000308578; -.
DR   iPTMnet; Q8TF32; -.
DR   PhosphoSitePlus; Q8TF32; -.
DR   BioMuta; ZNF431; -.
DR   DMDM; 30173456; -.
DR   EPD; Q8TF32; -.
DR   jPOST; Q8TF32; -.
DR   MassIVE; Q8TF32; -.
DR   MaxQB; Q8TF32; -.
DR   PaxDb; 9606-ENSP00000308578; -.
DR   PeptideAtlas; Q8TF32; -.
DR   ProteomicsDB; 74546; -.
DR   Antibodypedia; 56857; 72 antibodies from 12 providers.
DR   DNASU; 170959; -.
DR   Ensembl; ENST00000311048.11; ENSP00000308578.6; ENSG00000196705.8.
DR   GeneID; 170959; -.
DR   KEGG; hsa:170959; -.
DR   MANE-Select; ENST00000311048.11; ENSP00000308578.6; NM_133473.4; NP_597730.2.
DR   UCSC; uc002npp.3; human.
DR   AGR; HGNC:20809; -.
DR   CTD; 170959; -.
DR   GeneCards; ZNF431; -.
DR   HGNC; HGNC:20809; ZNF431.
DR   HPA; ENSG00000196705; Low tissue specificity.
DR   MIM; 619505; gene.
DR   neXtProt; NX_Q8TF32; -.
DR   OpenTargets; ENSG00000196705; -.
DR   PharmGKB; PA134932493; -.
DR   VEuPathDB; HostDB:ENSG00000196705; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT01100000263507; -.
DR   HOGENOM; CLU_002678_44_5_1; -.
DR   InParanoid; Q8TF32; -.
DR   OMA; NCEECDN; -.
DR   OrthoDB; 3120079at2759; -.
DR   PhylomeDB; Q8TF32; -.
DR   TreeFam; TF342117; -.
DR   PathwayCommons; Q8TF32; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; Q8TF32; -.
DR   BioGRID-ORCS; 170959; 125 hits in 1115 CRISPR screens.
DR   ChiTaRS; ZNF431; human.
DR   GenomeRNAi; 170959; -.
DR   Pharos; Q8TF32; Tdark.
DR   PRO; PR:Q8TF32; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q8TF32; Protein.
DR   Bgee; ENSG00000196705; Expressed in lower esophagus mucosa and 173 other cell types or tissues.
DR   ExpressionAtlas; Q8TF32; baseline and differential.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS: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; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   Gene3D; 6.10.140.140; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 13.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23226; ZINC FINGER AND SCAN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR23226:SF313; ZINC FINGER PROTEIN 727; 1.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 9.
DR   Pfam; PF13465; zf-H2C2_2; 1.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 12.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 7.
DR   SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
DR   Genevisible; Q8TF32; HS.
PE   2: Evidence at transcript level;
KW   Differentiation; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..576
FT                   /note="Zinc finger protein 431"
FT                   /id="PRO_0000047579"
FT   DOMAIN          35..106
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         176..198
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         204..226
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         232..254
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         260..282
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         288..310
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         316..338
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         344..366
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         372..394
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         400..422
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         428..450
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         456..478
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         484..506
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         512..534
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   VARIANT         3
FT                   /note="D -> G (in dbSNP:rs17445374)"
FT                   /id="VAR_052825"
FT   CONFLICT        198
FT                   /note="H -> R (in Ref. 4; AAH40506)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   576 AA;  67217 MW;  532774BF69EC9E2A CRC64;
     MDDLKYGVYP LKEASGCPGA ERNLLVYSYF EKETLTFRDV AIEFSLEEWE CLNPAQQNLY
     MNVMLENYKN LVFLGVAVSK QDPVTCLEQE KEPWNMKRHE MVDEPPAMCS YFTKDLWPEQ
     DIKDSFQQVI LRRYGKCEHE NLQLRKGSAS VDEYKVHKEG YNELNQCLTT TQSKIFPCDK
     YVKVFHKFLN ANRHKTRHTG KKPFKCKKCG KSFCMLLHLS QHKRIHIREN SYQCEECGKA
     FKWFSTLTRH KRIHTGEKPF KCEECGKAFK QSSTLTTHKI IHTGEKPYRC EECGKAFNRS
     SHLTTHKIIH TGEKPYKCEE CGKAFNQSST LSTHKFIHAG EKPYKCEECD KAFNRFSYLT
     KHKIIHTGEK SYKCEECGKG FNWSSTLTKH KRIHTGEKPY KCEVCGKAFN ESSNLTTHKM
     IHTGEKPYKC EECGKAFNRS PQLTAHKIIH TGEKPYKCEE CGKAFSQSSI LTTHKRIHTG
     EKPYKCEECG KAFNRSSNLT KHKIIHTGEK SYKCEECGKA FNQSSTLTKH RKIHTRQKPY
     NCEECDNTFN QSSNLIKQNN SYWRETLQMS RMWESL
//