ZN431_HUMAN
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 03-AUG-2022, entry version 175.
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 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; Q8TF32; -.
DR PeptideAtlas; Q8TF32; -.
DR PRIDE; Q8TF32; -.
DR ProteomicsDB; 74546; -.
DR Antibodypedia; 56857; 68 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 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; ENSGT01050000244908; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; Q8TF32; -.
DR OMA; NCEECDN; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8TF32; -.
DR TreeFam; TF342117; -.
DR PathwayCommons; Q8TF32; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q8TF32; -.
DR BioGRID-ORCS; 170959; 121 hits in 1037 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 172 other tissues.
DR ExpressionAtlas; Q8TF32; baseline and differential.
DR Genevisible; Q8TF32; HS.
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 transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 11.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
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
