MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Zinc finger protein 431; AltName: Full=Zinc finger protein 932; |
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| MyHits synonyms | ZN431_MOUSE , E9QAG8 , 1F7F44631FEB1BA2 |
 Legends: 1, CONFLICT I -> T (in Ref. 2; BC012405). {ECO:0000305}; 2, KRAB. {ECO:0000255|PROSITE- ProRule:PRU00119}; 3, ZN_FING C2H2-type 1. {ECO:0000255|PROSITE- ProRule:PRU00042}; 4, ZN_FING C2H2-type 2. {ECO:0000255|PROSITE- ProRule:PRU00042}; 5, ZN_FING C2H2-type 3. {ECO:0000255|PROSITE- ProRule:PRU00042}; 6, ZN_FING C2H2-type 4. {ECO:0000255|PROSITE- ProRule:PRU00042}; 7, ZN_FING C2H2-type 5. {ECO:0000255|PROSITE- ProRule:PRU00042}; 8, ZN_FING C2H2-type 6. {ECO:0000255|PROSITE- ProRule:PRU00042}; 9, ZN_FING C2H2-type 7. {ECO:0000255|PROSITE- ProRule:PRU00042}; 10, ZN_FING C2H2-type 8. {ECO:0000255|PROSITE- ProRule:PRU00042}; 11, ZN_FING C2H2-type 9. {ECO:0000255|PROSITE- ProRule:PRU00042}; 12, ZN_FING C2H2-type 10. {ECO:0000255|PROSITE- ProRule:PRU00042}; 13, ZN_FING C2H2-type 11. {ECO:0000255|PROSITE- ProRule:PRU00042}; 14, ZN_FING C2H2-type 12. {ECO:0000255|PROSITE- ProRule:PRU00042}; 15, ZN_FING C2H2-type 13. {ECO:0000255|PROSITE- ProRule:PRU00042}; 16, ZN_FING C2H2-type 14. {ECO:0000255|PROSITE- ProRule:PRU00042}; 17, ZN_FING C2H2-type 15. {ECO:0000255|PROSITE- ProRule:PRU00042}; 18, ipat:ZINC_FINGER_C2H2_1 [T]; 19, ismart:ZnF_C2H2 [T]; 20, iprf:ZINC_FINGER_C2H2_2 [T]; 21, ismart:KRAB [T]; 22, ipfam:KRAB [T].
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ID ZN431_MOUSE Reviewed; 526 AA.
AC E9QAG8;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 02-NOV-2016, entry version 48.
DE RecName: Full=Zinc finger protein 431;
DE AltName: Full=Zinc finger protein 932;
GN Name=Znf431; Synonyms=Zfp431, Zfp932;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of
RT the mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP FUNCTION, INTERACTION WITH HDAC1 AND HDAC2, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=21177534; DOI=10.1074/jbc.M110.178780;
RA He Z., Cai J., Lim J.W., Kroll K., Ma L.;
RT "A novel KRAB domain-containing zinc finger transcription factor
RT ZNF431 directly represses Patched1 transcription.";
RL J. Biol. Chem. 286:7279-7289(2011).
RN [4]
RP FUNCTION, INTERACTION WITH HDAC2, AND DEVELOPMENTAL STAGE.
RX PubMed=22391310; DOI=10.1016/B978-0-12-394622-5.00014-6;
RA Huang G.J., He Z., Ma L.;
RT "ZFP932 suppresses cellular Hedgehog response and Patched1
RT transcription.";
RL Vitam. Horm. 88:309-332(2012).
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
CC for PTCH1 during embryonic development. Required for osteoblast
CC differentiation and sonic hedgehog/SHH signaling response. Binds
CC to the consensus site 5'-GCGCCC-3' in the promoter of PTCH1.
CC {ECO:0000269|PubMed:21177534, ECO:0000269|PubMed:22391310}.
CC -!- SUBUNIT: Interacts (via KRAB domain) with HDAC2; the interaction
CC is direct. Interacts (via KRAB domain) with HDAC1.
CC {ECO:0000269|PubMed:21177534, ECO:0000269|PubMed:22391310}.
CC -!- INTERACTION:
CC O09106:Hdac1; NbExp=3; IntAct=EBI-9549639, EBI-301912;
CC P70288:Hdac2; NbExp=3; IntAct=EBI-9549639, EBI-302251;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21177534}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, lung, thymus,
CC spleen, lymph node, liver, kidney, muscle, testis, ovary, skin and
CC uterus. {ECO:0000269|PubMed:21177534}.
CC -!- DEVELOPMENTAL STAGE: Expressed in limb mesenchyme at 10.5 dpc.
CC Expressed in tooth, submandibular glands, thymus, thyroid,
CC vibrissa follicles at 14.5 dpc. {ECO:0000269|PubMed:21177534,
CC ECO:0000269|PubMed:22391310}.
CC -!- DOMAIN: The KRAB domain is necessary for its repressive activity.
CC -!- SIMILARITY: Contains 15 C2H2-type zinc fingers.
CC {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC -!- SIMILARITY: Contains 1 KRAB domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00119}.
DR EMBL; AC123679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012405; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS59681.1; -.
DR RefSeq; NP_663538.2; NM_145563.2.
DR UniGene; Mm.441438; -.
DR ProteinModelPortal; E9QAG8; -.
DR SMR; E9QAG8; -.
DR BioGrid; 213490; 2.
DR IntAct; E9QAG8; 2.
DR STRING; 10090.ENSMUSP00000108159; -.
DR iPTMnet; E9QAG8; -.
DR PhosphoSitePlus; E9QAG8; -.
DR PaxDb; E9QAG8; -.
DR PRIDE; E9QAG8; -.
DR Ensembl; ENSMUST00000112540; ENSMUSP00000108159; ENSMUSG00000066613.
DR GeneID; 69504; -.
DR KEGG; mmu:69504; -.
DR UCSC; uc008ypn.1; mouse.
DR CTD; 69504; -.
DR MGI; MGI:1916754; Zfp932.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; COG5048; LUCA.
DR GeneTree; ENSGT00760000119089; -.
DR InParanoid; E9QAG8; -.
DR OMA; KACNQAS; -.
DR TreeFam; TF338854; -.
DR PRO; PR:E9QAG8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR Bgee; ENSMUSG00000066613; -.
DR ExpressionAtlas; E9QAG8; baseline and differential.
DR Genevisible; E9QAG8; MM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; TAS:UniProtKB.
DR GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR CDD; cd07765; KRAB_A-box; 1.
DR Gene3D; 3.30.160.60; -; 16.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR015880; Znf_C2H2-like.
DR InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR Pfam; PF13912; zf-C2H2_6; 2.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF109640; SSF109640; 1.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 15.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
PE 1: Evidence at protein level;
KW Complete proteome; Differentiation; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1 526 Zinc finger protein 431.
FT /FTId=PRO_0000425265.
FT DOMAIN 5 76 KRAB. {ECO:0000255|PROSITE-
FT ProRule:PRU00119}.
FT ZN_FING 104 126 C2H2-type 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 132 154 C2H2-type 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 160 182 C2H2-type 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 188 210 C2H2-type 4. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 216 238 C2H2-type 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 244 266 C2H2-type 6. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 272 294 C2H2-type 7. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 300 322 C2H2-type 8. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 328 350 C2H2-type 9. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 356 378 C2H2-type 10. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 384 406 C2H2-type 11. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 412 434 C2H2-type 12. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 440 462 C2H2-type 13. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 468 490 C2H2-type 14. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 496 518 C2H2-type 15. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT CONFLICT 323 323 I -> T (in Ref. 2; BC012405).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 190 210 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 246 266 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 216 238 ismart:ZnF_C2H2 [T]
FT MYHIT 300 327 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 160 182 ismart:ZnF_C2H2 [T]
FT MYHIT 468 490 ismart:ZnF_C2H2 [T]
FT MYHIT 162 182 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 384 406 ismart:ZnF_C2H2 [T]
FT MYHIT 106 126 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 160 187 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 5 61 ismart:KRAB [T]
FT MYHIT 328 355 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 272 299 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 440 462 ismart:ZnF_C2H2 [T]
FT MYHIT 244 271 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 218 238 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 412 434 ismart:ZnF_C2H2 [T]
FT MYHIT 496 523 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 470 490 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 5 45 ipfam:KRAB [T]
FT MYHIT 414 434 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 498 518 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 300 322 ismart:ZnF_C2H2 [T]
FT MYHIT 496 518 ismart:ZnF_C2H2 [T]
FT MYHIT 384 411 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 412 439 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 328 350 ismart:ZnF_C2H2 [T]
FT MYHIT 468 495 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 442 462 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 104 131 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 134 154 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 386 406 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 330 350 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 244 266 ismart:ZnF_C2H2 [T]
FT MYHIT 358 378 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 188 215 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 274 294 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 272 294 ismart:ZnF_C2H2 [T]
FT MYHIT 440 467 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 302 322 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 188 210 ismart:ZnF_C2H2 [T]
FT MYHIT 104 126 ismart:ZnF_C2H2 [T]
FT MYHIT 356 378 ismart:ZnF_C2H2 [T]
FT MYHIT 132 154 ismart:ZnF_C2H2 [T]
FT MYHIT 356 383 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 5 76 iprf:KRAB [T]
FT MYHIT 216 243 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 132 159 iprf:ZINC_FINGER_C2H2_2 [T]
SQ SEQUENCE 526 AA; 61280 MW; 1F7F44631FEB1BA2 CRC64;
MVDALTYDDV YVNFTQEEWA LLNPSQKSLY KDVMLETYRN LNAVGYNWED SNIEEHCESS
RRHGRHERNH TGEKPYEGIQ YGEAFVHHSS LQMRKIIHTG EKRYKCNQCD KAYSRHSILQ
IHKRTHSGEK PYECNQCGKA FTQHSHLKIH MVTHTGEKPY KCDQCGKAFA FHSTLQVHKR
THTGEKPYEC NQCSKAFAHH CHLRVHKRIH TGEKPYKCDQ CGKAFVGQND LKRHERVHTG
EKPYKCNECG KAFVCNASLR THKTTHTGVK PYECKQCTKS FASHGQLQKH ERIHTGEKPY
KCDQCGKAFA SHDKFQKHER IHIGEKPYKC KQCTKSFASH DKLQKHERIH TGEKPYECKQ
CTKSFASHNK LQKHERIHTG EKPYKCDQCN KAFVYESYLQ VHKKTHTGEK PYKCNECGKA
FARHSHLKVH KITHTGEKPY KCNQCGKALA YHSTLQVHQR THTGEKPYEC EQCGKAFANQ
SYFQVHKRIH TGEKPYKCDQ CGKAFVGSSD LKRHERVHTG RETLQM
//
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