ZNF81_HUMAN
ID ZNF81_HUMAN Reviewed; 661 AA.
AC P51508; Q6RX22; Q96QH6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Zinc finger protein 81;
DE AltName: Full=HFZ20;
GN Name=ZNF81;
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 [MRNA], VARIANTS VAL-3; SER-157; ASN-179; LEU-185 AND
RP VAL-499, AND CHROMOSOMAL TRANSLOCATION.
RX PubMed=15121780; DOI=10.1136/jmg.2003.016972;
RA Kleefstra T., Yntema H.G., Oudakker A.R., Banning M.J.G., Kalscheuer V.M.,
RA Chelly J., Moraine C., Ropers H.-H., Fryns J.-P., Janssen I.M.,
RA Sistermans E.A., Nillesen W.N., de Vries L.B.A., Hamel B.C.J.,
RA van Bokhoven H.;
RT "Zinc finger 81 (ZNF81) mutations associated with X-linked mental
RT retardation.";
RL J. Med. Genet. 41:394-399(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 325-661.
RX PubMed=8507979; DOI=10.1007/bf00417431;
RA Marino M., Archidiacono N., Franze A., Rosati M., Rocchi M., Ballabio A.,
RA Grimaldi G.;
RT "A novel X-linked member of the human zinc finger protein gene family:
RT isolation, mapping, and expression.";
RL Mamm. Genome 4:252-257(1993).
RN [4]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-266, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DISEASE: Note=A chromosomal aberration involving ZNF81 is found in a
CC severe intellectual disability patient. Translocation
CC t(X;9)(p11.23;q34.3). {ECO:0000269|PubMed:15121780}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY487248; AAS17752.1; -; mRNA.
DR EMBL; AL591394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL022578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z98304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X68011; CAA48148.1; -; Genomic_DNA.
DR CCDS; CCDS43933.1; -.
DR PIR; S60520; S60520.
DR RefSeq; NP_009068.2; NM_007137.3.
DR RefSeq; XP_005272657.1; XM_005272600.3.
DR RefSeq; XP_011542201.1; XM_011543899.2.
DR RefSeq; XP_011542202.1; XM_011543900.2.
DR RefSeq; XP_016884975.1; XM_017029486.1.
DR RefSeq; XP_016884976.1; XM_017029487.1.
DR AlphaFoldDB; P51508; -.
DR SMR; P51508; -.
DR BioGRID; 131424; 7.
DR IntAct; P51508; 1.
DR STRING; 9606.ENSP00000366153; -.
DR iPTMnet; P51508; -.
DR PhosphoSitePlus; P51508; -.
DR BioMuta; ZNF81; -.
DR DMDM; 55977803; -.
DR MassIVE; P51508; -.
DR MaxQB; P51508; -.
DR PaxDb; P51508; -.
DR PeptideAtlas; P51508; -.
DR PRIDE; P51508; -.
DR ProteomicsDB; 56311; -.
DR Antibodypedia; 5409; 137 antibodies from 20 providers.
DR DNASU; 347344; -.
DR Ensembl; ENST00000338637.13; ENSP00000341151.7; ENSG00000197779.15.
DR Ensembl; ENST00000376954.6; ENSP00000366153.1; ENSG00000197779.15.
DR GeneID; 347344; -.
DR KEGG; hsa:347344; -.
DR MANE-Select; ENST00000338637.13; ENSP00000341151.7; NM_007137.5; NP_009068.2.
DR UCSC; uc010nhy.3; human.
DR CTD; 347344; -.
DR DisGeNET; 347344; -.
DR GeneCards; ZNF81; -.
DR HGNC; HGNC:13156; ZNF81.
DR HPA; ENSG00000197779; Low tissue specificity.
DR MalaCards; ZNF81; -.
DR MIM; 314998; gene.
DR neXtProt; NX_P51508; -.
DR OpenTargets; ENSG00000197779; -.
DR Orphanet; 777; X-linked non-syndromic intellectual disability.
DR PharmGKB; PA37730; -.
DR VEuPathDB; HostDB:ENSG00000197779; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162553; -.
DR HOGENOM; CLU_002678_17_1_1; -.
DR InParanoid; P51508; -.
DR OMA; TMEKPHE; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; P51508; -.
DR TreeFam; TF350810; -.
DR PathwayCommons; P51508; -.
DR SignaLink; P51508; -.
DR BioGRID-ORCS; 347344; 3 hits in 715 CRISPR screens.
DR ChiTaRS; ZNF81; human.
DR GenomeRNAi; 347344; -.
DR Pharos; P51508; Tbio.
DR PRO; PR:P51508; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P51508; protein.
DR Bgee; ENSG00000197779; Expressed in colonic epithelium and 164 other tissues.
DR ExpressionAtlas; P51508; baseline and differential.
DR Genevisible; P51508; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0006357; P:regulation of transcription by RNA polymerase II; 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; 12.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 1: Evidence at protein level;
KW Chromosomal rearrangement; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..661
FT /note="Zinc finger protein 81"
FT /id="PRO_0000047395"
FT DOMAIN 21..92
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 330..352
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 358..380
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 386..408
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 414..436
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 442..464
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 470..492
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 498..520
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 526..548
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 554..576
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 582..604
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 610..632
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 638..660
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 266
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 3
FT /note="A -> V (in dbSNP:rs183846665)"
FT /evidence="ECO:0000269|PubMed:15121780"
FT /id="VAR_019939"
FT VARIANT 117
FT /note="G -> V (in dbSNP:rs17147793)"
FT /id="VAR_038806"
FT VARIANT 157
FT /note="N -> S (in dbSNP:rs41312157)"
FT /evidence="ECO:0000269|PubMed:15121780"
FT /id="VAR_019940"
FT VARIANT 179
FT /note="S -> N (found in a family with intellectual
FT disability; unknown pathological significance;
FT dbSNP:rs28933691)"
FT /evidence="ECO:0000269|PubMed:15121780"
FT /id="VAR_019941"
FT VARIANT 185
FT /note="S -> L (in dbSNP:rs186251256)"
FT /evidence="ECO:0000269|PubMed:15121780"
FT /id="VAR_019942"
FT VARIANT 213
FT /note="A -> E (in dbSNP:rs537825)"
FT /id="VAR_052765"
FT VARIANT 499
FT /note="I -> V (in dbSNP:rs182239885)"
FT /evidence="ECO:0000269|PubMed:15121780"
FT /id="VAR_019943"
SQ SEQUENCE 661 AA; 75960 MW; 6583905D2DB96975 CRC64;
MPANEDAPQP GEHGSACEVS VSFEDVTVDF SREEWQQLDS TQRRLYQDVM LENYSHLLSV
GFEVPKPEVI FKLEQGEGPW TLEGEAPHQS CSDGKFGIKP SQRRISGKST FHSEMEGEDT
RDDSLYSILE ELWQDAEQIK RCQEKHNKLL SRTTFLNKKI LNTEWDYEYK DFGKFVHPSP
NLILSQKRPH KRDSFGKSFK HNLDLHIHNK SNAAKNLDKT IGHGQVFTQN SSYSHHENTH
TGVKFCERNQ CGKVLSLKHS LSQNVKFPIG EKANTCTEFG KIFTQRSHFF APQKIHTVEK
PHELSKCVNV FTQKPLLSIY LRVHRDEKLY ICTKCGKAFI QNSELIMHEK THTREKPYKC
NECGKSFFQV SSLLRHQTTH TGEKLFECSE CGKGFSLNSA LNIHQKIHTG ERHHKCSECG
KAFTQKSTLR MHQRIHTGER SYICTQCGQA FIQKAHLIAH QRIHTGEKPY ECSDCGKSFP
SKSQLQMHKR IHTGEKPYIC TECGKAFTNR SNLNTHQKSH TGEKSYICAE CGKAFTDRSN
FNKHQTIHTG EKPYVCADCG RAFIQKSELI THQRIHTTEK PYKCPDCEKS FSKKPHLKVH
QRIHTGEKPY ICAECGKAFT DRSNFNKHQT IHTGDKPYKC SDCGKGFTQK SVLSMHRNIH
T
