GenomeNet

Database: UniProt
Entry: P51508
LinkDB: P51508
Original site: P51508 
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   25-OCT-2017, entry version 156.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-3; SER-157; ASN-179; LEU-185
RP   AND 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.,
RA   Kalscheuer V.M., Chelly J., Moraine C., Ropers H.-H., Fryns J.-P.,
RA   Janssen I.M., Sistermans E.A., Nillesen W.N., de Vries L.B.A.,
RA   Hamel B.C.J., 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.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   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.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   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.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   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.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   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.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., 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.,
RA   Ballabio A., 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
RP   MASS 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-
RT   modification 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
CC       a severe mental retardation 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}.
DR   EMBL; AY487248; AAS17752.1; -; mRNA.
DR   EMBL; AL591394; CAI39462.1; -; Genomic_DNA.
DR   EMBL; AL022578; CAI39462.1; JOINED; Genomic_DNA.
DR   EMBL; Z98304; CAI39462.1; JOINED; Genomic_DNA.
DR   EMBL; AL022578; CAI42739.1; -; Genomic_DNA.
DR   EMBL; AL591394; CAI42739.1; JOINED; Genomic_DNA.
DR   EMBL; Z98304; CAI42739.1; JOINED; Genomic_DNA.
DR   EMBL; Z98304; CAI42943.1; -; Genomic_DNA.
DR   EMBL; AL022578; CAI42943.1; JOINED; Genomic_DNA.
DR   EMBL; AL591394; CAI42943.1; JOINED; 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   UniGene; Hs.114246; -.
DR   UniGene; Hs.710432; -.
DR   ProteinModelPortal; P51508; -.
DR   SMR; P51508; -.
DR   BioGrid; 131424; 1.
DR   STRING; 9606.ENSP00000341151; -.
DR   iPTMnet; P51508; -.
DR   PhosphoSitePlus; P51508; -.
DR   BioMuta; ZNF81; -.
DR   DMDM; 55977803; -.
DR   MaxQB; P51508; -.
DR   PaxDb; P51508; -.
DR   PeptideAtlas; P51508; -.
DR   PRIDE; P51508; -.
DR   DNASU; 347344; -.
DR   Ensembl; ENST00000338637; ENSP00000341151; ENSG00000197779.
DR   Ensembl; ENST00000376954; ENSP00000366153; ENSG00000197779.
DR   GeneID; 347344; -.
DR   KEGG; hsa:347344; -.
DR   UCSC; uc010nhy.3; human.
DR   CTD; 347344; -.
DR   DisGeNET; 347344; -.
DR   EuPathDB; HostDB:ENSG00000197779.13; -.
DR   GeneCards; ZNF81; -.
DR   HGNC; HGNC:13156; ZNF81.
DR   HPA; HPA001689; -.
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   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00880000137993; -.
DR   HOGENOM; HOG000234617; -.
DR   HOVERGEN; HBG018163; -.
DR   InParanoid; P51508; -.
DR   KO; K09228; -.
DR   OMA; KILNTEW; -.
DR   OrthoDB; EOG091G02KC; -.
DR   PhylomeDB; P51508; -.
DR   TreeFam; TF350810; -.
DR   ChiTaRS; ZNF81; human.
DR   GenomeRNAi; 347344; -.
DR   PRO; PR:P51508; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   Bgee; ENSG00000197779; -.
DR   CleanEx; HS_ZNF81; -.
DR   ExpressionAtlas; P51508; baseline and differential.
DR   Genevisible; P51508; HS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   Gene3D; 2.40.155.10; -; 2.
DR   Gene3D; 3.30.40.10; -; 4.
DR   InterPro; IPR009017; GFP.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF01352; KRAB; 1.
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; Complete proteome; DNA-binding;
KW   Isopeptide bond; Metal-binding; Nucleus; Polymorphism;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1    661       Zinc finger protein 81.
FT                                /FTId=PRO_0000047395.
FT   DOMAIN       21     92       KRAB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00119}.
FT   ZN_FING     330    352       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     358    380       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     386    408       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     414    436       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     442    464       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     470    492       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     498    520       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     526    548       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     554    576       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     582    604       C2H2-type 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     610    632       C2H2-type 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     638    660       C2H2-type 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   CROSSLNK    266    266       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   VARIANT       3      3       A -> V (in dbSNP:rs183846665).
FT                                {ECO:0000269|PubMed:15121780}.
FT                                /FTId=VAR_019939.
FT   VARIANT     117    117       G -> V (in dbSNP:rs17147793).
FT                                /FTId=VAR_038806.
FT   VARIANT     157    157       N -> S (in dbSNP:rs41312157).
FT                                {ECO:0000269|PubMed:15121780}.
FT                                /FTId=VAR_019940.
FT   VARIANT     179    179       S -> N (found in a family with mental
FT                                retardation; unknown pathological
FT                                significance; dbSNP:rs28933691).
FT                                {ECO:0000269|PubMed:15121780}.
FT                                /FTId=VAR_019941.
FT   VARIANT     185    185       S -> L (in dbSNP:rs186251256).
FT                                {ECO:0000269|PubMed:15121780}.
FT                                /FTId=VAR_019942.
FT   VARIANT     213    213       A -> E (in dbSNP:rs537825).
FT                                /FTId=VAR_052765.
FT   VARIANT     499    499       I -> V (in dbSNP:rs182239885).
FT                                {ECO:0000269|PubMed:15121780}.
FT                                /FTId=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
//
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