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Database: UniProt
Entry: O15391
LinkDB: O15391
Original site: O15391 
ID   TYY2_HUMAN              Reviewed;         372 AA.
AC   O15391; B2RP10; Q6Q1S4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   24-JAN-2024, entry version 179.
DE   RecName: Full=Transcription factor YY2;
DE   AltName: Full=Yin and yang 2;
DE            Short=YY-2;
DE   AltName: Full=Zinc finger protein 631;
GN   Name=YY2; Synonyms=ZNF631;
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=15087442; DOI=10.1074/jbc.m402525200;
RA   Nguyen N., Zhang X., Olashaw N., Seto E.;
RT   "Molecular cloning and functional characterization of the transcription
RT   factor YY2.";
RL   J. Biol. Chem. 279:25927-25934(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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].
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   [4]
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   [5]
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=16260628; DOI=10.1128/mcb.25.22.10159-10170.2005;
RA   Klar M., Bode J.;
RT   "Enhanceosome formation over the beta interferon promoter underlies a
RT   remote-control mechanism mediated by YY1 and YY2.";
RL   Mol. Cell. Biol. 25:10159-10170(2005).
RN   [7]
RP   IDENTIFICATION.
RX   PubMed=16377127; DOI=10.1016/j.ygeno.2005.11.001;
RA   Luo C., Lu X., Stubbs L., Kim J.;
RT   "Rapid evolution of a recently retroposed transcription factor YY2 in
RT   mammalian genomes.";
RL   Genomics 87:348-355(2006).
RN   [8]
RP   VARIANT [LARGE SCALE ANALYSIS] ASN-103.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Functions as a multifunctional transcription factor that may
CC       exhibit positive and negative control on a large number of genes. May
CC       antagonize YY1 and function in development and differentiation.
CC       {ECO:0000269|PubMed:16260628}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in kidney, liver, spleen and testis but
CC       not in colon. {ECO:0000269|PubMed:15087442}.
CC   -!- MISCELLANEOUS: The gene encoding this protein appears to have arisen by
CC       retrotransposition of the YY1 gene in placental mammals. It is encoded
CC       by a single exon found in an intron of the gene MBTPS2.
CC   -!- SIMILARITY: Belongs to the YY transcription factor family.
CC       {ECO:0000305}.
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DR   EMBL; AY567472; AAS68634.1; -; mRNA.
DR   EMBL; AK091850; BAG52427.1; -; mRNA.
DR   EMBL; U73479; AAD08633.1; -; Genomic_DNA.
DR   EMBL; CH471074; EAW98983.1; -; Genomic_DNA.
DR   EMBL; BC137215; AAI37216.1; -; mRNA.
DR   EMBL; BC137217; AAI37218.1; -; mRNA.
DR   CCDS; CCDS14202.1; -.
DR   RefSeq; NP_996806.2; NM_206923.3.
DR   AlphaFoldDB; O15391; -.
DR   SMR; O15391; -.
DR   BioGRID; 135656; 11.
DR   IntAct; O15391; 7.
DR   MINT; O15391; -.
DR   STRING; 9606.ENSP00000389381; -.
DR   iPTMnet; O15391; -.
DR   PhosphoSitePlus; O15391; -.
DR   BioMuta; YY2; -.
DR   EPD; O15391; -.
DR   jPOST; O15391; -.
DR   MassIVE; O15391; -.
DR   MaxQB; O15391; -.
DR   PaxDb; 9606-ENSP00000389381; -.
DR   PeptideAtlas; O15391; -.
DR   ProteomicsDB; 48626; -.
DR   Pumba; O15391; -.
DR   Antibodypedia; 58542; 91 antibodies from 16 providers.
DR   DNASU; 404281; -.
DR   Ensembl; ENST00000429584.3; ENSP00000389381.2; ENSG00000230797.3.
DR   GeneID; 404281; -.
DR   KEGG; hsa:404281; -.
DR   MANE-Select; ENST00000429584.3; ENSP00000389381.2; NM_206923.4; NP_996806.2.
DR   UCSC; uc011mjp.2; human.
DR   AGR; HGNC:31684; -.
DR   CTD; 404281; -.
DR   DisGeNET; 404281; -.
DR   GeneCards; YY2; -.
DR   HGNC; HGNC:31684; YY2.
DR   HPA; ENSG00000230797; Tissue enhanced (testis).
DR   MIM; 300570; gene.
DR   neXtProt; NX_O15391; -.
DR   OpenTargets; ENSG00000230797; -.
DR   PharmGKB; PA134976542; -.
DR   VEuPathDB; HostDB:ENSG00000230797; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000167584; -.
DR   HOGENOM; CLU_002678_42_2_1; -.
DR   InParanoid; O15391; -.
DR   OMA; WVHGGHH; -.
DR   OrthoDB; 47408at2759; -.
DR   PhylomeDB; O15391; -.
DR   TreeFam; TF106493; -.
DR   PathwayCommons; O15391; -.
DR   SignaLink; O15391; -.
DR   SIGNOR; O15391; -.
DR   BioGRID-ORCS; 404281; 12 hits in 800 CRISPR screens.
DR   GenomeRNAi; 404281; -.
DR   Pharos; O15391; Tbio.
DR   PRO; PR:O15391; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; O15391; Protein.
DR   Bgee; ENSG00000230797; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 98 other cell types or tissues.
DR   Genevisible; O15391; HS.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0031519; C:PcG protein complex; IBA:GO_Central.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 4.
DR   InterPro; IPR017114; YY1-like.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR14003:SF17; TRANSCRIPTION FACTOR YY2; 1.
DR   PANTHER; PTHR14003; TRANSCRIPTIONAL REPRESSOR PROTEIN YY; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   PIRSF; PIRSF037113; TF_Yin_yang; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..372
FT                   /note="Transcription factor YY2"
FT                   /id="PRO_0000323760"
FT   ZN_FING         254..278
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         283..305
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         311..335
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         341..365
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          32..102
FT                   /note="Mediates transcriptional activation"
FT   REGION          126..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          186..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..372
FT                   /note="Mediates transcriptional repression"
FT   COMPBIAS        186..200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         103
FT                   /note="D -> N (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs147081325)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_039586"
FT   CONFLICT        9
FT                   /note="I -> T (in Ref. 1; AAS68634)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        144
FT                   /note="K -> R (in Ref. 1; AAS68634)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   372 AA;  41347 MW;  5AEAB49C09CE6FF3 CRC64;
     MASNEDFSIT QDLEIPADIV ELHDINVEPL PMEDIPTESV QYEDVDGNWI YGGHNHPPLM
     VLQPLFTNTG YGDHDQEMLM LQTQEEVVGY CDSDNQLGND LEDQLALPDS IEDEHFQMTL
     ASLSASAAST STSTQSRSKK PSKKPSGKSA TSTEANPAGS SSSLGTRKWE QKQMQVKTLE
     GEFSVTMWSP NDNNDQGAVG EGQAENPPDY SEYLKGKKLP PGGLPGIDLS DPKQLAEFTK
     VKPKRSKGEP PKTVPCSYSG CEKMFRDYAA MRKHLHIHGP RVHVCAECGK AFLESSKLRR
     HQLVHTGEKP FQCTFEGCGK RFSLDFNLRT HLRIHTGDKP FVCPFDVCNR KFAQSTNLKT
     HILTHVKTKN NP
//
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