YAF2_MOUSE
ID YAF2_MOUSE Reviewed; 179 AA.
AC Q99LW6; Q3UFD4; Q9DBE4;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=YY1-associated factor 2;
GN Name=Yaf2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:AAH02192.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH RNF2.
RC TISSUE=Brain {ECO:0000312|EMBL:BAC97817.1};
RX PubMed=14557078; DOI=10.1016/s0378-1119(03)00800-x;
RA Kaneko T., Miyagishima H., Hasegawa T., Mizutani-Koseki Y., Isono K.,
RA Koseki H.;
RT "The mouse YAF2 gene generates two distinct transcripts and is expressed in
RT pre- and postimplantation embryos.";
RL Gene 315:183-192(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Liver, and Sympathetic ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland {ECO:0000269|PubMed:15489334};
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Binds to MYC and inhibits MYC-mediated transactivation. Also
CC binds to MYCN and enhances MYCN-dependent transcriptional activation.
CC Increases calpain 2-mediated proteolysis of YY1 in vitro. Component of
CC the E2F6.com-1 complex, a repressive complex that methylates 'Lys-9' of
CC histone H3, suggesting that it is involved in chromatin-remodeling.
CC -!- SUBUNIT: Interacts with MYC, MYCN, RNF2/RING1B and YY1. Part of the
CC E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3,
CC BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2.
CC {ECO:0000269|PubMed:14557078}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14557078}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:14557078}; Synonyms=YAF2-a
CC {ECO:0000269|PubMed:14557078};
CC IsoId=Q99LW6-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:14557078}; Synonyms=YAF2-b
CC {ECO:0000269|PubMed:14557078};
CC IsoId=Q99LW6-2; Sequence=VSP_050619, VSP_050620;
CC -!- TISSUE SPECIFICITY: In the mesoderm, expressed in the region close to
CC the surface ectoderm. {ECO:0000269|PubMed:14557078}.
CC -!- DEVELOPMENTAL STAGE: Expressed in both pre- and post-implantation
CC embryos. {ECO:0000269|PubMed:14557078}.
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DR EMBL; AB100452; BAC97817.1; -; mRNA.
DR EMBL; AB100453; BAC97818.1; -; mRNA.
DR EMBL; AK005008; BAB23741.1; -; mRNA.
DR EMBL; AK148634; BAE28627.1; -; mRNA.
DR EMBL; BC002192; AAH02192.1; -; mRNA.
DR CCDS; CCDS27765.1; -. [Q99LW6-1]
DR RefSeq; NP_077151.3; NM_024189.6. [Q99LW6-1]
DR AlphaFoldDB; Q99LW6; -.
DR SMR; Q99LW6; -.
DR BioGRID; 211908; 2.
DR IntAct; Q99LW6; 3.
DR STRING; 10090.ENSMUSP00000079179; -.
DR iPTMnet; Q99LW6; -.
DR PhosphoSitePlus; Q99LW6; -.
DR EPD; Q99LW6; -.
DR MaxQB; Q99LW6; -.
DR PaxDb; Q99LW6; -.
DR PeptideAtlas; Q99LW6; -.
DR PRIDE; Q99LW6; -.
DR ProteomicsDB; 299614; -. [Q99LW6-1]
DR ProteomicsDB; 299615; -. [Q99LW6-2]
DR Antibodypedia; 13166; 158 antibodies from 26 providers.
DR DNASU; 67057; -.
DR Ensembl; ENSMUST00000080299; ENSMUSP00000079179; ENSMUSG00000022634. [Q99LW6-1]
DR Ensembl; ENSMUST00000133736; ENSMUSP00000155669; ENSMUSG00000022634. [Q99LW6-2]
DR GeneID; 67057; -.
DR KEGG; mmu:67057; -.
DR UCSC; uc007xis.2; mouse. [Q99LW6-1]
DR CTD; 10138; -.
DR MGI; MGI:1914307; Yaf2.
DR VEuPathDB; HostDB:ENSMUSG00000022634; -.
DR eggNOG; KOG4477; Eukaryota.
DR GeneTree; ENSGT00390000013995; -.
DR HOGENOM; CLU_095374_0_1_1; -.
DR InParanoid; Q99LW6; -.
DR OMA; VCTFRNG; -.
DR OrthoDB; 1634090at2759; -.
DR PhylomeDB; Q99LW6; -.
DR TreeFam; TF350501; -.
DR Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
DR BioGRID-ORCS; 67057; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Yaf2; mouse.
DR PRO; PR:Q99LW6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q99LW6; protein.
DR Bgee; ENSMUSG00000022634; Expressed in CA1 field of hippocampus and 274 other tissues.
DR Genevisible; Q99LW6; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR039958; RYBP/YAF2.
DR InterPro; IPR038039; YAF2.
DR InterPro; IPR033774; YAF2_RYBP.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR12920; PTHR12920; 1.
DR PANTHER; PTHR12920:SF2; PTHR12920:SF2; 1.
DR Pfam; PF17219; YAF2_RYBP; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..179
FT /note="YY1-associated factor 2"
FT /id="PRO_0000066114"
FT ZN_FING 19..48
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 52..68
FT /note="KPRPVSQLVAQQVTQQF -> STFSEAIANALRTKGPL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14557078"
FT /id="VSP_050619"
FT VAR_SEQ 69..179
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14557078"
FT /id="VSP_050620"
FT CONFLICT 98
FT /note="H -> S (in Ref. 2; BAB23741)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="N -> Y (in Ref. 2; BAB23741)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="S -> F (in Ref. 2; BAB23741)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 179 AA; 19655 MW; 7DDB7B7F171CB547 CRC64;
MGDKKSPTRP KRQPKPASDE GYWDCSVCTF RNSAEAFKCM MCDVRKGTST RKPRPVSQLV
AQQVTQQFVP PTQSKKEKKD RVEKDKSEKE AASKKNCHKK TRPRLKNVDR SSAQHLEVTV
GDLTVIITDF KEKAKSAPAS SAAGDQHSQG SCSSDSTERG VSRSSSPRGE ASSLNGESH
