ZN277_MOUSE
ID ZN277_MOUSE Reviewed; 583 AA.
AC E9Q6D6; Q3U0V6; Q3UM86; Q80UK2; Q8BVL5; Q8BVX7;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Zinc finger protein 277 {ECO:0000312|MGI:MGI:1890393};
GN Name=Znf277 {ECO:0000250|UniProtKB:Q9NRM2};
GN Synonyms=Zfp277 {ECO:0000312|MGI:MGI:1890393};
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|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:BAC36074.1, ECO:0000312|EMBL:BAC36784.1, ECO:0000312|EMBL:BAE26212.1, ECO:0000312|EMBL:BAE33745.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC36784.1}, and
RC NOD {ECO:0000312|EMBL:BAE33745.1};
RC TISSUE=Embryonic stem cell {ECO:0000312|EMBL:BAC36074.1},
RC Head {ECO:0000312|EMBL:BAC36784.1},
RC Mammary gland {ECO:0000312|EMBL:BAE26212.1}, and
RC Spleen {ECO:0000312|EMBL:BAE33745.1};
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 [2] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:AAH43453.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N-3 {ECO:0000312|EMBL:AAH43453.1};
RC TISSUE=Mammary cancer {ECO:0000312|EMBL:AAH43453.1};
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] {ECO:0000305}
RP FUNCTION, INTERACTION WITH BMI1, AND INDUCTION.
RX PubMed=20808772; DOI=10.1371/journal.pone.0012373;
RA Negishi M., Saraya A., Mochizuki S., Helin K., Koseki H., Iwama A.;
RT "A novel zinc finger protein Zfp277 mediates transcriptional repression of
RT the Ink4a/arf locus through polycomb repressive complex 1.";
RL PLoS ONE 5:e12373-e12373(2010).
CC -!- FUNCTION: Probable transcription factor (PubMed:20808772). Involved in
CC modulation of cellular senescence; represses transcription of the tumor
CC suppressor gene INK4A/ARF, perhaps acting via the Polycomb group (PcG)
CC complex PRC1 (PubMed:20808772). {ECO:0000269|PubMed:20808772}.
CC -!- SUBUNIT: Interacts (via zinc-finger domains) with RPS2/40S ribosomal
CC protein S2, perhaps as nascent RPS2 is synthesized during translation;
CC the interaction is direct; the interaction is extra-ribosomal.
CC Interaction with RPS2 competes with the binding of RPS2 to protein
CC arginine methyltransferase PRMT3 (By similarity). Interacts with
CC Polycomb group (PcG) complex protein BMI1 (PubMed:20808772). May be
CC part of a complex including at least ZNF277, BMI1 and RNF2/RING2
CC (PubMed:20808772). {ECO:0000250|UniProtKB:Q9NRM2,
CC ECO:0000269|PubMed:20808772}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NRM2}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9NRM2}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9NRM2}. Chromosome
CC {ECO:0000269|PubMed:20808772}. Note=Probably localized to nucleolus and
CC cytoplasm in complex with 40S ribosomal protein S2/RPS2.
CC {ECO:0000250|UniProtKB:Q9NRM2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=E9Q6D6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E9Q6D6-2; Sequence=VSP_061466;
CC -!- INDUCTION: Down-regulated by oxidative stress.
CC {ECO:0000269|PubMed:20808772}.
CC -!- SIMILARITY: Belongs to the ZNF277 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; BC043453; AAH43453.1; -; mRNA.
DR EMBL; AK075945; BAC36074.1; -; mRNA.
DR EMBL; AK077401; BAC36784.1; -; mRNA.
DR EMBL; AK145060; BAE26212.1; -; mRNA.
DR EMBL; AK156529; BAE33745.1; -; mRNA.
DR RefSeq; NP_766163.2; NM_172575.3.
DR RefSeq; NP_849173.2; NM_178845.3.
DR AlphaFoldDB; E9Q6D6; -.
DR SMR; E9Q6D6; -.
DR IntAct; E9Q6D6; 4.
DR STRING; 10090.ENSMUSP00000064226; -.
DR PhosphoSitePlus; E9Q6D6; -.
DR EPD; E9Q6D6; -.
DR MaxQB; E9Q6D6; -.
DR PaxDb; E9Q6D6; -.
DR PeptideAtlas; E9Q6D6; -.
DR PRIDE; E9Q6D6; -.
DR ProteomicsDB; 335213; -.
DR ProteomicsDB; 363643; -.
DR Antibodypedia; 17357; 108 antibodies from 23 providers.
DR DNASU; 246196; -.
DR Ensembl; ENSMUST00000069637; ENSMUSP00000068032; ENSMUSG00000055917. [E9Q6D6-2]
DR Ensembl; ENSMUST00000069692; ENSMUSP00000064226; ENSMUSG00000055917. [E9Q6D6-1]
DR GeneID; 246196; -.
DR KEGG; mmu:246196; -.
DR UCSC; uc007nla.2; mouse. [E9Q6D6-1]
DR CTD; 246196; -.
DR MGI; MGI:1890393; Zfp277.
DR VEuPathDB; HostDB:ENSMUSG00000055917; -.
DR eggNOG; KOG2482; Eukaryota.
DR GeneTree; ENSGT00390000010852; -.
DR HOGENOM; CLU_033436_0_0_1; -.
DR InParanoid; E9Q6D6; -.
DR OMA; HEFEQYC; -.
DR OrthoDB; 1498904at2759; -.
DR PhylomeDB; E9Q6D6; -.
DR TreeFam; TF318036; -.
DR BioGRID-ORCS; 246196; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Zfp277; mouse.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; E9Q6D6; protein.
DR Bgee; ENSMUSG00000055917; Expressed in primary oocyte and 253 other tissues.
DR ExpressionAtlas; E9Q6D6; baseline and differential.
DR Genevisible; E9Q6D6; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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; IDA:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:MGI.
DR GO; GO:2000772; P:regulation of cellular senescence; IMP:MGI.
DR InterPro; IPR041661; ZN622/Rei1/Reh1_Znf-C2H2.
DR InterPro; IPR040048; ZNF277.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR13267; PTHR13267; 1.
DR Pfam; PF12756; zf-C2H2_2; 2.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..583
FT /note="Zinc finger protein 277"
FT /id="PRO_0000455248"
FT ZN_FING 351..375
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 482..508
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT VAR_SEQ 32..157
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_061466"
FT CONFLICT 177
FT /note="T -> A (in Ref. 3; AAH43453 and 1; BAE26212)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="N -> K (in Ref. 1; BAC36074)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="A -> T (in Ref. 1; BAE26212)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="E -> K (in Ref. 1; BAC36784)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 583 AA; 67644 MW; 6F90ABF919E4C6AA CRC64;
MAASEVQGLP VDPREAGVRG VRGGIGHTDH EGHLGSFQLL ATINKAAMNI VEHVSFLPVG
TSSGYIAASS GITMSNFLRN RQTDFQSGCT SLQSHQQWRS VPLSPHPHQH LLSPEFLILA
ILTGVRWNLR IALICISLMI KDAEHFFRCF SAIWYSSDSK DCILEPLSLP ESPGGTTALE
GSPSVPCIFC EEHFPMAEQD KLLKHMIIEH KIVIADVKLV ADFRRYILYW RKRFTEQPIT
DFCSVIRINS TAPFEEQDNY YLLCDALPED RILREELQKH KLKEVLDQQQ RERNDTSFHG
VCMFCSEEFR GNRSVLLNHM AREHAFNIGL PDNIVNCAEF LCTLQKKLDN LQCLYCEKTF
RDKNTLKDHM RKKQHRRINP KNREYDRFYV INYLELGKSW EEVQSEDDRE LLDLQEDDWS
DWQEYPVSAV CLFCEKQEET IDKLYVHMKD THEFDLLRIK SELGLNFYQQ VKLVNFIRRQ
VHQCKCYSCH VKFKSKADLR THMEDTKHTS LLPDRKTWDQ LEYYFPTYEN DTLLCTLSDS
ESDLTAQEQT ENVPVISEDT SRLCALKQSS VLNQLLLQGC LEN
