ZN277_HUMAN
ID ZN277_HUMAN Reviewed; 450 AA.
AC Q9NRM2; Q75MZ2; Q75MZ3; Q8WY14;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Zinc finger protein 277;
DE AltName: Full=Nuclear receptor-interacting factor 4;
GN Name=ZNF277; Synonyms=NRIF4, ZNF277P;
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].
RX PubMed=10860669; DOI=10.1006/geno.2000.6198;
RA Liang H., Guo W., Nagarajan L.;
RT "Chromosomal mapping and genomic organization of an evolutionarily
RT conserved zinc finger gene ZNF277.";
RL Genomics 66:226-228(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li D., Desai-Yajnik V., Samuels H.H.;
RT "The putative nuclear receptor coregulator NRIF4.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [6]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-332 AND PHE-445.
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).
RN [7]
RP INTERACTION WITH RPS2, AND MUTAGENESIS OF 175-CYS--HIS-197;
RP 226-CYS--HIS-248; 304-CYS--HIS-325 AND 359-CYS--HIS-381.
RX PubMed=30530495; DOI=10.1074/jbc.ra118.004928;
RA Dionne K.L., Bergeron D., Landry-Voyer A.M., Bachand F.;
RT "The 40S ribosomal protein uS5 (RPS2) assembles into an extraribosomal
RT complex with human ZNF277 that competes with the PRMT3-uS5 interaction.";
RL J. Biol. Chem. 294:1944-1955(2019).
CC -!- FUNCTION: Probable transcription factor. Involved in modulation of
CC cellular senescence; represses transcription of the tumor suppressor
CC gene INK4A/ARF, perhaps acting via the Polycomb group (PcG) complex
CC PRC1. {ECO:0000250|UniProtKB:E9Q6D6}.
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 (PubMed:30530495). Interaction with RPS2 competes with the binding of
CC RPS2 to protein arginine methyltransferase PRMT3 (PubMed:30530495).
CC Interacts with Polycomb group (PcG) complex protein BMI1 (By
CC similarity). May be part of a complex including at least ZNF277, BMI1
CC and RNF2/RING2 (By similarity). {ECO:0000250|UniProtKB:E9Q6D6,
CC ECO:0000269|PubMed:30530495}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- INDUCTION: Down-regulated by oxidative stress.
CC {ECO:0000250|UniProtKB:E9Q6D6}.
CC -!- SIMILARITY: Belongs to the ZNF277 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF85941.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS07413.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF209198; AAF85941.1; ALT_INIT; mRNA.
DR EMBL; AF308819; AAL55819.1; -; mRNA.
DR EMBL; AC004112; AAS07407.1; -; Genomic_DNA.
DR EMBL; AC004111; AAS07413.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH471070; EAW83461.1; -; Genomic_DNA.
DR CCDS; CCDS5755.2; -.
DR RefSeq; NP_068834.2; NM_021994.2.
DR AlphaFoldDB; Q9NRM2; -.
DR SMR; Q9NRM2; -.
DR BioGRID; 116349; 29.
DR IntAct; Q9NRM2; 23.
DR STRING; 9606.ENSP00000354501; -.
DR iPTMnet; Q9NRM2; -.
DR PhosphoSitePlus; Q9NRM2; -.
DR BioMuta; ZNF277; -.
DR DMDM; 251757417; -.
DR EPD; Q9NRM2; -.
DR jPOST; Q9NRM2; -.
DR MassIVE; Q9NRM2; -.
DR MaxQB; Q9NRM2; -.
DR PaxDb; Q9NRM2; -.
DR PeptideAtlas; Q9NRM2; -.
DR PRIDE; Q9NRM2; -.
DR ProteomicsDB; 82389; -.
DR Antibodypedia; 17357; 108 antibodies from 23 providers.
DR DNASU; 11179; -.
DR Ensembl; ENST00000361822.8; ENSP00000354501.3; ENSG00000198839.10.
DR GeneID; 11179; -.
DR KEGG; hsa:11179; -.
DR MANE-Select; ENST00000361822.8; ENSP00000354501.3; NM_021994.3; NP_068834.2.
DR UCSC; uc003vge.3; human.
DR CTD; 11179; -.
DR DisGeNET; 11179; -.
DR GeneCards; ZNF277; -.
DR HGNC; HGNC:13070; ZNF277.
DR HPA; ENSG00000198839; Low tissue specificity.
DR MIM; 605465; gene.
DR neXtProt; NX_Q9NRM2; -.
DR OpenTargets; ENSG00000198839; -.
DR PharmGKB; PA37646; -.
DR VEuPathDB; HostDB:ENSG00000198839; -.
DR eggNOG; KOG2482; Eukaryota.
DR GeneTree; ENSGT00390000010852; -.
DR HOGENOM; CLU_033436_0_0_1; -.
DR InParanoid; Q9NRM2; -.
DR OMA; HEFEQYC; -.
DR OrthoDB; 1498904at2759; -.
DR PhylomeDB; Q9NRM2; -.
DR TreeFam; TF318036; -.
DR PathwayCommons; Q9NRM2; -.
DR SignaLink; Q9NRM2; -.
DR BioGRID-ORCS; 11179; 9 hits in 1089 CRISPR screens.
DR ChiTaRS; ZNF277; human.
DR GeneWiki; ZNF277P; -.
DR GenomeRNAi; 11179; -.
DR Pharos; Q9NRM2; Tbio.
DR PRO; PR:Q9NRM2; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9NRM2; protein.
DR Bgee; ENSG00000198839; Expressed in calcaneal tendon and 193 other tissues.
DR ExpressionAtlas; Q9NRM2; baseline and differential.
DR Genevisible; Q9NRM2; HS.
DR GO; GO:0005634; C:nucleus; 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; IEA:Ensembl.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:2000772; P:regulation of cellular senescence; IEA:Ensembl.
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; 3.
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 Acetylation; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..450
FT /note="Zinc finger protein 277"
FT /id="PRO_0000047503"
FT ZN_FING 224..248
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 355..381
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VARIANT 174
FT /note="V -> I (in dbSNP:rs34571830)"
FT /id="VAR_059908"
FT VARIANT 332
FT /note="I -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035574"
FT VARIANT 364
FT /note="V -> M (in dbSNP:rs11539696)"
FT /id="VAR_057415"
FT VARIANT 445
FT /note="L -> F (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035575"
FT MUTAGEN 175..197
FT /note="CMFCNEEFLGNRSVILNHMAREH->SMFCNEEFLGNRSVILNHMAREA:
FT Modest reduction in binding to RPS2."
FT /evidence="ECO:0000269|PubMed:30530495"
FT MUTAGEN 226..248
FT /note="CLYCEKTFRDKNTLKDHMRKKQH->SLYCEKTFRDKNTLKDHMRKKQA:
FT Modest reduction in binding to RPS2."
FT /evidence="ECO:0000269|PubMed:30530495"
FT MUTAGEN 304..325
FT /note="CLFCEKQAETIEKLYVHMEDAH->SLFCEKQAETIEKLYVHMEDAA:
FT Drastic reduction in binding to RPS2."
FT /evidence="ECO:0000269|PubMed:30530495"
FT MUTAGEN 359..381
FT /note="CYGCHVKFKSKADLRTHMEETKH->SYGCHVKFKSKADLRTHMEETKA:
FT Modest reduction in binding to RPS2."
FT /evidence="ECO:0000269|PubMed:30530495"
SQ SEQUENCE 450 AA; 52788 MW; 07A35E08BB6E9521 CRC64;
MAASKTQGAV ARMQEDRDGS CSTVGGVGYG DSKDCILEPL SLPESPGGTT TLEGSPSVPC
IFCEEHFPVA EQDKLLKHMI IEHKIVIADV KLVADFQRYI LYWRKRFTEQ PITDFCSVIR
INSTAPFEEQ ENYFLLCDVL PEDRILREEL QKQRLREILE QQQQERNDTN FHGVCMFCNE
EFLGNRSVIL NHMAREHAFN IGLPDNIVNC NEFLCTLQKK LDNLQCLYCE KTFRDKNTLK
DHMRKKQHRK INPKNREYDR FYVINYLELG KSWEEVQLED DRELLDHQED DWSDWEEHPA
SAVCLFCEKQ AETIEKLYVH MEDAHEFDLL KIKSELGLNF YQQVKLVNFI RRQVHQCRCY
GCHVKFKSKA DLRTHMEETK HTSLLPDRKT WDQLEYYFPT YENDTLLCTL SDSESDLTAQ
EQNENVPIIS EDTSKLYALK QSSILNQLLL
