ZN275_HUMAN
ID ZN275_HUMAN Reviewed; 429 AA.
AC Q9NSD4; A6NE92;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Zinc finger protein 275;
GN Name=ZNF275;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=10854409; DOI=10.1101/gr.10.6.758;
RA Mallon A.-M., Platzer M., Bate R., Gloeckner G., Botcherby M.R.M.,
RA Nordsiek G., Strivens M.A., Kioschis P., Dangel A., Cunningham D.,
RA Straw R.N.A., Weston P., Gilbert M., Fernando S., Goodall K., Hunter G.,
RA Greystrong J.S., Clarke D., Kimberley C., Goerdes M., Blechschmidt K.,
RA Rump A., Hinzmann B., Mundy C.R., Miller W., Poustka A., Herman G.E.,
RA Rhodes M., Denny P., Rosenthal A., Brown S.D.M.;
RT "Comparative genome sequence analysis of the Bpa/Str region in mouse and
RT man.";
RL Genome Res. 10:758-775(2000).
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., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q9NSD4; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-17263125, EBI-742750;
CC Q9NSD4; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-17263125, EBI-10172052;
CC Q9NSD4; Q9H9Z2: LIN28A; NbExp=3; IntAct=EBI-17263125, EBI-2462365;
CC Q9NSD4; P98175: RBM10; NbExp=3; IntAct=EBI-17263125, EBI-721525;
CC Q9NSD4; P78317: RNF4; NbExp=3; IntAct=EBI-17263125, EBI-2340927;
CC Q9NSD4; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-17263125, EBI-3650647;
CC Q9NSD4; Q8WV44: TRIM41; NbExp=6; IntAct=EBI-17263125, EBI-725997;
CC Q9NSD4; Q86UD4: ZNF329; NbExp=3; IntAct=EBI-17263125, EBI-7233259;
CC Q9NSD4; Q5T619: ZNF648; NbExp=3; IntAct=EBI-17263125, EBI-11985915;
CC Q9NSD4; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-17263125, EBI-10240849;
CC Q9NSD4; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-17263125, EBI-11962574;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NSD4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NSD4-2; Sequence=VSP_055944;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U82670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC152007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC152008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72883.1; -; Genomic_DNA.
DR EMBL; BC136634; AAI36635.1; -; mRNA.
DR AlphaFoldDB; Q9NSD4; -.
DR SMR; Q9NSD4; -.
DR BioGRID; 116051; 20.
DR IntAct; Q9NSD4; 12.
DR STRING; 9606.ENSP00000359271; -.
DR iPTMnet; Q9NSD4; -.
DR PhosphoSitePlus; Q9NSD4; -.
DR BioMuta; ZNF275; -.
DR DMDM; 308153531; -.
DR jPOST; Q9NSD4; -.
DR MassIVE; Q9NSD4; -.
DR MaxQB; Q9NSD4; -.
DR PaxDb; Q9NSD4; -.
DR PeptideAtlas; Q9NSD4; -.
DR PRIDE; Q9NSD4; -.
DR ProteomicsDB; 82534; -. [Q9NSD4-1]
DR ProteomicsDB; 969; -.
DR Antibodypedia; 407; 76 antibodies from 13 providers.
DR Ensembl; ENST00000370249.3; ENSP00000359269.2; ENSG00000063587.15. [Q9NSD4-2]
DR Ensembl; ENST00000650114.2; ENSP00000496975.2; ENSG00000063587.15. [Q9NSD4-1]
DR MANE-Select; ENST00000650114.2; ENSP00000496975.2; NM_001367757.1; NP_001354686.1.
DR UCSC; uc065bsr.1; human. [Q9NSD4-1]
DR GeneCards; ZNF275; -.
DR HGNC; HGNC:13069; ZNF275.
DR HPA; ENSG00000063587; Tissue enhanced (adrenal).
DR neXtProt; NX_Q9NSD4; -.
DR OpenTargets; ENSG00000063587; -.
DR VEuPathDB; HostDB:ENSG00000063587; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000153582; -.
DR HOGENOM; CLU_002678_93_1_1; -.
DR InParanoid; Q9NSD4; -.
DR OMA; MPFECEE; -.
DR PhylomeDB; Q9NSD4; -.
DR PathwayCommons; Q9NSD4; -.
DR SignaLink; Q9NSD4; -.
DR ChiTaRS; ZNF275; human.
DR Pharos; Q9NSD4; Tdark.
DR PRO; PR:Q9NSD4; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9NSD4; protein.
DR Bgee; ENSG00000063587; Expressed in adrenal cortex and 184 other tissues.
DR ExpressionAtlas; Q9NSD4; baseline and differential.
DR Genevisible; Q9NSD4; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 9.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..429
FT /note="Zinc finger protein 275"
FT /id="PRO_0000047502"
FT ZN_FING 101..123
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 129..151
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 181..203
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 209..231
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 237..259
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 265..287
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 293..315
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 321..343
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 349..371
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 377..399
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 405..427
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 31..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055944"
SQ SEQUENCE 429 AA; 48443 MW; 85601FAC3129FB3A CRC64;
MMSHPCVSLL GVPVLNPALV PHLAQGQVLL VSDPSPNTDP AKYSESTSAT RHQMKGEDAQ
PQEMASTSFP RASGPSPEFR QHGDSDGKRG SPQNLPIEHH FACKECGDTF RLKVLLVQHQ
RVHSEEKGWE CGDCGKVFRG VAEFNEHRKS HVAAEPQPGP SRALENAAEK REQMEREAKP
FECEECGKRF KKNAGLSQHL RVHSREKPFD CEECGRSFKV NTHLFRHQKL HTSEKPFACK
ACSRDFLDRQ ELLKHQRMHT GHLPFDCDDC GKSFRGVNGL AEHQRIHSGA KPYGCPHCGK
LFRRSSELTK HRRIHTGEKP YACGQCGKAF RQSSSLLEHA RIHSGERPYA CGECGKAFRG
PSDLIKHRRI HSGLKPYECD KCGKAFRRSS GLSRHRRIHS GARRCECSQC GRVFKRRSAL
QKHQPTHHE
