ZN264_HUMAN
ID ZN264_HUMAN Reviewed; 627 AA.
AC O43296; A8K8Y9; Q9P1V0;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Zinc finger protein 264;
GN Name=ZNF264; Synonyms=KIAA0412;
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 MRNA].
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-343 AND TYR-511, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-425, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC O43296; Q8NHQ1: CEP70; NbExp=4; IntAct=EBI-4395808, EBI-739624;
CC O43296; Q92997: DVL3; NbExp=3; IntAct=EBI-4395808, EBI-739789;
CC O43296; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-4395808, EBI-5916454;
CC O43296; O15397: IPO8; NbExp=3; IntAct=EBI-4395808, EBI-358808;
CC O43296; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-4395808, EBI-12012928;
CC O43296; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-4395808, EBI-10172290;
CC O43296; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-4395808, EBI-10171774;
CC O43296; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-4395808, EBI-14065470;
CC O43296; P23508: MCC; NbExp=3; IntAct=EBI-4395808, EBI-307531;
CC O43296; Q99750: MDFI; NbExp=3; IntAct=EBI-4395808, EBI-724076;
CC O43296; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-4395808, EBI-79165;
CC O43296; Q8WV44: TRIM41; NbExp=4; IntAct=EBI-4395808, EBI-725997;
CC O43296; Q9Y473: ZNF175; NbExp=5; IntAct=EBI-4395808, EBI-3438881;
CC O43296; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-4395808, EBI-11035148;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Relatively highly expressed in kidney, thymus,
CC testis, ovary, brain, lung, placenta, and prostate, and relatively low
CC expression in heart, liver, skeletal muscle, pancreas, spleen, and
CC small intestine.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA24842.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB007872; BAA24842.2; ALT_INIT; mRNA.
DR EMBL; AK292504; BAF85193.1; -; mRNA.
DR EMBL; AC005261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025588; AAF42766.1; -; Genomic_DNA.
DR CCDS; CCDS33127.1; -.
DR RefSeq; NP_003408.1; NM_003417.4.
DR AlphaFoldDB; O43296; -.
DR SMR; O43296; -.
DR BioGRID; 114815; 41.
DR IntAct; O43296; 29.
DR STRING; 9606.ENSP00000263095; -.
DR iPTMnet; O43296; -.
DR PhosphoSitePlus; O43296; -.
DR BioMuta; ZNF264; -.
DR EPD; O43296; -.
DR jPOST; O43296; -.
DR MassIVE; O43296; -.
DR MaxQB; O43296; -.
DR PaxDb; O43296; -.
DR PeptideAtlas; O43296; -.
DR PRIDE; O43296; -.
DR ProteomicsDB; 48870; -.
DR Antibodypedia; 19635; 147 antibodies from 19 providers.
DR DNASU; 9422; -.
DR Ensembl; ENST00000263095.10; ENSP00000263095.5; ENSG00000083844.10.
DR Ensembl; ENST00000536056.1; ENSP00000440376.1; ENSG00000083844.10.
DR GeneID; 9422; -.
DR KEGG; hsa:9422; -.
DR MANE-Select; ENST00000263095.10; ENSP00000263095.5; NM_003417.5; NP_003408.1.
DR UCSC; uc002qob.3; human.
DR CTD; 9422; -.
DR DisGeNET; 9422; -.
DR GeneCards; ZNF264; -.
DR HGNC; HGNC:13057; ZNF264.
DR HPA; ENSG00000083844; Low tissue specificity.
DR MIM; 604668; gene.
DR neXtProt; NX_O43296; -.
DR OpenTargets; ENSG00000083844; -.
DR PharmGKB; PA37635; -.
DR VEuPathDB; HostDB:ENSG00000083844; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159953; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; O43296; -.
DR OMA; TSCEPTL; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O43296; -.
DR TreeFam; TF341817; -.
DR PathwayCommons; O43296; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; O43296; -.
DR BioGRID-ORCS; 9422; 8 hits in 1094 CRISPR screens.
DR ChiTaRS; ZNF264; human.
DR GeneWiki; ZNF264; -.
DR GenomeRNAi; 9422; -.
DR Pharos; O43296; Tdark.
DR PRO; PR:O43296; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O43296; protein.
DR Bgee; ENSG00000083844; Expressed in buccal mucosa cell and 188 other tissues.
DR ExpressionAtlas; O43296; baseline and differential.
DR Genevisible; O43296; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 11.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..627
FT /note="Zinc finger protein 264"
FT /id="PRO_0000047492"
FT DOMAIN 14..85
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 203..225
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 231..253
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 259..281
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 287..309
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 315..337
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 343..365
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 371..393
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 399..421
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 427..449
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 455..477
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 483..505
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 511..533
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 539..561
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 74..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 343
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 511
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT CROSSLNK 425
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 181
FT /note="R -> T (in dbSNP:rs2074858)"
FT /id="VAR_052803"
FT VARIANT 183
FT /note="R -> H (in dbSNP:rs917340)"
FT /id="VAR_052804"
SQ SEQUENCE 627 AA; 70587 MW; BF0A6460AD07CECB CRC64;
MAAAVLTDRA QVSVTFDDVA VTFTKEEWGQ LDLAQRTLYQ EVMLENCGLL VSLGCPVPKA
ELICHLEHGQ EPWTRKEDLS QDTCPGDKGK PKTTEPTTCE PALSEGISLQ GQVTQGNSVD
SQLGQAEDQD GLSEMQEGHF RPGIDPQEKS PGKMSPECDG LGTADGVCSR IGQEQVSPGD
RVRSHNSCES GKDPMIQEEE NNFKCSECGK VFNKKHLLAG HEKIHSGVKP YECTECGKTF
IKSTHLLQHH MIHTGERPYE CMECGKAFNR KSYLTQHQRI HSGEKPYKCN ECGKAFTHRS
NFVLHNRRHT GEKSFVCTEC GQVFRHRPGF LRHYVVHSGE NPYECLECGK VFKHRSYLMW
HQQTHTGEKP YECSECGKVF LESAALIHHY VIHTGEKPFE CLECGKAFNH RSYLKRHQRI
HTGEKPFVCS ECGKAFTHCS TFILHKRAHT GEKPFECKEC GKAFSNRKDL IRHFSIHTGE
KPYECVECGK AFTRMSGLTR HKRIHSGEKP YECVECGKSF CWSTNLIRHA IIHTGEKPYK
CSECGKAFSR SSSLTQHQRM HTGKNPISVT DVGRPFTSGQ TSVTLRELLL GKDFLNVTTE
ANILPEETSS SASDQPYQRE TPQVSSL
