ZN350_HUMAN
ID ZN350_HUMAN Reviewed; 532 AA.
AC Q9GZX5; Q96G73; Q9HAQ4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Zinc finger protein 350;
DE AltName: Full=KRAB zinc finger protein ZFQR;
DE AltName: Full=Zinc finger and BRCA1-interacting protein with a KRAB domain 1;
DE AltName: Full=Zinc finger protein ZBRK1;
GN Name=ZNF350; Synonyms=ZBRK1;
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], VARIANTS PRO-66 AND SER-501, FUNCTION, AND
RP INTERACTION WITH BRCA1.
RX PubMed=11090615; DOI=10.1016/s1097-2765(00)00075-7;
RA Zheng L., Pan H., Li S., Flesken-Nikitin A., Chen L.P., Boyer G.T.,
RA Lee H.W.;
RT "Sequence-specific transcriptional corepressor function for BRCA1 through a
RT novel zinc finger protein, ZBRK1.";
RL Mol. Cell 6:757-768(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-524, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11161714; DOI=10.1006/excr.2000.5068;
RA Ran Q., Wadhwa R., Bischof O., Venable S., Smith J.R., Pereira-Smith O.M.;
RT "Characterization of a novel zinc finger gene with increased expression in
RT nondividing normal human cells.";
RL Exp. Cell Res. 263:156-162(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PRO-66 AND SER-501.
RC TISSUE=Placenta;
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=23665872; DOI=10.1007/s00018-013-1359-4;
RA Wang W., Cai J., Wu Y., Hu L., Chen Z., Hu J., Chen Z., Li W., Guo M.,
RA Huang Z.;
RT "Novel activity of KRAB domain that functions to reinforce nuclear
RT localization of KRAB-containing zinc finger proteins by interacting with
RT KAP1.";
RL Cell. Mol. Life Sci. 70:3947-3958(2013).
RN [8]
RP VARIANTS PRO-66; PRO-472; SER-501 AND ILE-524.
RX PubMed=12872252; DOI=10.1002/humu.10238;
RA Rutter J.L., Smith A.M., Davila M.R., Sigurdson A.J., Giusti R.M.,
RA Pineda M.A., Doody M.M., Tucker M.A., Greene M.H., Zhang J.,
RA Struewing J.P.;
RT "Mutational analysis of the BRCA1-interacting genes ZNF350/ZBRK1 and
RT BRIP1/BACH1 among BRCA1 and BRCA2-negative probands from breast-ovarian
RT cancer families and among early-onset breast cancer cases and reference
RT individuals.";
RL Hum. Mutat. 22:121-128(2003).
RN [9]
RP INTERACTION WITH RNF11.
RX PubMed=14755250; DOI=10.1038/sj.onc.1207319;
RA Li H., Seth A.K.;
RT "An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein.";
RL Oncogene 23:1801-1808(2004).
CC -!- FUNCTION: Transcriptional repressor. Binds to a specific sequence, 5'-
CC GGGxxxCAGxxxTTT-3', within GADD45 intron 3.
CC {ECO:0000269|PubMed:11090615}.
CC -!- SUBUNIT: Interacts with BRCA1. Interacts with RNF11.
CC {ECO:0000269|PubMed:11090615, ECO:0000269|PubMed:14755250}.
CC -!- INTERACTION:
CC Q9GZX5; P38398: BRCA1; NbExp=3; IntAct=EBI-396421, EBI-349905;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus matrix. Note=Associated with the
CC nuclear matrix.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11161714}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF295096; AAG17439.1; -; mRNA.
DR EMBL; AF309561; AAG25714.1; -; mRNA.
DR EMBL; AK023467; BAB14583.1; -; mRNA.
DR EMBL; AC011460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW72056.1; -; Genomic_DNA.
DR EMBL; BC009921; AAH09921.1; -; mRNA.
DR CCDS; CCDS12845.1; -.
DR RefSeq; NP_067645.3; NM_021632.3.
DR RefSeq; XP_016882587.1; XM_017027098.1.
DR RefSeq; XP_016882588.1; XM_017027099.1.
DR RefSeq; XP_016882589.1; XM_017027100.1.
DR AlphaFoldDB; Q9GZX5; -.
DR SMR; Q9GZX5; -.
DR BioGRID; 121889; 21.
DR CORUM; Q9GZX5; -.
DR IntAct; Q9GZX5; 8.
DR MINT; Q9GZX5; -.
DR STRING; 9606.ENSP00000243644; -.
DR iPTMnet; Q9GZX5; -.
DR PhosphoSitePlus; Q9GZX5; -.
DR BioMuta; ZNF350; -.
DR DMDM; 313104255; -.
DR EPD; Q9GZX5; -.
DR jPOST; Q9GZX5; -.
DR MassIVE; Q9GZX5; -.
DR MaxQB; Q9GZX5; -.
DR PaxDb; Q9GZX5; -.
DR PeptideAtlas; Q9GZX5; -.
DR PRIDE; Q9GZX5; -.
DR ProteomicsDB; 80166; -.
DR Antibodypedia; 49600; 206 antibodies from 25 providers.
DR DNASU; 59348; -.
DR Ensembl; ENST00000243644.9; ENSP00000243644.3; ENSG00000256683.7.
DR GeneID; 59348; -.
DR KEGG; hsa:59348; -.
DR MANE-Select; ENST00000243644.9; ENSP00000243644.3; NM_021632.4; NP_067645.3.
DR UCSC; uc002pyd.4; human.
DR CTD; 59348; -.
DR DisGeNET; 59348; -.
DR GeneCards; ZNF350; -.
DR HGNC; HGNC:16656; ZNF350.
DR HPA; ENSG00000256683; Low tissue specificity.
DR MIM; 605422; gene.
DR neXtProt; NX_Q9GZX5; -.
DR OpenTargets; ENSG00000256683; -.
DR PharmGKB; PA134972827; -.
DR VEuPathDB; HostDB:ENSG00000256683; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162449; -.
DR HOGENOM; CLU_002678_0_2_1; -.
DR InParanoid; Q9GZX5; -.
DR OMA; HADSEQF; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9GZX5; -.
DR TreeFam; TF340593; -.
DR PathwayCommons; Q9GZX5; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR SignaLink; Q9GZX5; -.
DR BioGRID-ORCS; 59348; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; ZNF350; human.
DR GeneWiki; ZNF350; -.
DR GenomeRNAi; 59348; -.
DR Pharos; Q9GZX5; Tbio.
DR PRO; PR:Q9GZX5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9GZX5; protein.
DR Bgee; ENSG00000256683; Expressed in calcaneal tendon and 148 other tissues.
DR ExpressionAtlas; Q9GZX5; baseline and differential.
DR Genevisible; Q9GZX5; HS.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
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:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
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; 8.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..532
FT /note="Zinc finger protein 350"
FT /id="PRO_0000047546"
FT DOMAIN 8..79
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 206..228
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 234..256
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 262..284
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 290..312
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 318..340
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 346..368
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 374..396
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 402..424
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 427..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 37
FT /note="M -> I (in dbSNP:rs4987241)"
FT /id="VAR_046718"
FT VARIANT 66
FT /note="L -> P (in dbSNP:rs2278420)"
FT /evidence="ECO:0000269|PubMed:11090615,
FT ECO:0000269|PubMed:12872252, ECO:0000269|PubMed:14702039"
FT /id="VAR_019902"
FT VARIANT 69
FT /note="I -> T (in dbSNP:rs4987042)"
FT /id="VAR_046719"
FT VARIANT 132
FT /note="R -> C (in dbSNP:rs28997584)"
FT /id="VAR_046720"
FT VARIANT 406
FT /note="E -> K (in dbSNP:rs3764539)"
FT /id="VAR_046721"
FT VARIANT 472
FT /note="S -> P (in dbSNP:rs4986771)"
FT /evidence="ECO:0000269|PubMed:12872252"
FT /id="VAR_019903"
FT VARIANT 501
FT /note="R -> S (in dbSNP:rs2278415)"
FT /evidence="ECO:0000269|PubMed:11090615,
FT ECO:0000269|PubMed:12872252, ECO:0000269|PubMed:14702039"
FT /id="VAR_019904"
FT VARIANT 524
FT /note="V -> I (in dbSNP:rs4988337)"
FT /evidence="ECO:0000269|PubMed:11161714,
FT ECO:0000269|PubMed:12872252"
FT /id="VAR_019905"
SQ SEQUENCE 532 AA; 60011 MW; FEF12A92F95BAC8A CRC64;
MIQAQESITL EDVAVDFTWE EWQLLGAAQK DLYRDVMLEN YSNLVAVGYQ ASKPDALFKL
EQGEQLWTIE DGIHSGACSD IWKVDHVLER LQSESLVNRR KPCHEHDAFE NIVHCSKSQF
LLGQNHDIFD LRGKSLKSNL TLVNQSKGYE IKNSVEFTGN GDSFLHANHE RLHTAIKFPA
SQKLISTKSQ FISPKHQKTR KLEKHHVCSE CGKAFIKKSW LTDHQVMHTG EKPHRCSLCE
KAFSRKFMLT EHQRTHTGEK PYECPECGKA FLKKSRLNIH QKTHTGEKPY ICSECGKGFI
QKGNLIVHQR IHTGEKPYIC NECGKGFIQK TCLIAHQRFH TGKTPFVCSE CGKSCSQKSG
LIKHQRIHTG EKPFECSECG KAFSTKQKLI VHQRTHTGER PYGCNECGKA FAYMSCLVKH
KRIHTREKQE AAKVENPPAE RHSSLHTSDV MQEKNSANGA TTQVPSVAPQ TSLNISGLLA
NRNVVLVGQP VVRCAASGDN RGFAQDRNLV NAVNVVVPSV INYVLFYVTE NP
