ZN205_HUMAN
ID ZN205_HUMAN Reviewed; 554 AA.
AC O95201; A8MZK0; D3DUB4; Q9BU95;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Zinc finger protein 205;
DE AltName: Full=Zinc finger protein 210;
GN Name=ZNF205; Synonyms=ZNF210;
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=9787081; DOI=10.1006/geno.1998.5430;
RA Deng Z., Centola M., Chen X., Sood R., Vedula A., Fischel-Ghodsian N.,
RA Kastner D.L.;
RT "Identification of two Kruppel-related zinc finger genes (ZNF200 and
RT ZNF210) from human chromosome 16p13.3.";
RL Genomics 53:97-103(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-43.
RC TISSUE=Placenta;
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-292, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-219, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-219, 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 O95201; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-747343, EBI-5916454;
CC O95201; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-747343, EBI-79165;
CC O95201; Q63HR2: TNS2; NbExp=3; IntAct=EBI-747343, EBI-949753;
CC O95201; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-747343, EBI-744794;
CC O95201; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-747343, EBI-947187;
CC O95201; Q9NRR5: UBQLN4; NbExp=2; IntAct=EBI-747343, EBI-711226;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, pancreas and
CC brain. Weakly expressed in placenta, lung, liver, kidney and thymus.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC70007.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF060865; AAC70007.1; ALT_INIT; mRNA.
DR EMBL; AC108134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85396.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85398.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85399.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85400.1; -; Genomic_DNA.
DR EMBL; BC002810; AAH02810.1; -; mRNA.
DR CCDS; CCDS10494.2; -.
DR RefSeq; NP_001035893.1; NM_001042428.1.
DR RefSeq; NP_001265087.1; NM_001278158.1.
DR RefSeq; NP_003447.2; NM_003456.2.
DR RefSeq; XP_005255615.1; XM_005255558.2.
DR AlphaFoldDB; O95201; -.
DR SMR; O95201; -.
DR BioGRID; 113539; 21.
DR IntAct; O95201; 17.
DR MINT; O95201; -.
DR STRING; 9606.ENSP00000480401; -.
DR iPTMnet; O95201; -.
DR PhosphoSitePlus; O95201; -.
DR BioMuta; ZNF205; -.
DR EPD; O95201; -.
DR jPOST; O95201; -.
DR MassIVE; O95201; -.
DR MaxQB; O95201; -.
DR PaxDb; O95201; -.
DR PeptideAtlas; O95201; -.
DR PRIDE; O95201; -.
DR ProteomicsDB; 50709; -.
DR Antibodypedia; 822; 106 antibodies from 17 providers.
DR DNASU; 7755; -.
DR Ensembl; ENST00000219091.9; ENSP00000219091.4; ENSG00000122386.11.
DR Ensembl; ENST00000382192.7; ENSP00000371627.3; ENSG00000122386.11.
DR Ensembl; ENST00000620094.4; ENSP00000480401.1; ENSG00000122386.11.
DR GeneID; 7755; -.
DR KEGG; hsa:7755; -.
DR MANE-Select; ENST00000219091.9; ENSP00000219091.4; NM_001042428.2; NP_001035893.1.
DR UCSC; uc002cua.4; human.
DR CTD; 7755; -.
DR DisGeNET; 7755; -.
DR GeneCards; ZNF205; -.
DR HGNC; HGNC:12996; ZNF205.
DR HPA; ENSG00000122386; Low tissue specificity.
DR MIM; 603436; gene.
DR neXtProt; NX_O95201; -.
DR OpenTargets; ENSG00000122386; -.
DR PharmGKB; PA37576; -.
DR VEuPathDB; HostDB:ENSG00000122386; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161865; -.
DR HOGENOM; CLU_002678_9_0_1; -.
DR InParanoid; O95201; -.
DR OMA; EWRGAYT; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O95201; -.
DR TreeFam; TF338003; -.
DR PathwayCommons; O95201; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; O95201; -.
DR BioGRID-ORCS; 7755; 15 hits in 1102 CRISPR screens.
DR ChiTaRS; ZNF205; human.
DR GenomeRNAi; 7755; -.
DR Pharos; O95201; Tbio.
DR PRO; PR:O95201; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O95201; protein.
DR Bgee; ENSG00000122386; Expressed in tendon of biceps brachii and 176 other tissues.
DR ExpressionAtlas; O95201; baseline and differential.
DR Genevisible; O95201; HS.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0010729; P:positive regulation of hydrogen peroxide biosynthetic process; IMP:BHF-UCL.
DR GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IMP:BHF-UCL.
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; NAS: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; 5.
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; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..554
FT /note="Zinc finger protein 205"
FT /id="PRO_0000047451"
FT DOMAIN 124..193
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 308..330
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 336..358
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 364..386
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 392..414
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 420..442
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 448..470
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 476..498
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 504..526
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..275
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VARIANT 43
FT /note="T -> A (in dbSNP:rs909410)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028798"
FT VARIANT 255
FT /note="A -> D (in dbSNP:rs12445220)"
FT /id="VAR_028799"
SQ SEQUENCE 554 AA; 60630 MW; B70DC15F0DFDC7FC CRC64;
MSADGGGIQD TQDKETPPEV PDRGHPHQEM PSKLGEAVPS GDTQESLHIK MEPEEPHSEG
ASQEDGAQGA WGWAPLSHGS KEKALFLPGG ALPSPRIPVL SREGRTRDRQ MAAALLTAWS
QMPVTFEDVA LYLSREEWGR LDHTQQNFYR DVLQKKNGLS LGFPFSRPFW APQAHGKGEA
SGSSRQAGDE KEWRGACTGA VEVGQRVQTS SVAALGNVKP FRTRAGRVQW GVPQCAQEAA
CGRSSGPAKD SGQPAEPDRT PDAAPPDPSP TEPQEYRVPE KPNEEEKGAP ESGEEGLAPD
SEVGRKSYRC EQCGKGFSWH SHLVTHRRTH TGEKPYACTD CGKRFGRSSH LIQHQIIHTG
EKPYTCPACR KSFSHHSTLI QHQRIHTGEK PYVCDRCAKR FTRRSDLVTH QGTHTGAKPH
KCPICAKCFT QSSALVTHQR THTGVKPYPC PECGKCFSQR SNLIAHNRTH TGEKPYHCLD
CGKSFSHSSH LTAHQRTHRG VRPYACPLCG KSFSRRSNLH RHEKIHTTGP KALAMLMLGA
AAAGALATPP PAPT
