ZN219_HUMAN
ID ZN219_HUMAN Reviewed; 722 AA.
AC Q9P2Y4; D3DS16; Q53Y57; Q8IYC1; Q9BW28;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Zinc finger protein 219;
GN Name=ZNF219;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10819330; DOI=10.1093/dnares/7.2.137;
RA Sakai T., Toyoda A., Hashimoto K., Maeda H.;
RT "Isolation and characterization of a novel zinc finger gene, ZNF219, and
RT mapping to the human chromosome 14q11 region.";
RL DNA Res. 7:137-141(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-260.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
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 THR-260.
RC TISSUE=Brain, and 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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14621294; DOI=10.1093/dnares/10.4.155;
RA Sakai T., Hino K., Wada S., Maeda H.;
RT "Identification of the DNA binding specificity of the human ZNF219 protein
RT and its function as a transcriptional repressor.";
RL DNA Res. 10:155-165(2003).
RN [6]
RP FUNCTION.
RX PubMed=19549071; DOI=10.1111/j.1471-4159.2009.06250.x;
RA Clough R.L., Dermentzaki G., Stefanis L.;
RT "Functional dissection of the alpha-synuclein promoter: transcriptional
RT regulation by ZSCAN21 and ZNF219.";
RL J. Neurochem. 110:1479-1490(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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: Transcriptional regulator (PubMed:14621294, PubMed:19549071).
CC Recognizes and binds 2 copies of the core DNA sequence motif 5'-GGGGG-
CC 3' (PubMed:14621294). Binds to the HMGN1 promoter and may repress HMGN1
CC expression (PubMed:14621294). Regulates SNCA expression in primary
CC cortical neurons (PubMed:19549071). Binds to the COL2A1 promoter and
CC activates COL2A1 expression, as part of a complex with SOX9 (By
CC similarity). Plays a role in chondrocyte differentiation (By
CC similarity). {ECO:0000250|UniProtKB:Q6IQX8,
CC ECO:0000269|PubMed:14621294, ECO:0000269|PubMed:19549071}.
CC -!- SUBUNIT: Interacts with SOX9 (via C-terminus).
CC {ECO:0000250|UniProtKB:Q6IQX8}.
CC -!- INTERACTION:
CC Q9P2Y4; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-3937106, EBI-541426;
CC Q9P2Y4; Q01658: DR1; NbExp=3; IntAct=EBI-3937106, EBI-750300;
CC Q9P2Y4; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-3937106, EBI-745689;
CC Q9P2Y4; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-3937106, EBI-717919;
CC Q9P2Y4; P25800: LMO1; NbExp=3; IntAct=EBI-3937106, EBI-8639312;
CC Q9P2Y4; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-3937106, EBI-725997;
CC Q9P2Y4; Q5I0X7: TTC32; NbExp=3; IntAct=EBI-3937106, EBI-8636434;
CC Q9P2Y4; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-3937106, EBI-7353612;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10819330,
CC ECO:0000269|PubMed:14621294}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10819330}.
CC -!- DOMAIN: C2H2-type zinc-finger domains 5 and 6 are important for the
CC interaction with SOX9. {ECO:0000250|UniProtKB:Q6IQX8}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AB015427; BAA90526.1; -; mRNA.
DR EMBL; BT006956; AAP35602.1; -; mRNA.
DR EMBL; CH471078; EAW66404.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66405.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66406.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66407.1; -; Genomic_DNA.
DR EMBL; BC000694; AAH00694.1; -; mRNA.
DR EMBL; BC036105; AAH36105.1; -; mRNA.
DR CCDS; CCDS9568.1; -.
DR RefSeq; NP_001095142.1; NM_001101672.1.
DR RefSeq; NP_001095924.1; NM_001102454.1.
DR RefSeq; NP_057507.2; NM_016423.2.
DR RefSeq; XP_006720226.1; XM_006720163.2.
DR RefSeq; XP_006720227.1; XM_006720164.3.
DR RefSeq; XP_016876843.1; XM_017021354.1.
DR RefSeq; XP_016876844.1; XM_017021355.1.
DR AlphaFoldDB; Q9P2Y4; -.
DR BioGRID; 119387; 78.
DR IntAct; Q9P2Y4; 50.
DR MINT; Q9P2Y4; -.
DR STRING; 9606.ENSP00000354206; -.
DR iPTMnet; Q9P2Y4; -.
DR PhosphoSitePlus; Q9P2Y4; -.
DR BioMuta; ZNF219; -.
DR DMDM; 55977885; -.
DR EPD; Q9P2Y4; -.
DR jPOST; Q9P2Y4; -.
DR MassIVE; Q9P2Y4; -.
DR MaxQB; Q9P2Y4; -.
DR PaxDb; Q9P2Y4; -.
DR PeptideAtlas; Q9P2Y4; -.
DR PRIDE; Q9P2Y4; -.
DR ProteomicsDB; 83913; -.
DR Antibodypedia; 22098; 129 antibodies from 25 providers.
DR DNASU; 51222; -.
DR Ensembl; ENST00000360947.8; ENSP00000354206.3; ENSG00000165804.16.
DR Ensembl; ENST00000421093.6; ENSP00000392401.2; ENSG00000165804.16.
DR Ensembl; ENST00000451119.6; ENSP00000388558.2; ENSG00000165804.16.
DR GeneID; 51222; -.
DR KEGG; hsa:51222; -.
DR MANE-Select; ENST00000360947.8; ENSP00000354206.3; NM_016423.3; NP_057507.2.
DR UCSC; uc001vzr.3; human.
DR CTD; 51222; -.
DR DisGeNET; 51222; -.
DR GeneCards; ZNF219; -.
DR HGNC; HGNC:13011; ZNF219.
DR HPA; ENSG00000165804; Low tissue specificity.
DR MIM; 605036; gene.
DR neXtProt; NX_Q9P2Y4; -.
DR OpenTargets; ENSG00000165804; -.
DR PharmGKB; PA37590; -.
DR VEuPathDB; HostDB:ENSG00000165804; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161408; -.
DR HOGENOM; CLU_008125_1_0_1; -.
DR InParanoid; Q9P2Y4; -.
DR OMA; DASPPYV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9P2Y4; -.
DR TreeFam; TF332241; -.
DR PathwayCommons; Q9P2Y4; -.
DR SignaLink; Q9P2Y4; -.
DR BioGRID-ORCS; 51222; 26 hits in 1098 CRISPR screens.
DR ChiTaRS; ZNF219; human.
DR GeneWiki; ZNF219; -.
DR GenomeRNAi; 51222; -.
DR Pharos; Q9P2Y4; Tbio.
DR PRO; PR:Q9P2Y4; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9P2Y4; protein.
DR Bgee; ENSG00000165804; Expressed in right adrenal gland and 143 other tissues.
DR ExpressionAtlas; Q9P2Y4; baseline and differential.
DR Genevisible; Q9P2Y4; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
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; IDA:NTNU_SB.
DR GO; GO:0004969; F:histamine receptor activity; IEA:InterPro.
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; IDA:NTNU_SB.
DR GO; GO:0060174; P:limb bud formation; IEA:Ensembl.
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:0032332; P:positive regulation of chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0001505; P:regulation of neurotransmitter levels; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR InterPro; IPR003980; Histamine_H3_rcpt.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 6.
DR PRINTS; PR01471; HISTAMINEH3R.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..722
FT /note="Zinc finger protein 219"
FT /id="PRO_0000047461"
FT ZN_FING 57..79
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 85..107
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 163..186
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 189..212
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 274..296
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 302..324
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 498..520
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 526..548
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 646..668
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..272
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQX8"
FT MOD_RES 695
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQX8"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQX8"
FT VARIANT 260
FT /note="P -> T (in dbSNP:rs17853549)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_067624"
FT CONFLICT 232..233
FT /note="Missing (in Ref. 4; AAH00694)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="E -> Q (in Ref. 1; BAA90526)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 722 AA; 76877 MW; AB2B6B37904FC14B CRC64;
MEGSRPRAPS GHLAPSPPAF DGELDLQRYS NGPAVSAGSL GMGAVSWSES RAGERRFPCP
VCGKRFRFNS ILALHLRAHP GAQAFQCPHC GHRAAQRALL RSHLRTHQPE RPRSPAARLL
LELEERALLR EARLGRARSS GGMQATPATE GLARPQAPSS SAFRCPYCKG KFRTSAERER
HLHILHRPWK CGLCSFGSSQ EEELLHHSLT AHGAPERPLA ATSAAPPPQP QPQPPPQPEP
RSVPQPEPEP EPEREATPTP APAAPEEPPA PPEFRCQVCG QSFTQSWFLK GHMRKHKASF
DHACPVCGRC FKEPWFLKNH MKVHASKLGP LRAPGPASGP ARAPQPPDLG LLAYEPLGPA
LLLAPAPTPA ERREPPSLLG YLSLRAGEGR PNGEGAEPGP GRSFGGFRPL SSALPARARR
HRAEEPEEEE EVVEAEEETW ARGRSLGSLA SLHPRPGEGP GHSASAAGAQ ARSTATQEEN
GLLVGGTRPE GGRGATGKDC PFCGKSFRSA HHLKVHLRVH TGERPYKCPH CDYAGTQSGS
LKYHLQRHHR EQRSGAGPGP PPEPPPPSQR GSAPQSGAKP SPQPATWVEG ASSPRPPSSG
AGPGSRRKPA SPGRTLRNGR GGEAEPLDLS LRAGPGGEAG PGGALHRCLF CPFATGAPEL
MALHLQVHHS RRARGRRPPQ ADASPPYARV PSGETPPSPS QEGEEGSGLS RPGEAGLGGQ
ER
