ZN219_MOUSE
ID ZN219_MOUSE Reviewed; 726 AA.
AC Q6IQX8; Q921W9; Q924S6; Q9CVF3;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Zinc finger protein 219 {ECO:0000303|PubMed:20940257};
GN Name=Znf219 {ECO:0000303|PubMed:20940257};
GN Synonyms=Zfp219 {ECO:0000312|MGI:MGI:1917140};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:BAB25714.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB61057.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAB61057.1}, and
RC Small intestine {ECO:0000312|EMBL:BAB25714.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:EDL42263.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAH71271.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH10447.1};
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-696; THR-699; SER-702 AND
RP SER-710, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SOX9, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DOMAIN.
RX PubMed=20940257; DOI=10.1242/jcs.071373;
RA Takigawa Y., Hata K., Muramatsu S., Amano K., Ono K., Wakabayashi M.,
RA Matsuda A., Takada K., Nishimura R., Yoneda T.;
RT "The transcription factor Znf219 regulates chondrocyte differentiation by
RT assembling a transcription factory with Sox9.";
RL J. Cell Sci. 123:3780-3788(2010).
CC -!- FUNCTION: Transcriptional regulator (PubMed:20940257). Recognizes and
CC binds 2 copies of the core DNA sequence motif 5'-GGGGG-3'
CC (PubMed:20940257). Binds to the HMGN1 promoter and may repress HMGN1
CC expression (By similarity). Regulates SNCA expression in primary
CC cortical neurons (By similarity). Binds to the COL2A1 promoter and
CC activates COL2A1 expression, as part of a complex with SOX9
CC (PubMed:20940257). Plays a role in chondrocyte differentiation
CC (PubMed:20940257). {ECO:0000250|UniProtKB:Q9P2Y4,
CC ECO:0000269|PubMed:20940257}.
CC -!- SUBUNIT: Interacts with SOX9 (via C-terminus).
CC {ECO:0000269|PubMed:20940257}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20940257}.
CC -!- TISSUE SPECIFICITY: Highly expressed in primary chondrocytes, heart,
CC pancreas and testis. {ECO:0000269|PubMed:20940257}.
CC -!- DEVELOPMENTAL STAGE: Expressed in proliferating chondrocytes in the
CC tibia at embryonic stage 15.5 dpc (at protein level). Expressed in limb
CC buds at stage 11.5 dpc, where it colocalizes with Col2a1 and Sox9.
CC {ECO:0000269|PubMed:20940257}.
CC -!- DOMAIN: C2H2-type zinc-finger domains 5 and 6 are important for the
CC interaction with SOX9. {ECO:0000269|PubMed:20940257}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK008516; BAB25714.1; -; mRNA.
DR EMBL; AB063578; BAB61057.1; -; mRNA.
DR EMBL; AC157572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466659; EDL42263.1; -; Genomic_DNA.
DR EMBL; CH466659; EDL42264.1; -; Genomic_DNA.
DR EMBL; CH466659; EDL42265.1; -; Genomic_DNA.
DR EMBL; BC010447; AAH10447.1; -; mRNA.
DR EMBL; BC071271; AAH71271.1; -; mRNA.
DR CCDS; CCDS36916.1; -.
DR RefSeq; NP_001240623.1; NM_001253694.1.
DR RefSeq; NP_001240624.1; NM_001253695.1.
DR RefSeq; NP_081524.2; NM_027248.2.
DR RefSeq; XP_006519561.1; XM_006519498.3.
DR RefSeq; XP_006519562.1; XM_006519499.3.
DR RefSeq; XP_006519564.1; XM_006519501.3.
DR RefSeq; XP_006519565.1; XM_006519502.3.
DR RefSeq; XP_006519566.1; XM_006519503.2.
DR RefSeq; XP_006519567.1; XM_006519504.3.
DR RefSeq; XP_006519568.1; XM_006519505.1.
DR RefSeq; XP_011243478.1; XM_011245176.2.
DR RefSeq; XP_011243479.1; XM_011245177.1.
DR RefSeq; XP_017171669.1; XM_017316180.1.
DR AlphaFoldDB; Q6IQX8; -.
DR IntAct; Q6IQX8; 11.
DR MINT; Q6IQX8; -.
DR STRING; 10090.ENSMUSP00000126854; -.
DR iPTMnet; Q6IQX8; -.
DR PhosphoSitePlus; Q6IQX8; -.
DR EPD; Q6IQX8; -.
DR jPOST; Q6IQX8; -.
DR MaxQB; Q6IQX8; -.
DR PaxDb; Q6IQX8; -.
DR PeptideAtlas; Q6IQX8; -.
DR PRIDE; Q6IQX8; -.
DR Antibodypedia; 22098; 129 antibodies from 25 providers.
DR DNASU; 69890; -.
DR Ensembl; ENSMUST00000067549; ENSMUSP00000068184; ENSMUSG00000049295.
DR Ensembl; ENSMUST00000166169; ENSMUSP00000126854; ENSMUSG00000049295.
DR Ensembl; ENSMUST00000226522; ENSMUSP00000154709; ENSMUSG00000049295.
DR GeneID; 69890; -.
DR KEGG; mmu:69890; -.
DR UCSC; uc007tnv.3; mouse.
DR CTD; 69890; -.
DR MGI; MGI:1917140; Zfp219.
DR VEuPathDB; HostDB:ENSMUSG00000049295; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161408; -.
DR HOGENOM; CLU_008125_1_0_1; -.
DR InParanoid; Q6IQX8; -.
DR OMA; DASPPYV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q6IQX8; -.
DR TreeFam; TF332241; -.
DR BioGRID-ORCS; 69890; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Zfp219; mouse.
DR PRO; PR:Q6IQX8; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q6IQX8; protein.
DR Bgee; ENSMUSG00000049295; Expressed in ventricular zone and 288 other tissues.
DR ExpressionAtlas; Q6IQX8; baseline and differential.
DR Genevisible; Q924S6; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS: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; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0060174; P:limb bud formation; IEP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 6.
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; Differentiation; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..726
FT /note="Zinc finger protein 219"
FT /id="PRO_0000442537"
FT ZN_FING 61..83
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 89..111
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 167..190
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 193..216
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 277..299
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 305..327
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 501..523
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 529..551
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 650..672
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255"
FT REGION 139..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..242
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..275
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..574
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2Y4"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 699
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 48
FT /note="A -> Q (in Ref. 1; BAB61057)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="P -> T (in Ref. 1; BAB61057)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 726 AA; 77796 MW; 7F0E43159B73B0F4 CRC64;
MEGSRPRILV GHLEPSPPAF DGELDLQRYS NGPGVSGTPG PGSPGMGAVG WSETRAGERR
FPCPVCGKRF RFNSILALHL RAHPGAQAFQ CPHCGHRAAQ RALLRSHLRT HQPERPRSPA
ARLLLELEER ALLREARLGR ARSSGGMQSS PAAEGLARPQ VPSSSAFRCP FCKGKFRTSA
ERERHLHILH RPWKCSLCSF GSSQEEELLH HSLTAHGASE RPLAATSTPE PPPPPQQEPR
SALEPEPEPE PRPEPDREAN PAPTPAPPEE PPAPPEFRCQ VCGQSFTQSW FLKGHMRKHK
ASFDHACPVC GRCFKEPWFL KNHMKVHTSK LGPLRAPGPG SAPARAPQPP DLSLLAYEPL
GPALLLAPAP APAERREPPS LLGYLSVRAG EVRPNGEGAD PGGGRSYGGF RPLPSALPNR
ARRHRTEEPE EEEEVVEAEE ESWARGRSLG SLTSLHPNPG EGSGQPAPAA GTQARSTATQ
EENGLLVGGT RSEAGRGATG KDCPFCGKSF RSAHHLKVHL RVHTGERPYK CPHCDYAGTQ
SGSLKYHLQR HHREQRSSAG PGPPPEPPPP SQRGSLQPQS GAKPTQASAT WVEGTASTRP
PSSSTGPGSR RKPASPGRTL RNGRGGEAEP LDLSLRAGPG GEAGAGGALH RCLFCPFATG
APELMALHLQ VHHSRRARGR RQPRADTSPT YVRAPSGETP PSPPLEEEGS PGLSRSGEAG
LGGQER
