ZN513_MOUSE
ID ZN513_MOUSE Reviewed; 541 AA.
AC Q6PD29; Q3U4K1; Q8BWH6;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Zinc finger protein 513;
GN Name=Znf513; Synonyms=Zfp513;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryonic lung;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=20797688; DOI=10.1016/j.ajhg.2010.08.003;
RA Li L., Nakaya N., Chavali V.R., Ma Z., Jiao X., Sieving P.A., Riazuddin S.,
RA Tomarev S.I., Ayyagari R., Riazuddin S.A., Hejtmancik J.F.;
RT "A mutation in ZNF513, a putative regulator of photoreceptor development,
RT causes autosomal-recessive retinitis pigmentosa.";
RL Am. J. Hum. Genet. 87:400-409(2010).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
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).
CC -!- FUNCTION: Transcriptional regulator that plays a role in retinal
CC development and maintenance. {ECO:0000250}.
CC -!- SUBUNIT: Binds DNA. Can associate with the proximal promoter regions of
CC PAX6 and SP4, and their known targets including ARR3, RHO, OPN1MW2 and
CC OPN1SW. {ECO:0000269|PubMed:20797688}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PD29-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PD29-2; Sequence=VSP_035626;
CC -!- TISSUE SPECIFICITY: Widely expressed. In the eye, expression is
CC greatest in the retina and least in the lens and cornea.
CC {ECO:0000269|PubMed:20797688}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH58976.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC35001.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AK052459; BAC35001.1; ALT_SEQ; mRNA.
DR EMBL; AK154195; BAE32430.1; -; mRNA.
DR EMBL; BC058976; AAH58976.1; ALT_INIT; mRNA.
DR CCDS; CCDS19178.2; -. [Q6PD29-1]
DR CCDS; CCDS51458.1; -. [Q6PD29-2]
DR RefSeq; NP_001171372.1; NM_001177901.1. [Q6PD29-2]
DR RefSeq; NP_780520.3; NM_175311.4. [Q6PD29-1]
DR RefSeq; XP_006503720.2; XM_006503657.2.
DR AlphaFoldDB; Q6PD29; -.
DR SMR; Q6PD29; -.
DR BioGRID; 221569; 29.
DR IntAct; Q6PD29; 5.
DR STRING; 10090.ENSMUSP00000110238; -.
DR iPTMnet; Q6PD29; -.
DR PhosphoSitePlus; Q6PD29; -.
DR EPD; Q6PD29; -.
DR MaxQB; Q6PD29; -.
DR PaxDb; Q6PD29; -.
DR PeptideAtlas; Q6PD29; -.
DR PRIDE; Q6PD29; -.
DR ProteomicsDB; 275083; -. [Q6PD29-1]
DR ProteomicsDB; 275084; -. [Q6PD29-2]
DR Antibodypedia; 55939; 77 antibodies from 18 providers.
DR DNASU; 101023; -.
DR Ensembl; ENSMUST00000031562; ENSMUSP00000031562; ENSMUSG00000043059. [Q6PD29-2]
DR Ensembl; ENSMUST00000114590; ENSMUSP00000110238; ENSMUSG00000043059. [Q6PD29-1]
DR GeneID; 101023; -.
DR KEGG; mmu:101023; -.
DR UCSC; uc008wxn.1; mouse. [Q6PD29-2]
DR UCSC; uc008wxo.2; mouse. [Q6PD29-1]
DR CTD; 101023; -.
DR MGI; MGI:2141255; Zfp513.
DR VEuPathDB; HostDB:ENSMUSG00000043059; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158687; -.
DR HOGENOM; CLU_002678_58_1_1; -.
DR InParanoid; Q6PD29; -.
DR OMA; SICGYSC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q6PD29; -.
DR TreeFam; TF350015; -.
DR BioGRID-ORCS; 101023; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Zfp513; mouse.
DR PRO; PR:Q6PD29; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6PD29; protein.
DR Bgee; ENSMUSG00000043059; Expressed in secondary oocyte and 233 other tissues.
DR ExpressionAtlas; Q6PD29; baseline and differential.
DR Genevisible; Q6PD29; MM.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
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:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0060041; P:retina development in camera-type eye; ISS:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..541
FT /note="Zinc finger protein 513"
FT /id="PRO_0000353093"
FT ZN_FING 150..172
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 178..200
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 206..228
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 360..382
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 388..410
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 416..438
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 444..466
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 472..494
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..57
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N8E2"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..18
FT /note="MPRRKQSHPQPVKCEGVK -> MGTAWEGDSTSTLPSL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035626"
FT CONFLICT 504
FT /note="L -> R (in Ref. 1; BAC35001)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 58067 MW; 4F284BE3EBCABB7F CRC64;
MPRRKQSHPQ PVKCEGVKVD TEDSFDEGPG ALVLESDLLL GQDLEFEEEE EEDEGDGHND
QLMGFERDSE GDSQGARPGL PYGLSDDESG GGRALSAESE VEEPARGPGE ARGERPGPAC
QLCGGPTGEG PCCGAGGPGG GPPLPPRLLY SCRLCAFVSH YSSHLKRHMQ THSGEKPFRC
GRCPYASAQL VNLTRHTRTH TGEKPYRCPH CPFACSSLGN LRRHQRTHTG PPTPPCPTCG
FRCCAPRPTR PPSPTEQEGT MPRRSEDALI LPDLSLHVPP GGASFLPDCG QLRGEGESLC
GTGSEPLPEL LFPWTCRGCG QELEEGEGSR LGAAMCGRCM RGEAGGVATG GPQGPGDKGF
ACSLCPFATH YPNHLARHMK THSGEKPFRC ARCPYASAHL DNLKRHQRVH TGEKPYKCPL
CPYACGNLAN LKRHGRIHSG DKPFRCSLCN YSCNQSMNLK RHMLRHTGEK PFRCATCAYT
TGHWDNYKRH QKVHGHGGAG GPGLSAPEGW APPHSPPSVL STRGPAALGA TGSRALHSDS
P
