ZN512_MOUSE
ID ZN512_MOUSE Reviewed; 562 AA.
AC Q69Z99; Q3U365; Q3UDU3; Q3UJQ0; Q5FWY0; Q8BJF3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Zinc finger protein 512;
GN Name=Znf512; Synonyms=Kiaa1805, Zfp512;
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].
RC TISSUE=Embryonic intestine;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and NOD; TISSUE=Bone marrow, and Eye;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32545.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173267; BAD32545.1; ALT_INIT; mRNA.
DR EMBL; AK084205; BAC39137.1; -; mRNA.
DR EMBL; AK146353; BAE27105.1; -; mRNA.
DR EMBL; AK149921; BAE29168.1; -; mRNA.
DR EMBL; AK154918; BAE32924.1; -; mRNA.
DR EMBL; BC089160; AAH89160.1; -; mRNA.
DR CCDS; CCDS19183.1; -.
DR RefSeq; NP_766581.2; NM_172993.3.
DR AlphaFoldDB; Q69Z99; -.
DR BioGRID; 234688; 4.
DR IntAct; Q69Z99; 2.
DR MINT; Q69Z99; -.
DR STRING; 10090.ENSMUSP00000075613; -.
DR iPTMnet; Q69Z99; -.
DR PhosphoSitePlus; Q69Z99; -.
DR EPD; Q69Z99; -.
DR MaxQB; Q69Z99; -.
DR PaxDb; Q69Z99; -.
DR PeptideAtlas; Q69Z99; -.
DR PRIDE; Q69Z99; -.
DR Antibodypedia; 34858; 95 antibodies from 19 providers.
DR DNASU; 269639; -.
DR Ensembl; ENSMUST00000076264; ENSMUSP00000075613; ENSMUSG00000062761.
DR GeneID; 269639; -.
DR KEGG; mmu:269639; -.
DR UCSC; uc008wyg.2; mouse.
DR CTD; 269639; -.
DR MGI; MGI:1917345; Zfp512.
DR VEuPathDB; HostDB:ENSMUSG00000062761; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158595; -.
DR HOGENOM; CLU_481412_0_0_1; -.
DR InParanoid; Q69Z99; -.
DR OMA; PFFPESG; -.
DR OrthoDB; 222563at2759; -.
DR PhylomeDB; Q69Z99; -.
DR TreeFam; TF331185; -.
DR BioGRID-ORCS; 269639; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Zfp512; mouse.
DR PRO; PR:Q69Z99; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q69Z99; protein.
DR Bgee; ENSMUSG00000062761; Expressed in embryonic brain and 229 other tissues.
DR ExpressionAtlas; Q69Z99; baseline and differential.
DR Genevisible; Q69Z99; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..562
FT /note="Zinc finger protein 512"
FT /id="PRO_0000333737"
FT ZN_FING 200..223
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 290..313
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 442..465
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..141
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96ME7"
FT CROSSLNK 84
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96ME7"
FT CROSSLNK 230
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96ME7"
FT CROSSLNK 335
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96ME7"
FT CONFLICT 81
FT /note="R -> G (in Ref. 2; BAE32924)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="R -> G (in Ref. 2; BAC39137)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="K -> E (in Ref. 2; BAE29168)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="R -> G (in Ref. 2; BAE32924)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="I -> M (in Ref. 2; BAC39137)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="E -> K (in Ref. 2; BAE27105)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 562 AA; 63908 MW; DB522267A7113189 CRC64;
MSSRLGAVTA TPGPTSLKQQ RSTRIVGAKN NRAQCSIKDN SFQYTIPHED SLSGSSSASS
CEPVSDFTAT LRKSTYWMKM RRIKPAATSQ VEGAGEKEKE RAKGKRNVKQ EEDEDYRELP
QKKHKLYGRK QRPKAQPHPK PQARRVRKEP PVYAAGSMEE KWYLEIMDKG SVSCPTCQAV
GRKTIEGLKK HMENCKQEMF TCHHCGKQLH SLAGMKYHVM ANHNSLPILK AGDEVDEPSE
RERLRTVLKR MGKLRCMRES CSSTFTSIMG YLYHVRKCGK EASELEKLAL KCHHCGKPYR
SKAGLAYHMR SEHGPVFFPE SEQPDCLKEM SLEAKGGGRV QRRSAKIAVY HLQELASAEL
TKEWPKRKVL QDLVPDDRKL KYTRPGLPTF SQEVLHKWKT DIKKYHRIQC PNQGCEAVYS
SVSGLKAHLG SCTLGTFVAG KYKCLLCEKE FVSESGVKYH INSVHAEDWF VVNPTTTKSF
EKLMKIKQRQ QEEEKQRQQH GRRRSLRRQQ QPCMEPPESQ LEPKAGKEQG GNEELVGPDP
EPVPAQPQKA EPAKTTHKRG RK
