ZN592_MOUSE
ID ZN592_MOUSE Reviewed; 1262 AA.
AC Q8BHZ4; Q80XM1;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Zinc finger protein 592;
DE Short=Zfp-592;
GN Name=Znf592; Synonyms=Kiaa0211, Zfp592;
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 tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
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. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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] OF 162-1217.
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Liver;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-145; SER-146;
RP SER-573; SER-1198 AND SER-1202, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, 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 [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20531441; DOI=10.1038/ejhg.2010.82;
RA Nicolas E., Poitelon Y., Chouery E., Salem N., Levy N., Megarbane A.,
RA Delague V.;
RT "CAMOS, a nonprogressive, autosomal recessive, congenital cerebellar
RT ataxia, is caused by a mutant zinc-finger protein, ZNF592.";
RL Eur. J. Hum. Genet. 18:1107-1113(2010).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain.
CC {ECO:0000269|PubMed:20531441}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryo at least from 10 dpc until
CC birth. {ECO:0000269|PubMed:20531441}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC31327.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC97899.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129089; BAC97899.1; ALT_INIT; mRNA.
DR EMBL; AK042675; BAC31327.1; ALT_FRAME; mRNA.
DR EMBL; BC044728; AAH44728.1; -; mRNA.
DR EMBL; BC059073; AAH59073.1; -; mRNA.
DR CCDS; CCDS40003.2; -.
DR RefSeq; NP_848822.2; NM_178707.4.
DR AlphaFoldDB; Q8BHZ4; -.
DR BioGRID; 231411; 6.
DR IntAct; Q8BHZ4; 4.
DR MINT; Q8BHZ4; -.
DR STRING; 10090.ENSMUSP00000102976; -.
DR iPTMnet; Q8BHZ4; -.
DR PhosphoSitePlus; Q8BHZ4; -.
DR EPD; Q8BHZ4; -.
DR jPOST; Q8BHZ4; -.
DR MaxQB; Q8BHZ4; -.
DR PaxDb; Q8BHZ4; -.
DR PRIDE; Q8BHZ4; -.
DR ProteomicsDB; 275016; -.
DR Antibodypedia; 15495; 128 antibodies from 19 providers.
DR DNASU; 233410; -.
DR Ensembl; ENSMUST00000107353; ENSMUSP00000102976; ENSMUSG00000005621.
DR GeneID; 233410; -.
DR KEGG; mmu:233410; -.
DR UCSC; uc009ibp.2; mouse.
DR CTD; 233410; -.
DR MGI; MGI:2443541; Zfp592.
DR VEuPathDB; HostDB:ENSMUSG00000005621; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158357; -.
DR HOGENOM; CLU_006283_0_0_1; -.
DR InParanoid; Q8BHZ4; -.
DR OMA; SVKKYPC; -.
DR OrthoDB; 180681at2759; -.
DR PhylomeDB; Q8BHZ4; -.
DR TreeFam; TF329009; -.
DR BioGRID-ORCS; 233410; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Zfp592; mouse.
DR PRO; PR:Q8BHZ4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BHZ4; protein.
DR Bgee; ENSMUSG00000005621; Expressed in animal zygote and 234 other tissues.
DR Genevisible; Q8BHZ4; 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; IPR045914; Zn532-like.
DR InterPro; IPR041697; Znf-C2H2_11.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR47222; PTHR47222; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR Pfam; PF16622; zf-C2H2_11; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
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..1262
FT /note="Zinc finger protein 592"
FT /id="PRO_0000047683"
FT ZN_FING 587..612
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 615..639
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 711..731
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 740..764
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 768..790
FT /note="C2H2-type 5; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 799..822
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 827..850
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 892..915
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 983..1006
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1013..1036
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1043..1069
FT /note="C2H2-type 11; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1124..1146
FT /note="C2H2-type 12; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1153..1176
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 23..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1222..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92610"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92610"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92610"
FT MOD_RES 1089
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92610"
FT MOD_RES 1198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 200
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92610"
FT CROSSLNK 204
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92610"
FT CROSSLNK 546
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92610"
FT CONFLICT 510..521
FT /note="LVPHSVAASVTA -> PRVRPRVRPRVR (in Ref. 3; AAH44728)"
FT /evidence="ECO:0000305"
FT CONFLICT 625
FT /note="L -> F (in Ref. 1; BAC97899)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="I -> V (in Ref. 1; BAC97899 and 3; AAH44728)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1262 AA; 137514 MW; 5C3FD264D0330B96 CRC64;
MGDMKTPDFD DLLAAFDIPD PTSLDAKEAI QAPSEENESP LKSSGMCIDE NVSLSHSGSA
PDVPAVSVIV KNTSRQESFE AEKDHIAPSL LHNGFRGSDL PPDSHHCGKF DSTFINGDSA
RSFTSKLEPS KSEPLPTFNQ FSPISSPEPE DPVKDNGFGI KSKHSDSYFP PPPGTVGGPV
LEALSKFPVP ELHMFDHFCK KEPKPEPLPL ESQQEHEQGG QKVVEPHKDL DSSRFFGEAL
EFNSHPSNSI GEPKKLAPEL SACSSVPPRQ RLKPAHSKLS SCVAALVALQ AKRVANVTKE
DQPGHTKDSS GPTKEGSKGS PKMPKSPKSP RSPLEATRKS IKPSDSPRSI CSDSSSKGSP
SVAASSPPAI PKVRIKTIKT SSGEIKRTVT RILPDPDDPS KSPAESPAGS TITEAPSEAP
GDEGTAMPVE EHFSEAGIHS GSPQGDRKGD ENMIKTSDSS SPCRISGSRV PKGSALNSQA
SKKQQSTAPQ ASTPAASLLP KAVHLANLNL VPHSVAASVT AKSSAQRRSQ PQVTQMTVPL
VHQVKKAAPL IVEVFNKVLH SSNPVPLYAP NLSPPADSRI HVPASGYCCL ECGDAFALEK
SLSQHYSRRS VHIEVLCTLC SKTLLFFNKC SLLRHARDHK SKGLVMQCSQ LLVKPISADQ
MFVAAPVNST APATPAASSS PKPSPTLDNA SSVIPALPLY PDPVRLIRYG TKCPECHKQM
RDYMVLATHF QRTTEETEGL TCQVCQMLLP NQCSFCAHQR IHAHKSPYCC PECGVLCRSA
YFQTHVKENC LHYARKVGYR CIHCGVIHLT LALLKSHIQE RHCQVFHKCA FCPMAFKTAS
STMDHSTTQH PTQPHKPSQL IYKCSCEMVF NKKRHIQQHF YQNVSKTQAG VFKCPECPLL
FLQKPELMQH VKNTHGVPRN VEELSSLQSS TDTSSNRPGS RAPAEPPATN VAARGSSLTA
GRWGRPEAHR RAEARPRMRS TGWTCQECQE WVPDRESYVS HMKKSHGRTL KRYPCRQCEQ
SFHNPSSLRK HIRNNHDTVK KVYTCGYCTE DSPSFPRPSL LESHISLMHG IRNPDLSQTS
KVRHPGGPSP QVNHLKRPVS RMADAPGTSN GATVSSTKRH KSLFQCAKCT FATDSELEFQ
SHIPQHQVDS STAQCLLCGL CYTSTSSLNR HLFIVHKVRD QEEGGEDIVE VKVEAPDSEA
CSGEEVAMET KENGLEECAS EPLVTDLGGQ QGLALDEDSA QDPQNQPQAS QDQNSHALSP
QV
