ZN592_HUMAN
ID ZN592_HUMAN Reviewed; 1267 AA.
AC Q92610; Q2M1T2; Q504Y9;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Zinc finger protein 592;
GN Name=ZNF592; Synonyms=KIAA0211;
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 [LARGE SCALE MRNA], AND VARIANT ASN-926.
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-926.
RC 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-146; SER-573 AND
RP SER-691, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573; SER-691 AND SER-1089,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-529; SER-573 AND
RP SER-691, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689 AND SER-691, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-202; LYS-206 AND LYS-546, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [13]
RP VARIANT ARG-1046, AND TISSUE SPECIFICITY.
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 -!- INTERACTION:
CC Q92610; Q9Y4C2: TCAF1; NbExp=3; IntAct=EBI-1210420, EBI-750484;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in skeletal
CC muscle. Expressed throughout the central nervous system, including in
CC the cerebellum and cerebellar vermis, with higher expression in the
CC substantia nigra. Widely expressed in fetal tissues.
CC {ECO:0000269|PubMed:20531441}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13202.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D86966; BAA13202.2; ALT_INIT; mRNA.
DR EMBL; CH471101; EAX01957.1; -; Genomic_DNA.
DR EMBL; BC094688; AAH94688.1; -; mRNA.
DR EMBL; BC112232; AAI12233.1; -; mRNA.
DR EMBL; BC112234; AAI12235.1; -; mRNA.
DR CCDS; CCDS32317.1; -.
DR RefSeq; NP_055445.2; NM_014630.2.
DR RefSeq; XP_005255053.1; XM_005254996.3.
DR RefSeq; XP_011520548.1; XM_011522246.2.
DR RefSeq; XP_011520549.1; XM_011522247.2.
DR RefSeq; XP_016878223.1; XM_017022734.1.
DR AlphaFoldDB; Q92610; -.
DR BioGRID; 114999; 57.
DR IntAct; Q92610; 21.
DR MINT; Q92610; -.
DR STRING; 9606.ENSP00000452877; -.
DR GlyGen; Q92610; 3 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q92610; -.
DR PhosphoSitePlus; Q92610; -.
DR BioMuta; ZNF592; -.
DR DMDM; 209572705; -.
DR CPTAC; CPTAC-1216; -.
DR EPD; Q92610; -.
DR jPOST; Q92610; -.
DR MassIVE; Q92610; -.
DR MaxQB; Q92610; -.
DR PaxDb; Q92610; -.
DR PeptideAtlas; Q92610; -.
DR PRIDE; Q92610; -.
DR ProteomicsDB; 75355; -.
DR Antibodypedia; 15495; 128 antibodies from 19 providers.
DR DNASU; 9640; -.
DR Ensembl; ENST00000299927.4; ENSP00000299927.3; ENSG00000166716.10.
DR Ensembl; ENST00000560079.7; ENSP00000452877.2; ENSG00000166716.10.
DR GeneID; 9640; -.
DR KEGG; hsa:9640; -.
DR MANE-Select; ENST00000560079.7; ENSP00000452877.2; NM_014630.3; NP_055445.2.
DR UCSC; uc002bld.4; human.
DR CTD; 9640; -.
DR DisGeNET; 9640; -.
DR GeneCards; ZNF592; -.
DR HGNC; HGNC:28986; ZNF592.
DR HPA; ENSG00000166716; Low tissue specificity.
DR MalaCards; ZNF592; -.
DR MIM; 613624; gene.
DR neXtProt; NX_Q92610; -.
DR OpenTargets; ENSG00000166716; -.
DR Orphanet; 83472; CAMOS syndrome.
DR PharmGKB; PA134918837; -.
DR VEuPathDB; HostDB:ENSG00000166716; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158357; -.
DR HOGENOM; CLU_006283_0_0_1; -.
DR InParanoid; Q92610; -.
DR OMA; SVKKYPC; -.
DR OrthoDB; 180681at2759; -.
DR PhylomeDB; Q92610; -.
DR TreeFam; TF329009; -.
DR PathwayCommons; Q92610; -.
DR SignaLink; Q92610; -.
DR BioGRID-ORCS; 9640; 28 hits in 1101 CRISPR screens.
DR ChiTaRS; ZNF592; human.
DR GenomeRNAi; 9640; -.
DR Pharos; Q92610; Tbio.
DR PRO; PR:Q92610; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q92610; protein.
DR Bgee; ENSG00000166716; Expressed in pancreatic ductal cell and 169 other tissues.
DR ExpressionAtlas; Q92610; baseline and differential.
DR Genevisible; Q92610; HS.
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..1267
FT /note="Zinc finger protein 592"
FT /id="PRO_0000047682"
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 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1089
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHZ4"
FT MOD_RES 1250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT CROSSLNK 202
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 206
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 546
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 926
FT /note="S -> N (in dbSNP:rs8182086)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9039502"
FT /id="VAR_047033"
FT VARIANT 1046
FT /note="G -> R (found in a patient with clinical features of
FT Galloway-Mowat syndrome; unknown pathological significance;
FT dbSNP:rs150829393)"
FT /evidence="ECO:0000269|PubMed:20531441"
FT /id="VAR_064583"
SQ SEQUENCE 1267 AA; 137528 MW; 5BD1CF586BB30E53 CRC64;
MGDMKTPDFD DLLAAFDIPD PTSLDAKEAI QTPSEENESP LKPPGICMDE SVSLSHSGSA
PDVPAVSVIV KNTSRQESFE AEKDHITPSL LHNGFRGSDL PPDPHNCGKF DSTFMNGDSA
RSFPGKLEPP KSEPLPTFNQ FSPISSPEPE DPIKDNGFGI KPKHSDSYFP PPLGCGAVGG
PVLEALAKFP VPELHMFDHF CKKEPKPEPL PLGSQQEHEQ SGQNTVEPHK DPDATRFFGE
ALEFNSHPSN SIGESKGLAR ELGTCSSVPP RQRLKPAHSK LSSCVAALVA LQAKRVASVT
KEDQPGHTKD LSGPTKESSK GSPKMPKSPK SPRSPLEATR KSIKPSDSPR SICSDSSSKG
SPSVAASSPP AIPKVRIKTI KTSSGEIKRT VTRILPDPDD PSKSPVGSPL GSAIAEAPSE
MPGDEVPVEE HFPEAGTNSG SPQGARKGDE SMTKASDSSS PSCSSGPRVP KGAAPGSQTG
KKQQSTALQA STLAPANLLP KAVHLANLNL VPHSVAASVT AKSSVQRRSQ PQLTQMSVPL
VHQVKKAAPL IVEVFNKVLH SSNPVPLYAP NLSPPADSRI HVPASGYCCL ECGDAFALEK
SLSQHYGRRS VHIEVLCTLC SKTLLFFNKC SLLRHARDHK SKGLVMQCSQ LLVKPISADQ
MFVSAPVNST APAAPAPSSS PKHGLTSGSA SPPPPALPLY PDPVRLIRYS IKCLECHKQM
RDYMVLAAHF QRTTEETEGL TCQVCQMLLP NQCSFCAHQR IHAHKSPYCC PECGVLCRSA
YFQTHVKENC LHYARKVGYR CIHCGVVHLT LALLKSHIQE RHCQVFHKCA FCPMAFKTAS
STADHSATQH PTQPHRPSQL IYKCSCEMVF NKKRHIQQHF YQNVSKTQVG VFKCPECPLL
FVQKPELMQH VKSTHGVPRN VDELSSLQSS ADTSSSRPGS RVPTEPPATS VAARSSSLPS
GRWGRPEAHR RVEARPRLRN TGWTCQECQE WVPDRESYVS HMKKSHGRTL KRYPCRQCEQ
SFHTPNSLRK HIRNNHDTVK KFYTCGYCTE DSPSFPRPSL LESHISLMHG IRNPDLSQTS
KVKPPGGHSP QVNHLKRPVS GVGDAPGTSN GATVSSTKRH KSLFQCAKCS FATDSGLEFQ
SHIPQHQVDS STAQCLLCGL CYTSASSLSR HLFIVHKVRD QEEEEEEEAA AAEMAVEVAE
PEEGSGEEVP METRENGLEE CAGEPLSADP EARRLLGPAP EDDGGHNDHS QPQASQDQDS
HTLSPQV
