ZN148_HUMAN
ID ZN148_HUMAN Reviewed; 794 AA.
AC Q9UQR1; D3DN27; O00389; O43591; Q58EY5; Q6PJ98;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Zinc finger protein 148;
DE AltName: Full=Transcription factor ZBP-89;
DE AltName: Full=Zinc finger DNA-binding protein 89;
GN Name=ZNF148; Synonyms=ZBP89;
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 [MRNA] (ISOFORM 1).
RX PubMed=9457682; DOI=10.1007/s003359900711;
RA Law D.J., Tarle S.A., Merchant J.L.;
RT "The human ZBP-89 homolog, located at chromosome 3q21, represses gastrin
RT gene expression.";
RL Mamm. Genome 9:165-167(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10359087; DOI=10.1016/s0014-5793(99)00509-8;
RA Ye S., Whatling C., Watkins H., Henney A.;
RT "Human stromelysin gene promoter activity is modulated by transcription
RT factor ZBP-89.";
RL FEBS Lett. 450:268-272(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=B-cell, and Kidney;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 262-665.
RA Law D.J., Chen X.N., Korenberg J.R., Mortensen E.R., Merchant J.L.;
RT "The growth-regulating transcription factor ZBP-89 is located at human
RT chromosome 3q21 and mouse chromosome 8B1.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH HNRNPDL.
RX PubMed=15190078; DOI=10.1074/jbc.m403160200;
RA Boopathi E., Lenka N., Prabu S.K., Fang J.-K., Wilkinson F., Atchison M.,
RA Giallongo A., Avadhani N.G.;
RT "Regulation of murine cytochrome c oxidase Vb gene expression during
RT myogenesis: YY-1 and heterogeneous nuclear ribonucleoprotein D-like protein
RT (JKTBP1) reciprocally regulate transcription activity by physical
RT interaction with the BERF-1/ZBP-89 factor.";
RL J. Biol. Chem. 279:35242-35254(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-194; SER-250; SER-306;
RP SER-412 AND SER-784, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-784, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-607, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-665 AND SER-784, AND
RP 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-412 AND SER-665, AND
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-412, 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-356, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-356, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-356, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [20]
RP INVOLVEMENT IN GDACCF.
RX PubMed=27964749; DOI=10.1186/s13073-016-0386-9;
RA Stevens S.J., van Essen A.J., van Ravenswaaij C.M., Elias A.F., Haven J.A.,
RA Lelieveld S.H., Pfundt R., Nillesen W.M., Yntema H.G., van Roozendaal K.,
RA Stegmann A.P., Gilissen C., Brunner H.G.;
RT "Truncating de novo mutations in the Krueppel-type zinc-finger gene ZNF148
RT in patients with corpus callosum defects, developmental delay, short
RT stature, and dysmorphisms.";
RL Genome Med. 8:131-131(2016).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-88; LYS-115; LYS-132;
RP LYS-291; LYS-308; LYS-356; LYS-402; LYS-421 AND LYS-424, AND IDENTIFICATION
RP 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).
CC -!- FUNCTION: Involved in transcriptional regulation. Represses the
CC transcription of a number of genes including gastrin, stromelysin and
CC enolase. Binds to the G-rich box in the enhancer region of these genes.
CC -!- SUBUNIT: Interacts with HNRNPDL (PubMed:15190078). Interacts with the
CC 5FMC complex; the interaction requires association with CHTOP.
CC Interacts with CAVIN1 (By similarity). {ECO:0000250|UniProtKB:Q61624,
CC ECO:0000269|PubMed:15190078}.
CC -!- INTERACTION:
CC Q9UQR1; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-2688184, EBI-739624;
CC Q9UQR1; Q05D60: DEUP1; NbExp=3; IntAct=EBI-2688184, EBI-748597;
CC Q9UQR1; B7ZLH0: FAM22F; NbExp=3; IntAct=EBI-2688184, EBI-10220102;
CC Q9UQR1; O76003: GLRX3; NbExp=3; IntAct=EBI-2688184, EBI-374781;
CC Q9UQR1; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-2688184, EBI-739467;
CC Q9UQR1; Q15323: KRT31; NbExp=3; IntAct=EBI-2688184, EBI-948001;
CC Q9UQR1; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-2688184, EBI-747107;
CC Q9UQR1; Q9UDY6: TRIM10; NbExp=3; IntAct=EBI-2688184, EBI-6427325;
CC Q9UQR1-2; Q96MT8-3: CEP63; NbExp=3; IntAct=EBI-11742222, EBI-11522539;
CC Q9UQR1-2; B7ZLH0: FAM22F; NbExp=3; IntAct=EBI-11742222, EBI-10220102;
CC Q9UQR1-2; Q9H8Y8: GORASP2; NbExp=5; IntAct=EBI-11742222, EBI-739467;
CC Q9UQR1-2; Q6IE81-3: JADE1; NbExp=3; IntAct=EBI-11742222, EBI-12120084;
CC Q9UQR1-2; O76011: KRT34; NbExp=3; IntAct=EBI-11742222, EBI-1047093;
CC Q9UQR1-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-11742222, EBI-739832;
CC Q9UQR1-2; Q99471: PFDN5; NbExp=3; IntAct=EBI-11742222, EBI-357275;
CC Q9UQR1-2; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-11742222, EBI-949255;
CC Q9UQR1-2; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-11742222, EBI-302345;
CC Q9UQR1-2; P78424: POU6F2; NbExp=3; IntAct=EBI-11742222, EBI-12029004;
CC Q9UQR1-2; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-11742222, EBI-11975223;
CC Q9UQR1-2; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-11742222, EBI-12030590;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UQR1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UQR1-2; Sequence=VSP_055938, VSP_055939;
CC -!- PTM: Sumoylated with SUMO2. Desumoylated by SENP3, resulting in the
CC stimulation of transcription of its target genes (By similarity).
CC {ECO:0000250}.
CC -!- DISEASE: Global developmental delay, absent or hypoplastic corpus
CC callosum, and dysmorphic facies (GDACCF) [MIM:617260]: An autosomal
CC dominant syndrome characterized by underdevelopment of the corpus
CC callosum, mild to moderate developmental delay and intellectual
CC disability, variable microcephaly or mild macrocephaly, short stature,
CC feeding problems, facial dysmorphisms, and cardiac and renal
CC malformations. {ECO:0000269|PubMed:27964749}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF039019; AAC39926.1; -; mRNA.
DR EMBL; AJ236885; CAA15422.1; -; mRNA.
DR EMBL; AC108688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79394.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79395.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79396.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79398.1; -; Genomic_DNA.
DR EMBL; BC018971; AAH18971.1; -; mRNA.
DR EMBL; BC050260; AAH50260.1; -; mRNA.
DR EMBL; U96633; AAB57692.1; -; Genomic_DNA.
DR CCDS; CCDS3031.1; -. [Q9UQR1-1]
DR RefSeq; NP_001335353.1; NM_001348424.1. [Q9UQR1-1]
DR RefSeq; NP_001335354.1; NM_001348425.1. [Q9UQR1-1]
DR RefSeq; NP_001335355.1; NM_001348426.1. [Q9UQR1-1]
DR RefSeq; NP_001335356.1; NM_001348427.1. [Q9UQR1-1]
DR RefSeq; NP_001335357.1; NM_001348428.1. [Q9UQR1-1]
DR RefSeq; NP_001335358.1; NM_001348429.1. [Q9UQR1-1]
DR RefSeq; NP_001335359.1; NM_001348430.1. [Q9UQR1-1]
DR RefSeq; NP_001335360.1; NM_001348431.1. [Q9UQR1-1]
DR RefSeq; NP_001335361.1; NM_001348432.1. [Q9UQR1-1]
DR RefSeq; NP_001335362.1; NM_001348433.1. [Q9UQR1-1]
DR RefSeq; NP_068799.2; NM_021964.2. [Q9UQR1-1]
DR AlphaFoldDB; Q9UQR1; -.
DR SMR; Q9UQR1; -.
DR BioGRID; 113501; 106.
DR IntAct; Q9UQR1; 65.
DR MINT; Q9UQR1; -.
DR STRING; 9606.ENSP00000353863; -.
DR GlyGen; Q9UQR1; 6 sites, 1 O-linked glycan (6 sites).
DR iPTMnet; Q9UQR1; -.
DR PhosphoSitePlus; Q9UQR1; -.
DR BioMuta; ZNF148; -.
DR DMDM; 12643385; -.
DR EPD; Q9UQR1; -.
DR jPOST; Q9UQR1; -.
DR MassIVE; Q9UQR1; -.
DR MaxQB; Q9UQR1; -.
DR PaxDb; Q9UQR1; -.
DR PeptideAtlas; Q9UQR1; -.
DR PRIDE; Q9UQR1; -.
DR ProteomicsDB; 67196; -.
DR ProteomicsDB; 85574; -. [Q9UQR1-1]
DR Antibodypedia; 901; 258 antibodies from 29 providers.
DR DNASU; 7707; -.
DR Ensembl; ENST00000360647.9; ENSP00000353863.4; ENSG00000163848.20. [Q9UQR1-1]
DR Ensembl; ENST00000484491.5; ENSP00000420335.1; ENSG00000163848.20. [Q9UQR1-1]
DR Ensembl; ENST00000485866.5; ENSP00000420448.1; ENSG00000163848.20. [Q9UQR1-1]
DR Ensembl; ENST00000492394.5; ENSP00000419322.1; ENSG00000163848.20. [Q9UQR1-1]
DR GeneID; 7707; -.
DR KEGG; hsa:7707; -.
DR MANE-Select; ENST00000360647.9; ENSP00000353863.4; NM_021964.3; NP_068799.2.
DR UCSC; uc003ehx.5; human. [Q9UQR1-1]
DR CTD; 7707; -.
DR DisGeNET; 7707; -.
DR GeneCards; ZNF148; -.
DR HGNC; HGNC:12933; ZNF148.
DR HPA; ENSG00000163848; Low tissue specificity.
DR MalaCards; ZNF148; -.
DR MIM; 601897; gene.
DR MIM; 617260; phenotype.
DR neXtProt; NX_Q9UQR1; -.
DR OpenTargets; ENSG00000163848; -.
DR PharmGKB; PA37520; -.
DR VEuPathDB; HostDB:ENSG00000163848; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157406; -.
DR HOGENOM; CLU_025987_1_0_1; -.
DR InParanoid; Q9UQR1; -.
DR OMA; FEQNFKS; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9UQR1; -.
DR TreeFam; TF331779; -.
DR PathwayCommons; Q9UQR1; -.
DR SignaLink; Q9UQR1; -.
DR SIGNOR; Q9UQR1; -.
DR BioGRID-ORCS; 7707; 49 hits in 1118 CRISPR screens.
DR ChiTaRS; ZNF148; human.
DR GeneWiki; ZNF148; -.
DR GenomeRNAi; 7707; -.
DR Pharos; Q9UQR1; Tbio.
DR PRO; PR:Q9UQR1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UQR1; protein.
DR Bgee; ENSG00000163848; Expressed in caput epididymis and 213 other tissues.
DR ExpressionAtlas; Q9UQR1; baseline and differential.
DR Genevisible; Q9UQR1; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR GO; GO:0007276; P:gamete generation; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA-binding; Dwarfism;
KW Intellectual disability; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..794
FT /note="Zinc finger protein 148"
FT /id="PRO_0000047427"
FT ZN_FING 171..193
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 199..221
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 227..249
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 255..278
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 298..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61624"
FT MOD_RES 194
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61624"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 607
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 88
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 291
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 308
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 356
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 356
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 402
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 421
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..205
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055938"
FT VAR_SEQ 233..690
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055939"
FT CONFLICT 287
FT /note="R -> T (in Ref. 2; CAA15422)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="L -> V (in Ref. 2; CAA15422)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="E -> K (in Ref. 6; AAB57692)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="A -> R (in Ref. 2; CAA15422)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="T -> N (in Ref. 6; AAB57692)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 794 AA; 88976 MW; 50413723459EBD1F CRC64;
MNIDDKLEGL FLKCGGIDEM QSSRTMVVMG GVSGQSTVSG ELQDSVLQDR SMPHQEILAA
DEVLQESEMR QQDMISHDEL MVHEETVKND EEQMETHERL PQGLQYALNV PISVKQEITF
TDVSEQLMRD KKQIREPVDL QKKKKRKQRS PAKILTINED GSLGLKTPKS HVCEHCNAAF
RTNYHLQRHV FIHTGEKPFQ CSQCDMRFIQ KYLLQRHEKI HTGEKPFRCD ECGMRFIQKY
HMERHKRTHS GEKPYQCEYC LQYFSRTDRV LKHKRMCHEN HDKKLNRCAI KGGLLTSEED
SGFSTSPKDN SLPKKKRQKT EKKSSGMDKE SALDKSDLKK DKNDYLPLYS SSTKVKDEYM
VAEYAVEMPH SSVGGSHLED ASGEIHPPKL VLKKINSKRS LKQPLEQNQT ISPLSTYEES
KVSKYAFELV DKQALLDSEG NADIDQVDNL QEGPSKPVHS STNYDDAMQF LKKKRYLQAA
SNNSREYALN VGTIASQPSV TQAAVASVID ESTTASILES QALNVEIKSN HDKNVIPDEV
LQTLLDHYSH KANGQHEISF SVADTEVTSS ISINSSEVPE VTPSENVGSS SQASSSDKAN
MLQEYSKFLQ QALDRTSQND AYLNSPSLNF VTDNQTLPNQ PAFSSIDKQV YATMPINSFR
SGMNSPLRTT PDKSHFGLIV GDSQHSFPFS GDETNHASAT STQDFLDQVT SQKKAEAQPV
HQAYQMSSFE QPFRAPYHGS RAGIATQFST ANGQVNLRGP GTSAEFSEFP LVNVNDNRAG
MTSSPDATTG QTFG
