ZBT44_HUMAN
ID ZBT44_HUMAN Reviewed; 570 AA.
AC Q8NCP5; Q6IPT8; Q86VJ7; Q86XX5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Zinc finger and BTB domain-containing protein 44;
DE AltName: Full=BTB/POZ domain-containing protein 15;
DE AltName: Full=Zinc finger protein 851;
GN Name=ZBTB44; Synonyms=BTBD15, ZNF851;
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] (ISOFORMS 1; 2; 3 AND 4), AND
RP VARIANT GLU-185.
RC TISSUE=Brain, Liver, and Testis;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY
RP 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-194, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY
RP 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161 AND SER-194, 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 [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-290, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4, AND IDENTIFICATION BY MASS
RP 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: May be involved in transcriptional regulation. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8NCP5; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-5658292, EBI-541426;
CC Q8NCP5; Q86V42: FAM124A; NbExp=3; IntAct=EBI-5658292, EBI-744506;
CC Q8NCP5; O76003: GLRX3; NbExp=3; IntAct=EBI-5658292, EBI-374781;
CC Q8NCP5; Q9UNA4: POLI; NbExp=3; IntAct=EBI-5658292, EBI-741774;
CC Q8NCP5; P60900: PSMA6; NbExp=3; IntAct=EBI-5658292, EBI-357793;
CC Q8NCP5; P54725: RAD23A; NbExp=3; IntAct=EBI-5658292, EBI-746453;
CC Q8NCP5; Q8NB12: SMYD1; NbExp=5; IntAct=EBI-5658292, EBI-8463848;
CC Q8NCP5; Q8IZQ1-2: WDFY3; NbExp=3; IntAct=EBI-5658292, EBI-10264625;
CC Q8NCP5-3; P40337-2: VHL; NbExp=3; IntAct=EBI-25895743, EBI-12157263;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8NCP5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NCP5-2; Sequence=VSP_022834;
CC Name=3;
CC IsoId=Q8NCP5-3; Sequence=VSP_022836, VSP_022837;
CC Name=4;
CC IsoId=Q8NCP5-4; Sequence=VSP_022835;
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DR EMBL; BC030580; AAH30580.1; -; mRNA.
DR EMBL; BC049375; AAH49375.1; -; mRNA.
DR EMBL; BC050723; AAH50723.1; -; mRNA.
DR EMBL; BC071729; AAH71729.1; -; mRNA.
DR CCDS; CCDS44776.1; -. [Q8NCP5-3]
DR CCDS; CCDS73414.1; -. [Q8NCP5-1]
DR CCDS; CCDS73415.1; -. [Q8NCP5-2]
DR RefSeq; NP_001288027.1; NM_001301098.1.
DR RefSeq; NP_001288028.1; NM_001301099.1. [Q8NCP5-2]
DR RefSeq; NP_054874.3; NM_014155.4. [Q8NCP5-3]
DR RefSeq; XP_016873112.1; XM_017017623.1.
DR AlphaFoldDB; Q8NCP5; -.
DR SMR; Q8NCP5; -.
DR BioGRID; 118842; 63.
DR IntAct; Q8NCP5; 26.
DR MINT; Q8NCP5; -.
DR STRING; 9606.ENSP00000380861; -.
DR iPTMnet; Q8NCP5; -.
DR PhosphoSitePlus; Q8NCP5; -.
DR BioMuta; ZBTB44; -.
DR DMDM; 74760158; -.
DR EPD; Q8NCP5; -.
DR jPOST; Q8NCP5; -.
DR MassIVE; Q8NCP5; -.
DR MaxQB; Q8NCP5; -.
DR PaxDb; Q8NCP5; -.
DR PeptideAtlas; Q8NCP5; -.
DR PRIDE; Q8NCP5; -.
DR ProteomicsDB; 72915; -. [Q8NCP5-1]
DR ProteomicsDB; 72916; -. [Q8NCP5-2]
DR ProteomicsDB; 72917; -. [Q8NCP5-3]
DR ProteomicsDB; 72918; -. [Q8NCP5-4]
DR Antibodypedia; 33097; 169 antibodies from 24 providers.
DR DNASU; 29068; -.
DR Ensembl; ENST00000445008.6; ENSP00000408079.1; ENSG00000196323.14. [Q8NCP5-4]
DR Ensembl; ENST00000525842.5; ENSP00000433457.1; ENSG00000196323.14. [Q8NCP5-3]
DR Ensembl; ENST00000530205.5; ENSP00000434177.1; ENSG00000196323.14. [Q8NCP5-2]
DR GeneID; 29068; -.
DR KEGG; hsa:29068; -.
DR UCSC; uc001qfz.4; human. [Q8NCP5-1]
DR CTD; 29068; -.
DR DisGeNET; 29068; -.
DR GeneCards; ZBTB44; -.
DR HGNC; HGNC:25001; ZBTB44.
DR HPA; ENSG00000196323; Low tissue specificity.
DR neXtProt; NX_Q8NCP5; -.
DR OpenTargets; ENSG00000196323; -.
DR PharmGKB; PA162409447; -.
DR VEuPathDB; HostDB:ENSG00000196323; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000153306; -.
DR HOGENOM; CLU_034849_1_0_1; -.
DR InParanoid; Q8NCP5; -.
DR PhylomeDB; Q8NCP5; -.
DR TreeFam; TF332673; -.
DR PathwayCommons; Q8NCP5; -.
DR SignaLink; Q8NCP5; -.
DR BioGRID-ORCS; 29068; 12 hits in 1136 CRISPR screens.
DR ChiTaRS; ZBTB44; human.
DR GenomeRNAi; 29068; -.
DR Pharos; Q8NCP5; Tdark.
DR PRO; PR:Q8NCP5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8NCP5; protein.
DR Bgee; ENSG00000196323; Expressed in sperm and 191 other tissues.
DR ExpressionAtlas; Q8NCP5; baseline and differential.
DR Genevisible; Q8NCP5; 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 Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..570
FT /note="Zinc finger and BTB domain-containing protein 44"
FT /id="PRO_0000274608"
FT DOMAIN 31..98
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 399..421
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 427..449
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 455..479
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 487..511
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 194..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0A2"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0A2"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 200
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0A2"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 290
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364"
FT VAR_SEQ 451..570
FT /note="GKRCFRCQICSATFTSFGEYKHHMRVSRHIIRKPRIYECKTCGAMLTNSGNL
FT IVHLRSLNHEASELANYFQSSDFLVPDYLNQEQEETLVQYDLGEHGFESNSSVQMPVIS
FT QYHSKGKEP -> VPLQRQGTMIDNSQAVDEMTRNGE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022834"
FT VAR_SEQ 451..570
FT /note="GKRCFRCQICSATFTSFGEYKHHMRVSRHIIRKPRIYECKTCGAMLTNSGNL
FT IVHLRSLNHEASELANYFQSSDFLVPDYLNQEQEETLVQYDLGEHGFESNSSVQMPVIS
FT QYHSKGKEP -> GHPRKSASRSSSATNCC (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022835"
FT VAR_SEQ 451..558
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022836"
FT VAR_SEQ 562..570
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022837"
FT VARIANT 185
FT /note="K -> E (in dbSNP:rs17857365)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030336"
SQ SEQUENCE 570 AA; 63848 MW; 9C0E64DB7D0343DF CRC64;
MGVKTFTHSS SSHSQEMLGK LNMLRNDGHF CDITIRVQDK IFRAHKVVLA ACSDFFRTKL
VGQAEDENKN VLDLHHVTVT GFIPLLEYAY TATLSINTEN IIDVLAAASY MQMFSVASTC
SEFMKSSILW NTPNSQPEKG LDAGQENNSN CNFTSRDGSI SPVSSECSVV ERTIPVCRES
RRKRKSYIVM SPESPVKCGT QTSSPQVLNS SASYSENRNQ PVDSSLAFPW TFPFGIDRRI
QPEKVKQAEN TRTLELPGPS ETGRRMADYV TCESTKTTLP LGTEEDVRVK VERLSDEEVH
EEVSQPVSAS QSSLSDQQTV PGSEQVQEDL LISPQSSSIG SVDEGVSEGL PTLQSTSSTN
APPDDDDRLE NVQYPYQLYI APSTSSTERP SPNGPDRPFQ CPTCGVRFTR IQNLKQHMLI
HSGIKPFQCD RCGKKFTRAY SLKMHRLKHE GKRCFRCQIC SATFTSFGEY KHHMRVSRHI
IRKPRIYECK TCGAMLTNSG NLIVHLRSLN HEASELANYF QSSDFLVPDY LNQEQEETLV
QYDLGEHGFE SNSSVQMPVI SQYHSKGKEP