ZBTB5_HUMAN
ID ZBTB5_HUMAN Reviewed; 677 AA.
AC O15062;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Zinc finger and BTB domain-containing protein 5;
GN Name=ZBTB5; Synonyms=KIAA0354;
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].
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371, AND IDENTIFICATION BY
RP 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-371, 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 [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-404, 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 [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-239; LYS-322; LYS-330; LYS-404;
RP LYS-415; LYS-541; LYS-594; LYS-597; LYS-645 AND LYS-658, 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: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC O15062; O95429: BAG4; NbExp=3; IntAct=EBI-722671, EBI-2949658;
CC O15062; O43602: DCX; NbExp=3; IntAct=EBI-722671, EBI-8646694;
CC O15062; O43602-2: DCX; NbExp=3; IntAct=EBI-722671, EBI-14148644;
CC O15062; Q9NRN9: METTL5; NbExp=3; IntAct=EBI-722671, EBI-12360031;
CC O15062; Q9UH65: SWAP70; NbExp=3; IntAct=EBI-722671, EBI-310749;
CC O15062; O15156: ZBTB7B; NbExp=3; IntAct=EBI-722671, EBI-740434;
CC O15062; O15156-2: ZBTB7B; NbExp=3; IntAct=EBI-722671, EBI-11522250;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20811.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB002352; BAA20811.2; ALT_INIT; mRNA.
DR EMBL; BC010007; AAH10007.1; -; mRNA.
DR CCDS; CCDS6610.1; -.
DR RefSeq; NP_055687.1; NM_014872.2.
DR RefSeq; XP_005251691.1; XM_005251634.1.
DR AlphaFoldDB; O15062; -.
DR SMR; O15062; -.
DR BioGRID; 115253; 47.
DR DIP; DIP-41566N; -.
DR IntAct; O15062; 26.
DR MINT; O15062; -.
DR STRING; 9606.ENSP00000307604; -.
DR iPTMnet; O15062; -.
DR PhosphoSitePlus; O15062; -.
DR BioMuta; ZBTB5; -.
DR EPD; O15062; -.
DR jPOST; O15062; -.
DR MassIVE; O15062; -.
DR PaxDb; O15062; -.
DR PeptideAtlas; O15062; -.
DR PRIDE; O15062; -.
DR ProteomicsDB; 48414; -.
DR Antibodypedia; 26273; 145 antibodies from 24 providers.
DR DNASU; 9925; -.
DR Ensembl; ENST00000307750.5; ENSP00000307604.4; ENSG00000168795.5.
DR GeneID; 9925; -.
DR KEGG; hsa:9925; -.
DR MANE-Select; ENST00000307750.5; ENSP00000307604.4; NM_014872.3; NP_055687.1.
DR CTD; 9925; -.
DR DisGeNET; 9925; -.
DR GeneCards; ZBTB5; -.
DR HGNC; HGNC:23836; ZBTB5.
DR HPA; ENSG00000168795; Low tissue specificity.
DR MIM; 616590; gene.
DR neXtProt; NX_O15062; -.
DR OpenTargets; ENSG00000168795; -.
DR PharmGKB; PA134969268; -.
DR VEuPathDB; HostDB:ENSG00000168795; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160246; -.
DR HOGENOM; CLU_407055_0_0_1; -.
DR InParanoid; O15062; -.
DR OMA; EKDHMRV; -.
DR OrthoDB; 339939at2759; -.
DR PhylomeDB; O15062; -.
DR TreeFam; TF330979; -.
DR PathwayCommons; O15062; -.
DR SignaLink; O15062; -.
DR BioGRID-ORCS; 9925; 11 hits in 1119 CRISPR screens.
DR ChiTaRS; ZBTB5; human.
DR GenomeRNAi; 9925; -.
DR Pharos; O15062; Tbio.
DR PRO; PR:O15062; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O15062; protein.
DR Bgee; ENSG00000168795; Expressed in esophagus squamous epithelium and 178 other tissues.
DR ExpressionAtlas; O15062; baseline and differential.
DR Genevisible; O15062; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
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; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
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..677
FT /note="Zinc finger and BTB domain-containing protein 5"
FT /id="PRO_0000047713"
FT DOMAIN 24..93
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 613..635
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 641..664
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 158..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 322
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 330
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 404
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 415
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 541
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 594
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 597
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 645
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 658
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 300
FT /note="D -> G (in dbSNP:rs17502738)"
FT /id="VAR_052915"
SQ SEQUENCE 677 AA; 74278 MW; 0F17A0AEE3FD827B CRC64;
MDFPGHFEQI FQQLNYQRLH GQLCDCVIVV GNRHFKAHRS VLAACSTHFR ALFSVAEGDQ
TMNMIQLDSE VVTAEAFAAL IDMMYTSTLM LGESNVMDVL LAASHLHLNS VVKACKHYLT
TRTLPMSPPS ERVQEQSARM QRSFMLQQLG LSIVSSALNS SQNGEEQPAP MSSSMRSNLD
QRTPFPMRRL HKRKQSAEER ARQRLRPSID ESAISDVTPE NGPSGVHSRE EFFSPDSLKI
VDNPKADGMT DNQEDSAIMF DQSFGTQEDA QVPSQSDNSA GNMAQLSMAS RATQVETSFD
QEAAPEKSSF QCENPEVGLG EKEHMRVVVK SEPLSSPEPQ DEVSDVTSQA EGSESVEVEG
VVVSAEKIDL SPESSDRSFS DPQSSTDRVG DIHILEVTNN LEHKSTFSIS NFLNKSRGNN
FTANQNNDDN IPNTTSDCRL ESEAPYLLSP EAGPAGGPSS APGSHVENPF SEPADSHFVR
PMQEVMGLPC VQTSGYQGGE QFGMDFSRSG LGLHSSFSRV MIGSPRGGAS NFPYYRRIAP
KMPVVTSVRS SQIPENSTSS QLMMNGATSS FENGHPSQPG PPQLTRASAD VLSKCKKALS
EHNVLVVEGA RKYACKICCK TFLTLTDCKK HIRVHTGEKP YACLKCGKRF SQSSHLYKHS
KTTCLRWQSS NLPSTLL
