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ZBT45_HUMAN
ID   ZBT45_HUMAN             Reviewed;         511 AA.
AC   Q96K62;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 45;
DE   AltName: Full=Zinc finger protein 499;
GN   Name=ZBTB45; Synonyms=ZNF499;
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=Mammary gland;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cervix;
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).
CC   -!- FUNCTION: May be involved in transcriptional regulation (Probable). In
CC       the central nervous system, may play a role in glial cell
CC       differentiation (By similarity). {ECO:0000250|UniProtKB:Q52KG4,
CC       ECO:0000305}.
CC   -!- INTERACTION:
CC       Q96K62; O95429: BAG4; NbExp=3; IntAct=EBI-714373, EBI-2949658;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AK027392; BAB55079.1; -; mRNA.
DR   EMBL; BC024738; AAH24738.1; -; mRNA.
DR   CCDS; CCDS12984.1; -.
DR   RefSeq; NP_001303907.1; NM_001316978.1.
DR   RefSeq; NP_001303908.1; NM_001316979.1.
DR   RefSeq; NP_001303909.1; NM_001316980.1.
DR   RefSeq; NP_001303910.1; NM_001316981.1.
DR   RefSeq; NP_001303911.1; NM_001316982.1.
DR   RefSeq; NP_116181.1; NM_032792.3.
DR   RefSeq; XP_006723508.1; XM_006723445.3.
DR   AlphaFoldDB; Q96K62; -.
DR   SMR; Q96K62; -.
DR   BioGRID; 124322; 6.
DR   DIP; DIP-62048N; -.
DR   IntAct; Q96K62; 4.
DR   STRING; 9606.ENSP00000469089; -.
DR   iPTMnet; Q96K62; -.
DR   PhosphoSitePlus; Q96K62; -.
DR   BioMuta; ZBTB45; -.
DR   DMDM; 45477325; -.
DR   EPD; Q96K62; -.
DR   jPOST; Q96K62; -.
DR   MassIVE; Q96K62; -.
DR   PaxDb; Q96K62; -.
DR   PeptideAtlas; Q96K62; -.
DR   PRIDE; Q96K62; -.
DR   ProteomicsDB; 77044; -.
DR   Antibodypedia; 19698; 78 antibodies from 20 providers.
DR   DNASU; 84878; -.
DR   Ensembl; ENST00000354590.7; ENSP00000346603.2; ENSG00000119574.13.
DR   Ensembl; ENST00000594051.6; ENSP00000469089.1; ENSG00000119574.13.
DR   Ensembl; ENST00000600990.1; ENSP00000473072.1; ENSG00000119574.13.
DR   GeneID; 84878; -.
DR   KEGG; hsa:84878; -.
DR   MANE-Select; ENST00000594051.6; ENSP00000469089.1; NM_001316979.2; NP_001303908.1.
DR   UCSC; uc002qtd.3; human.
DR   CTD; 84878; -.
DR   DisGeNET; 84878; -.
DR   GeneCards; ZBTB45; -.
DR   HGNC; HGNC:23715; ZBTB45.
DR   HPA; ENSG00000119574; Low tissue specificity.
DR   neXtProt; NX_Q96K62; -.
DR   OpenTargets; ENSG00000119574; -.
DR   PharmGKB; PA162409464; -.
DR   VEuPathDB; HostDB:ENSG00000119574; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000160859; -.
DR   HOGENOM; CLU_019055_1_0_1; -.
DR   InParanoid; Q96K62; -.
DR   OMA; THTAWKG; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q96K62; -.
DR   TreeFam; TF335684; -.
DR   PathwayCommons; Q96K62; -.
DR   SignaLink; Q96K62; -.
DR   BioGRID-ORCS; 84878; 31 hits in 1135 CRISPR screens.
DR   ChiTaRS; ZBTB45; human.
DR   GenomeRNAi; 84878; -.
DR   Pharos; Q96K62; Tdark.
DR   PRO; PR:Q96K62; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q96K62; protein.
DR   Bgee; ENSG00000119574; Expressed in parotid gland and 134 other tissues.
DR   ExpressionAtlas; Q96K62; baseline and differential.
DR   Genevisible; Q96K62; HS.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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   Pfam; PF00096; zf-C2H2; 4.
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   DNA-binding; Metal-binding; Neurogenesis; Nucleus; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..511
FT                   /note="Zinc finger and BTB domain-containing protein 45"
FT                   /id="PRO_0000047619"
FT   DOMAIN          33..96
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         403..425
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         431..453
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         459..481
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         486..508
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          159..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..224
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..364
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         293
FT                   /note="D -> E (in dbSNP:rs35430780)"
FT                   /id="VAR_052924"
SQ   SEQUENCE   511 AA;  54008 MW;  6E691746C51CB988 CRC64;
     MAAAEAVHHI HLQNFSRSLL ETLNGQRLGG HFCDVTVRIR EASLRAHRCV LAAGSPFFQD
     KLLLGHSEIR VPPVVPAQTV RQLVEFLYSG SLVVAQGEAL QVLTAASVLR IQTVIDECTQ
     IIARARAPGT SAPTPLPTPV PPPLAPAQLR HRLRHLLAAR PPGHPGAAHS RKQRQPARLQ
     LPAPPTPAKA EGPDADPSLS AAPDDRGDED DEESDDETDG EDGEGGGPGE GQAPPSFPDC
     AAGFLTAAAD SACEEPPAPT GLADYSGAGR DFLRGAGSAE DVFPDSYVST WHDEDGAVPE
     GCPTETPVQP DCILSGSRPP GVKTPGPPVA LFPFHLGAPG PPAPPPSAPS GPAPAPPPAF
     YPTLQPEAAP STQLGEVPAP SAAPTTAPSG TPARTPGAEP PTYECSHCRK TFSSRKNYTK
     HMFIHSGEKP HQCAVCWRSF SLRDYLLKHM VTHTGVRAFQ CAVCAKRFTQ KSSLNVHMRT
     HRPERAPCPA CGKVFSHRAL LERHLAAHPA P
 
 
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