ZBT37_HUMAN
ID ZBT37_HUMAN Reviewed; 503 AA.
AC Q5TC79; Q5TC80; Q96M87; Q9BQ88;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Zinc finger and BTB domain-containing protein 37;
GN Name=ZBTB37;
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] (ISOFORM 3).
RC TISSUE=Testis;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5TC79-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5TC79-2; Sequence=VSP_014441, VSP_014442;
CC Name=3;
CC IsoId=Q5TC79-3; Sequence=VSP_014440;
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DR EMBL; AK057310; BAB71422.1; -; mRNA.
DR EMBL; AL136170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003116; AAH03116.1; -; mRNA.
DR EMBL; BC006315; AAH06315.1; -; mRNA.
DR CCDS; CCDS1312.1; -. [Q5TC79-2]
DR CCDS; CCDS44278.1; -. [Q5TC79-1]
DR CCDS; CCDS86033.1; -. [Q5TC79-3]
DR RefSeq; NP_001116242.1; NM_001122770.2. [Q5TC79-1]
DR RefSeq; NP_001333044.1; NM_001346115.1. [Q5TC79-3]
DR RefSeq; NP_115911.1; NM_032522.4. [Q5TC79-2]
DR RefSeq; XP_006711641.1; XM_006711578.3. [Q5TC79-1]
DR RefSeq; XP_011508364.1; XM_011510062.2. [Q5TC79-3]
DR RefSeq; XP_016858045.1; XM_017002556.1. [Q5TC79-1]
DR RefSeq; XP_016858046.1; XM_017002557.1. [Q5TC79-3]
DR RefSeq; XP_016858047.1; XM_017002558.1. [Q5TC79-3]
DR AlphaFoldDB; Q5TC79; -.
DR SMR; Q5TC79; -.
DR BioGRID; 124146; 5.
DR IntAct; Q5TC79; 3.
DR MINT; Q5TC79; -.
DR STRING; 9606.ENSP00000356674; -.
DR iPTMnet; Q5TC79; -.
DR PhosphoSitePlus; Q5TC79; -.
DR BioMuta; ZBTB37; -.
DR DMDM; 68566168; -.
DR jPOST; Q5TC79; -.
DR MassIVE; Q5TC79; -.
DR PaxDb; Q5TC79; -.
DR PeptideAtlas; Q5TC79; -.
DR PRIDE; Q5TC79; -.
DR ProteomicsDB; 64940; -. [Q5TC79-1]
DR ProteomicsDB; 64941; -. [Q5TC79-2]
DR ProteomicsDB; 64942; -. [Q5TC79-3]
DR Antibodypedia; 20565; 73 antibodies from 19 providers.
DR DNASU; 84614; -.
DR Ensembl; ENST00000367701.9; ENSP00000356674.4; ENSG00000185278.15. [Q5TC79-1]
DR Ensembl; ENST00000367702.1; ENSP00000356675.1; ENSG00000185278.15. [Q5TC79-2]
DR Ensembl; ENST00000367704.5; ENSP00000356677.1; ENSG00000185278.15. [Q5TC79-3]
DR Ensembl; ENST00000427304.5; ENSP00000415293.1; ENSG00000185278.15. [Q5TC79-1]
DR GeneID; 84614; -.
DR KEGG; hsa:84614; -.
DR MANE-Select; ENST00000367701.10; ENSP00000356674.4; NM_001122770.3; NP_001116242.1.
DR UCSC; uc001gjp.1; human. [Q5TC79-1]
DR CTD; 84614; -.
DR DisGeNET; 84614; -.
DR GeneCards; ZBTB37; -.
DR HGNC; HGNC:28365; ZBTB37.
DR HPA; ENSG00000185278; Tissue enhanced (brain).
DR neXtProt; NX_Q5TC79; -.
DR OpenTargets; ENSG00000185278; -.
DR PharmGKB; PA134911383; -.
DR VEuPathDB; HostDB:ENSG00000185278; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159554; -.
DR HOGENOM; CLU_903017_0_0_1; -.
DR InParanoid; Q5TC79; -.
DR OMA; TERMEDW; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q5TC79; -.
DR TreeFam; TF331184; -.
DR PathwayCommons; Q5TC79; -.
DR SignaLink; Q5TC79; -.
DR BioGRID-ORCS; 84614; 8 hits in 1136 CRISPR screens.
DR GenomeRNAi; 84614; -.
DR Pharos; Q5TC79; Tdark.
DR PRO; PR:Q5TC79; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5TC79; protein.
DR Bgee; ENSG00000185278; Expressed in sperm and 166 other tissues.
DR Genevisible; Q5TC79; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
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; 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: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; 2.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..503
FT /note="Zinc finger and BTB domain-containing protein 37"
FT /id="PRO_0000047741"
FT DOMAIN 32..96
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 373..395
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 401..423
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 429..452
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 140..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 309..503
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014440"
FT VAR_SEQ 343..361
FT /note="EESAMMGVSGYVEYLREQE -> WSCGFRTALVVGGIATVYE (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014441"
FT VAR_SEQ 362..503
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014442"
FT CONFLICT 153
FT /note="H -> R (in Ref. 1; BAB71422)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 56055 MW; 169ECA3DBB556A7B CRC64;
MEKGGNIQLE IPDFSNSVLS HLNQLRMQGR LCDIVVNVQG QAFRAHKVVL AASSPYFRDH
MSLNEMSTVS ISVIKNPTVF EQLLSFCYTG RICLQLADII SYLTAASFLQ MQHIIDKCTQ
ILEGIHFKIN VAEVEAELSQ TRTKHQERPP ESHRVTPNLN RSLSPRHNTP KGNRRGQVSA
VLDIRELSPP EESTSPQIIE PSSDVESREP ILRINRAGQW YVETGVADRG GRSDDEVRVL
GAVHIKTENL EEWLGPENQP SGEDGSSAEE VTAMVIDTTG HGSVGQENYT LGSSGAKVAR
PTSSEVDRFS PSGSVVPLTE RHRARSESPG RMDEPKQPSS QVEESAMMGV SGYVEYLREQ
EVSERWFRYN PRLTCIYCAK SFNQKGSLDR HMRLHMGITP FVCRMCGKKY TRKDQLEYHI
RKHTGNKPFH CHVCGKSFPF QAILNQHFRK NHPGCIPLEG PHSISPETTV TSRGQAEEES
PSQEETVAPG EAVQGSVSTT GPD
