BTBD1_HUMAN
ID BTBD1_HUMAN Reviewed; 482 AA.
AC Q9H0C5; A6NMI8; Q9BX71; Q9NWN4;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=BTB/POZ domain-containing protein 1;
DE AltName: Full=Hepatitis C virus NS5A-transactivated protein 8;
DE Short=HCV NS5A-transactivated protein 8;
GN Name=BTBD1; Synonyms=C15orf1, NS5ATP8;
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), AND TISSUE SPECIFICITY.
RX PubMed=11179693; DOI=10.1016/s0378-1119(00)00513-8;
RA Carim-Todd L., Sumoy L., Andreu N., Estivill X., Escarceller M.;
RT "Identification and characterization of BTBD1, a novel BTB domain
RT containing gene on human chromosome 15q24.";
RL Gene 262:275-281(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TOP1, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11818025; DOI=10.1186/1471-2164-3-1;
RA Xu L., Yang L., Hashimoto K., Anderson M., Kohlhagen G., Pommier Y.,
RA D'Arpa P.;
RT "Characterization of BTBD1 and BTBD2, two similar BTB-domain-containing
RT Kelch-like proteins that interact with topoisomerase I.";
RL BMC Genomics 3:1-1(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Liu Y., Cheng J., Wang G., Wang J., Zhang L., Chen J., Li L.;
RT "Cloning and identification of human gene 8 transactivated by hepatitis C
RT virus NS5A protein.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TRIM5.
RX PubMed=12878161; DOI=10.1016/s0014-4827(03)00187-3;
RA Xu L., Yang L., Moitra P.K., Hashimoto K., Rallabhandi P., Kaul S.,
RA Meroni G., Jensen J.P., Weissman A.M., D'Arpa P.;
RT "BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite
RT motif protein, TRIM5delta.";
RL Exp. Cell Res. 288:84-93(2003).
RN [9]
RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, AND INTERACTION WITH CUL3.
RX PubMed=14528312; DOI=10.1038/ncb1056;
RA Furukawa M., He Y.J., Borchers C., Xiong Y.;
RT "Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin
RT ligases.";
RL Nat. Cell Biol. 5:1001-1007(2003).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-79, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Probable substrate-specific adapter of an E3 ubiquitin-
CC protein ligase complex which mediates the ubiquitination and subsequent
CC proteasomal degradation of target proteins (PubMed:14528312). Seems to
CC regulate expression levels and/or subnuclear distribution of TOP1, via
CC an unknown mechanism (By similarity). May play a role in mesenchymal
CC differentiation where it promotes myogenic differentiation and
CC suppresses adipogenesis (By similarity). {ECO:0000250|UniProtKB:P58544,
CC ECO:0000269|PubMed:14528312}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts (via C-terminus) with TOP1 (PubMed:11818025).
CC Interacts with TRIM5 isoform Delta (PubMed:12878161). Interacts with
CC CUL3 (PubMed:14528312). {ECO:0000269|PubMed:11818025,
CC ECO:0000269|PubMed:12878161, ECO:0000269|PubMed:14528312}.
CC -!- INTERACTION:
CC Q9H0C5; P31749: AKT1; NbExp=3; IntAct=EBI-935503, EBI-296087;
CC Q9H0C5; P23560-2: BDNF; NbExp=3; IntAct=EBI-935503, EBI-12275524;
CC Q9H0C5; Q9H0C5: BTBD1; NbExp=3; IntAct=EBI-935503, EBI-935503;
CC Q9H0C5; Q13618: CUL3; NbExp=7; IntAct=EBI-935503, EBI-456129;
CC Q9H0C5; P07900: HSP90AA1; NbExp=4; IntAct=EBI-935503, EBI-296047;
CC Q9H0C5; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-935503, EBI-739832;
CC Q9H0C5; Q13368: MPP3; NbExp=3; IntAct=EBI-935503, EBI-716157;
CC Q9H0C5; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-935503, EBI-741158;
CC Q9H0C5; Q16401: PSMD5; NbExp=3; IntAct=EBI-935503, EBI-752143;
CC Q9H0C5; P78317: RNF4; NbExp=3; IntAct=EBI-935503, EBI-2340927;
CC Q9H0C5; Q13148: TARDBP; NbExp=3; IntAct=EBI-935503, EBI-372899;
CC Q9H0C5; P03120: E2; Xeno; NbExp=3; IntAct=EBI-935503, EBI-1779322;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11818025,
CC ECO:0000269|PubMed:12878161}. Note=Localizes to punctate or elongated
CC cytoplasmic bodies. {ECO:0000269|PubMed:11818025,
CC ECO:0000269|PubMed:12878161}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H0C5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H0C5-2; Sequence=VSP_047146, VSP_047147;
CC -!- TISSUE SPECIFICITY: Ubiquitous; highest levels in testes, heart and
CC skeletal muscle. {ECO:0000269|PubMed:11179693,
CC ECO:0000269|PubMed:11818025}.
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DR EMBL; AL136853; CAB66787.1; -; mRNA.
DR EMBL; AF355402; AAK25825.1; -; mRNA.
DR EMBL; AF257241; AAK17068.1; -; mRNA.
DR EMBL; AK000731; BAA91345.1; -; mRNA.
DR EMBL; AF529369; AAQ09603.1; -; mRNA.
DR EMBL; AC022558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC024270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028097; AAH28097.1; -; mRNA.
DR CCDS; CCDS10322.1; -. [Q9H0C5-1]
DR CCDS; CCDS32313.1; -. [Q9H0C5-2]
DR RefSeq; NP_001011885.1; NM_001011885.1. [Q9H0C5-2]
DR RefSeq; NP_079514.1; NM_025238.3. [Q9H0C5-1]
DR AlphaFoldDB; Q9H0C5; -.
DR SMR; Q9H0C5; -.
DR BioGRID; 119740; 123.
DR IntAct; Q9H0C5; 67.
DR MINT; Q9H0C5; -.
DR STRING; 9606.ENSP00000261721; -.
DR iPTMnet; Q9H0C5; -.
DR PhosphoSitePlus; Q9H0C5; -.
DR BioMuta; BTBD1; -.
DR DMDM; 20137477; -.
DR EPD; Q9H0C5; -.
DR jPOST; Q9H0C5; -.
DR MassIVE; Q9H0C5; -.
DR MaxQB; Q9H0C5; -.
DR PaxDb; Q9H0C5; -.
DR PeptideAtlas; Q9H0C5; -.
DR PRIDE; Q9H0C5; -.
DR ProteomicsDB; 1542; -.
DR ProteomicsDB; 80253; -. [Q9H0C5-1]
DR TopDownProteomics; Q9H0C5-1; -. [Q9H0C5-1]
DR Antibodypedia; 28167; 182 antibodies from 27 providers.
DR DNASU; 53339; -.
DR Ensembl; ENST00000261721.9; ENSP00000261721.4; ENSG00000064726.10. [Q9H0C5-1]
DR Ensembl; ENST00000379403.2; ENSP00000368713.2; ENSG00000064726.10. [Q9H0C5-2]
DR GeneID; 53339; -.
DR KEGG; hsa:53339; -.
DR MANE-Select; ENST00000261721.9; ENSP00000261721.4; NM_025238.4; NP_079514.1.
DR UCSC; uc002bjn.4; human. [Q9H0C5-1]
DR CTD; 53339; -.
DR DisGeNET; 53339; -.
DR GeneCards; BTBD1; -.
DR HGNC; HGNC:1120; BTBD1.
DR HPA; ENSG00000064726; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 608530; gene.
DR neXtProt; NX_Q9H0C5; -.
DR OpenTargets; ENSG00000064726; -.
DR PharmGKB; PA25438; -.
DR VEuPathDB; HostDB:ENSG00000064726; -.
DR eggNOG; KOG2075; Eukaryota.
DR GeneTree; ENSGT00940000156756; -.
DR HOGENOM; CLU_015899_2_1_1; -.
DR InParanoid; Q9H0C5; -.
DR OMA; IDKNTMD; -.
DR PhylomeDB; Q9H0C5; -.
DR TreeFam; TF106482; -.
DR PathwayCommons; Q9H0C5; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9H0C5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 53339; 14 hits in 1120 CRISPR screens.
DR ChiTaRS; BTBD1; human.
DR GeneWiki; BTBD1; -.
DR GenomeRNAi; 53339; -.
DR Pharos; Q9H0C5; Tbio.
DR PRO; PR:Q9H0C5; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9H0C5; protein.
DR Bgee; ENSG00000064726; Expressed in skeletal muscle tissue of rectus abdominis and 208 other tissues.
DR ExpressionAtlas; Q9H0C5; baseline and differential.
DR Genevisible; Q9H0C5; HS.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:LIFEdb.
DR GO; GO:0097602; F:cullin family protein binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0022008; P:neurogenesis; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0043393; P:regulation of protein binding; NAS:UniProtKB.
DR Gene3D; 2.60.120.820; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR012983; PHR.
DR InterPro; IPR038648; PHR_sf.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF08005; PHR; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Differentiation; Methylation; Myogenesis;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..482
FT /note="BTB/POZ domain-containing protein 1"
FT /id="PRO_0000186208"
FT DOMAIN 69..145
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 184..284
FT /note="BACK"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 353..386
FT /note="FTVNRRISIVGFGLYGSIHGPTDYQVNIQIIEYE -> SLNMRKSKPWDRMI
FT PALVVMGQLTHSGSCSRNP (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047146"
FT VAR_SEQ 387..482
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047147"
FT CONFLICT 406
FT /note="T -> A (in Ref. 5; BAA91345)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="C -> G (in Ref. 2; AAK25825)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="L -> P (in Ref. 5; BAA91345)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 52771 MW; 525A49E01728AFF0 CRC64;
MASLGPAAAG EQASGAEAEP GPAGPPPPPS PSSLGPLLPL QREPLYNWQA TKASLKERFA
FLFNSELLSD VRFVLGKGRG AAAAGGPQRI PAHRFVLAAG SAVFDAMFNG GMATTSAEIE
LPDVEPAAFL ALLRFLYSDE VQIGPETVMT TLYTAKKYAV PALEAHCVEF LTKHLRADNA
FMLLTQARLF DEPQLASLCL DTIDKSTMDA ISAEGFTDID IDTLCAVLER DTLSIRESRL
FGAVVRWAEA ECQRQQLPVT FGNKQKVLGK ALSLIRFPLM TIEEFAAGPA QSGILSDREV
VNLFLHFTVN PKPRVEYIDR PRCCLRGKEC CINRFQQVES RWGYSGTSDR IRFTVNRRIS
IVGFGLYGSI HGPTDYQVNI QIIEYEKKQT LGQNDTGFSC DGTANTFRVM FKEPIEILPN
VCYTACATLK GPDSHYGTKG LKKVVHETPA ASKTVFFFFS SPGNNNGTSI EDGQIPEIIF
YT
