BTB2_SCHPO
ID BTB2_SCHPO Reviewed; 284 AA.
AC O74778;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=BTB/POZ domain-containing protein 2;
GN Name=btb2; ORFNames=SPBC25B2.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP INTERACTION WITH CUL3.
RX PubMed=14527422; DOI=10.1016/s1097-2765(03)00341-1;
RA Geyer R., Wee S., Anderson S., Yates J. III, Wolf D.A.;
RT "BTB/POZ domain proteins are putative substrate adaptors for cullin 3
RT ubiquitin ligases.";
RL Mol. Cell 12:783-790(2003).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with cul3. {ECO:0000269|PubMed:14527422}.
CC -!- INTERACTION:
CC O74778; Q09760: cul3; NbExp=2; IntAct=EBI-3648173, EBI-3647930;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329671; CAA21264.1; -; Genomic_DNA.
DR PIR; T39982; T39982.
DR RefSeq; NP_596074.1; NM_001021986.2.
DR AlphaFoldDB; O74778; -.
DR SMR; O74778; -.
DR BioGRID; 277073; 16.
DR IntAct; O74778; 2.
DR STRING; 4896.SPBC25B2.06c.1; -.
DR MaxQB; O74778; -.
DR PaxDb; O74778; -.
DR EnsemblFungi; SPBC25B2.06c.1; SPBC25B2.06c.1:pep; SPBC25B2.06c.
DR GeneID; 2540546; -.
DR KEGG; spo:SPBC25B2.06c; -.
DR PomBase; SPBC25B2.06c; btb2.
DR VEuPathDB; FungiDB:SPBC25B2.06c; -.
DR eggNOG; ENOG502QUCE; Eukaryota.
DR HOGENOM; CLU_1019987_0_0_1; -.
DR InParanoid; O74778; -.
DR OMA; GFQTGNY; -.
DR PhylomeDB; O74778; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O74778; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000151; C:ubiquitin ligase complex; IPI:PomBase.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISM:PomBase.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..284
FT /note="BTB/POZ domain-containing protein 2"
FT /id="PRO_0000278358"
FT DOMAIN 37..108
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
SQ SEQUENCE 284 AA; 31776 MW; DE50CC8EACBF0AA7 CRC64;
MSMNSSTEIS QEPSIMKPVS SISSFVFNAG FLQGTFSDTT LIIKGETYHL HALFLGRSPV
LLQKLIENNP KGDVHYTIEV ETEDPYVTKE SCLFVLSTLY CDSPRIPAEV NVCSVLAVSD
LLGLDTLAFE ASSLIEKSIR PETMESVIRF LDPNFEGLER LKMGMYPRFT SGLFNKAIQV
MYNTLVSNWN TEYARLLCNL PFEVIKDLLE SDKLTVGASS MARYKLANEI VKMRASFRKQ
NHIEGKGDES VVLAFDEGSR GIQLVHIAPG AESRRKIWKA TSVR
