ABTB1_MOUSE
ID ABTB1_MOUSE Reviewed; 478 AA.
AC Q99LJ2; Q8C2K7; Q91XU4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Ankyrin repeat and BTB/POZ domain-containing protein 1;
GN Name=Abtb1 {ECO:0000312|MGI:MGI:1933148}; Synonyms=Bpoz;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:BAB55652.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6NJcl {ECO:0000312|EMBL:BAB55652.1};
RC TISSUE=Lung {ECO:0000312|EMBL:BAB55652.1};
RX PubMed=11494141; DOI=10.1038/sj.onc.1204608;
RA Unoki M., Nakamura Y.;
RT "Growth-suppressive effects of BPOZ and EGR2, two genes involved in the
RT PTEN signaling pathway.";
RL Oncogene 20:4457-4465(2001).
RN [2] {ECO:0000312|EMBL:BAC40352.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD {ECO:0000312|EMBL:BAC40352.1};
RC TISSUE=Thymus {ECO:0000312|EMBL:BAC40352.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|EMBL:AAH03234.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH03234.1};
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 act as a mediator of the PTEN growth-suppressive
CC signaling pathway. May play a role in developmental processes (By
CC similarity). {ECO:0000250|UniProtKB:Q969K4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q969K4}.
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DR EMBL; AB053477; BAB55652.1; -; mRNA.
DR EMBL; AK088437; BAC40352.1; -; mRNA.
DR EMBL; BC003234; AAH03234.1; -; mRNA.
DR CCDS; CCDS20339.1; -.
DR RefSeq; NP_084527.2; NM_030251.3.
DR AlphaFoldDB; Q99LJ2; -.
DR SMR; Q99LJ2; -.
DR BioGRID; 219771; 3.
DR IntAct; Q99LJ2; 3.
DR STRING; 10090.ENSMUSP00000032169; -.
DR iPTMnet; Q99LJ2; -.
DR PhosphoSitePlus; Q99LJ2; -.
DR PaxDb; Q99LJ2; -.
DR PRIDE; Q99LJ2; -.
DR ProteomicsDB; 286025; -.
DR DNASU; 80283; -.
DR GeneID; 80283; -.
DR KEGG; mmu:80283; -.
DR UCSC; uc009cvs.2; mouse.
DR CTD; 80325; -.
DR MGI; MGI:1933148; Abtb1.
DR eggNOG; KOG0511; Eukaryota.
DR InParanoid; Q99LJ2; -.
DR OrthoDB; 871743at2759; -.
DR PhylomeDB; Q99LJ2; -.
DR TreeFam; TF329194; -.
DR BioGRID-ORCS; 80283; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q99LJ2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99LJ2; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.30.710.10; -; 2.
DR InterPro; IPR044515; ABTB1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR46231; PTHR46231; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00651; BTB; 2.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00225; BTB; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF54695; SSF54695; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50097; BTB; 2.
PE 2: Evidence at transcript level;
KW ANK repeat; Coiled coil; Cytoplasm; Elongation factor;
KW Protein biosynthesis; Reference proteome; Repeat.
FT CHAIN 1..478
FT /note="Ankyrin repeat and BTB/POZ domain-containing protein
FT 1"
FT /id="PRO_0000248268"
FT REPEAT 1..31
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 35..64
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT DOMAIN 115..182
FT /note="BTB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 272..346
FT /note="BTB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT COILED 451..477
FT /evidence="ECO:0000255"
FT CONFLICT 92
FT /note="T -> A (in Ref. 2; BAC40352)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="H -> Y (in Ref. 1; BAB55652)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 54058 MW; 65AAB8C27E179553 CRC64;
MDTSDLFASC RKGDVGRVRY LLEQRDVEVN VRDKWDSTPL YYACLCGHEE LVRYLLANGA
RCEANTFDGE RCLYGALSDP IRRALRDYKQ VTASCRRRDY YDDFLQRLLE QGIHSDVVFV
VHGKPFRAHR CILGARSTYF ANMLDTKWKG KSVVVLRHPL INPVAFGALL QYLYTGRLDI
GVEHVSDCER LAKQCQLWDL LDDLEAKCEK VSEFVASKPG TCVKVLTIEP PPADPRLRAD
MALLADCALP SELRGDLGEL PFPCPDGFSS CPDICFRVAD SSFLCHKAFF CGRSDYFRAL
LDDHFQESEE PAASGDPPVV TLHDISPDIF IHVLYYVYSD HTELPPELAY DVLSVADMYL
LPGLKRLCGR SLAQLLEEDS VVGVWRIAKM FRLARLEDQC TEYMAKVIEK LVEREDFVEA
VREEAAAVAA RQETDSIPLV DDIRFHVAST VQTYSAIEEA QQRLRALEDL LVSIGLDC
