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KBTB8_MOUSE
ID   KBTB8_MOUSE             Reviewed;         599 AA.
AC   Q3UQV5; Q3TJB2; Q5M7B2; Q8CH97;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Kelch repeat and BTB domain-containing protein 8;
GN   Name=Kbtbd8; Synonyms=Kiaa1842;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Liver;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-599 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic germ cell;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-599 (ISOFORMS 1/2).
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT   complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT   screening of terminal sequences of cDNA clones randomly sampled from size-
RT   fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=26399832; DOI=10.1038/nature14978;
RA   Werner A., Iwasaki S., McGourty C.A., Medina-Ruiz S., Teerikorpi N.,
RA   Fedrigo I., Ingolia N.T., Rape M.;
RT   "Cell-fate determination by ubiquitin-dependent regulation of
RT   translation.";
RL   Nature 525:523-527(2015).
CC   -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC       ubiquitin ligase complex that acts as a regulator of neural crest
CC       specification. The BCR(KBTBD8) complex acts by mediating
CC       monoubiquitination of NOLC1 and TCOF1: monoubiquitination promotes the
CC       formation of a NOLC1-TCOF1 complex that acts as a platform to connect
CC       RNA polymerase I with enzymes responsible for ribosomal processing and
CC       modification, leading to remodel the translational program of
CC       differentiating cells in favor of neural crest specification.
CC       {ECO:0000250|UniProtKB:Q8NFY9}.
CC   -!- SUBUNIT: Component of the BCR(KBTBD8) E3 ubiquitin ligase complex, at
CC       least composed of CUL3, KBTBD8 and RBX1.
CC       {ECO:0000250|UniProtKB:Q8NFY9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250|UniProtKB:Q8NFY9}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:Q8NFY9}. Note=Translocates to the spindle
CC       apparatus during mitosis. {ECO:0000250|UniProtKB:Q8NFY9}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UQV5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UQV5-2; Sequence=VSP_023186;
CC   -!- DEVELOPMENTAL STAGE: Down-regulated in differentiating embryonic stem
CC       cells (ESCs). {ECO:0000269|PubMed:26399832}.
CC   -!- SIMILARITY: Belongs to the KBTBD8 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH88734.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK142080; BAE24933.1; -; mRNA.
DR   EMBL; AK167507; BAE39583.1; -; mRNA.
DR   EMBL; BC088734; AAH88734.1; ALT_INIT; mRNA.
DR   EMBL; AB093302; BAC41484.1; -; mRNA.
DR   CCDS; CCDS51856.1; -. [Q3UQV5-1]
DR   CCDS; CCDS51857.1; -. [Q3UQV5-2]
DR   RefSeq; NP_001008785.2; NM_001008785.5. [Q3UQV5-1]
DR   RefSeq; NP_001096140.1; NM_001102670.2. [Q3UQV5-2]
DR   AlphaFoldDB; Q3UQV5; -.
DR   SMR; Q3UQV5; -.
DR   BioGRID; 232538; 8.
DR   STRING; 10090.ENSMUSP00000032107; -.
DR   iPTMnet; Q3UQV5; -.
DR   PhosphoSitePlus; Q3UQV5; -.
DR   EPD; Q3UQV5; -.
DR   MaxQB; Q3UQV5; -.
DR   PaxDb; Q3UQV5; -.
DR   PeptideAtlas; Q3UQV5; -.
DR   PRIDE; Q3UQV5; -.
DR   ProteomicsDB; 263480; -. [Q3UQV5-1]
DR   ProteomicsDB; 263481; -. [Q3UQV5-2]
DR   Antibodypedia; 51228; 70 antibodies from 15 providers.
DR   Ensembl; ENSMUST00000032107; ENSMUSP00000032107; ENSMUSG00000030031. [Q3UQV5-1]
DR   Ensembl; ENSMUST00000119582; ENSMUSP00000113739; ENSMUSG00000030031. [Q3UQV5-2]
DR   GeneID; 243574; -.
DR   KEGG; mmu:243574; -.
DR   UCSC; uc009czw.3; mouse. [Q3UQV5-1]
DR   CTD; 84541; -.
DR   MGI; MGI:2661430; Kbtbd8.
DR   VEuPathDB; HostDB:ENSMUSG00000030031; -.
DR   eggNOG; KOG4441; Eukaryota.
DR   GeneTree; ENSGT00940000158653; -.
DR   HOGENOM; CLU_004253_14_6_1; -.
DR   InParanoid; Q3UQV5; -.
DR   OMA; AAVYNDS; -.
DR   OrthoDB; 398028at2759; -.
DR   PhylomeDB; Q3UQV5; -.
DR   TreeFam; TF332672; -.
DR   Reactome; R-MMU-8951664; Neddylation.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   BioGRID-ORCS; 243574; 0 hits in 73 CRISPR screens.
DR   PRO; PR:Q3UQV5; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q3UQV5; protein.
DR   Bgee; ENSMUSG00000030031; Expressed in secondary oocyte and 199 other tissues.
DR   ExpressionAtlas; Q3UQV5; baseline and differential.
DR   Genevisible; Q3UQV5; MM.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0014032; P:neural crest cell development; ISS:UniProtKB.
DR   GO; GO:0014029; P:neural crest formation; ISS:UniProtKB.
DR   GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.80; -; 1.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR011705; BACK.
DR   InterPro; IPR017096; BTB-kelch_protein.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR028764; KBTBD8.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   PANTHER; PTHR24412:SF433; PTHR24412:SF433; 1.
DR   Pfam; PF07707; BACK; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF01344; Kelch_1; 3.
DR   PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR   SMART; SM00875; BACK; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00612; Kelch; 3.
DR   SUPFAM; SSF117281; SSF117281; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW   Kelch repeat; Reference proteome; Repeat; Translation regulation;
KW   Ubl conjugation pathway.
FT   CHAIN           1..599
FT                   /note="Kelch repeat and BTB domain-containing protein 8"
FT                   /id="PRO_0000278221"
FT   DOMAIN          49..117
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          152..254
FT                   /note="BACK"
FT   REPEAT          334..388
FT                   /note="Kelch 1"
FT   REPEAT          389..439
FT                   /note="Kelch 2"
FT   REPEAT          441..479
FT                   /note="Kelch 3"
FT   REPEAT          481..530
FT                   /note="Kelch 4"
FT   REPEAT          540..586
FT                   /note="Kelch 5"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..77
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_023186"
FT   CONFLICT        420
FT                   /note="M -> V (in Ref. 1; BAE39583)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   599 AA;  68660 MW;  822093A49ECF9960 CRC64;
     MAASADLSKS SPTPNGIPSS DTANDTMDPF HACSILKQLK TMYDEGQLTD IVVEVDHGKT
     FSCHRNVLAA ISPYFRSMFT SGLTESTQKE VRIIGVEAES MDLVLNYAYT SRVILTEANV
     QALFTTASIF QIPSIQDQCA KYMISHLDPQ NSIGVFIFAD HYGHQELGDR SKEYIRKKFL
     CVTKEQEFLQ LTKDQLISIL DSDDLNVDRE EHVYESIIRW FEHEQSEREV HLPEIFAKCI
     RFPLMEDTFI EKIPPQFAQA IVKSCGEPSN TSGCTQRLGM TASEMIICFD AAHKHSGKKQ
     TVPCLDIVTG RVFKLCKPPN DLREVGILVS PDNDIYIAGG YRPSSSEVSI DHKAENDFWM
     YDHSTNRWLS KPSLLRARIG CKLVYCCGKM YAIGGRVYEG DGRNSLKSVE CYDSRENCWM
     TVCAMPVAME FHNAVEHKEK IYVLQGEFFL FYEPQKDYWG FLTPMTVPRI QGLAAVYKDS
     IYYIAGTCGN HQRVFTVEAY DIELNKWTRK KDFPCDQSIN PYLKLVLFQN KLHLFVRATQ
     VTVEEHIFRT SRKNSLYQYD DIADQWMKVY ETPDRLWDLG RHFECAVAKL YPQCLQKVL
 
 
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