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CTBL1_MOUSE
ID   CTBL1_MOUSE             Reviewed;         563 AA.
AC   Q9CWL8; Q3UL41; Q80X64; Q8VHE3;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Beta-catenin-like protein 1;
DE   AltName: Full=Nuclear-associated protein;
DE            Short=NAP;
GN   Name=Ctnnbl1;
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 [MRNA].
RX   PubMed=12659813; DOI=10.1016/s0888-7543(02)00038-1;
RA   Jabbour L.S., Welter J.F., Kollar J., Hering T.M.;
RT   "Sequence, gene structure, and expression pattern of CTNNBL1, a minor-class
RT   intron-containing gene - evidence for a role in apoptosis.";
RL   Genomics 81:292-303(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Retina;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   FUNCTION.
RX   PubMed=20585033; DOI=10.4049/jimmunol.1001643;
RA   Han L., Masani S., Yu K.;
RT   "Cutting edge: CTNNBL1 is dispensable for Ig class switch recombination.";
RL   J. Immunol. 185:1379-1381(2010).
CC   -!- FUNCTION: Component of the PRP19-CDC5L complex that forms an integral
CC       part of the spliceosome and is required for activating pre-mRNA
CC       splicing. May induce apoptosis (By similarity). Participates in
CC       AID/AICDA-mediated Ig class switching recombination (CSR).
CC       {ECO:0000250, ECO:0000269|PubMed:20585033}.
CC   -!- SUBUNIT: Component of the PRP19-CDC5L splicing complex composed of a
CC       core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and
CC       BCAS2, and at least three less stably associated proteins CTNNBL1,
CC       CWC15 and HSPA8. Interacts directly with CWC15 and CDC5L in the
CC       complex. Interacts with AICDA; the interaction is important for the
CC       antibody diversification activity of AICDA. Interacts with PRPF31 (via
CC       its NLS). Interacts (via its N-terminal NLS) with KPNA1 and KPNA2 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The surface residues of the concave side of the superhelical
CC       ARM repeat region contribute to, but are not essential for NLS binding.
CC       {ECO:0000250}.
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DR   EMBL; AY009405; AAK27389.1; -; mRNA.
DR   EMBL; AK010547; BAB27020.1; -; mRNA.
DR   EMBL; AK044690; BAC32034.1; -; mRNA.
DR   EMBL; AK077616; BAC36902.1; -; mRNA.
DR   EMBL; AK145598; BAE26532.1; -; mRNA.
DR   EMBL; AK145719; BAE26609.1; -; mRNA.
DR   EMBL; BC050787; AAH50787.1; -; mRNA.
DR   CCDS; CCDS16982.1; -.
DR   RefSeq; NP_079956.3; NM_025680.4.
DR   AlphaFoldDB; Q9CWL8; -.
DR   SMR; Q9CWL8; -.
DR   BioGRID; 211616; 31.
DR   ComplexPortal; CPX-5825; PRP19-CDC5L complex.
DR   IntAct; Q9CWL8; 13.
DR   STRING; 10090.ENSMUSP00000029178; -.
DR   iPTMnet; Q9CWL8; -.
DR   PhosphoSitePlus; Q9CWL8; -.
DR   EPD; Q9CWL8; -.
DR   jPOST; Q9CWL8; -.
DR   MaxQB; Q9CWL8; -.
DR   PaxDb; Q9CWL8; -.
DR   PeptideAtlas; Q9CWL8; -.
DR   PRIDE; Q9CWL8; -.
DR   ProteomicsDB; 277913; -.
DR   Antibodypedia; 750; 329 antibodies from 35 providers.
DR   DNASU; 66642; -.
DR   Ensembl; ENSMUST00000029178; ENSMUSP00000029178; ENSMUSG00000027649.
DR   GeneID; 66642; -.
DR   KEGG; mmu:66642; -.
DR   UCSC; uc008nph.2; mouse.
DR   CTD; 56259; -.
DR   MGI; MGI:1913892; Ctnnbl1.
DR   VEuPathDB; HostDB:ENSMUSG00000027649; -.
DR   eggNOG; KOG2734; Eukaryota.
DR   GeneTree; ENSGT00390000006931; -.
DR   HOGENOM; CLU_017098_2_1_1; -.
DR   InParanoid; Q9CWL8; -.
DR   OMA; TDWREQE; -.
DR   OrthoDB; 724270at2759; -.
DR   PhylomeDB; Q9CWL8; -.
DR   TreeFam; TF314294; -.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   BioGRID-ORCS; 66642; 23 hits in 74 CRISPR screens.
DR   ChiTaRS; Ctnnbl1; mouse.
DR   PRO; PR:Q9CWL8; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9CWL8; protein.
DR   Bgee; ENSMUSG00000027649; Expressed in ear vesicle and 252 other tissues.
DR   Genevisible; Q9CWL8; MM.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:ComplexPortal.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0016445; P:somatic diversification of immunoglobulins; ISO:MGI.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR039678; CTNNBL1.
DR   InterPro; IPR013180; CTNNBL1_N.
DR   PANTHER; PTHR14978; PTHR14978; 1.
DR   Pfam; PF08216; CTNNBL; 1.
DR   SMART; SM01156; DUF1716; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Coiled coil; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..563
FT                   /note="Beta-catenin-like protein 1"
FT                   /id="PRO_0000079491"
FT   REPEAT          79..129
FT                   /note="HEAT 1"
FT   REPEAT          134..176
FT                   /note="HEAT 2"
FT   REPEAT          178..228
FT                   /note="ARM 1"
FT   REPEAT          229..273
FT                   /note="ARM 2"
FT   REPEAT          274..323
FT                   /note="ARM 3"
FT   REPEAT          325..363
FT                   /note="ARM 4"
FT   REPEAT          364..417
FT                   /note="ARM 5"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          476..540
FT                   /evidence="ECO:0000250"
FT   MOTIF           16..33
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   MOTIF           130..140
FT                   /note="Nuclear export signal (NES)"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        14..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WYA6"
FT   MOD_RES         91
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WYA6"
FT   MOD_RES         389
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WYA6"
FT   MOD_RES         545
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WYA6"
FT   CONFLICT        121
FT                   /note="I -> V (in Ref. 2; BAC32034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="G -> C (in Ref. 3; AAH50787)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        399..400
FT                   /note="TE -> QQ (in Ref. 1; AAK27389)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        418
FT                   /note="L -> M (in Ref. 2; BAC36902)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   563 AA;  64980 MW;  89B67CF3A379C3D2 CRC64;
     MDVGELLSYQ PNRGTKRPRD DEEEELKTRR KQTGPRERGR YREEEATAAE DTADDKKRLL
     QIIDRDGEEE EEEEEPLDES SVKKMILTFE KRSYKNQELR IKFPDNPEKF MESELDLNDI
     IQEMHVVATM PDLYHLLVEL SAVQSLLGLL GHDNTDVSIA VVDLLQELTD IDTLHESEEG
     AEVLIDALVD GQVAALLVQN LERLDESVRE EADGVHNTLA IVENMAEFRP EMCTEAAQQG
     LLQWLLKRLK AKMPFDANKL YCSEVLAILL QDNDENRELL GELDGIDVLL QQLSVFKRHN
     PSTAEEQEMM ENLFDALCSC LMLSSNRERF LKGEGLQLMN LMLREKKVSR SSALKVLDHA
     MIGPEGTDNC HKFVDILGLR TIFPLFMKSP RKIKKVGTTE KEHEEHVCSI LASLLRNLRG
     QQRTRLLNKF TENDSEKVDR LMELHFKYLS AMQVADKKIE GEKHDIVRRG EIIDNDMEDE
     FYLRRLDAGL FILQHICYIM AEICNANVPQ IRQRVHQILN MRGSSIKIVR HIIKEYAENI
     GDGRSPEFRE TEQKRILALL ENF
 
 
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