BUD13_MOUSE
ID BUD13_MOUSE Reviewed; 637 AA.
AC Q8R149; Q8BQC0; Q8CB03;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=BUD13 homolog;
GN Name=Bud13;
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=Thymus, and Vagina;
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] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-144; THR-170; THR-183;
RP THR-196; THR-209 AND THR-222, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131; SER-148; SER-174;
RP SER-187; THR-196; THR-209; SER-226; SER-297; SER-341; SER-344; SER-371 AND
RP SER-376, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, 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).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the activated
CC spliceosome. {ECO:0000250|UniProtKB:Q9BRD0}.
CC -!- SUBUNIT: Part of the activated spliceosome B/catalytic step 1
CC spliceosome, one of the forms of the spliceosome which has a well-
CC formed active site but still cannot catalyze the branching reaction and
CC is composed of at least 52 proteins, the U2, U5 and U6 snRNAs and the
CC pre-mRNA. {ECO:0000250|UniProtKB:Q9BRD0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BRD0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R149-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R149-2; Sequence=VSP_025591;
CC -!- SIMILARITY: Belongs to the CWC26 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK037134; BAC29716.1; -; mRNA.
DR EMBL; AK038126; BAE20531.1; -; mRNA.
DR EMBL; AK051047; BAC34509.1; -; mRNA.
DR EMBL; BC025490; AAH25490.1; -; mRNA.
DR CCDS; CCDS23145.1; -. [Q8R149-1]
DR RefSeq; NP_666112.1; NM_146000.2. [Q8R149-1]
DR AlphaFoldDB; Q8R149; -.
DR BioGRID; 229592; 11.
DR IntAct; Q8R149; 11.
DR STRING; 10090.ENSMUSP00000074490; -.
DR iPTMnet; Q8R149; -.
DR PhosphoSitePlus; Q8R149; -.
DR EPD; Q8R149; -.
DR jPOST; Q8R149; -.
DR MaxQB; Q8R149; -.
DR PaxDb; Q8R149; -.
DR PeptideAtlas; Q8R149; -.
DR PRIDE; Q8R149; -.
DR ProteomicsDB; 265321; -. [Q8R149-1]
DR ProteomicsDB; 265322; -. [Q8R149-2]
DR Antibodypedia; 52338; 100 antibodies from 21 providers.
DR DNASU; 215051; -.
DR Ensembl; ENSMUST00000074957; ENSMUSP00000074490; ENSMUSG00000032077. [Q8R149-1]
DR GeneID; 215051; -.
DR KEGG; mmu:215051; -.
DR UCSC; uc009phi.1; mouse. [Q8R149-1]
DR CTD; 84811; -.
DR MGI; MGI:2443443; Bud13.
DR VEuPathDB; HostDB:ENSMUSG00000032077; -.
DR eggNOG; KOG2654; Eukaryota.
DR GeneTree; ENSGT00390000014500; -.
DR HOGENOM; CLU_024195_3_1_1; -.
DR InParanoid; Q8R149; -.
DR OMA; LDSKGDC; -.
DR OrthoDB; 1558074at2759; -.
DR PhylomeDB; Q8R149; -.
DR TreeFam; TF315331; -.
DR BioGRID-ORCS; 215051; 6 hits in 71 CRISPR screens.
DR PRO; PR:Q8R149; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8R149; protein.
DR Bgee; ENSMUSG00000032077; Expressed in animal zygote and 206 other tissues.
DR ExpressionAtlas; Q8R149; baseline and differential.
DR Genevisible; Q8R149; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0070274; C:RES complex; IBA:GO_Central.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR InterPro; IPR018609; Bud13.
DR Pfam; PF09736; Bud13; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Isopeptide bond; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome;
KW Ubl conjugation.
FT CHAIN 1..637
FT /note="BUD13 homolog"
FT /id="PRO_0000287689"
FT REGION 18..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 490..538
FT /evidence="ECO:0000255"
FT COMPBIAS 104..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 131
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4QQU1"
FT MOD_RES 144
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 157
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 209
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 222
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 512
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT VAR_SEQ 608..637
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025591"
FT CONFLICT 174
FT /note="S -> Y (in Ref. 1; BAC34509)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="P -> H (in Ref. 1; BAC34509)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 637 AA; 72139 MW; CA381776034D1A89 CRC64;
MAAAPPLTKA EYLKRYLSGT DAGLEGGPEA GRKRRKKRPK PGGAGGKGMR IVDDDVGWAA
ISTAKPEKEE EEDGDLPVVA EFVDERPEEV KQMEAFRSSA KWKLLGGHGE DGHFHHDDQD
SSPPRRVRHD TPDTSPPRKA RHDTPDPSPP RKARHDTPDT SPPRKARHDT PDPSPPRKAR
HDTPDPSPPR RVRHDTPDLS PPRRVRHDTP DLSPPRRVRH DTPDPSPPRR VRHDLDASPP
RKSHRNSSAV SPRRGHHGSL GTSSPRQTHN HSPTAAQHRR TLDSSGTQHL RRAHHESPDL
ELHKAKSSKA AERAPSKAAS QSGLGPSHPS LSTNSKYEHD SDLSPPRKRQ AKAHFEAKKQ
LDSKGVYQKA SDSDLSPPRK KKNSGHQDSD SDLSPPRNRP RRQSSDSDLS PPRRRQRTKS
SDSDLSPPRR SPRPGKKTAH MYSGAKTGLV TDVQREHQEL KKQDQDTTDL GAQFEFTETV
FRDKSGRKRN LKLERLEQRR KAEKDSERDE LYAQWGKGLA QSRQQQQNVE DAMKEMQKPL
ARYIDDEDLD RMLREQEREG DPMANFIKKN KAKENKNKKV KPRYSGPAPP PNRFNIWPGY
RWDGVDRSNG FEQKRFARLA SKKAVEELAY KWSVEDM