BUD13_RAT
ID BUD13_RAT Reviewed; 636 AA.
AC Q4QQU1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=BUD13 homolog;
GN Name=Bud13;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131; SER-135; THR-144;
RP SER-148; THR-157; SER-161; SER-182; SER-186; THR-208; SER-212; THR-221;
RP SER-225; SER-296 AND SER-343, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SIMILARITY: Belongs to the CWC26 family. {ECO:0000305}.
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DR EMBL; BC097995; AAH97995.1; -; mRNA.
DR RefSeq; NP_001020448.1; NM_001025277.1.
DR AlphaFoldDB; Q4QQU1; -.
DR STRING; 10116.ENSRNOP00000025232; -.
DR iPTMnet; Q4QQU1; -.
DR PhosphoSitePlus; Q4QQU1; -.
DR PaxDb; Q4QQU1; -.
DR PRIDE; Q4QQU1; -.
DR GeneID; 300687; -.
DR KEGG; rno:300687; -.
DR UCSC; RGD:1308076; rat.
DR CTD; 84811; -.
DR RGD; 1308076; Bud13.
DR eggNOG; KOG2654; Eukaryota.
DR InParanoid; Q4QQU1; -.
DR OrthoDB; 1558074at2759; -.
DR PhylomeDB; Q4QQU1; -.
DR PRO; PR:Q4QQU1; -.
DR Proteomes; UP000002494; Unplaced.
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 Coiled coil; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome; Ubl conjugation.
FT CHAIN 1..636
FT /note="BUD13 homolog"
FT /id="PRO_0000287690"
FT REGION 18..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 448..537
FT /evidence="ECO:0000255"
FT COMPBIAS 108..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..570
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:22673903"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 144
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 157
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 208
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 221
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 258
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 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 283
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 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R149"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R149"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R149"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRD0"
FT MOD_RES 511
FT /note="Phosphotyrosine"
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"
SQ SEQUENCE 636 AA; 71869 MW; C509E44F8CC0E56F CRC64;
MAAAPPLSKA EYLKRYLSGT DAGLEGGPES GRKRRKKRPK PGGAGGKGMR IVDDDVGWAA
ISTDKLEKEE EEDGDLPVVA EFVDERPEEV KQMEAFRSST KWKLLGGYSE DGHFHNDDQD
PSPPRKARHD TPDASPPRRV RHGTPEPSPP RRVRHDTPDP SPPRRVRHDS PDPSPTRRGH
DSPDPSPTRR VHHDSPDPSP PRRVRHDTPD PSPPRRVRHD TPDPSPPRRV RHDSDASPPR
RSHRNSSAVS PKRGHHGSSG TSSPRQAHNH SPAAAQHRRT LDSSGAQHHR RARHDSPDLE
LPKAKSSKAA ERPSSKTVSQ SGLGPPHPSL SMNSKYEHDS DLSPPRKRQA KAHFGAKKQL
DSKGVCQKAS DSDLSPPRKN SKSGHQDSDS DLSPPRNRPR RQSSDSDLSP PRRRQRTKSS
DSDLSPSRRS PRSGKKTPHM YSGAKTGLVA DVQREHQELK KQDQDATDLG AQFEFTETVF
RDKSGRKRNL KLERLEQRRK AEKDSERDEL YAQWGKGLAQ SRQQQQNVED AMKEMQKPLA
RYIDDEDLDR MLREQEREGD PMANFIKKNK AKENKNKKVR PRYNGPAPPP NRFNIWPGYR
WDGVDRSNGF EQKRFARLAS KKAVEELAYK WSVEDM
