SYF2_MOUSE
ID SYF2_MOUSE Reviewed; 242 AA.
AC Q9D198;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Pre-mRNA-splicing factor SYF2;
DE AltName: Full=CCNDBP1-interactor;
DE AltName: Full=mp29 {ECO:0000303|PubMed:12437976};
DE AltName: Full=p29 {ECO:0000303|Ref.2};
GN Name=Syf2; Synonyms=Cbpin, Gcipip;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ;
RX PubMed=12437976; DOI=10.1016/s0006-291x(02)02605-0;
RA Chang M.-S., Chen C.-Y., Yeh H.-I., Fan C.-C., Huang C.-J., Yang Y.-C.;
RT "Cloning, expression, and genomic organization of mouse mp29 gene.";
RL Biochem. Biophys. Res. Commun. 299:241-246(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Xia C., Liu M.;
RT "Identification of GCIP-interacting protein p29 (p29) in mouse.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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: Involved in pre-mRNA splicing as component of the
CC spliceosome. {ECO:0000250|UniProtKB:O95926}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Interacts with
CC CCNDBP1. {ECO:0000250|UniProtKB:O95926}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12437976}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the heart, liver and
CC kidney. Expressed at lower level other tissues.
CC {ECO:0000269|PubMed:12437976}.
CC -!- SIMILARITY: Belongs to the SYF2 family. {ECO:0000305}.
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DR EMBL; AY155574; AAO06147.1; -; Genomic_DNA.
DR EMBL; AY033432; AAK54459.1; -; mRNA.
DR EMBL; AK003787; BAB22995.1; -; mRNA.
DR EMBL; AK152794; BAE31500.1; -; mRNA.
DR EMBL; BC051484; AAH51484.1; -; mRNA.
DR CCDS; CCDS18781.1; -.
DR RefSeq; NP_081056.1; NM_026780.3.
DR AlphaFoldDB; Q9D198; -.
DR BioGRID; 212941; 3.
DR IntAct; Q9D198; 2.
DR MINT; Q9D198; -.
DR STRING; 10090.ENSMUSP00000030622; -.
DR PhosphoSitePlus; Q9D198; -.
DR EPD; Q9D198; -.
DR MaxQB; Q9D198; -.
DR PaxDb; Q9D198; -.
DR PeptideAtlas; Q9D198; -.
DR PRIDE; Q9D198; -.
DR ProteomicsDB; 258686; -.
DR Antibodypedia; 34977; 214 antibodies from 32 providers.
DR DNASU; 68592; -.
DR Ensembl; ENSMUST00000030622; ENSMUSP00000030622; ENSMUSG00000028821.
DR GeneID; 68592; -.
DR KEGG; mmu:68592; -.
DR UCSC; uc008vga.1; mouse.
DR CTD; 25949; -.
DR MGI; MGI:1915842; Syf2.
DR VEuPathDB; HostDB:ENSMUSG00000028821; -.
DR eggNOG; KOG2609; Eukaryota.
DR GeneTree; ENSGT00390000017845; -.
DR HOGENOM; CLU_051065_3_0_1; -.
DR InParanoid; Q9D198; -.
DR OMA; RRRMHND; -.
DR OrthoDB; 1565402at2759; -.
DR PhylomeDB; Q9D198; -.
DR TreeFam; TF313041; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 68592; 17 hits in 74 CRISPR screens.
DR ChiTaRS; Syf2; mouse.
DR PRO; PR:Q9D198; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D198; protein.
DR Bgee; ENSMUSG00000028821; Expressed in animal zygote and 260 other tissues.
DR Genevisible; Q9D198; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR GO; GO:0000974; C:Prp19 complex; IBA:GO_Central.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISS:UniProtKB.
DR GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR GO; GO:0007369; P:gastrulation; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR InterPro; IPR013260; mRNA_splic_SYF2.
DR PANTHER; PTHR13264; PTHR13264; 1.
DR Pfam; PF08231; SYF2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Spliceosome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95926"
FT CHAIN 2..242
FT /note="Pre-mRNA-splicing factor SYF2"
FT /id="PRO_0000250377"
FT COILED 65..91
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O95926"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95926"
FT CROSSLNK 233
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95926"
SQ SEQUENCE 242 AA; 28712 MW; FFCC25142541B847 CRC64;
MAAVTEVVVP ADGAEARPLA AEELAAQKRE QRLRKFRELH LKRNEARKLN HQEVVEEDKR
LKLPANWEAK KARLEWELQE EEKKKECAAR GEDYEKVKLL EISAEDAERW ERRKKKKNPD
LGFSDYAAAQ LRQYHRLTKQ IKPDMESYER QREKHGEDFF PTSNSLLHGT HVPSSEEIDR
MVLDLEKQIE KRDKYSRRRP YNDDADIDYI NERNAKFNKK AERFYGKYTA EIKQNLERGT
AV
