GEMI2_MOUSE
ID GEMI2_MOUSE Reviewed; 269 AA.
AC Q9CQQ4; Q9DAD7;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Gem-associated protein 2;
DE Short=Gemin-2;
DE AltName: Full=Component of gems 2;
DE AltName: Full=Survival of motor neuron protein-interacting protein 1;
DE Short=SMN-interacting protein 1;
GN Name=Gemin2 {ECO:0000312|MGI:MGI:1913853}; Synonyms=Sip1;
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].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Pancreas, and Testis;
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).
CC -!- FUNCTION: The SMN complex catalyzes the assembly of small nuclear
CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC and thereby plays an important role in the splicing of cellular pre-
CC mRNAs (By similarity). Most spliceosomal snRNPs contain a common set of
CC Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that
CC assemble in a heptameric protein ring on the Sm site of the small
CC nuclear RNA to form the core snRNP (Sm core) (By similarity). In the
CC cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG (5Sm)
CC are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A
CC that controls the assembly of the core snRNP (By similarity). To
CC assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins
CC from CLNS1A (By similarity). Binding of snRNA inside 5Sm ultimately
CC triggers eviction of the SMN complex, thereby allowing binding of
CC SNRPD3 and SNRPB to complete assembly of the core snRNP (By
CC similarity). Within the SMN complex, GEMIN2 constrains the conformation
CC of 5Sm, thereby promoting 5Sm binding to snRNA containing the snRNP
CC code (a nonameric Sm site and a 3'-adjacent stem-loop), thus preventing
CC progression of assembly until a cognate substrate is bound (By
CC similarity). {ECO:0000250|UniProtKB:O14893}.
CC -!- SUBUNIT: Monomer (By similarity). Part of the core SMN complex that
CC contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6,
CC GEMIN7, GEMIN8 and STRAP/UNRIP. Part of the SMN-Sm complex that
CC contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6,
CC GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2,
CC SNRPD3, SNRPE, SNRPF and SNRPG (By similarity). Interacts with GEMIN5;
CC the interaction is direct (By similarity). Interacts (via C-terminus)
CC with SMN1; the interaction is direct (By similarity). Interacts with
CC GEMIN5; the interaction is direct (By similarity). Interacts with
CC SNRPD1; the interaction is direct (By similarity). Interacts with
CC SNRPD2; the interaction is direct (By similarity). Interacts (via N-
CC terminus) with SNRPF; the interaction is direct (By similarity).
CC Interacts (via N-terminus) with SNRPE; the interaction is direct (By
CC similarity). Interacts (via N-terminus) with SNRPG; the interaction is
CC direct (By similarity). {ECO:0000250|UniProtKB:O14893}.
CC -!- SUBCELLULAR LOCATION: Nucleus, gem {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Note=Localized in subnuclear structures next to coiled
CC bodies, called gems, which are highly enriched in spliceosomal snRNPs.
CC Also found in the cytoplasm (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the gemin-2 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; AK005928; BAB24321.1; -; mRNA.
DR EMBL; AK007515; BAB25083.1; -; mRNA.
DR EMBL; AK013414; BAB28842.1; -; mRNA.
DR CCDS; CCDS36457.1; -.
DR RefSeq; NP_079932.2; NM_025656.5.
DR AlphaFoldDB; Q9CQQ4; -.
DR SMR; Q9CQQ4; -.
DR BioGRID; 211588; 2.
DR IntAct; Q9CQQ4; 3.
DR STRING; 10090.ENSMUSP00000021379; -.
DR iPTMnet; Q9CQQ4; -.
DR PhosphoSitePlus; Q9CQQ4; -.
DR EPD; Q9CQQ4; -.
DR MaxQB; Q9CQQ4; -.
DR PaxDb; Q9CQQ4; -.
DR PeptideAtlas; Q9CQQ4; -.
DR PRIDE; Q9CQQ4; -.
DR ProteomicsDB; 268861; -.
DR Antibodypedia; 4218; 371 antibodies from 40 providers.
DR DNASU; 66603; -.
DR Ensembl; ENSMUST00000021379; ENSMUSP00000021379; ENSMUSG00000060121.
DR GeneID; 66603; -.
DR KEGG; mmu:66603; -.
DR UCSC; uc007npx.2; mouse.
DR CTD; 8487; -.
DR MGI; MGI:1913853; Gemin2.
DR VEuPathDB; HostDB:ENSMUSG00000060121; -.
DR eggNOG; ENOG502QPK4; Eukaryota.
DR GeneTree; ENSGT00390000013814; -.
DR HOGENOM; CLU_053222_0_0_1; -.
DR InParanoid; Q9CQQ4; -.
DR OMA; PTPEWRD; -.
DR OrthoDB; 1235594at2759; -.
DR PhylomeDB; Q9CQQ4; -.
DR TreeFam; TF105864; -.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR BioGRID-ORCS; 66603; 20 hits in 74 CRISPR screens.
DR ChiTaRS; Gemin2; mouse.
DR PRO; PR:Q9CQQ4; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9CQQ4; protein.
DR Bgee; ENSMUSG00000060121; Expressed in morula and 255 other tissues.
DR Genevisible; Q9CQQ4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032797; C:SMN complex; ISS:UniProtKB.
DR GO; GO:0034719; C:SMN-Sm protein complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:InterPro.
DR GO; GO:1905215; P:negative regulation of RNA binding; ISO:MGI.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:InterPro.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR InterPro; IPR017364; GEMIN2.
DR InterPro; IPR035426; Gemin2/Brr1.
DR Pfam; PF04938; SIP1; 1.
DR PIRSF; PIRSF038038; SMN_Gemin2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..269
FT /note="Gem-associated protein 2"
FT /id="PRO_0000087456"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14893"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14893"
FT CONFLICT 241
FT /note="D -> E (in Ref. 1; BAB24321)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 30441 MW; 6BB65AC800F8B329 CRC64;
MAWVPAESAV EELMPRLLPV EPCDLTEGFD PSVPPRTPQE YLRRVQIEAA QCPDVVVAQI
DPKKLKRKQS VNISLSGCQP APEGYSPTLQ WQQQQVAHFS TVRQSVHKHR NHWKSQQLDS
NVAMPKSEDE EGWKKFCLGE RLCAEGATGP STEESPGIDY VQVGFPPLLS IVSRMNQTTI
TSVLEYLSNW FGERDFTPEL GRWFYALLAC LEKPLLPEAH SLIRQLARRC SEVRLLVGSK
DDERVPALNL LICLVSRYFD QRDLADEPS
