GEMI2_HUMAN
ID GEMI2_HUMAN Reviewed; 280 AA.
AC O14893; B2R9W8; Q2M3B3; Q9H4F5; Q9NS77; Q9NS78; Q9NS79;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 191.
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|HGNC:HGNC:10884}; Synonyms=SIP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Mammary cancer;
RX PubMed=9323129; DOI=10.1016/s0092-8674(00)80367-0;
RA Liu Q., Fischer U., Wang F., Dreyfuss G.;
RT "The spinal muscular atrophy disease gene product, SMN, and its associated
RT protein SIP1 are in a complex with spliceosomal snRNP proteins.";
RL Cell 90:1013-1021(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Spinal cord;
RX PubMed=11943600; DOI=10.1016/s1357-2725(01)00150-9;
RA Aerbajinai W., Ishihara T., Arahata K., Tsukahara T.;
RT "Increased expression level of the splicing variant of SIP1 in motor neuron
RT diseases.";
RL Int. J. Biochem. Cell Biol. 34:699-707(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10909848; DOI=10.1038/sj.ejhg.5200479;
RA Helmken C., Wetter A., Rudnik-Schoeneborn S., Liehr T., Zerres K.,
RA Wirth B.;
RT "An essential SMN interacting protein (SIP1) is not involved in the
RT phenotypic variability of spinal muscular atrophy (SMA).";
RL Eur. J. Hum. Genet. 8:493-499(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [6]
RP INTERACTION WITH SMN1.
RX PubMed=10500148; DOI=10.1073/pnas.96.20.11167;
RA Pellizzoni L., Charroux B., Dreyfuss G.;
RT "SMN mutants of spinal muscular atrophy patients are defective in binding
RT to snRNP proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11167-11172(1999).
RN [7]
RP INTERACTION WITH GEMIN5 AND THE SMN COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=11714716; DOI=10.1074/jbc.m109448200;
RA Gubitz A.K., Mourelatos Z., Abel L., Rappsilber J., Mann M., Dreyfuss G.;
RT "Gemin5, a novel WD repeat protein component of the SMN complex that binds
RT Sm proteins.";
RL J. Biol. Chem. 277:5631-5636(2002).
RN [8]
RP FUNCTION, IDENTIFICATION IN THE SMN COMPLEX, AND IDENTIFICATION IN SMN-SM
RP COMPLEX.
RX PubMed=16314521; DOI=10.1128/mcb.25.24.10989-11004.2005;
RA Golembe T.J., Yong J., Dreyfuss G.;
RT "Specific sequence features, recognized by the SMN complex, identify snRNAs
RT and determine their fate as snRNPs.";
RL Mol. Cell. Biol. 25:10989-11004(2005).
RN [9]
RP IDENTIFICATION IN THE SMN COMPLEX, AND INTERACTION WITH GEMIN5 AND SMN1.
RX PubMed=17178713; DOI=10.1074/jbc.m608528200;
RA Otter S., Grimmler M., Neuenkirchen N., Chari A., Sickmann A., Fischer U.;
RT "A comprehensive interaction map of the human survival of motor neuron
RT (SMN) complex.";
RL J. Biol. Chem. 282:5825-5833(2007).
RN [10]
RP FUNCTION IN SNRNP BIOGENESIS, AND IDENTIFICATION IN SMN-SM COMPLEX.
RX PubMed=18984161; DOI=10.1016/j.cell.2008.09.020;
RA Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B.,
RA Englbrecht C., Sickmann A., Stark H., Fischer U.;
RT "An assembly chaperone collaborates with the SMN complex to generate
RT spliceosomal SnRNPs.";
RL Cell 135:497-509(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP INTERACTION WITH SMN1.
RX PubMed=23022347; DOI=10.1016/j.str.2012.08.024;
RA Martin R., Gupta K., Ninan N.S., Perry K., Van Duyne G.D.;
RT "The survival motor neuron protein forms soluble glycine zipper
RT oligomers.";
RL Structure 20:1929-1939(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP SUBUNIT, AND INTERACTION WITH SMN1.
RX PubMed=26092730; DOI=10.1074/jbc.m115.667279;
RA Gupta K., Martin R., Sharp R., Sarachan K.L., Ninan N.S., Van Duyne G.D.;
RT "Oligomeric Properties of Survival Motor Neuron.Gemin2 Complexes.";
RL J. Biol. Chem. 290:20185-20199(2015).
RN [18] {ECO:0007744|PDB:5XJL}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH SNRPD1; SNRPD2;
RP SNRPE; SNRPF; SNRPG AND SMN1, FUNCTION, INTERACTION WITH SNRPD1; SNRPD2;
RP SNRPE; SNRPF; SNRPG AND SMN1, AND MUTAGENESIS OF TYR-52 AND ARG-213.
RX PubMed=21816274; DOI=10.1016/j.cell.2011.06.043;
RA Zhang R., So B.R., Li P., Yong J., Glisovic T., Wan L., Dreyfuss G.;
RT "Structure of a key intermediate of the SMN complex reveals Gemin2's
RT crucial function in snRNP assembly.";
RL Cell 146:384-395(2011).
RN [19] {ECO:0007744|PDB:2LEH}
RP STRUCTURE BY NMR OF 95-280, AND INTERACTION WITH SMN1.
RX PubMed=22607171; DOI=10.1042/bj20120241;
RA Sarachan K.L., Valentine K.G., Gupta K., Moorman V.R., Gledhill J.M.,
RA Bernens M., Tommos C., Wand A.J., Van Duyne G.D.;
RT "Solution structure of the core SMN-Gemin2 complex.";
RL Biochem. J. 445:361-370(2012).
RN [20] {ECO:0007744|PDB:5XJQ, ECO:0007744|PDB:5XJR, ECO:0007744|PDB:5XJS}
RP X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS) OF 40-280 IN COMPLEX WITH SNRPD1;
RP SNRPD2; SNRPE; SNRPF; SNRPG AND SMN1, FUNCTION, AND INTERACTION WITH
RP SNRPD1; SNRPD2; SNRPE; SNRPF AND SMN1.
RX PubMed=31799625; DOI=10.1093/nar/gkz1135;
RA Yi H., Mu L., Shen C., Kong X., Wang Y., Hou Y., Zhang R.;
RT "Negative cooperativity between Gemin2 and RNA provides insights into RNA
RT selection and the SMN complex's release in snRNP assembly.";
RL Nucleic Acids Res. 48:895-911(2020).
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 (PubMed:18984161, PubMed:9323129). Most spliceosomal snRNPs
CC contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3,
CC SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on
CC the Sm site of the small nuclear RNA to form the core snRNP (Sm core)
CC (PubMed:18984161). In the cytosol, the Sm proteins SNRPD1, SNRPD2,
CC SNRPE, SNRPF and SNRPG (5Sm) are trapped in an inactive 6S pICln-Sm
CC complex by the chaperone CLNS1A that controls the assembly of the core
CC snRNP (PubMed:18984161). To assemble core snRNPs, the SMN complex
CC accepts the trapped 5Sm proteins from CLNS1A (PubMed:18984161,
CC PubMed:9323129). Binding of snRNA inside 5Sm ultimately triggers
CC eviction of the SMN complex, thereby allowing binding of SNRPD3 and
CC SNRPB to complete assembly of the core snRNP (PubMed:31799625). Within
CC the SMN complex, GEMIN2 constrains the conformation of 5Sm, thereby
CC promoting 5Sm binding to snRNA containing the snRNP code (a nonameric
CC Sm site and a 3'-adjacent stem-loop), thus preventing progression of
CC assembly until a cognate substrate is bound (PubMed:31799625,
CC PubMed:21816274, PubMed:16314521). {ECO:0000269|PubMed:16314521,
CC ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:21816274,
CC ECO:0000269|PubMed:31799625, ECO:0000269|PubMed:9323129}.
CC -!- SUBUNIT: Monomer (PubMed:26092730). Part of the core SMN complex that
CC contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6,
CC GEMIN7, GEMIN8 and STRAP/UNRIP (PubMed:11714716, PubMed:9323129,
CC PubMed:16314521, PubMed:17178713). 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 (PubMed:18984161, PubMed:9323129,
CC PubMed:16314521). Interacts with GEMIN5; the interaction is direct
CC (PubMed:11714716). Interacts (via C-terminus) with SMN1; the
CC interaction is direct (PubMed:21816274, PubMed:26092730,
CC PubMed:10500148, PubMed:31799625, PubMed:17178713, PubMed:22607171,
CC PubMed:23022347). Interacts with GEMIN5; the interaction is direct
CC (PubMed:17178713). Interacts with SNRPD1; the interaction is direct
CC (PubMed:21816274, PubMed:31799625). Interacts with SNRPD2; the
CC interaction is direct (PubMed:21816274, PubMed:31799625). Interacts
CC (via N-terminus) with SNRPF; the interaction is direct
CC (PubMed:21816274, PubMed:31799625). Interacts (via N-terminus) with
CC SNRPE; the interaction is direct (PubMed:21816274, PubMed:31799625).
CC Interacts (via N-terminus) with SNRPG; the interaction is direct
CC (PubMed:21816274). {ECO:0000269|PubMed:10500148,
CC ECO:0000269|PubMed:11714716, ECO:0000269|PubMed:16314521,
CC ECO:0000269|PubMed:17178713, ECO:0000269|PubMed:18984161,
CC ECO:0000269|PubMed:21816274, ECO:0000269|PubMed:22607171,
CC ECO:0000269|PubMed:23022347, ECO:0000269|PubMed:26092730,
CC ECO:0000269|PubMed:31799625, ECO:0000269|PubMed:9323129}.
CC -!- INTERACTION:
CC O14893; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-443648, EBI-10181188;
CC O14893; P28358: HOXD10; NbExp=3; IntAct=EBI-443648, EBI-12690664;
CC O14893; Q0VD86: INCA1; NbExp=3; IntAct=EBI-443648, EBI-6509505;
CC O14893; O60684: KPNA6; NbExp=5; IntAct=EBI-443648, EBI-359923;
CC O14893; P50221: MEOX1; NbExp=3; IntAct=EBI-443648, EBI-2864512;
CC O14893; P26367: PAX6; NbExp=3; IntAct=EBI-443648, EBI-747278;
CC O14893; P20618: PSMB1; NbExp=3; IntAct=EBI-443648, EBI-372273;
CC O14893; O95059: RPP14; NbExp=3; IntAct=EBI-443648, EBI-366542;
CC O14893; Q16637: SMN2; NbExp=20; IntAct=EBI-443648, EBI-395421;
CC O14893; Q16637-2: SMN2; NbExp=4; IntAct=EBI-443648, EBI-16014970;
CC O14893; P62306: SNRPF; NbExp=11; IntAct=EBI-443648, EBI-356900;
CC O14893; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-443648, EBI-742688;
CC -!- SUBCELLULAR LOCATION: Nucleus, gem. Cytoplasm. Note=Localized in
CC subnuclear structures next to coiled bodies, called gems, which are
CC highly enriched in spliceosomal snRNPs. Also found in the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=5;
CC Name=1; Synonyms=SIP1-alpha;
CC IsoId=O14893-1; Sequence=Displayed;
CC Name=2; Synonyms=SIP1-beta;
CC IsoId=O14893-2; Sequence=VSP_013545;
CC Name=3; Synonyms=SIP1-gamma;
CC IsoId=O14893-3; Sequence=VSP_013546, VSP_013547;
CC Name=4; Synonyms=SIP1-delta;
CC IsoId=O14893-4; Sequence=VSP_013543, VSP_013544;
CC Name=5;
CC IsoId=O14893-5; Sequence=VSP_061433;
CC -!- SIMILARITY: Belongs to the gemin-2 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-12 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC16117.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF027150; AAB82297.1; -; mRNA.
DR EMBL; AB037701; BAB03508.1; -; mRNA.
DR EMBL; AB037702; BAB03509.1; -; mRNA.
DR EMBL; AB037703; BAB03510.1; -; mRNA.
DR EMBL; AJ250932; CAC16117.2; ALT_INIT; Genomic_DNA.
DR EMBL; AJ250933; CAC16117.2; JOINED; Genomic_DNA.
DR EMBL; AJ250934; CAC16117.2; JOINED; Genomic_DNA.
DR EMBL; AJ250935; CAC16117.2; JOINED; Genomic_DNA.
DR EMBL; AJ250936; CAC16117.2; JOINED; Genomic_DNA.
DR EMBL; AJ250937; CAC16117.2; JOINED; Genomic_DNA.
DR EMBL; AJ250938; CAC16117.2; JOINED; Genomic_DNA.
DR EMBL; AJ250939; CAC16117.2; JOINED; Genomic_DNA.
DR EMBL; AK313947; BAG36665.1; -; mRNA.
DR EMBL; BC104968; AAI04969.1; -; mRNA.
DR CCDS; CCDS9669.1; -. [O14893-5]
DR RefSeq; NP_001009182.1; NM_001009182.1.
DR RefSeq; NP_001009183.1; NM_001009183.1.
DR RefSeq; NP_003607.1; NM_003616.2.
DR PDB; 2LEH; NMR; -; A=95-280.
DR PDB; 5XJL; X-ray; 2.50 A; 2=1-280.
DR PDB; 5XJQ; X-ray; 3.28 A; 2=1-280.
DR PDB; 5XJR; X-ray; 3.12 A; 2=40-280.
DR PDB; 5XJS; X-ray; 3.38 A; 2=40-280.
DR PDB; 5XJT; X-ray; 2.92 A; 2=1-280.
DR PDB; 5XJU; X-ray; 2.58 A; 2=40-280.
DR PDBsum; 2LEH; -.
DR PDBsum; 5XJL; -.
DR PDBsum; 5XJQ; -.
DR PDBsum; 5XJR; -.
DR PDBsum; 5XJS; -.
DR PDBsum; 5XJT; -.
DR PDBsum; 5XJU; -.
DR AlphaFoldDB; O14893; -.
DR BMRB; O14893; -.
DR SMR; O14893; -.
DR BioGRID; 114059; 116.
DR ComplexPortal; CPX-6031; SMN complex.
DR CORUM; O14893; -.
DR DIP; DIP-32605N; -.
DR IntAct; O14893; 59.
DR MINT; O14893; -.
DR STRING; 9606.ENSP00000308533; -.
DR GlyGen; O14893; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14893; -.
DR PhosphoSitePlus; O14893; -.
DR BioMuta; GEMIN2; -.
DR EPD; O14893; -.
DR jPOST; O14893; -.
DR MassIVE; O14893; -.
DR MaxQB; O14893; -.
DR PaxDb; O14893; -.
DR PeptideAtlas; O14893; -.
DR PRIDE; O14893; -.
DR ProteomicsDB; 48281; -. [O14893-1]
DR ProteomicsDB; 48282; -. [O14893-2]
DR ProteomicsDB; 48283; -. [O14893-3]
DR ProteomicsDB; 48284; -. [O14893-4]
DR Antibodypedia; 4218; 371 antibodies from 40 providers.
DR DNASU; 8487; -.
DR Ensembl; ENST00000308317.12; ENSP00000308533.7; ENSG00000092208.19. [O14893-5]
DR GeneID; 8487; -.
DR KEGG; hsa:8487; -.
DR MANE-Select; ENST00000308317.12; ENSP00000308533.7; NM_003616.3; NP_003607.2. [O14893-5]
DR UCSC; uc001wuq.4; human. [O14893-1]
DR CTD; 8487; -.
DR DisGeNET; 8487; -.
DR GeneCards; GEMIN2; -.
DR GeneReviews; GEMIN2; -.
DR HGNC; HGNC:10884; GEMIN2.
DR HPA; ENSG00000092208; Low tissue specificity.
DR MalaCards; GEMIN2; -.
DR MIM; 602595; gene.
DR neXtProt; NX_O14893; -.
DR OpenTargets; ENSG00000092208; -.
DR PharmGKB; PA35784; -.
DR VEuPathDB; HostDB:ENSG00000092208; -.
DR eggNOG; ENOG502QPK4; Eukaryota.
DR GeneTree; ENSGT00390000013814; -.
DR HOGENOM; CLU_053222_0_0_1; -.
DR InParanoid; O14893; -.
DR OMA; PTPEWRD; -.
DR OrthoDB; 1235594at2759; -.
DR PhylomeDB; O14893; -.
DR TreeFam; TF105864; -.
DR PathwayCommons; O14893; -.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR SignaLink; O14893; -.
DR SIGNOR; O14893; -.
DR BioGRID-ORCS; 8487; 243 hits in 1078 CRISPR screens.
DR ChiTaRS; GEMIN2; human.
DR GenomeRNAi; 8487; -.
DR Pharos; O14893; Tbio.
DR PRO; PR:O14893; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O14893; protein.
DR Bgee; ENSG00000092208; Expressed in buccal mucosa cell and 191 other tissues.
DR ExpressionAtlas; O14893; baseline and differential.
DR Genevisible; O14893; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032797; C:SMN complex; IDA:UniProtKB.
DR GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:1905215; P:negative regulation of RNA binding; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; TAS:UniProtKB.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
DR GO; GO:0000245; P:spliceosomal complex assembly; TAS:ProtInc.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR IDEAL; IID00524; -.
DR InterPro; IPR017364; GEMIN2.
DR InterPro; IPR035426; Gemin2/Brr1.
DR Pfam; PF04938; SIP1; 1.
DR PIRSF; PIRSF038038; SMN_Gemin2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Alternative splicing; Cytoplasm;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..280
FT /note="Gem-associated protein 2"
FT /id="PRO_0000087455"
FT REGION 1..39
FT /note="May play a minor inhibitory role in snRNA binding to
FT 5Sm (SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG) during snRNP
FT assembly by inserting into the RNA binding pocket of 5Sm"
FT /evidence="ECO:0000269|PubMed:21816274"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform 5)"
FT /id="VSP_061433"
FT VAR_SEQ 31..44
FT /note="VEPCDLTEGFDPSV -> DRSSSMSRCCGSSN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11943600"
FT /id="VSP_013543"
FT VAR_SEQ 45..280
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11943600"
FT /id="VSP_013544"
FT VAR_SEQ 173..187
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11943600"
FT /id="VSP_013545"
FT VAR_SEQ 249..250
FT /note="DS -> VF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11943600"
FT /id="VSP_013546"
FT VAR_SEQ 251..280
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11943600"
FT /id="VSP_013547"
FT MUTAGEN 52
FT /note="Y->D: Impairs binding to Sm complex proteins."
FT /evidence="ECO:0000269|PubMed:21816274"
FT MUTAGEN 213
FT /note="R->D: Impairs binding to SMN1."
FT /evidence="ECO:0000269|PubMed:21816274"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:5XJL"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:5XJL"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:5XJT"
FT HELIX 100..120
FT /evidence="ECO:0007829|PDB:5XJL"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:5XJU"
FT HELIX 141..149
FT /evidence="ECO:0007829|PDB:5XJL"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:2LEH"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:2LEH"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:2LEH"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:2LEH"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:5XJL"
FT HELIX 188..204
FT /evidence="ECO:0007829|PDB:5XJL"
FT HELIX 209..221
FT /evidence="ECO:0007829|PDB:5XJL"
FT HELIX 228..244
FT /evidence="ECO:0007829|PDB:5XJL"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:5XJU"
FT HELIX 255..268
FT /evidence="ECO:0007829|PDB:5XJL"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:5XJL"
SQ SEQUENCE 280 AA; 31585 MW; 3232F410EA98EB81 CRC64;
MRRAELAGLK TMAWVPAESA VEELMPRLLP VEPCDLTEGF DPSVPPRTPQ EYLRRVQIEA
AQCPDVVVAQ IDPKKLKRKQ SVNISLSGCQ PAPEGYSPTL QWQQQQVAQF STVRQNVNKH
RSHWKSQQLD SNVTMPKSED EEGWKKFCLG EKLCADGAVG PATNESPGID YVQIGFPPLL
SIVSRMNQAT VTSVLEYLSN WFGERDFTPE LGRWLYALLA CLEKPLLPEA HSLIRQLARR
CSEVRLLVDS KDDERVPALN LLICLVSRYF DQRDLADEPS
