GPSM2_MOUSE
ID GPSM2_MOUSE Reviewed; 679 AA.
AC Q8VDU0; Q8BLX3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=G-protein-signaling modulator 2;
DE AltName: Full=Pins homolog {ECO:0000303|PubMed:12571286};
GN Name=Gpsm2; Synonyms=Lgn, Pins {ECO:0000303|PubMed:12571286};
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], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=12571286; DOI=10.1242/jcs.00297;
RA Yu F., Morin X., Kaushik R., Bahri S., Yang X., Chia W.;
RT "A mouse homologue of Drosophila pins can asymmetrically localize and
RT substitute for pins function in Drosophila neuroblasts.";
RL J. Cell Sci. 116:887-896(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-640.
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
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 INTERACTION WITH INSC AND F2RL2.
RC STRAIN=CD-1; TISSUE=Epidermis;
RX PubMed=16094321; DOI=10.1038/nature03922;
RA Lechler T., Fuchs E.;
RT "Asymmetric cell divisions promote stratification and differentiation of
RT mammalian skin.";
RL Nature 437:275-280(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408 AND SER-564, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, and Spleen;
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).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=26766442; DOI=10.1016/j.devcel.2015.12.016;
RA Chiu C.W., Monat C., Robitaille M., Lacomme M., Daulat A.M., Macleod G.,
RA McNeill H., Cayouette M., Angers S.;
RT "SAPCD2 controls spindle orientation and asymmetric divisions by negatively
RT regulating the Galphai-LGN-NuMA ternary complex.";
RL Dev. Cell 36:50-62(2016).
RN [8]
RP INTERACTION WITH TASOR, AND TISSUE SPECIFICITY.
RX PubMed=31112734; DOI=10.1016/j.yexcr.2019.05.018;
RA Gresakova V., Novosadova V., Prochazkova M., Bhargava S., Jenickova I.,
RA Prochazka J., Sedlacek R.;
RT "Fam208a orchestrates interaction protein network essential for early
RT embryonic development and cell division.";
RL Exp. Cell Res. 382:111437-111437(2019).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 198-357 IN COMPLEXES WITH NUMA1
RP AND INSC, INTERACTION WITH NUMA1 AND INSC, AND MUTAGENESIS OF ASN-210;
RP ARG-228; ARG-243; PHE-254 AND ASN-290.
RX PubMed=21816348; DOI=10.1016/j.molcel.2011.07.011;
RA Zhu J., Wen W., Zheng Z., Shang Y., Wei Z., Xiao Z., Pan Z., Du Q.,
RA Wang W., Zhang M.;
RT "LGN/mInsc and LGN/NuMA complex structures suggest distinct functions in
RT asymmetric cell division for the Par3/mInsc/LGN and Galphai/LGN/NuMA
RT pathways.";
RL Mol. Cell 43:418-431(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 594-618 AND 628-652 IN COMPLEXES
RP WITH GNAI1; GNAI3 AND GDP, INTERACTION WITH GNAI1 AND GNAI3, DOMAIN, AND
RP MUTAGENESIS OF LEU-601; ILE-635; ARG-642 AND ARG-647.
RX PubMed=22952234; DOI=10.1074/jbc.m112.391607;
RA Jia M., Li J., Zhu J., Wen W., Zhang M., Wang W.;
RT "Crystal structures of the scaffolding protein LGN reveal the general
RT mechanism by which GoLoco binding motifs inhibit the release of GDP from
RT Galphai.";
RL J. Biol. Chem. 287:36766-36776(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 22-357 IN COMPLEX WITH FRMPD1,
RP INTERACTION WITH FRMPD1 AND NUMA1, AND MUTAGENESIS OF ARG-228 AND ARG-243.
RX PubMed=23318951; DOI=10.1016/j.jmb.2013.01.003;
RA Pan Z., Shang Y., Jia M., Zhang L., Xia C., Zhang M., Wang W., Wen W.;
RT "Structural and biochemical characterization of the interaction between LGN
RT and Frmpd1.";
RL J. Mol. Biol. 425:1039-1049(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 96-357 AND 593-651 IN COMPLEXES
RP WITH GNAI1 AND GNAI3, INTERACTION WITH NUMA1; GNAI1 AND GNAI3, AND DOMAIN.
RX PubMed=23665171; DOI=10.1016/j.str.2013.04.005;
RA Pan Z., Zhu J., Shang Y., Wei Z., Jia M., Xia C., Wen W., Wang W.,
RA Zhang M.;
RT "An autoinhibited conformation of LGN reveals a distinct interaction mode
RT between GoLoco motifs and TPR motifs.";
RL Structure 21:1007-1017(2013).
CC -!- FUNCTION: Plays an important role in mitotic spindle pole organization
CC via its interaction with NUMA1 (PubMed:21816348). Required for cortical
CC dynein-dynactin complex recruitment during metaphase (By similarity).
CC Plays a role in metaphase spindle orientation (By similarity). Plays an
CC important role in asymmetric cell divisions (PubMed:12571286,
CC PubMed:21816348). Has guanine nucleotide dissociation inhibitor (GDI)
CC activity towards G(i) alpha proteins, such as GNAI1 and GNAI3, and
CC thereby regulates their activity (PubMed:22952234).
CC {ECO:0000250|UniProtKB:P81274, ECO:0000269|PubMed:12571286,
CC ECO:0000269|PubMed:21816348, ECO:0000269|PubMed:22952234}.
CC -!- SUBUNIT: Interacts with the dynein-dynactin complex; this interaction
CC is inhibited in a PLK1-dependent manner (By similarity). Part of a
CC spindle orientation complex at least composed of GNAI1, GPSM2 and NUMA1
CC (By similarity). Interacts with LLGL2 (By similarity). Interacts (via
CC TPR repeat region) with INSC/inscuteable (PubMed:16094321,
CC PubMed:21816348). Interacts (via TPR repeat region) with NUMA1 (via C-
CC terminus); this interaction is direct, inhibited in a PLK1-dependent
CC manner and promotes spindle pole organization (PubMed:21816348,
CC PubMed:23318951, PubMed:23665171). INSC and NUMA1 compete for the same
CC binding site, but INSC has higher affinity and can displace NUMA1 (in
CC vitro) (PubMed:21816348). Interacts with GNAI2 (By similarity).
CC Interacts (via GoLoco domains) with the GDP-bound form of GNAI1 and
CC GNAI3; has much lower affinity for the GTP-bound form (PubMed:22952234,
CC PubMed:23665171). Interaction with GDP-bound GNAI3 strongly enhances
CC the affinity for NUMA1 (PubMed:23665171). Interacts (via TPR repeat
CC region) with FRMPD1 (PubMed:23318951). INSC and FRMPD1 compete for the
CC same binding site, but INSC has higher affinity and can displace FRMPD1
CC (in vitro) (PubMed:23318951). Interacts (via TPR repeat region) with
CC FRMPD4. Identified in a complex with INSC and F2RL2/Par3 (By
CC similarity). Interacts with TASOR (PubMed:31112734).
CC {ECO:0000250|UniProtKB:P81274, ECO:0000269|PubMed:16094321,
CC ECO:0000269|PubMed:21816348, ECO:0000269|PubMed:22952234,
CC ECO:0000269|PubMed:23318951, ECO:0000269|PubMed:23665171,
CC ECO:0000269|PubMed:31112734}.
CC -!- INTERACTION:
CC Q8VDU0; Q62696: Dlg1; Xeno; NbExp=7; IntAct=EBI-7575403, EBI-389325;
CC Q8VDU0; P78352: DLG4; Xeno; NbExp=7; IntAct=EBI-7575403, EBI-80389;
CC Q8VDU0; Q14980-2: NUMA1; Xeno; NbExp=2; IntAct=EBI-7575403, EBI-10981450;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P81274}.
CC Cytoplasm, cell cortex {ECO:0000269|PubMed:26766442}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P81274}. Lateral cell
CC membrane {ECO:0000269|PubMed:26766442}. Note=Localizes in the cytoplasm
CC during interphase and at cell cortex during metaphase. Colocalizes with
CC NUMA1 to mitotic spindle poles. Localized at the central and lateral
CC cell cortex regions in a RanGTP-dependent manner (By similarity). In
CC horizontally retinal progenitor dividing cells, localized to the
CC lateral cortical region (PubMed:26766442). In vertically retinal
CC progenitor dividing cells, localized at the polar cortical region
CC (PubMed:26766442). {ECO:0000250|UniProtKB:P81274,
CC ECO:0000269|PubMed:26766442}.
CC -!- TISSUE SPECIFICITY: Detected in brain and liver (at protein level).
CC Detected in brain, spleen, liver and testis, and at lower levels in
CC heart, lung and kidney. Enriched in the ventricular zone of the
CC developing central nervous systems (PubMed:12571286). Expressed in
CC proximal colon, ileum, ovary, Sertoli cells of the testis and granular
CC cells within the cerebellum (PubMed:31112734).
CC {ECO:0000269|PubMed:12571286, ECO:0000269|PubMed:31112734}.
CC -!- DOMAIN: Each GoLoco domain can bind one GNAI3 (PubMed:22952234). In the
CC auto-inhibited conformation, the GoLoco domains interact with the TPR
CC repeat region (PubMed:23665171). {ECO:0000269|PubMed:22952234,
CC ECO:0000269|PubMed:23665171}.
CC -!- SIMILARITY: Belongs to the GPSM family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-8 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21308.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL87447.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY081187; AAL87447.1; ALT_INIT; mRNA.
DR EMBL; BC021308; AAH21308.1; ALT_INIT; mRNA.
DR EMBL; AK040996; BAC30775.1; -; mRNA.
DR CCDS; CCDS51048.1; -.
DR RefSeq; NP_083798.2; NM_029522.2.
DR PDB; 3RO2; X-ray; 2.30 A; A=22-357.
DR PDB; 3RO3; X-ray; 1.10 A; A=198-357.
DR PDB; 4G2V; X-ray; 2.40 A; A=22-357.
DR PDB; 4G5O; X-ray; 2.90 A; E/F/G/H=628-653.
DR PDB; 4G5Q; X-ray; 2.90 A; E/F/G/H=628-652.
DR PDB; 4G5R; X-ray; 3.48 A; E/F/G/Z=628-652.
DR PDB; 4G5S; X-ray; 3.62 A; E/F/G/Z=594-618.
DR PDB; 4JHR; X-ray; 2.80 A; A/B=96-357, A/B=593-651.
DR PDBsum; 3RO2; -.
DR PDBsum; 3RO3; -.
DR PDBsum; 4G2V; -.
DR PDBsum; 4G5O; -.
DR PDBsum; 4G5Q; -.
DR PDBsum; 4G5R; -.
DR PDBsum; 4G5S; -.
DR PDBsum; 4JHR; -.
DR AlphaFoldDB; Q8VDU0; -.
DR SMR; Q8VDU0; -.
DR BioGRID; 217976; 3.
DR DIP; DIP-60164N; -.
DR IntAct; Q8VDU0; 5.
DR MINT; Q8VDU0; -.
DR STRING; 10090.ENSMUSP00000029482; -.
DR iPTMnet; Q8VDU0; -.
DR PhosphoSitePlus; Q8VDU0; -.
DR MaxQB; Q8VDU0; -.
DR PaxDb; Q8VDU0; -.
DR PRIDE; Q8VDU0; -.
DR ProteomicsDB; 269623; -.
DR Antibodypedia; 1983; 205 antibodies from 34 providers.
DR DNASU; 76123; -.
DR Ensembl; ENSMUST00000029482; ENSMUSP00000029482; ENSMUSG00000027883.
DR GeneID; 76123; -.
DR KEGG; mmu:76123; -.
DR UCSC; uc008qzo.2; mouse.
DR CTD; 29899; -.
DR MGI; MGI:1923373; Gpsm2.
DR VEuPathDB; HostDB:ENSMUSG00000027883; -.
DR eggNOG; KOG1130; Eukaryota.
DR GeneTree; ENSGT00940000161257; -.
DR HOGENOM; CLU_012445_1_0_1; -.
DR InParanoid; Q8VDU0; -.
DR OMA; PEDRSFH; -.
DR OrthoDB; 733786at2759; -.
DR PhylomeDB; Q8VDU0; -.
DR TreeFam; TF328344; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 76123; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q8VDU0; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8VDU0; protein.
DR Bgee; ENSMUSG00000027883; Expressed in retinal neural layer and 213 other tissues.
DR ExpressionAtlas; Q8VDU0; baseline and differential.
DR Genevisible; Q8VDU0; MM.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0099738; C:cell cortex region; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0097575; C:lateral cell cortex; IDA:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097431; C:mitotic spindle pole; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0070840; F:dynein complex binding; ISS:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:UniProtKB.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR GO; GO:0051661; P:maintenance of centrosome location; ISS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:1904778; P:positive regulation of protein localization to cell cortex; ISS:UniProtKB.
DR GO; GO:1905832; P:positive regulation of spindle assembly; ISS:UniProtKB.
DR GO; GO:0031291; P:Ran protein signal transduction; ISS:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR003109; GoLoco_motif.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF02188; GoLoco; 4.
DR Pfam; PF13176; TPR_7; 2.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00390; GoLoco; 4.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50877; GOLOCO; 4.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell membrane; Cytoplasm;
KW Cytoskeleton; Membrane; Mitosis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Transport.
FT CHAIN 1..679
FT /note="G-protein-signaling modulator 2"
FT /id="PRO_0000106359"
FT REPEAT 24..57
FT /note="TPR 1"
FT REPEAT 62..95
FT /note="TPR 2"
FT REPEAT 102..135
FT /note="TPR 3"
FT REPEAT 142..184
FT /note="TPR 4"
FT REPEAT 202..235
FT /note="TPR 5"
FT REPEAT 242..275
FT /note="TPR 6"
FT REPEAT 282..315
FT /note="TPR 7"
FT REPEAT 322..355
FT /note="TPR 8"
FT DOMAIN 490..512
FT /note="GoLoco 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT DOMAIN 543..565
FT /note="GoLoco 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT DOMAIN 594..616
FT /note="GoLoco 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT DOMAIN 628..650
FT /note="GoLoco 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT REGION 22..357
FT /note="Important for interaction with NUMA1; INSC and
FT FRMPD1"
FT /evidence="ECO:0000269|PubMed:21816348,
FT ECO:0000269|PubMed:23318951"
FT BINDING 608
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:22952234,
FT ECO:0007744|PDB:4G5S"
FT BINDING 613
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:22952234,
FT ECO:0007744|PDB:4G5S"
FT BINDING 642
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:22952234,
FT ECO:0007744|PDB:4G5O, ECO:0007744|PDB:4G5Q"
FT BINDING 647
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:22952234,
FT ECO:0007744|PDB:4G5O, ECO:0007744|PDB:4G5Q"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P81274"
FT MOD_RES 487
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P81274"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P81274"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MUTAGEN 210
FT /note="N->F: Nearly abolishes interaction with NUMA1."
FT /evidence="ECO:0000269|PubMed:21816348"
FT MUTAGEN 228
FT /note="R->A: Abolishes interaction with NUMA1; when
FT associated with A-243. Abolishes interaction with FRMPD1;
FT when associated with A-243."
FT /evidence="ECO:0000269|PubMed:21816348,
FT ECO:0000269|PubMed:23318951"
FT MUTAGEN 243
FT /note="R->A: Abolishes interaction with NUMA1; when
FT associated with A-228. Abolishes interaction with FRMPD1;
FT when associated with A-228."
FT /evidence="ECO:0000269|PubMed:21816348,
FT ECO:0000269|PubMed:23318951"
FT MUTAGEN 254
FT /note="F->E: Abolishes interaction with INSC."
FT /evidence="ECO:0000269|PubMed:21816348"
FT MUTAGEN 290
FT /note="N->E: Abolishes interaction with INSC."
FT /evidence="ECO:0000269|PubMed:21816348"
FT MUTAGEN 601
FT /note="L->E: Disrupts one GNAI3 binding site."
FT /evidence="ECO:0000269|PubMed:22952234"
FT MUTAGEN 635
FT /note="I->E: Disrupts one GNAI3 binding site."
FT /evidence="ECO:0000269|PubMed:22952234"
FT MUTAGEN 642
FT /note="R->A,G: Reduces affinity for GDP-bound GNAI3 50-
FT fold. Reduces affinity for GDP-bound GNAI3 500-fold; when
FT associated with A-647."
FT /evidence="ECO:0000269|PubMed:22952234"
FT MUTAGEN 647
FT /note="R->A: Reduces affinity for GDP-bound GNAI3 500-fold;
FT when associated with A-642."
FT /evidence="ECO:0000269|PubMed:22952234"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:3RO2"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:3RO2"
FT HELIX 58..74
FT /evidence="ECO:0007829|PDB:3RO2"
FT HELIX 78..95
FT /evidence="ECO:0007829|PDB:3RO2"
FT HELIX 98..114
FT /evidence="ECO:0007829|PDB:3RO2"
FT HELIX 118..134
FT /evidence="ECO:0007829|PDB:3RO2"
FT HELIX 138..157
FT /evidence="ECO:0007829|PDB:3RO2"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:3RO2"
FT HELIX 172..195
FT /evidence="ECO:0007829|PDB:3RO2"
FT HELIX 198..214
FT /evidence="ECO:0007829|PDB:3RO3"
FT HELIX 218..235
FT /evidence="ECO:0007829|PDB:3RO3"
FT HELIX 238..254
FT /evidence="ECO:0007829|PDB:3RO3"
FT HELIX 258..274
FT /evidence="ECO:0007829|PDB:3RO3"
FT HELIX 278..294
FT /evidence="ECO:0007829|PDB:3RO3"
FT HELIX 298..314
FT /evidence="ECO:0007829|PDB:3RO3"
FT HELIX 318..335
FT /evidence="ECO:0007829|PDB:3RO3"
FT HELIX 338..352
FT /evidence="ECO:0007829|PDB:3RO3"
FT HELIX 631..640
FT /evidence="ECO:0007829|PDB:4G5O"
FT HELIX 644..646
FT /evidence="ECO:0007829|PDB:4G5O"
SQ SEQUENCE 679 AA; 75591 MW; 8005F2A52FE66D77 CRC64;
MEGNLISMRE DHSFHVRYRM EASCLELALE GERLCKSGDC RAGVSFFEAA VQVGTEDLKT
LSAIYSQLGN AYFYLHDYAK ALEYHHHDLT LARTIGDQLG EAKASGNLGN TLKVLGNFDE
AIVCCQRHLD ISRELNDKVG EARALYNLGN VYHAKGKSFG CPGPQDTGEF PEDVRNALQA
AVDLYEENLS LVTALGDRAA QGRAFGNLGN THYLLGNFRD AVIAHEQRLL IAKEFGDKAA
ERRAYSNLGN AYIFLGEFET ASEYYKKTLL LARQLKDRAV EAQSCYSLGN TYTLLQDYEK
AIDYHLKHLA IAQELKDRIG EGRACWSLGN AYTALGNHDQ AMHFAEKHLE ISREVGDKSG
ELTARLNLSD LQMVLGLSYS TNNSMMSENI EIDGSLHGAG AKLGRRHSME NLELMKLTPE
KVPNWNSEIL AKQKPLIAKP SAKLLFVNRL KGKKYKSGSA CTKVLQDASN SVDHRAPRSQ
KKISSDTIGD EGFFDLLRRF QSNRMDDQRC HLQGNCRTTS TAAASATPKL MKAPSVSVVS
PNTDEFLDLL ASSQSRRLDD QRASFSNLPG LRLTKGNSPS VLERLMTNDK KEPDEDFFDI
LVKCQGSRLD DQRCAPPSAA TKGPTVPDED FFSLILRSQA KRMDEQRVLL QRDPNRDSEF
GLKELLQNNA LLEFKHSGK
