ID   SYGP1_RAT               Reviewed;        1308 AA.
AC   Q9QUH6; O88449; Q9ESK6; Q9ET81; Q9QX02; Q9QX06; Q9QX12;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=Ras/Rap GTPase-activating protein SynGAP;
DE   AltName: Full=Neuronal RasGAP;
DE   AltName: Full=Synaptic Ras GTPase-activating protein 1;
DE            Short=Synaptic Ras-GAP 1;
DE   AltName: Full=p135 SynGAP;
GN   Name=Syngap1;
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 [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
RP   16-276 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 1264-1290 (ISOFORM 5),
RP   AND PROTEIN SEQUENCE OF 32-47; 242-248; 259-272; 300-321; 325-329; 340-354;
RP   419-429; 588-596; 804-815; 923-940; 968-1002; 1086-1102 AND 1276-1286.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=9620694; DOI=10.1016/s0896-6273(00)80471-7;
RA   Chen H.-J., Rojas-Soto M., Oguni A., Kennedy M.B.;
RT   "A synaptic Ras-GTPase activating protein (p135 SynGAP) inhibited by CaM
RT   kinase II.";
RL   Neuron 20:895-904(1998).
RN   [2]
RP   ERRATUM OF PUBMED:9620694.
RA   Oh J.S., Chen H.-J., Rojas-Soto M., Oguni A., Kennedy M.B.;
RL   Neuron 33:151-151(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND INTERACTION WITH DLG3
RP   AND DLG4.
RC   TISSUE=Hippocampus;
RX   PubMed=9581761; DOI=10.1016/s0896-6273(00)81008-9;
RA   Kim J.H., Liao D., Lau L.-F., Huganir R.L.;
RT   "SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein
RT   family.";
RL   Neuron 20:683-691(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC   STRAIN=Sprague-Dawley;
RX   PubMed=11278737; DOI=10.1074/jbc.m010744200;
RA   Li W., Okano A., Tian Q.B., Nakayama K., Furihata T., Nawa H., Suzuki T.;
RT   "Characterization of a novel synGAP isoform, synGAP-beta.";
RL   J. Biol. Chem. 276:21417-21424(2001).
RN   [5]
RP   INTERACTION WITH MPDZ; DLG4; CAMK2A AND CAMK2B, PHOSPHORYLATION, AND
RP   FUNCTION.
RX   PubMed=15312654; DOI=10.1016/j.neuron.2004.08.003;
RA   Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.;
RT   "SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity
RT   and NMDA receptor-dependent synaptic AMPA receptor potentiation.";
RL   Neuron 43:563-574(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=15500970; DOI=10.1016/j.neulet.2004.08.044;
RA   Yang S.-N., Huang C.-B., Yang C.-H., Lai M.-C., Chen W.-F., Wang C.-L.,
RA   Wu C.-L., Huang L.-T.;
RT   "Impaired SynGAP expression and long-term spatial learning and memory in
RT   hippocampal CA1 area from rats previously exposed to perinatal hypoxia-
RT   induced insults: beneficial effects of A68930.";
RL   Neurosci. Lett. 371:73-78(2004).
RN   [7]
RP   INTERACTION WITH KLHL17.
RX   PubMed=16054660; DOI=10.1016/j.neuropharm.2005.05.022;
RA   Chen Y., Li M.;
RT   "Interactions between CAP70 and actinfilin are important for integrity of
RT   actin cytoskeleton structures in neurons.";
RL   Neuropharmacology 49:1026-1041(2005).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=16507876; DOI=10.1074/mcp.d500009-mcp200;
RA   Cheng D., Hoogenraad C.C., Rush J., Ramm E., Schlager M.A., Duong D.M.,
RA   Xu P., Wijayawardana S.R., Hanfelt J., Nakagawa T., Sheng M., Peng J.;
RT   "Relative and absolute quantification of postsynaptic density proteome
RT   isolated from rat forebrain and cerebellum.";
RL   Mol. Cell. Proteomics 5:1158-1170(2006).
RN   [9]
RP   FUNCTION.
RX   PubMed=16537406; DOI=10.1073/pnas.0600084103;
RA   Rumbaugh G., Adams J.P., Kim J.H., Huganir R.L.;
RT   "SynGAP regulates synaptic strength and mitogen-activated protein kinases
RT   in cultured neurons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:4344-4351(2006).
RN   [10]
RP   PHOSPHORYLATION AT SER-379; SER-385; SER-449; SER-466; SER-836; SER-840;
RP   SER-842 AND SER-895, AND MUTAGENESIS OF SER-385; SER-449; SER-840 AND
RP   SER-842.
RX   PubMed=21382555; DOI=10.1016/j.neuron.2011.02.004;
RA   Lee K.J., Lee Y., Rozeboom A., Lee J.Y., Udagawa N., Hoe H.S., Pak D.T.;
RT   "Requirement for Plk2 in orchestrated ras and rap signaling, homeostatic
RT   structural plasticity, and memory.";
RL   Neuron 69:957-973(2011).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-371; SER-752;
RP   SER-766; SER-780; SER-892; SER-895; SER-898; SER-1114; SER-1118; SER-1121
RP   AND SER-1204, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 252-734, FUNCTION, DOMAIN C2, AND
RP   MUTAGENESIS OF ARG-485 AND ASN-487.
RX   PubMed=18323856; DOI=10.1038/embor.2008.20;
RA   Pena V., Hothorn M., Eberth A., Kaschau N., Parret A., Gremer L.,
RA   Bonneau F., Ahmadian M.R., Scheffzek K.;
RT   "The C2 domain of SynGAP is essential for stimulation of the Rap GTPase
RT   reaction.";
RL   EMBO Rep. 9:350-355(2008).
CC   -!- FUNCTION: Major constituent of the PSD essential for postsynaptic
CC       signaling. Inhibitory regulator of the Ras-cAMP pathway. Member of the
CC       NMDAR signaling complex in excitatory synapses, it may play a role in
CC       NMDAR-dependent control of AMPAR potentiation, AMPAR membrane
CC       trafficking and synaptic plasticity. Regulates AMPAR-mediated miniature
CC       excitatory postsynaptic currents. Exhibits dual GTPase-activating
CC       specificity for Ras and Rap. May be involved in certain forms of brain
CC       injury, leading to long-term learning and memory deficits.
CC       {ECO:0000269|PubMed:15312654, ECO:0000269|PubMed:15500970,
CC       ECO:0000269|PubMed:16537406, ECO:0000269|PubMed:18323856}.
CC   -!- SUBUNIT: Isoforms containing the PDZ-binding domain associate with DLG4
CC       and DLG3 to form the PSD protein complex colocalized with GRIN2B at
CC       synapses. Interacts with MPDZ, KLHL17 CAMK2A and CAMK2B.
CC       {ECO:0000269|PubMed:15312654, ECO:0000269|PubMed:16054660,
CC       ECO:0000269|PubMed:9581761}.
CC   -!- INTERACTION:
CC       Q9QUH6; P31016: Dlg4; NbExp=3; IntAct=EBI-2310349, EBI-375655;
CC       Q9QUH6; Q8K430: Klhl17; NbExp=2; IntAct=EBI-2310349, EBI-7713653;
CC       Q9QUH6; Q9JJ40: Pdzk1; NbExp=6; IntAct=EBI-2310349, EBI-7713572;
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Synapse.
CC       Note=Mostly in excitatory glutamatergic synapses.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1;
CC         IsoId=Q9QUH6-1; Sequence=Displayed;
CC       Name=2; Synonyms=SynGAP-a;
CC         IsoId=Q9QUH6-2; Sequence=VSP_026378, VSP_007979;
CC       Name=3; Synonyms=SynGAP-b;
CC         IsoId=Q9QUH6-3; Sequence=VSP_007974;
CC       Name=4; Synonyms=SynGAP-c;
CC         IsoId=Q9QUH6-4; Sequence=VSP_007976, VSP_007980;
CC       Name=5; Synonyms=SynGAP-d, SynGAP-beta;
CC         IsoId=Q9QUH6-5; Sequence=VSP_007975, VSP_007977, VSP_007978;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain; predominantly in the
CC       cortex, hippocampus and olfactory bulb. Present in the postsynaptic
CC       density of central excitatory synapses. {ECO:0000269|PubMed:16507876}.
CC   -!- DOMAIN: The PDZ-binding domain interacts with all three PDZ domains of
CC       DGL4. {ECO:0000269|PubMed:18323856}.
CC   -!- DOMAIN: The C2 domain is required for RapGAP activity.
CC       {ECO:0000269|PubMed:18323856}.
CC   -!- PTM: Phosphorylated by CaM-kinase II. Dephosphorylated upon NMDA
CC       receptor activation or SYNGAP1/MPDZ complex disruption. Phosphorylation
CC       by PLK2 promotes its activity. {ECO:0000269|PubMed:15312654,
CC       ECO:0000269|PubMed:21382555}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-16 is the initiator
CC       methionine. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC08071.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF048976; AAC08071.1; ALT_INIT; mRNA.
DR   EMBL; AF053938; AAC23491.1; -; mRNA.
DR   EMBL; AF055883; AAC23492.1; -; mRNA.
DR   EMBL; AF058789; AAC63510.2; -; mRNA.
DR   EMBL; AF058790; AAC63511.1; -; mRNA.
DR   EMBL; AF050183; AAC40082.2; -; mRNA.
DR   EMBL; AB016962; BAA74972.1; -; mRNA.
DR   PIR; T13958; T13958.
DR   PIR; T14259; T14259.
DR   PIR; T14270; T14270.
DR   PDB; 3BXJ; X-ray; 3.00 A; A/B=252-734.
DR   PDBsum; 3BXJ; -.
DR   AlphaFoldDB; Q9QUH6; -.
DR   SMR; Q9QUH6; -.
DR   CORUM; Q9QUH6; -.
DR   ELM; Q9QUH6; -.
DR   IntAct; Q9QUH6; 7.
DR   MINT; Q9QUH6; -.
DR   STRING; 10116.ENSRNOP00000044041; -.
DR   ChEMBL; CHEMBL2176804; -.
DR   GlyGen; Q9QUH6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9QUH6; -.
DR   PhosphoSitePlus; Q9QUH6; -.
DR   PaxDb; 10116-ENSRNOP00000044041; -.
DR   UCSC; RGD:621090; rat. [Q9QUH6-1]
DR   AGR; RGD:621090; -.
DR   RGD; 621090; Syngap1.
DR   eggNOG; KOG3508; Eukaryota.
DR   InParanoid; Q9QUH6; -.
DR   PhylomeDB; Q9QUH6; -.
DR   Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR   EvolutionaryTrace; Q9QUH6; -.
DR   PRO; PR:Q9QUH6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0043198; C:dendritic shaft; ISO:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR   GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR   GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR   GO; GO:0045202; C:synapse; IDA:CACAO.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:RGD.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR   GO; GO:0016358; P:dendrite development; ISO:RGD.
DR   GO; GO:0098880; P:maintenance of postsynaptic specialization structure; ISO:RGD.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR   GO; GO:0050771; P:negative regulation of axonogenesis; ISO:RGD.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR   GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IDA:UniProtKB.
DR   GO; GO:0051402; P:neuron apoptotic process; ISO:RGD.
DR   GO; GO:0007389; P:pattern specification process; ISO:RGD.
DR   GO; GO:0007265; P:Ras protein signal transduction; ISO:RGD.
DR   GO; GO:0043113; P:receptor clustering; ISO:RGD.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD.
DR   GO; GO:0043408; P:regulation of MAPK cascade; ISO:RGD.
DR   GO; GO:0050803; P:regulation of synapse structure or activity; ISO:RGD.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IDA:UniProtKB.
DR   GO; GO:0008542; P:visual learning; ISO:RGD.
DR   CDD; cd04013; C2_SynGAP_like; 1.
DR   CDD; cd13375; PH_SynGAP; 1.
DR   CDD; cd05136; RasGAP_DAB2IP; 1.
DR   CDD; cd22265; UDM1_RNF168; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR021887; DAB2P_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR039360; Ras_GTPase.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR001936; RasGAP_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR037779; SynGAP_PH.
DR   PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR   PANTHER; PTHR10194:SF25; RAS_RAP GTPASE-ACTIVATING PROTEIN SYNGAP; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF12004; DAB2P_C; 1.
DR   Pfam; PF00616; RasGAP; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00323; RasGAP; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   GTPase activation; Membrane; Phosphoprotein; Reference proteome;
KW   SH3-binding; Synapse.
FT   CHAIN           1..1308
FT                   /note="Ras/Rap GTPase-activating protein SynGAP"
FT                   /id="PRO_0000056655"
FT   DOMAIN          150..251
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          242..363
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          443..635
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT   REGION          92..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          725..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..809
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          932..1017
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1033..1153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1197..1308
FT                   /note="Interaction with MPDZ"
FT                   /evidence="ECO:0000269|PubMed:15312654"
FT   REGION          1276..1308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           785..815
FT                   /note="SH3-binding"
FT                   /evidence="ECO:0000255"
FT   MOTIF           1305..1308
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        92..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..742
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1068..1115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1132..1153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1276..1293
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         34
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:F6SEU4"
FT   MOD_RES         39
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:F6SEU4"
FT   MOD_RES         117
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         371
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         379
FT                   /note="Phosphoserine; by PLK2"
FT                   /evidence="ECO:0000269|PubMed:21382555"
FT   MOD_RES         385
FT                   /note="Phosphoserine; by PLK2"
FT                   /evidence="ECO:0000269|PubMed:21382555"
FT   MOD_RES         449
FT                   /note="Phosphoserine; by PLK2"
FT                   /evidence="ECO:0000269|PubMed:21382555"
FT   MOD_RES         466
FT                   /note="Phosphoserine; by PLK2"
FT                   /evidence="ECO:0000269|PubMed:21382555"
FT   MOD_RES         752
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         766
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         780
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         823
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:F6SEU4"
FT   MOD_RES         825
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:F6SEU4"
FT   MOD_RES         828
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:F6SEU4"
FT   MOD_RES         836
FT                   /note="Phosphoserine; by PLK2"
FT                   /evidence="ECO:0000269|PubMed:21382555"
FT   MOD_RES         840
FT                   /note="Phosphoserine; by PLK2"
FT                   /evidence="ECO:0000269|PubMed:21382555"
FT   MOD_RES         842
FT                   /note="Phosphoserine; by PLK2"
FT                   /evidence="ECO:0000269|PubMed:21382555"
FT   MOD_RES         876
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:F6SEU4"
FT   MOD_RES         892
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         895
FT                   /note="Phosphoserine; by PLK2"
FT                   /evidence="ECO:0000269|PubMed:21382555,
FT                   ECO:0007744|PubMed:22673903"
FT   MOD_RES         898
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         985
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:F6SEU4"
FT   MOD_RES         1114
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1118
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:F6SEU4"
FT   MOD_RES         1204
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   VAR_SEQ         1..173
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:9581761"
FT                   /id="VSP_007976"
FT   VAR_SEQ         1..121
FT                   /note="MSRSRASIHRGSIPAMSYAPFRDVRGPPMHRTQYVHSPYDRPGWNPRFCIIS
FT                   GNQLLMLDEDEIHPLLIRDRRSESSRNKLLRRTVSVPVEGRPHGEHEYHLGRSRRKSVP
FT                   GGKQYSMEAA -> MEYF (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:11278737,
FT                   ECO:0000303|PubMed:9620694"
FT                   /id="VSP_007975"
FT   VAR_SEQ         1..98
FT                   /note="MSRSRASIHRGSIPAMSYAPFRDVRGPPMHRTQYVHSPYDRPGWNPRFCIIS
FT                   GNQLLMLDEDEIHPLLIRDRRSESSRNKLLRRTVSVPVEGRPHGEH -> MGLRPPTPT
FT                   PSGGSGSGSLPPPSHRQPLRRRCSSCCFPG (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:9581761,
FT                   ECO:0000303|PubMed:9620694"
FT                   /id="VSP_007974"
FT   VAR_SEQ         1..15
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9581761"
FT                   /id="VSP_026378"
FT   VAR_SEQ         1195..1196
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:11278737,
FT                   ECO:0000303|PubMed:9620694"
FT                   /id="VSP_007977"
FT   VAR_SEQ         1265..1308
FT                   /note="RLMLVEEELRRDHPAMAEPLPEPKKRLLDAQRGSFPPWVQQTRV -> SPSL
FT                   QADAGGGGAAPGPPRHG (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:11278737,
FT                   ECO:0000303|PubMed:9620694"
FT                   /id="VSP_007978"
FT   VAR_SEQ         1296..1308
FT                   /note="RGSFPPWVQQTRV -> LLIR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9581761"
FT                   /id="VSP_007979"
FT   VAR_SEQ         1296..1308
FT                   /note="RGSFPPWVQQTRV -> VERQLPPLGPTNPRVTLAPPWNGLAPPAPPPPPRL
FT                   QITENGEFRNTADH (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:9581761"
FT                   /id="VSP_007980"
FT   MUTAGEN         385
FT                   /note="S->A: Affects stimulation by PLK2."
FT                   /evidence="ECO:0000269|PubMed:21382555"
FT   MUTAGEN         449
FT                   /note="S->A: Affects stimulation by PLK2."
FT                   /evidence="ECO:0000269|PubMed:21382555"
FT   MUTAGEN         485
FT                   /note="R->K: Decreases RapGAP activity by 100-fold."
FT                   /evidence="ECO:0000269|PubMed:18323856"
FT   MUTAGEN         485
FT                   /note="R->P: Abolishes RapGAP activity."
FT                   /evidence="ECO:0000269|PubMed:18323856"
FT   MUTAGEN         487
FT                   /note="N->T: Decreases RapGAP activity by 20-fold."
FT                   /evidence="ECO:0000269|PubMed:18323856"
FT   MUTAGEN         840
FT                   /note="S->A: Blocks the gel mobility shift induced by PLK2
FT                   and affects stimulation by PLK2."
FT                   /evidence="ECO:0000269|PubMed:21382555"
FT   MUTAGEN         842
FT                   /note="S->A: Blocks the gel mobility shift induced by
FT                   PLK2."
FT                   /evidence="ECO:0000269|PubMed:21382555"
FT   CONFLICT        308..309
FT                   /note="WG -> GY (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        316
FT                   /note="N -> M (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        427..429
FT                   /note="HYR -> GQK (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        937..939
FT                   /note="DGP -> ADG (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1002
FT                   /note="H -> G (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1088
FT                   /note="S -> Q (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1277
FT                   /note="H -> L (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          257..262
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   STRAND          403..408
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           414..417
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           418..425
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           428..438
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           441..457
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           463..475
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   STRAND          477..481
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   STRAND          486..488
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           489..501
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           503..519
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   TURN            528..530
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   TURN            533..535
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           536..555
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           556..560
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           563..578
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           582..593
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   TURN            594..597
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           598..603
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   TURN            605..609
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           617..634
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   TURN            642..645
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           647..649
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           650..666
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           685..699
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           700..702
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           705..710
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   TURN            711..713
FT                   /evidence="ECO:0007829|PDB:3BXJ"
FT   HELIX           714..724
FT                   /evidence="ECO:0007829|PDB:3BXJ"
SQ   SEQUENCE   1308 AA;  144722 MW;  CA2536782C8C4DCB CRC64;
     MSRSRASIHR GSIPAMSYAP FRDVRGPPMH RTQYVHSPYD RPGWNPRFCI ISGNQLLMLD
     EDEIHPLLIR DRRSESSRNK LLRRTVSVPV EGRPHGEHEY HLGRSRRKSV PGGKQYSMEA
     APAAPFRPSQ GFLSRRLKSS IKRTKSQPKL DRTSSFRQIL PRFRSADHDR ARLMQSFKES
     HSHESLLSPS SAAEALELNL DEDSIIKPVH SSILGQEFCF EVTTSSGTKC FACRSAAERD
     KWIENLQRAV KPNKDNSRRV DNVLKLWIIE ARELPPKKRY YCELCLDDML YARTTSKPRS
     ASGDTVFWGE HFEFNNLPAV RALRLHLYRD SDKKRKKDKA GYVGLVTVPV ATLAGRHFTE
     QWYPVTLPTG SGGSGGMGSG GGGGSGGGSG GKGKGGCPAV RLKARYQTMS ILPMELYKEF
     AEYVTNHYRM LCAVLEPALN VKGKEEVASA LVHILQSTGK AKDFLSDMAM SEVDRFMERE
     HLIFRENTLA TKAIEEYMRL IGQKYLKDAI GEFIRALYES EENCEVDPIK CTASSLAEHQ
     ANLRMCCELA LCKVVNSHCV FPRELKEVFA SWRLRCAERG REDIADRLIS ASLFLRFLCP
     AIMSPSLFGL MQEYPDEQTS RTLTLIAKVI QNLANFSKFT SKEDFLGFMN EFLELEWGSM
     QQFLYEISNL DTLTNSSSFE GYIDLGRELS TLHALLWEVL PQLSKEALLK LGPLPRLLSD
     ISTALRNPNI QRQPSRQSER ARSQPMVLRG PSAEMQGYMM RDLNSSIDLQ SFMARGLNSS
     MDMARLPSPT KEKPPPPPPG GGKDLFYVSR PPLARSSPAY CTSSSDITEP EQKMLSVNKS
     VSMLDLQGDG PGGRLNSSSV SNLAAVGDLL HSSQASLTAA LGLRPAPAGR LSQGSGSSIT
     AAGMRLSQMG VTTDGVPAQQ LRIPLSFQNP LFHMAADGPG PPAGHGGSSG HGPPSSHHHH
     HHHHHHRGGE PPGDTFAPFH GYSKSEDLST GVPKPPAASI LHSHSYSDEF GPSGTDFTRR
     QLSLQDNLQH MLSPPQITIG PQRPAPSGPG GGSGGGSGGG GGGQPPPLQR GKSQQLTVSA
     AQKPRPSSGN LLQSPEPSYG PARPRQQSLS KEGSIGGSGG SGGGGGGGLK PSITKQHSQT
     PSTLNPTMPA SERTVAWVSN MPHLSADIES AHIEREEYKL KEYSKSMDES RLDRVKEYEE
     EIHSLKERLH MSNRKLEEYE RRLLSQEEQT SKILMQYQAR LEQSEKRLRQ QQVEKDSQIK
     SIIGRLMLVE EELRRDHPAM AEPLPEPKKR LLDAQRGSFP PWVQQTRV
//