SYGP1_RAT
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 03-AUG-2022, entry version 153.
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 iPTMnet; Q9QUH6; -.
DR PhosphoSitePlus; Q9QUH6; -.
DR PaxDb; Q9QUH6; -.
DR PRIDE; Q9QUH6; -.
DR UCSC; RGD:621090; rat. [Q9QUH6-1]
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:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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; IDA: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:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0098880; P:maintenance of postsynaptic specialization structure; 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: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:0043087; P:regulation of GTPase activity; IEA:InterPro.
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; cd13375; PH_SynGAP; 1.
DR Gene3D; 1.10.506.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 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; PTHR10194; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12004; DUF3498; 1.
DR Pfam; PF00616; RasGAP; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 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
