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Ras/Rap GTPase-activating protein SynGAP (Neuronal RasGAP) (Synaptic Ras GTPase-activating protein 1) (Synaptic Ras-GAP 1) (p135 SynGAP)

 SYGP1_RAT               Reviewed;        1308 AA.
Q9QUH6; O88449; Q9ESK6; Q9ET81; Q9QX02; Q9QX06; Q9QX12;
15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
26-JUN-2007, sequence version 2.
02-JUN-2021, entry version 150.
RecName: Full=Ras/Rap GTPase-activating protein SynGAP;
AltName: Full=Neuronal RasGAP;
AltName: Full=Synaptic Ras GTPase-activating protein 1;
Short=Synaptic Ras-GAP 1;
AltName: Full=p135 SynGAP;
Name=Syngap1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
16-276 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 1264-1290 (ISOFORM 5),
AND PROTEIN SEQUENCE OF 32-47; 242-248; 259-272; 300-321; 325-329; 340-354;
419-429; 588-596; 804-815; 923-940; 968-1002; 1086-1102 AND 1276-1286.
STRAIN=Sprague-Dawley;
PubMed=9620694; DOI=10.1016/s0896-6273(00)80471-7;
Chen H.-J., Rojas-Soto M., Oguni A., Kennedy M.B.;
"A synaptic Ras-GTPase activating protein (p135 SynGAP) inhibited by CaM
kinase II.";
Neuron 20:895-904(1998).
[2]
ERRATUM OF PUBMED:9620694.
Oh J.S., Chen H.-J., Rojas-Soto M., Oguni A., Kennedy M.B.;
Neuron 33:151-151(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND INTERACTION WITH DLG3
AND DLG4.
TISSUE=Hippocampus;
PubMed=9581761; DOI=10.1016/s0896-6273(00)81008-9;
Kim J.H., Liao D., Lau L.-F., Huganir R.L.;
"SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein
family.";
Neuron 20:683-691(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
STRAIN=Sprague-Dawley;
PubMed=11278737; DOI=10.1074/jbc.m010744200;
Li W., Okano A., Tian Q.B., Nakayama K., Furihata T., Nawa H., Suzuki T.;
"Characterization of a novel synGAP isoform, synGAP-beta.";
J. Biol. Chem. 276:21417-21424(2001).
[5]
INTERACTION WITH MPDZ; DLG4; CAMK2A AND CAMK2B, PHOSPHORYLATION, AND
FUNCTION.
PubMed=15312654; DOI=10.1016/j.neuron.2004.08.003;
Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.;
"SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity
and NMDA receptor-dependent synaptic AMPA receptor potentiation.";
Neuron 43:563-574(2004).
[6]
FUNCTION.
PubMed=15500970; DOI=10.1016/j.neulet.2004.08.044;
Yang S.-N., Huang C.-B., Yang C.-H., Lai M.-C., Chen W.-F., Wang C.-L.,
Wu C.-L., Huang L.-T.;
"Impaired SynGAP expression and long-term spatial learning and memory in
hippocampal CA1 area from rats previously exposed to perinatal hypoxia-
induced insults: beneficial effects of A68930.";
Neurosci. Lett. 371:73-78(2004).
[7]
INTERACTION WITH KLHL17.
PubMed=16054660; DOI=10.1016/j.neuropharm.2005.05.022;
Chen Y., Li M.;
"Interactions between CAP70 and actinfilin are important for integrity of
actin cytoskeleton structures in neurons.";
Neuropharmacology 49:1026-1041(2005).
[8]
TISSUE SPECIFICITY.
PubMed=16507876; DOI=10.1074/mcp.d500009-mcp200;
Cheng D., Hoogenraad C.C., Rush J., Ramm E., Schlager M.A., Duong D.M.,
Xu P., Wijayawardana S.R., Hanfelt J., Nakagawa T., Sheng M., Peng J.;
"Relative and absolute quantification of postsynaptic density proteome
isolated from rat forebrain and cerebellum.";
Mol. Cell. Proteomics 5:1158-1170(2006).
[9]
FUNCTION.
PubMed=16537406; DOI=10.1073/pnas.0600084103;
Rumbaugh G., Adams J.P., Kim J.H., Huganir R.L.;
"SynGAP regulates synaptic strength and mitogen-activated protein kinases
in cultured neurons.";
Proc. Natl. Acad. Sci. U.S.A. 103:4344-4351(2006).
[10]
PHOSPHORYLATION AT SER-379; SER-385; SER-449; SER-466; SER-836; SER-840;
SER-842 AND SER-895, AND MUTAGENESIS OF SER-385; SER-449; SER-840 AND
SER-842.
PubMed=21382555; DOI=10.1016/j.neuron.2011.02.004;
Lee K.J., Lee Y., Rozeboom A., Lee J.Y., Udagawa N., Hoe H.S., Pak D.T.;
"Requirement for Plk2 in orchestrated ras and rap signaling, homeostatic
structural plasticity, and memory.";
Neuron 69:957-973(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-371; SER-752;
SER-766; SER-780; SER-892; SER-895; SER-898; SER-1114; SER-1118; SER-1121
AND SER-1204, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14 different rat
organs and tissues.";
Nat. Commun. 3:876-876(2012).
[12]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 252-734, FUNCTION, DOMAIN C2, AND
MUTAGENESIS OF ARG-485 AND ASN-487.
PubMed=18323856; DOI=10.1038/embor.2008.20;
Pena V., Hothorn M., Eberth A., Kaschau N., Parret A., Gremer L.,
Bonneau F., Ahmadian M.R., Scheffzek K.;
"The C2 domain of SynGAP is essential for stimulation of the Rap GTPase
reaction.";
EMBO Rep. 9:350-355(2008).
-!- FUNCTION: Major constituent of the PSD essential for postsynaptic
signaling. Inhibitory regulator of the Ras-cAMP pathway. Member of the
NMDAR signaling complex in excitatory synapses, it may play a role in
NMDAR-dependent control of AMPAR potentiation, AMPAR membrane
trafficking and synaptic plasticity. Regulates AMPAR-mediated miniature
excitatory postsynaptic currents. Exhibits dual GTPase-activating
specificity for Ras and Rap. May be involved in certain forms of brain
injury, leading to long-term learning and memory deficits.
{ECO:0000269|PubMed:15312654, ECO:0000269|PubMed:15500970,
ECO:0000269|PubMed:16537406, ECO:0000269|PubMed:18323856}.
-!- SUBUNIT: Isoforms containing the PDZ-binding domain associate with DLG4
and DLG3 to form the PSD protein complex colocalized with GRIN2B at
synapses. Interacts with MPDZ, KLHL17 CAMK2A and CAMK2B.
{ECO:0000269|PubMed:15312654, ECO:0000269|PubMed:16054660,
ECO:0000269|PubMed:9581761}.
-!- INTERACTION:
Q9QUH6; P31016: Dlg4; NbExp=3; IntAct=EBI-2310349, EBI-375655;
Q9QUH6; Q8K430: Klhl17; NbExp=2; IntAct=EBI-2310349, EBI-7713653;
Q9QUH6; Q9JJ40: Pdzk1; NbExp=6; IntAct=EBI-2310349, EBI-7713572;
-!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Cell
junction, synapse. Note=Mostly in excitatory glutamatergic synapses.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q9QUH6-1; Sequence=Displayed;
Name=2; Synonyms=SynGAP-a;
IsoId=Q9QUH6-2; Sequence=VSP_026378, VSP_007979;
Name=3; Synonyms=SynGAP-b;
IsoId=Q9QUH6-3; Sequence=VSP_007974;
Name=4; Synonyms=SynGAP-c;
IsoId=Q9QUH6-4; Sequence=VSP_007976, VSP_007980;
Name=5; Synonyms=SynGAP-d, SynGAP-beta;
IsoId=Q9QUH6-5; Sequence=VSP_007975, VSP_007977, VSP_007978;
-!- TISSUE SPECIFICITY: Highly expressed in brain; predominantly in the
cortex, hippocampus and olfactory bulb. Present in the postsynaptic
density of central excitatory synapses. {ECO:0000269|PubMed:16507876}.
-!- DOMAIN: The PDZ-binding domain interacts with all three PDZ domains of
DGL4. {ECO:0000269|PubMed:18323856}.
-!- DOMAIN: The C2 domain is required for RapGAP activity.
{ECO:0000269|PubMed:18323856}.
-!- PTM: Phosphorylated by CaM-kinase II. Dephosphorylated upon NMDA
receptor activation or SYNGAP1/MPDZ complex disruption. Phosphorylation
by PLK2 promotes its activity. {ECO:0000269|PubMed:15312654,
ECO:0000269|PubMed:21382555}.
-!- CAUTION: It is uncertain whether Met-1 or Met-16 is the initiator
methionine. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC08071.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF048976; AAC08071.1; ALT_INIT; mRNA.
EMBL; AF053938; AAC23491.1; -; mRNA.
EMBL; AF055883; AAC23492.1; -; mRNA.
EMBL; AF058789; AAC63510.2; -; mRNA.
EMBL; AF058790; AAC63511.1; -; mRNA.
EMBL; AF050183; AAC40082.2; -; mRNA.
EMBL; AB016962; BAA74972.1; -; mRNA.
PIR; T13958; T13958.
PIR; T14259; T14259.
PIR; T14270; T14270.
PDB; 3BXJ; X-ray; 3.00 A; A/B=252-734.
PDBsum; 3BXJ; -.
SMR; Q9QUH6; -.
CORUM; Q9QUH6; -.
ELM; Q9QUH6; -.
IntAct; Q9QUH6; 7.
MINT; Q9QUH6; -.
STRING; 10116.ENSRNOP00000044041; -.
ChEMBL; CHEMBL2176804; -.
iPTMnet; Q9QUH6; -.
PhosphoSitePlus; Q9QUH6; -.
PaxDb; Q9QUH6; -.
PRIDE; Q9QUH6; -.
UCSC; RGD:621090; rat. [Q9QUH6-1]
RGD; 621090; Syngap1.
eggNOG; KOG3508; Eukaryota.
InParanoid; Q9QUH6; -.
PhylomeDB; Q9QUH6; -.
Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
EvolutionaryTrace; Q9QUH6; -.
PRO; PR:Q9QUH6; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0043198; C:dendritic shaft; ISO:RGD.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IEA:GOC.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
GO; GO:0045202; C:synapse; IDA:CACAO.
GO; GO:0005096; F:GTPase activator activity; IDA:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0016358; P:dendrite development; ISO:RGD.
GO; GO:0098880; P:maintenance of postsynaptic specialization structure; ISO:RGD.
GO; GO:0050771; P:negative regulation of axonogenesis; ISO:RGD.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IDA:UniProtKB.
GO; GO:0007389; P:pattern specification process; ISO:RGD.
GO; GO:0007265; P:Ras protein signal transduction; ISO:RGD.
GO; GO:0043113; P:receptor clustering; ISO:RGD.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD.
GO; GO:0043408; P:regulation of MAPK cascade; ISO:RGD.
GO; GO:0050803; P:regulation of synapse structure or activity; ISO:RGD.
GO; GO:0048167; P:regulation of synaptic plasticity; IDA:UniProtKB.
GO; GO:0008542; P:visual learning; ISO:RGD.
CDD; cd13375; PH_SynGAP; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR021887; DUF3498.
InterPro; IPR001849; PH_domain.
InterPro; IPR039360; Ras_GTPase.
InterPro; IPR023152; RasGAP_CS.
InterPro; IPR001936; RasGAP_dom.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR037779; SynGAP_PH.
PANTHER; PTHR10194; PTHR10194; 1.
Pfam; PF00168; C2; 1.
Pfam; PF12004; DUF3498; 1.
Pfam; PF00616; RasGAP; 2.
SMART; SM00239; C2; 1.
SMART; SM00233; PH; 1.
SMART; SM00323; RasGAP; 1.
SUPFAM; SSF48350; SSF48350; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction;
Direct protein sequencing; GTPase activation; Membrane; Phosphoprotein;
Reference proteome; SH3-binding; Synapse.
CHAIN 1..1308
/note="Ras/Rap GTPase-activating protein SynGAP"
/id="PRO_0000056655"
DOMAIN 150..251
/note="PH"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
DOMAIN 242..363
/note="C2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
DOMAIN 443..635
/note="Ras-GAP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
REGION 92..113
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 373..394
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 725..751
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 781..809
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 932..1017
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1033..1153
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1197..1308
/note="Interaction with MPDZ"
/evidence="ECO:0000269|PubMed:15312654"
REGION 1276..1308
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOTIF 785..815
/note="SH3-binding"
/evidence="ECO:0000255"
MOTIF 1305..1308
/note="PDZ-binding"
/evidence="ECO:0000255"
COMPBIAS 92..106
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 725..742
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1068..1115
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1132..1153
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1276..1293
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 34
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:F6SEU4"
MOD_RES 39
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:F6SEU4"
MOD_RES 117
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
MOD_RES 371
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
MOD_RES 379
/note="Phosphoserine; by PLK2"
/evidence="ECO:0000269|PubMed:21382555"
MOD_RES 385
/note="Phosphoserine; by PLK2"
/evidence="ECO:0000269|PubMed:21382555"
MOD_RES 449
/note="Phosphoserine; by PLK2"
/evidence="ECO:0000269|PubMed:21382555"
MOD_RES 466
/note="Phosphoserine; by PLK2"
/evidence="ECO:0000269|PubMed:21382555"
MOD_RES 752
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
MOD_RES 766
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
MOD_RES 780
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
MOD_RES 823
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:F6SEU4"
MOD_RES 825
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:F6SEU4"
MOD_RES 828
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:F6SEU4"
MOD_RES 836
/note="Phosphoserine; by PLK2"
/evidence="ECO:0000269|PubMed:21382555"
MOD_RES 840
/note="Phosphoserine; by PLK2"
/evidence="ECO:0000269|PubMed:21382555"
MOD_RES 842
/note="Phosphoserine; by PLK2"
/evidence="ECO:0000269|PubMed:21382555"
MOD_RES 876
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:F6SEU4"
MOD_RES 892
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
MOD_RES 895
/note="Phosphoserine; by PLK2"
/evidence="ECO:0000269|PubMed:21382555,
ECO:0007744|PubMed:22673903"
MOD_RES 898
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
MOD_RES 985
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:F6SEU4"
MOD_RES 1114
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
MOD_RES 1118
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
MOD_RES 1121
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
MOD_RES 1165
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:F6SEU4"
MOD_RES 1204
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
VAR_SEQ 1..173
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|PubMed:9581761"
/id="VSP_007976"
VAR_SEQ 1..121
/note="MSRSRASIHRGSIPAMSYAPFRDVRGPPMHRTQYVHSPYDRPGWNPRFCIIS
GNQLLMLDEDEIHPLLIRDRRSESSRNKLLRRTVSVPVEGRPHGEHEYHLGRSRRKSVP
GGKQYSMEAA -> MEYF (in isoform 5)"
/evidence="ECO:0000303|PubMed:11278737,
ECO:0000303|PubMed:9620694"
/id="VSP_007975"
VAR_SEQ 1..98
/note="MSRSRASIHRGSIPAMSYAPFRDVRGPPMHRTQYVHSPYDRPGWNPRFCIIS
GNQLLMLDEDEIHPLLIRDRRSESSRNKLLRRTVSVPVEGRPHGEH -> MGLRPPTPT
PSGGSGSGSLPPPSHRQPLRRRCSSCCFPG (in isoform 3)"
/evidence="ECO:0000303|PubMed:9581761,
ECO:0000303|PubMed:9620694"
/id="VSP_007974"
VAR_SEQ 1..15
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:9581761"
/id="VSP_026378"
VAR_SEQ 1195..1196
/note="Missing (in isoform 5)"
/evidence="ECO:0000303|PubMed:11278737,
ECO:0000303|PubMed:9620694"
/id="VSP_007977"
VAR_SEQ 1265..1308
/note="RLMLVEEELRRDHPAMAEPLPEPKKRLLDAQRGSFPPWVQQTRV -> SPSL
QADAGGGGAAPGPPRHG (in isoform 5)"
/evidence="ECO:0000303|PubMed:11278737,
ECO:0000303|PubMed:9620694"
/id="VSP_007978"
VAR_SEQ 1296..1308
/note="RGSFPPWVQQTRV -> LLIR (in isoform 2)"
/evidence="ECO:0000303|PubMed:9581761"
/id="VSP_007979"
VAR_SEQ 1296..1308
/note="RGSFPPWVQQTRV -> VERQLPPLGPTNPRVTLAPPWNGLAPPAPPPPPRL
QITENGEFRNTADH (in isoform 4)"
/evidence="ECO:0000303|PubMed:9581761"
/id="VSP_007980"
MUTAGEN 385
/note="S->A: Affects stimulation by PLK2."
/evidence="ECO:0000269|PubMed:21382555"
MUTAGEN 449
/note="S->A: Affects stimulation by PLK2."
/evidence="ECO:0000269|PubMed:21382555"
MUTAGEN 485
/note="R->K: Decreases RapGAP activity by 100-fold."
/evidence="ECO:0000269|PubMed:18323856"
MUTAGEN 485
/note="R->P: Abolishes RapGAP activity."
/evidence="ECO:0000269|PubMed:18323856"
MUTAGEN 487
/note="N->T: Decreases RapGAP activity by 20-fold."
/evidence="ECO:0000269|PubMed:18323856"
MUTAGEN 840
/note="S->A: Blocks the gel mobility shift induced by PLK2
and affects stimulation by PLK2."
/evidence="ECO:0000269|PubMed:21382555"
MUTAGEN 842
/note="S->A: Blocks the gel mobility shift induced by
PLK2."
/evidence="ECO:0000269|PubMed:21382555"
CONFLICT 308..309
/note="WG -> GY (in Ref. 1; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 316
/note="N -> M (in Ref. 1; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 427..429
/note="HYR -> GQK (in Ref. 1; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 937..939
/note="DGP -> ADG (in Ref. 1; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 1002
/note="H -> G (in Ref. 1; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 1088
/note="S -> Q (in Ref. 1; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 1277
/note="H -> L (in Ref. 1; AA sequence)"
/evidence="ECO:0000305"
STRAND 257..262
/evidence="ECO:0007829|PDB:3BXJ"
STRAND 403..408
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 414..417
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 418..425
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 428..438
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 441..457
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 463..475
/evidence="ECO:0007829|PDB:3BXJ"
STRAND 477..481
/evidence="ECO:0007829|PDB:3BXJ"
STRAND 486..488
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 489..501
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 503..519
/evidence="ECO:0007829|PDB:3BXJ"
TURN 528..530
/evidence="ECO:0007829|PDB:3BXJ"
TURN 533..535
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 536..555
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 556..560
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 563..578
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 582..593
/evidence="ECO:0007829|PDB:3BXJ"
TURN 594..597
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 598..603
/evidence="ECO:0007829|PDB:3BXJ"
TURN 605..609
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 617..634
/evidence="ECO:0007829|PDB:3BXJ"
TURN 642..645
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 647..649
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 650..666
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 685..699
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 700..702
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 705..710
/evidence="ECO:0007829|PDB:3BXJ"
TURN 711..713
/evidence="ECO:0007829|PDB:3BXJ"
HELIX 714..724
/evidence="ECO:0007829|PDB:3BXJ"
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


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Related Genes :
[Syngap1] Ras/Rap GTPase-activating protein SynGAP (Neuronal RasGAP) (Synaptic Ras GTPase-activating protein 1) (Synaptic Ras-GAP 1) (p135 SynGAP)
[SYNGAP1 KIAA1938] Ras/Rap GTPase-activating protein SynGAP (Neuronal RasGAP) (Synaptic Ras GTPase-activating protein 1) (Synaptic Ras-GAP 1)
[Syngap1] Ras/Rap GTPase-activating protein SynGAP (Neuronal RasGAP) (Synaptic Ras GTPase-activating protein 1) (Synaptic Ras-GAP 1)
[RASA1 GAP RASA] Ras GTPase-activating protein 1 (GAP) (GTPase-activating protein) (RasGAP) (Ras p21 protein activator) (p120GAP)
[RASA4 CAPRI GAPL KIAA0538] Ras GTPase-activating protein 4 (Calcium-promoted Ras inactivator) (Ras p21 protein activator 4) (RasGAP-activating-like protein 2)
[G3bp1 G3bp] Ras GTPase-activating protein-binding protein 1 (G3BP-1) (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent DNA helicase VIII) (GAP SH3 domain-binding protein 1) (HDH-VIII)
[rgaA DG1029 rasGAP1 DDB_G0287585] Ras GTPase-activating-like protein rgaA (DGAP1) (Developmental gene 1029 protein)
[HRAS HRAS1] GTPase HRas (EC 3.6.5.2) (H-Ras-1) (Ha-Ras) (Transforming protein p21) (c-H-ras) (p21ras) [Cleaved into: GTPase HRas, N-terminally processed]
[G3BP1 G3BP] Ras GTPase-activating protein-binding protein 1 (G3BP-1) (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent DNA helicase VIII) (hDH VIII) (GAP SH3 domain-binding protein 1)
[Khdrbs1] KH domain-containing, RNA-binding, signal transduction-associated protein 1 (GAP-associated tyrosine phosphoprotein p62) (Src-associated in mitosis 68 kDa protein) (Sam68) (p21 Ras GTPase-activating protein-associated p62) (p68)
[RAPGEF2 KIAA0313 NRAPGEP PDZGEF1] Rap guanine nucleotide exchange factor 2 (Cyclic nucleotide ras GEF) (CNrasGEF) (Neural RAP guanine nucleotide exchange protein) (nRap GEP) (PDZ domain-containing guanine nucleotide exchange factor 1) (PDZ-GEF1) (RA-GEF-1) (Ras/Rap1-associating GEF-1)
[Rapgef2 Pdzgef1] Rap guanine nucleotide exchange factor 2 (Cyclic nucleotide ras GEF) (CNrasGEF) (Neural RAP guanine nucleotide exchange protein) (nRap GEP) (PDZ domain-containing guanine nucleotide exchange factor 1) (PDZ-GEF1) (RA-GEF-1) (Ras/Rap1-associating GEF-1)
[KRAS KRAS2 RASK2] GTPase KRas (EC 3.6.5.2) (K-Ras 2) (Ki-Ras) (c-K-ras) (c-Ki-ras) [Cleaved into: GTPase KRas, N-terminally processed]
[IQGAP1 KIAA0051] Ras GTPase-activating-like protein IQGAP1 (p195)
[Rapgef2 Kiaa0313 Pdzgef1] Rap guanine nucleotide exchange factor 2 (Cyclic nucleotide ras GEF) (CNrasGEF) (Neural RAP guanine nucleotide exchange protein) (nRap GEP) (PDZ domain-containing guanine nucleotide exchange factor 1) (PDZ-GEF1) (RA-GEF-1) (Ras/Rap1-associating GEF-1)
[Iqgap1] Ras GTPase-activating-like protein IQGAP1
[RAPGEF2 NRAPGEP PDZGEF1] Rap guanine nucleotide exchange factor 2 (Cyclic nucleotide ras GEF) (CNrasGEF) (Neural RAP guanine nucleotide exchange protein) (nRap GEP) (PDZ domain-containing guanine nucleotide exchange factor 1) (PDZ-GEF1) (RA-GEF-1) (Ras/Rap1-associating GEF-1)
[RAPGEF2 NRAPGEP PDZGEF1] Rap guanine nucleotide exchange factor 2 (Cyclic nucleotide ras GEF) (CNrasGEF) (Neural RAP guanine nucleotide exchange protein) (nRap GEP) (PDZ domain-containing guanine nucleotide exchange factor 1) (PDZ-GEF1) (RA-GEF-1) (Ras/Rap1-associating GEF-1)
[RALGAPA1 GARNL1 KIAA0884 TULIP1] Ral GTPase-activating protein subunit alpha-1 (GAP-related-interacting partner to E12) (GRIPE) (GTPase-activating Rap/Ran-GAP domain-like 1) (Tuberin-like protein 1) (p240)
[Rasa4 Capri Kiaa0538] Ras GTPase-activating protein 4 (Calcium-promoted Ras inactivator) (Ras p21 protein activator 4) (RasGAP-activating-like protein 2)
[Sipa1l1 Spa1] Signal-induced proliferation-associated 1-like protein 1 (SIPA1-like protein 1) (SPA-1-like protein p1294) (Spine-associated Rap GTPase-activating protein) (SPAR)
[KHDRBS1 SAM68] KH domain-containing, RNA-binding, signal transduction-associated protein 1 (GAP-associated tyrosine phosphoprotein p62) (Src-associated in mitosis 68 kDa protein) (Sam68) (p21 Ras GTPase-activating protein-associated p62) (p68)
[RAC1 TC25 MIG5] Ras-related C3 botulinum toxin substrate 1 (EC 3.6.5.2) (Cell migration-inducing gene 5 protein) (Ras-like protein TC25) (p21-Rac1)
[Arhgap32 Grit Kiaa0712 Rics] Rho GTPase-activating protein 32 (Brain-specific Rho GTPase-activating protein) (GAB-associated Cdc42/Rac GTPase-activating protein) (GC-GAP) (Rho-type GTPase-activating protein 32) (Rho/Cdc42/Rac GTPase-activating protein RICS) (RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling) (p200RhoGAP) (p250GAP)
[GAPVD1 GAPEX5 KIAA1521 RAP6] GTPase-activating protein and VPS9 domain-containing protein 1 (GAPex-5) (Rab5-activating protein 6)
[Khdrbs1 Sam68] KH domain-containing, RNA-binding, signal transduction-associated protein 1 (GAP-associated tyrosine phosphoprotein p62) (Src-associated in mitosis 68 kDa protein) (Sam68) (p21 Ras GTPase-activating protein-associated p62) (p68)
[ced-10 rac-1 C09G12.8] Ras-related protein ced-10 (CErac1) (Cell death protein 10) (Cell-corpse engulfment protein ced-10) (Ras-related protein rac-1)
[Rac1] Ras-related C3 botulinum toxin substrate 1 (EC 3.6.5.2) (p21-Rac1)
[NRAS HRAS1] GTPase NRas (EC 3.6.5.2) (Transforming protein N-Ras)
[Rac1 Rac] Ras-related C3 botulinum toxin substrate 1 (EC 3.6.5.2) (p21-Rac1)

Bibliography :
No related Items