SRGAP2
entrez
23380
canonical
uniprot
O75044
canonical
ensembl
ENSG00000266028
resolver
ensp
ENSP00000397990
resolver
ensp
ENSP00000459615
resolver
ensp
ENSP00000473954
resolver
ensp
ENSP00000485517
resolver
ensp
ENSP00000604545
resolver
ensp
ENSP00000604547
resolver
ensp
ENSP00000669933
resolver
enst
ENST00000573034
resolver
enst
ENST00000605610
resolver
enst
ENST00000624873
resolver
enst
ENST00000934487
resolver
genesymbol
SRGAP2
resolver
genesymbol_syn
ARHGAP34
resolver
genesymbol_syn
FNBP2
resolver
genesymbol_syn
KIAA0456
resolver
genesymbol_syn
SRGAP2A
resolver
hgnc
HGNC:19751
resolver
uniprot
A0A075B7B5
resolver
uniprot
A0A096LPC6
resolver
uniprot
A0A1S5UZH8
resolver
uniprot
A2RUF3
resolver
uniprot
B4DFE5
resolver
uniprot
B7Z3G4
resolver
uniprot
B7ZM87
resolver
uniprot_entry
A0A075B7B5_HUMAN
resolver
uniprot_entry
A0A096LPC6_HUMAN
resolver
uniprot_entry
A0A1S5UZH8_HUMAN
resolver
uniprot_entry
B4DFE5_HUMAN
resolver
uniprot_entry
B7Z3G4_HUMAN
resolver
uniprot_entry
B7ZM87_HUMAN
resolver
uniprot_entry
SRGP2_HUMAN
resolver
uniprot_sec
A2RUF3
resolver
activity_regulation
ACTIVITY REGULATION: Activity is strongly inhibited by SRGAP2C, which heterodimerize with SRGAP2/SRGAP2A, thereby reducing SRGAP2/SRGAP2A levels through proteasome-dependent degradation. {ECO:0000269|PubMed:22559944, ECO:0000269|PubMed:27373832, ECO:0000269|PubMed:28333212}.
uniprot
proteins
amino_acid_sequence
MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDLIDQCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENLDATSDKQRLMEMYNNVFCPPMKFEFQPHMGDMASQLCAQQPVQSELVQRCQQLQSRLSTLKIENEEVKKTMEATLQTIQDIVTVEDFDVSDCFQYSNSMESVKSTVSETFMSKPSIAKRRANQQETEQFYFTKMKEYLEGRNLITKLQAKHDLLQKTLGESQRTDCSLARRSSTVRKQDSSQAIPLVVESCIRFISRHGLQHEGIFRVSGSQVEVNDIKNAFERGEDPLAGDQNDHDMDSIAGVLKLYFRGLEHPLFPKDIFHDLMACVTMDNLQERALHIRKVLLVLPKTTLIIMRYLFAFLNHLSQFSEENMMDPYNLAICFGPSLMSVPEGHDQVSCQAHVNELIKTIIIQHENIFPSPRELEGPVYSRGGSMEDYCDSPHGETTSVEDSTQDVTAEHHTSDDECEPIEAIAKFDYVGRTARELSFKKGASLLLYQRASDDWWEGRHNGIDGLIPHQYIVVQDTEDGVVERSSPKSEIEVISEPPEEKVTARAGASCPSGGHVADIYLANINKQRKRPESGSIRKTFRSDSHGLSSSLTDSSSPGVGASCRPSSQPIMSQSLPKEGPDKCSISGHGSLNSISRHSSLKNRLDSPQIRKTATAGRSKSFNNHRPMDPEVIAQDIEATMNSALNELRELERQSSVKHTPDVVLDTLEPLKTSPVVAPTSEPSSPLHTQLLKDPEPAFQRSASTAGDIACAFRPVKSVKMAAPVKPPATRPKPTVFPKTNATSPGVNSSTSPQSTDKSCTV
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration disrupting SRGAP2 has been found in a patient with early infantile epileptic encephalopathy. Balanced translocation t(1;9)(q32;q13) (PubMed:22106086). {ECO:0000269|PubMed:22106086}.
uniprot
proteins
function
FUNCTION: Postsynaptic RAC1 GTPase activating protein (GAP) that plays a key role in neuronal morphogenesis and migration mainly during development of the cerebral cortex (PubMed:20810653, PubMed:27373832, PubMed:28333212). Regulates excitatory and inhibitory synapse maturation and density in cortical pyramidal neurons (PubMed:22559944, PubMed:27373832). SRGAP2/SRGAP2A limits excitatory and inhibitory synapse density through its RAC1-specific GTPase activating activity, while it promotes maturation of both excitatory and inhibitory synapses through its ability to bind to the postsynaptic scaffolding protein HOMER1 at excitatory synapses, and the postsynaptic protein GPHN at inhibitory synapses (By similarity). Mechanistically, acts by binding and deforming membranes, thereby regulating actin dynamics to regulate cell migration and differentiation (PubMed:27373832). Promotes cell repulsion and contact inhibition of locomotion: localizes to protrusions with curved edges and controls the duration of RAC1 activity in contact protrusions (By similarity). In non-neuronal cells, may also play a role in cell migration by regulating the formation of lamellipodia and filopodia (PubMed:20810653, PubMed:21148482). {ECO:0000250|UniProtKB:Q91Z67, ECO:0000269|PubMed:20810653, ECO:0000269|PubMed:21148482, ECO:0000269|PubMed:22559944, ECO:0000269|PubMed:27373832, ECO:0000269|PubMed:28333212}.
uniprot
proteins
mass_dalton
120871
uniprot
proteins
mutagenesis
MUTAGEN 54..55; /note="RK->EE: In F-BARx-R5E mutant; abolished binding to membranes; when associated with 234--E--E-238."; /evidence="ECO:0000269|PubMed:28333212"; MUTAGEN 108; /note="R->K,L,S: Does not affect protein stability."; /evidence="ECO:0000269|PubMed:28333212"; MUTAGEN 108; /note="R->W: Decreased protein stability."; /evidence="ECO:0000269|PubMed:28333212"; MUTAGEN 234..238; /note="KRQAK->EEQAE: In F-BARx-R5E mutant; abolished binding to membranes; when associated with 54-E-E-55."; /evidence="ECO:0000269|PubMed:28333212"; MUTAGEN 527; /note="R->L: Abolished RAC1 GTPase activity; when associated with A-566."; /evidence="ECO:0000269|PubMed:27373832"; MUTAGEN 566; /note="K->A: Abolished RAC1 GTPase activity; when associated with L-527."; /evidence="ECO:0000269|PubMed:27373832"; MUTAGEN 765; /note="W->A: Abolished interaction with ROBO1."; /evidence="ECO:0000269|PubMed:26365803"; MUTAGEN 781; /note="Y->A: Abolished interaction with ROBO1."; /evidence="ECO:0000269|PubMed:26365803"; MUTAGEN 807; /note="P->Q: Increased interaction with ROBO1."; /evidence="ECO:0000269|PubMed:26365803"; MUTAGEN 927; /note="R->A: Loss of the ability to stimulate cell migration, to localize at the plasma membrane protrusions and to dimerize."; /evidence="ECO:0000269|PubMed:20810653
uniprot
proteins
post_translational_modification
PTM: Methylation at Arg-927 is required for the stimulation of cell migration, dimerization and localization at the plasma membrane protrusions. {ECO:0000269|PubMed:20810653}.
uniprot
proteins
pubmed
11672528
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19807924
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20810653
uniprot
proteins
pubmed
21148482
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22106086
uniprot
proteins
pubmed
22467852
uniprot
proteins
pubmed
22559944
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24419634
uniprot
proteins
pubmed
26365803
uniprot
proteins
pubmed
27373832
uniprot
proteins
pubmed
27917825
uniprot
proteins
pubmed
28333212
uniprot
proteins
pubmed
9455484
uniprot
proteins
sequence_length
1071
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21148482}. Cell projection, dendritic spine {ECO:0000303|PubMed:22559944}. Postsynaptic density {ECO:0000250|UniProtKB:Q91Z67}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q91Z67}. Cell projection, lamellipodium {ECO:0000269|PubMed:20810653}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q91Z67}. Nucleus {ECO:0000250|UniProtKB:D4A208}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q91Z67}. Note=Recruited to actin-rich phagosomes during phagocytosis (By similarity). Translocates from nucleus to cytoplasm during development (By similarity). {ECO:0000250|UniProtKB:D4A208, ECO:0000250|UniProtKB:Q91Z67}.
uniprot
proteins