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Rho GTPase-activating protein 35 (Glucocorticoid receptor DNA-binding factor 1) (Glucocorticoid receptor repression factor 1) (GRF-1) (Rho GAP p190A) (p190-A)

 RHG35_HUMAN             Reviewed;        1499 AA.
Q9NRY4; A7E2A4; Q14452; Q9C0E1;
04-APR-2003, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 3.
12-SEP-2018, entry version 183.
RecName: Full=Rho GTPase-activating protein 35 {ECO:0000312|HGNC:HGNC:4591};
AltName: Full=Glucocorticoid receptor DNA-binding factor 1;
AltName: Full=Glucocorticoid receptor repression factor 1;
Short=GRF-1;
AltName: Full=Rho GAP p190A;
Short=p190-A {ECO:0000303|PubMed:11054565};
Name=ARHGAP35 {ECO:0000312|HGNC:HGNC:4591};
Synonyms=GRF1 {ECO:0000303|PubMed:1894621},
GRLF1 {ECO:0000303|PubMed:1894621}, KIAA1722,
P190A {ECO:0000303|PubMed:19673492},
p190ARHOGAP {ECO:0000303|PubMed:19673492};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000312|EMBL:AAF80386.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=11214970; DOI=10.1093/dnares/7.6.347;
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:347-355(2000).
[2]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1491.
TISSUE=Mammary cancer;
PubMed=11054565; DOI=10.1016/S0378-1119(00)00387-5;
Tikoo A., Czekay S., Viars C., White S., Heath J.K., Arden K.,
Maruta H.;
"p190-A, a human tumor suppressor gene, maps to the chromosomal region
19q13.3 that is reportedly deleted in some gliomas.";
Gene 257:23-31(2000).
[6] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] OF 377-1453, AND FUNCTION.
TISSUE=Mammary cancer;
PubMed=1894621;
LeClerc S., Palaniswami R., Xie B.X., Govindan M.V.;
"Molecular cloning and characterization of a factor that binds the
human glucocorticoid receptor gene and represses its expression.";
J. Biol. Chem. 266:17333-17340(1991).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[9]
PHOSPHORYLATION AT TYR-1105.
PubMed=18829532; DOI=10.1158/0008-5472.CAN-08-0997;
Shen C.H., Chen H.Y., Lin M.S., Li F.Y., Chang C.C., Kuo M.L.,
Settleman J., Chen R.H.;
"Breast tumor kinase phosphorylates p190RhoGAP to regulate rho and ras
and promote breast carcinoma growth, migration, and invasion.";
Cancer Res. 68:7779-7787(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-970 AND SER-1179, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1179, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589; SER-970; SER-975;
SER-1150 AND SER-1179, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION AT SER-1221; THR-1226
AND SER-1236, MUTAGENESIS OF SER-1221; THR-1226 AND SER-1236, AND
BINDING TO PHOSPHOLIPIDS.
PubMed=19673492; DOI=10.1021/bi900667y;
Levay M., Settleman J., Ligeti E.;
"Regulation of the substrate preference of p190RhoGAP by protein
kinase C-mediated phosphorylation of a phospholipid binding site.";
Biochemistry 48:8615-8623(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589; SER-773; SER-975;
SER-1072; TYR-1087; TYR-1105; SER-1134 AND SER-1179, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
TISSUE SPECIFICITY.
PubMed=20675588; DOI=10.4049/jimmunol.0904163;
Nemeth T., Futosi K., Hably C., Brouns M.R., Jakob S.M., Kovacs M.,
Kertesz Z., Walzog B., Settleman J., Mocsai A.;
"Neutrophil functions and autoimmune arthritis in the absence of
p190RhoGAP: generation and analysis of a novel null mutation in
mice.";
J. Immunol. 185:3064-3075(2010).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589 AND SER-1179, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589; SER-1134; SER-1150
AND SER-1179, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589; SER-770; SER-773;
SER-1134; SER-1150; SER-1176 AND SER-1179, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589; SER-1001; SER-1150
AND SER-1179, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
FUNCTION, AND DOMAIN.
PubMed=28894085; DOI=10.1038/s41467-017-00483-x;
Stiegler A.L., Boggon T.J.;
"p190RhoGAP proteins contain pseudoGTPase domains.";
Nat. Commun. 8:506-506(2017).
[23] {ECO:0000244|PDB:3C5H}
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 13-249 IN COMPLEX WITH GTP
ANALOG.
Structural genomics consortium (SGC);
"Crystal structure of the Ras homolog domain of human GRLF1
(p190RhoGAP).";
Submitted (JAN-2008) to the PDB data bank.
[24] {ECO:0000244|PDB:3FK2}
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1212-1439.
Structural genomics consortium (SGC);
"Crystal structure of the RhoGAP domain of human glucocorticoid
receptor DNA-binding factor 1.";
Submitted (DEC-2008) to the PDB data bank.
[25]
STRUCTURE BY NMR OF 267-331, PHOSPHORYLATION AT TYR-308, AND
INTERACTION WITH GTF2I.
PubMed=19393245; DOI=10.1016/j.jmb.2009.04.035;
Bonet R., Ruiz L., Aragon E., Martin-Malpartida P., Macias M.J.;
"NMR structural studies on human p190-A RhoGAPFF1 revealed that domain
phosphorylation by the PDGF-receptor alpha requires its previous
unfolding.";
J. Mol. Biol. 389:230-237(2009).
-!- FUNCTION: Rho GTPase-activating protein (GAP) (PubMed:19673492,
PubMed:28894085). Binds several acidic phospholipids which
inhibits the Rho GAP activity to promote the Rac GAP activity
(PubMed:19673492). This binding is inhibited by phosphorylation by
PRKCA (PubMed:19673492). Involved in cell differentiation as well
as cell adhesion and migration, plays an important role in retinal
tissue morphogenesis, neural tube fusion, midline fusion of the
cerebral hemispheres and mammary gland branching morphogenesis (By
similarity). Transduces signals from p21-ras to the nucleus,
acting via the ras GTPase-activating protein (GAP) (By
similarity). Transduces SRC-dependent signals from cell-surface
adhesion molecules, such as laminin, to promote neurite outgrowth.
Regulates axon outgrowth, guidance and fasciculation (By
similarity). Modulates Rho GTPase-dependent F-actin
polymerization, organization and assembly, is involved in
polarized cell migration and in the positive regulation of
ciliogenesis and cilia elongation (By similarity). During mammary
gland development, is required in both the epithelial and stromal
compartments for ductal outgrowth (By similarity). Represses
transcription of the glucocorticoid receptor by binding to the
cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'; this
function is however unclear and would need additional experimental
evidences (PubMed:1894621). {ECO:0000250|UniProtKB:P81128,
ECO:0000250|UniProtKB:Q91YM2, ECO:0000269|PubMed:1894621,
ECO:0000269|PubMed:19673492, ECO:0000269|PubMed:28894085}.
-!- ACTIVITY REGULATION: Binding of acidic phospholipids inhibits the
Rho GAP activity and promotes the Rac GAP activity.
{ECO:0000269|PubMed:19673492}.
-!- SUBUNIT: Interacts with RASA1 (By similarity). Interacts with the
general transcription factor GTF2I, the interaction sequesters
GTF2I in the cytoplasm (PubMed:19393245).
{ECO:0000250|UniProtKB:Q91YM2, ECO:0000269|PubMed:19393245}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
{ECO:0000250|UniProtKB:Q91YM2}. Cytoplasm
{ECO:0000250|UniProtKB:Q91YM2}. Nucleus
{ECO:0000305|PubMed:1894621}. Cell membrane
{ECO:0000250|UniProtKB:Q91YM2}. Note=In response to integrins and
SDC4 and upon phosphorylation by PKC, relocalizes from the
cytoplasm to regions of plasma membrane ruffling where it
colocalizes with polymerized actin.
{ECO:0000250|UniProtKB:Q91YM2}.
-!- TISSUE SPECIFICITY: Detected in neutrophils (at protein level).
{ECO:0000269|PubMed:1894621}.
-!- DOMAIN: N-terminal part (1-266) has GTPase activity. Required for
proper cellular localization. {ECO:0000250|UniProtKB:Q91YM2}.
-!- DOMAIN: The pG1 pseudoGTPase domain does not bind GTP.
{ECO:0000269|PubMed:28894085}.
-!- PTM: Phosphorylation of Tyr-1105 by PTK6 promotes the association
with RASA1, inactivating RHOA while activating RAS.
Phosphorylation at Tyr-308 by PDGFRA inhibits binding to GTF2I
(PubMed:18829532, PubMed:19393245). Phosphorylated by PRKCA at
Ser-1221 and Thr-1226, induces relocalization from the cytoplasm
to regions of plasma membrane ruffling and prevents the binding
and substrate specificity regulation by phospholipids
(PubMed:19673492). In brain, phosphorylated by FYN and SRC (By
similarity). During focal adhesion formation, phosphorylated by
MAPK1 and MAPK3 at the C-terminal region, probably at Ser-1451,
Ser-1476, Thr-1480 and Ser-1483. Phosphorylation by MAPK1 and
MAPK3 inhibits GAP function and localizes ARGHAP35 away from newly
forming focal adhesions and stress fibers in cells spreading on
fibronectin (By similarity). Phosphorylation at Ser-1476 and Thr-
1480 by GSK3B requires priming by MAPK and inhibits RhoGAP
activity and modulates polarized cell migration (By similarity).
{ECO:0000250|UniProtKB:P81128, ECO:0000250|UniProtKB:Q91YM2,
ECO:0000269|PubMed:18829532, ECO:0000269|PubMed:19393245,
ECO:0000269|PubMed:19673492}.
-!- SEQUENCE CAUTION:
Sequence=AAA58618.1; Type=Frameshift; Positions=389, 533, 540, 607, 614, 1167, 1241, 1292, 1334, 1446; Evidence={ECO:0000305};
Sequence=AAF80386.1; Type=Frameshift; Positions=533, 540, 607, 614; Evidence={ECO:0000305};
Sequence=AAF80386.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
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EMBL; AB051509; BAB21813.2; -; mRNA.
EMBL; CH471126; EAW57450.1; -; Genomic_DNA.
EMBL; BC150257; AAI50258.1; -; mRNA.
EMBL; AF159851; AAF80386.1; ALT_SEQ; mRNA.
EMBL; M73077; AAA58618.1; ALT_FRAME; mRNA.
CCDS; CCDS46127.1; -.
RefSeq; NP_004482.4; NM_004491.4.
RefSeq; XP_016882203.1; XM_017026714.1.
UniGene; Hs.509447; -.
PDB; 2K85; NMR; -; A=267-331.
PDB; 3C5H; X-ray; 1.80 A; A=13-249.
PDB; 3FK2; X-ray; 2.80 A; A/B/C/D=1212-1439.
PDBsum; 2K85; -.
PDBsum; 3C5H; -.
PDBsum; 3FK2; -.
ProteinModelPortal; Q9NRY4; -.
SMR; Q9NRY4; -.
BioGrid; 109166; 14.
DIP; DIP-34578N; -.
IntAct; Q9NRY4; 5.
MINT; Q9NRY4; -.
STRING; 9606.ENSP00000385720; -.
iPTMnet; Q9NRY4; -.
PhosphoSitePlus; Q9NRY4; -.
BioMuta; ARHGAP35; -.
DMDM; 408360250; -.
EPD; Q9NRY4; -.
PaxDb; Q9NRY4; -.
PeptideAtlas; Q9NRY4; -.
PRIDE; Q9NRY4; -.
ProteomicsDB; 82441; -.
Ensembl; ENST00000404338; ENSP00000385720; ENSG00000160007.
Ensembl; ENST00000614079; ENSP00000483730; ENSG00000160007.
GeneID; 2909; -.
KEGG; hsa:2909; -.
UCSC; uc010ekv.4; human.
CTD; 2909; -.
DisGeNET; 2909; -.
EuPathDB; HostDB:ENSG00000160007.17; -.
GeneCards; ARHGAP35; -.
H-InvDB; HIX0015264; -.
HGNC; HGNC:4591; ARHGAP35.
HPA; CAB037311; -.
HPA; HPA055184; -.
HPA; HPA056470; -.
MIM; 605277; gene.
neXtProt; NX_Q9NRY4; -.
OpenTargets; ENSG00000160007; -.
PharmGKB; PA28988; -.
eggNOG; KOG4271; Eukaryota.
eggNOG; ENOG410XR4E; LUCA.
GeneTree; ENSGT00920000148997; -.
HOVERGEN; HBG051844; -.
InParanoid; Q9NRY4; -.
KO; K05732; -.
OMA; MLRAFLC; -.
OrthoDB; EOG091G00ZO; -.
TreeFam; TF324451; -.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-416550; Sema4D mediated inhibition of cell attachment and migration.
Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
SignaLink; Q9NRY4; -.
SIGNOR; Q9NRY4; -.
ChiTaRS; ARHGAP35; human.
EvolutionaryTrace; Q9NRY4; -.
GeneWiki; GRLF1; -.
GenomeRNAi; 2909; -.
PRO; PR:Q9NRY4; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000160007; Expressed in 226 organ(s), highest expression level in frontal cortex.
CleanEx; HS_GRLF1; -.
Genevisible; Q9NRY4; HS.
GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IC:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
GO; GO:0007413; P:axonal fasciculation; ISS:UniProtKB.
GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0031668; P:cellular response to extracellular stimulus; ISS:UniProtKB.
GO; GO:0021955; P:central nervous system neuron axonogenesis; ISS:UniProtKB.
GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; ISS:UniProtKB.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0030879; P:mammary gland development; ISS:UniProtKB.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0043116; P:negative regulation of vascular permeability; IEA:Ensembl.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0097485; P:neuron projection guidance; ISS:UniProtKB.
GO; GO:0045724; P:positive regulation of cilium assembly; ISS:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
GO; GO:0008064; P:regulation of actin polymerization or depolymerization; ISS:UniProtKB.
GO; GO:0050770; P:regulation of axonogenesis; ISS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; TAS:ProtInc.
GO; GO:0044319; P:wound healing, spreading of cells; ISS:UniProtKB.
Gene3D; 1.10.10.440; -; 2.
Gene3D; 1.10.555.10; -; 1.
InterPro; IPR002713; FF_domain.
InterPro; IPR036517; FF_domain_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR039007; pG1.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR032835; RhoGAP-FF1.
InterPro; IPR000198; RhoGAP_dom.
InterPro; IPR039006; RhoGAP_pG2.
InterPro; IPR001806; Small_GTPase.
Pfam; PF01846; FF; 1.
Pfam; PF00071; Ras; 1.
Pfam; PF00620; RhoGAP; 1.
Pfam; PF16512; RhoGAP-FF1; 1.
SMART; SM00441; FF; 4.
SMART; SM00324; RhoGAP; 1.
SUPFAM; SSF48350; SSF48350; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF81698; SSF81698; 1.
PROSITE; PS51676; FF; 4.
PROSITE; PS51852; PG1; 1.
PROSITE; PS51853; PG2; 1.
PROSITE; PS50238; RHOGAP; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Cell projection; Complete proteome;
Cytoplasm; Cytoskeleton; DNA-binding; GTP-binding; GTPase activation;
Lipid-binding; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation.
CHAIN 1 1499 Rho GTPase-activating protein 35.
/FTId=PRO_0000056730.
DOMAIN 270 327 FF 1.
DOMAIN 368 422 FF 2.
DOMAIN 429 483 FF 3.
DOMAIN 485 550 FF 4.
DOMAIN 592 767 pG1 pseudoGTPase. {ECO:0000255|PROSITE-
ProRule:PRU01199}.
DOMAIN 783 947 pG2 pseudoGTPase. {ECO:0000255|PROSITE-
ProRule:PRU01200}.
DOMAIN 1249 1436 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
NP_BIND 33 37 GTP. {ECO:0000244|PDB:3C5H,
ECO:0000269|Ref.23}.
NP_BIND 95 97 GTP. {ECO:0000244|PDB:3C5H,
ECO:0000269|Ref.23}.
NP_BIND 201 203 GTP. {ECO:0000244|PDB:3C5H,
ECO:0000269|Ref.23}.
NP_BIND 229 231 GTP. {ECO:0000244|PDB:3C5H,
ECO:0000269|Ref.23}.
REGION 1 266 Has GTPase activity, required for proper
localization.
{ECO:0000250|UniProtKB:Q91YM2}.
REGION 1213 1236 Required for phospholipid binding and
regulation of the substrate preference.
{ECO:0000269|PubMed:19673492}.
COMPBIAS 1440 1490 Pro-rich.
BINDING 28 28 GTP. {ECO:0000244|PDB:3C5H,
ECO:0000269|Ref.23}.
BINDING 52 52 GTP; via carbonyl oxygen.
{ECO:0000244|PDB:3C5H,
ECO:0000269|Ref.23}.
BINDING 56 56 GTP. {ECO:0000244|PDB:3C5H,
ECO:0000269|Ref.23}.
MOD_RES 308 308 Phosphotyrosine.
{ECO:0000269|PubMed:19393245}.
MOD_RES 589 589 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 770 770 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 773 773 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 970 970 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648}.
MOD_RES 975 975 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 985 985 Phosphoserine.
{ECO:0000250|UniProtKB:Q91YM2}.
MOD_RES 1001 1001 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1072 1072 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1087 1087 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1105 1105 Phosphotyrosine; by ABL2 and PTK6.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:18829532}.
MOD_RES 1134 1134 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1142 1142 Phosphoserine.
{ECO:0000250|UniProtKB:Q91YM2}.
MOD_RES 1150 1150 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1176 1176 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1179 1179 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1221 1221 Phosphoserine; by PKC/PRKCA.
{ECO:0000269|PubMed:19673492}.
MOD_RES 1226 1226 Phosphothreonine; by PKC/PRKCA.
{ECO:0000269|PubMed:19673492}.
MOD_RES 1236 1236 Phosphoserine; by PKC/PRKCA.
{ECO:0000269|PubMed:19673492}.
MOD_RES 1472 1472 Phosphoserine.
{ECO:0000250|UniProtKB:Q91YM2}.
MOD_RES 1476 1476 Phosphoserine.
{ECO:0000250|UniProtKB:Q91YM2}.
MOD_RES 1480 1480 Phosphothreonine.
{ECO:0000250|UniProtKB:Q91YM2}.
MOD_RES 1483 1483 Phosphoserine.
{ECO:0000250|UniProtKB:Q91YM2}.
MUTAGEN 1221 1221 S->A: No effect on total phosphorylation
levels. Abolishes inhibition of
phospholipid binding by PRKCA
phosphorylation. Decreases
phosphorylation by PRKCA; when associated
with A-1226. Abolishes phosphorylation by
PRKCA; when associated with A-1126 and A-
1236. {ECO:0000269|PubMed:19673492}.
MUTAGEN 1221 1221 S->D: Enhances Rac GAP activity.
{ECO:0000269|PubMed:19673492}.
MUTAGEN 1226 1226 T->A: No effect on total phosphorylation
levels. Abolishes inhibition of
phospholipid binding by PRKCA
phosphorylation. Decreases
phosphorylation by PRKCA; when associated
with A-1221. Abolishes phosphorylation by
PRKCA; when associated with A-1121 and A-
1236. {ECO:0000269|PubMed:19673492}.
MUTAGEN 1226 1226 T->D: Enhances Rac GAP activity.
{ECO:0000269|PubMed:19673492}.
MUTAGEN 1236 1236 S->A: No effect on total phosphorylation
levels. No effect on inhibition of
phospholipid binding by PRKCA
phosphorylation. Abolishes
phosphorylation by PRKCA; when associated
with A-1121 and A-1226.
{ECO:0000269|PubMed:19673492}.
CONFLICT 251 251 R -> P (in Ref. 5; AAF80386).
{ECO:0000305}.
CONFLICT 309 309 V -> D (in Ref. 5; AAF80386).
{ECO:0000305}.
CONFLICT 362 362 S -> G (in Ref. 5; AAF80386).
{ECO:0000305}.
CONFLICT 414 414 Q -> A (in Ref. 5; AAF80386 and 6;
AAA58618). {ECO:0000305}.
CONFLICT 474 474 M -> T (in Ref. 5; AAF80386 and 6;
AAA58618). {ECO:0000305}.
CONFLICT 978 978 C -> S (in Ref. 5; AAF80386).
{ECO:0000305}.
CONFLICT 1292 1292 M -> I (in Ref. 5; AAF80386).
{ECO:0000305}.
CONFLICT 1452 1453 PS -> RN (in Ref. 6; AAA58618).
{ECO:0000305}.
STRAND 14 21 {ECO:0000244|PDB:3C5H}.
TURN 25 30 {ECO:0000244|PDB:3C5H}.
HELIX 35 43 {ECO:0000244|PDB:3C5H}.
TURN 47 49 {ECO:0000244|PDB:3C5H}.
HELIX 60 63 {ECO:0000244|PDB:3C5H}.
TURN 66 70 {ECO:0000244|PDB:3C5H}.
STRAND 72 79 {ECO:0000244|PDB:3C5H}.
STRAND 91 96 {ECO:0000244|PDB:3C5H}.
TURN 102 104 {ECO:0000244|PDB:3C5H}.
HELIX 110 112 {ECO:0000244|PDB:3C5H}.
HELIX 116 120 {ECO:0000244|PDB:3C5H}.
STRAND 123 126 {ECO:0000244|PDB:3C5H}.
HELIX 136 138 {ECO:0000244|PDB:3C5H}.
HELIX 142 144 {ECO:0000244|PDB:3C5H}.
HELIX 151 153 {ECO:0000244|PDB:3C5H}.
STRAND 154 156 {ECO:0000244|PDB:3C5H}.
STRAND 159 165 {ECO:0000244|PDB:3C5H}.
HELIX 174 190 {ECO:0000244|PDB:3C5H}.
STRAND 195 200 {ECO:0000244|PDB:3C5H}.
HELIX 202 204 {ECO:0000244|PDB:3C5H}.
HELIX 207 218 {ECO:0000244|PDB:3C5H}.
STRAND 220 222 {ECO:0000244|PDB:3C5H}.
STRAND 225 227 {ECO:0000244|PDB:3C5H}.
TURN 230 233 {ECO:0000244|PDB:3C5H}.
HELIX 236 248 {ECO:0000244|PDB:3C5H}.
TURN 268 271 {ECO:0000244|PDB:2K85}.
HELIX 272 284 {ECO:0000244|PDB:2K85}.
STRAND 286 288 {ECO:0000244|PDB:2K85}.
HELIX 292 299 {ECO:0000244|PDB:2K85}.
HELIX 303 311 {ECO:0000244|PDB:2K85}.
HELIX 314 330 {ECO:0000244|PDB:2K85}.
HELIX 1251 1254 {ECO:0000244|PDB:3FK2}.
STRAND 1257 1259 {ECO:0000244|PDB:3FK2}.
HELIX 1263 1275 {ECO:0000244|PDB:3FK2}.
TURN 1280 1284 {ECO:0000244|PDB:3FK2}.
HELIX 1289 1301 {ECO:0000244|PDB:3FK2}.
HELIX 1308 1310 {ECO:0000244|PDB:3FK2}.
HELIX 1314 1327 {ECO:0000244|PDB:3FK2}.
STRAND 1328 1330 {ECO:0000244|PDB:3FK2}.
HELIX 1335 1344 {ECO:0000244|PDB:3FK2}.
HELIX 1350 1362 {ECO:0000244|PDB:3FK2}.
HELIX 1366 1383 {ECO:0000244|PDB:3FK2}.
HELIX 1386 1389 {ECO:0000244|PDB:3FK2}.
HELIX 1393 1405 {ECO:0000244|PDB:3FK2}.
STRAND 1409 1412 {ECO:0000244|PDB:3FK2}.
HELIX 1414 1430 {ECO:0000244|PDB:3FK2}.
HELIX 1432 1436 {ECO:0000244|PDB:3FK2}.
SEQUENCE 1499 AA; 170514 MW; 8CCB493414A7E3E6 CRC64;
MMMARKQDVR IPTYNISVVG LSGTEKEKGQ CGIGKSCLCN RFVRPSADEF HLDHTSVLST
SDFGGRVVNN DHFLYWGEVS RSLEDCVECK MHIVEQTEFI DDQTFQPHRS TALQPYIKRA
AATKLASAEK LMYFCTDQLG LEQDFEQKQM PDGKLLVDGF LLGIDVSRGM NRNFDDQLKF
VSNLYNQLAK TKKPIVVVLT KCDEGVERYI RDAHTFALSK KNLQVVETSA RSNVNVDLAF
STLVQLIDKS RGKTKIIPYF EALKQQSQQI ATAKDKYEWL VSRIVKNHNE NWLSVSRKMQ
ASPEYQDYVY LEGTQKAKKL FLQHIHRLKH EHIERRRKLY LAALPLAFEA LIPNLDEIDH
LSCIKAKKLL ETKPEFLKWF VVLEETPWDA TSHIDNMENE RIPFDLMDTV PAEQLYEAHL
EKLRNERKRV EMRRAFKENL ETSPFITPGK PWEEARSFIM NEDFYQWLEE SVYMDIYGKH
QKQIIDKAKE EFQELLLEYS ELFYELELDA KPSKEKMGVI QDVLGEEQRF KALQKLQAER
DALILKHIHF VYHPTKETCP SCPACVDAKI EHLISSRFIR PSDRNQKNSL SDPNIDRINL
VILGKDGLAR ELANEIRALC TNDDKYVIDG KMYELSLRPI EGNVRLPVNS FQTPTFQPHG
CLCLYNSKES LSYVVESIEK SRESTLGRRD NHLVHLPLTL ILVNKRGDTS GETLHSLIQQ
GQQIASKLQC VFLDPASAGI GYGRNINEKQ ISQVLKGLLD SKRNLNLVSS TASIKDLADV
DLRIVMCLMC GDPFSADDIL FPVLQSQTCK SSHCGSNNSV LLELPIGLHK KRIELSVLSY
HSSFSIRKSR LVHGYIVFYS AKRKASLAML RAFLCEVQDI IPIQLVALTD GAVDVLDNDL
SREQLTEGEE IAQEIDGRFT SIPCSQPQHK LEIFHPFFKD VVEKKNIIEA THMYDNAAEA
CSTTEEVFNS PRAGSPLCNS NLQDSEEDIE PSYSLFREDT SLPSLSKDHS KLSMELEGND
GLSFIMSNFE SKLNNKVPPP VKPKPPVHFE ITKGDLSYLD QGHRDGQRKS VSSSPWLPQD
GFDPSDYAEP MDAVVKPRNE EENIYSVPHD STQGKIITIR NINKAQSNGS GNGSDSEMDT
SSLERGRKVS IVSKPVLYRT RCTRLGRFAS YRTSFSVGSD DELGPIRKKE EDQASQGYKG
DNAVIPYETD EDPRRRNILR SLRRNTKKPK PKPRPSITKA TWESNYFGVP LTTVVTPEKP
IPIFIERCIE YIEATGLSTE GIYRVSGNKS EMESLQRQFD QDHNLDLAEK DFTVNTVAGA
MKSFFSELPD PLVPYNMQID LVEAHKINDR EQKLHALKEV LKKFPKENHE VFKYVISHLN
KVSHNNKVNL MTSENLSICF WPTLMRPDFS TMDALTATRT YQTIIELFIQ QCPFFFYNRP
ITEPPGARPS SPSAVASTVP FLTSTPVTSQ PSPPQSPPPT PQSPMQPLLP SQLQAEHTL


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