GenomeNet

Database: UniProt
Entry: RHG35_MOUSE
LinkDB: RHG35_MOUSE
Original site: RHG35_MOUSE 
ID   RHG35_MOUSE             Reviewed;        1499 AA.
AC   Q91YM2; Q3UGY1; Q69ZC4;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   16-OCT-2019, entry version 165.
DE   RecName: Full=Rho GTPase-activating protein 35 {ECO:0000312|MGI:MGI:1929494};
DE   AltName: Full=Glucocorticoid receptor DNA-binding factor 1;
GN   Name=Arhgap35 {ECO:0000312|MGI:MGI:1929494};
GN   Synonyms=Grlf1, Kiaa1722, P190A {ECO:0000303|PubMed:11044403},
GN   p190ARHOGAP {ECO:0000303|PubMed:11044403};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 163-1499.
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE
RP   SPECIFICITY, PHOSPHORYLATION BY PKC, AND DOMAIN.
RX   PubMed=11044403;
RA   Brouns M.R., Matheson S.F., Hu K.Q., Delalle I., Caviness V.S.,
RA   Silver J., Bronson R.T., Settleman J.;
RT   "The adhesion signaling molecule p190 RhoGAP is required for
RT   morphogenetic processes in neural development.";
RL   Development 127:4891-4903(2000).
RN   [4]
RP   FUNCTION, PHOSPHORYLATION BY SRC AND FYN, AND DOMAIN.
RX   PubMed=11283609; DOI=10.1038/35070042;
RA   Brouns M.R., Matheson S.F., Settleman J.;
RT   "p190 RhoGAP is the principal Src substrate in brain and regulates
RT   axon outgrowth, guidance and fasciculation.";
RL   Nat. Cell Biol. 3:361-367(2001).
RN   [5]
RP   PHOSPHORYLATION AT TYR-1105, INTERACTION WITH RASA1, AND FUNCTION.
RX   PubMed=16971514; DOI=10.1091/mbc.e06-02-0132;
RA   Bradley W.D., Hernandez S.E., Settleman J., Koleske A.J.;
RT   "Integrin signaling through Arg activates p190RhoGAP by promoting its
RT   binding to p120RasGAP and recruitment to the membrane.";
RL   Mol. Biol. Cell 17:4827-4836(2006).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1105, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Mast cell;
RX   PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   FUNCTION, PHOSPHORYLATION AT SER-1472; SER-1476; THR-1480 AND
RP   SER-1483, AND MUTAGENESIS OF SER-1472; SER-1476; THR-1480 AND
RP   SER-1483.
RX   PubMed=18502760; DOI=10.1074/jbc.m802588200;
RA   Jiang W., Betson M., Mulloy R., Foster R., Levay M., Ligeti E.,
RA   Settleman J.;
RT   "p190A RhoGAP is a glycogen synthase kinase-3-beta substrate required
RT   for polarized cell migration.";
RL   J. Biol. Chem. 283:20978-20988(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1105, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589; SER-773; SER-970;
RP   SER-975; SER-985; TYR-1087; TYR-1105; SER-1134; SER-1142 AND SER-1179,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [12]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=20675588; DOI=10.4049/jimmunol.0904163;
RA   Nemeth T., Futosi K., Hably C., Brouns M.R., Jakob S.M., Kovacs M.,
RA   Kertesz Z., Walzog B., Settleman J., Mocsai A.;
RT   "Neutrophil functions and autoimmune arthritis in the absence of
RT   p190RhoGAP: generation and analysis of a novel null mutation in
RT   mice.";
RL   J. Immunol. 185:3064-3075(2010).
RN   [13]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=21945077; DOI=10.1016/j.ydbio.2011.09.006;
RA   Heckman-Stoddard B.M., Vargo-Gogola T., Herrick M.P., Visbal A.P.,
RA   Lewis M.T., Settleman J., Rosen J.M.;
RT   "P190A RhoGAP is required for mammary gland development.";
RL   Dev. Biol. 360:1-10(2011).
RN   [14]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR
RP   LOCATION, AND MUTAGENESIS OF LEU-1396.
RX   PubMed=26859289; DOI=10.1371/journal.pgen.1005785;
RA   Stewart K., Gaitan Y., Shafer M.E., Aoudjit L., Hu D., Sharma R.,
RA   Tremblay M., Ishii H., Marcotte M., Stanga D., Tang Y.C.,
RA   Boualia S.K., Nguyen A.H., Takano T., Lamarche-Vane N., Vidal S.,
RA   Bouchard M.;
RT   "A point mutation in p190A RhoGAP affects ciliogenesis and leads to
RT   glomerulocystic kidney defects.";
RL   PLoS Genet. 12:E1005785-E1005785(2016).
CC   -!- FUNCTION: Rho GTPase-activating protein (GAP). Binds several
CC       acidic phospholipids which inhibits the Rho GAP activity to
CC       promote the Rac GAP activity (PubMed:16971514). This binding is
CC       inhibited by phosphorylation by PRKCA (By similarity). Involved in
CC       cell differentiation as well as cell adhesion and migration, plays
CC       an important role in retinal tissue morphogenesis, neural tube
CC       fusion, midline fusion of the cerebral hemispheres and mammary
CC       gland branching morphogenesis (PubMed:11044403, PubMed:11283609,
CC       PubMed:18502760, PubMed:21945077). Transduces signals from p21-ras
CC       to the nucleus, acting via the ras GTPase-activating protein (GAP)
CC       (PubMed:16971514). Transduces SRC-dependent signals from cell-
CC       surface adhesion molecules, such as laminin, to promote neurite
CC       outgrowth. Regulates axon outgrowth, guidance and fasciculation
CC       (PubMed:11283609). Modulates Rho GTPase-dependent F-actin
CC       polymerization, organization and assembly, is involved in
CC       polarized cell migration and in the positive regulation of
CC       ciliogenesis and cilia elongation (PubMed:11044403,
CC       PubMed:26859289, PubMed:18502760). During mammary gland
CC       development, is required in both the epithelial and stromal
CC       compartments for ductal outgrowth (PubMed:21945077). Represses
CC       transcription of the glucocorticoid receptor by binding to the
CC       cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'; this
CC       function is however unclear and would need additional experimental
CC       evidences (By similarity). {ECO:0000250|UniProtKB:Q9NRY4,
CC       ECO:0000269|PubMed:11044403, ECO:0000269|PubMed:11283609,
CC       ECO:0000269|PubMed:16971514, ECO:0000269|PubMed:18502760,
CC       ECO:0000269|PubMed:21945077, ECO:0000269|PubMed:26859289}.
CC   -!- SUBUNIT: Interacts with the general transcription factor GTF2I,
CC       the interaction sequesters GTF2I in the cytoplasm (By similarity).
CC       Interacts with RASA1 (PubMed:16971514). {ECO:0000250,
CC       ECO:0000269|PubMed:16971514}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000269|PubMed:26859289}. Cytoplasm
CC       {ECO:0000269|PubMed:11044403}. Nucleus {ECO:0000305}. Cell
CC       membrane {ECO:0000269|PubMed:11044403}. Note=In response to
CC       integrins and SDC4 and upon phosphorylation by PKC, relocalizes
CC       from the cytoplasm to regions of plasma membrane ruffling where it
CC       colocalizes with polymerized actin. {ECO:0000269|PubMed:11044403}.
CC   -!- TISSUE SPECIFICITY: Expressed in the developing kidneys
CC       (PubMed:26859289). Expressed in all regions of the mature nervous
CC       system (at protein level) (PubMed:11044403). Detected in
CC       neutrophils (at protein level) (PubMed:20675588).
CC       {ECO:0000269|PubMed:11044403, ECO:0000269|PubMed:20675588,
CC       ECO:0000269|PubMed:26859289}.
CC   -!- DEVELOPMENTAL STAGE: At 12.5 dpc, the highest level of expression
CC       is in the spinal cord and lower expression levels are seen in the
CC       developing brain. At 15.5 dpc, highly expressed in brain, spinal
CC       cord and eyes (PubMed:11044403). In developing kidney, at 17.5
CC       dpc, low expression is observed in the glomerulus, while high
CC       expression levels are detected in the proximal tubule
CC       (PubMed:26859289). At 14.5 dpc, is expressed within the epithelial
CC       compartment of the embryonic mammary bud and at lower level in the
CC       surrounding stroma and skin. Also expressed at terminal end bunds
CC       (TEB) at comparable levels in body and cap cells as well as in
CC       fibroblasts and stroma surrounding the TEB (PubMed:21945077).
CC       {ECO:0000269|PubMed:11044403, ECO:0000269|PubMed:21945077,
CC       ECO:0000269|PubMed:26859289}.
CC   -!- DOMAIN: N-terminal part (1-266) has GTPase activity. Required for
CC       proper cellular localization. Mutation of this region is a
CC       severely defective loss of function. Mutants have defective
CC       morphogenesis of neural retinal tissue, agenesis of the corpus
CC       callosum due to defectuous midline fusion of the cerebral
CC       hemispheres (PubMed:11044403). Mutants show defects in axon
CC       guidance and fasciculation (PubMed:11283609).
CC       {ECO:0000269|PubMed:11044403, ECO:0000269|PubMed:11283609}.
CC   -!- DOMAIN: The pG1 pseudoGTPase domain does not bind GTP.
CC       {ECO:0000250|UniProtKB:Q6NU25}.
CC   -!- PTM: Phosphorylation of Tyr-1105 by PTK6 promotes the association
CC       with RASA1, inactivating RHOA while activating RAS.
CC       Phosphorylation at Tyr-308 by PDGFRA inhibits binding to GTF2I (By
CC       similarity). Phosphorylated by PRKCA at Ser-1221 and Thr-1226,
CC       induces relocalization from the cytoplasm to regions of plasma
CC       membrane ruffling and prevents the binding and substrate
CC       specificity regulation by phospholipids (PubMed:11044403). In
CC       brain, phosphorylated by FYN and SRC (PubMed:11283609). During
CC       focal adhesion formation, phosphorylated by MAPK1 and MAPK3 at the
CC       C-terminal region, probably at Ser-1451, Ser-1476, Thr-1480 and
CC       Ser-1483. Phosphorylation by MAPK1 and MAPK3 inhibits GAP function
CC       and localizes ARGHAP35 away from newly forming focal adhesions and
CC       stress fibers in cells spreading on fibronectin (By similarity).
CC       Phosphorylation at Ser-1476 and Thr-1480 by GSK3B requires priming
CC       by MAPK and inhibits RhoGAP activity and modulates polarized cell
CC       migration (PubMed:18502760). {ECO:0000250|UniProtKB:P81128,
CC       ECO:0000250|UniProtKB:Q9NRY4, ECO:0000269|PubMed:11044403,
CC       ECO:0000269|PubMed:11283609, ECO:0000269|PubMed:18502760}.
CC   -!- DISRUPTION PHENOTYPE: Deficiency leads to perinatal lethality and
CC       defective neural development. One third of the fetuses show
CC       exencephaly and spina bifida as well as defective kidney
CC       development. {ECO:0000269|PubMed:20675588}.
DR   EMBL; AK147326; BAE27848.1; -; mRNA.
DR   EMBL; AK147688; BAE28076.1; -; mRNA.
DR   EMBL; AK173242; BAD32520.1; -; Transcribed_RNA.
DR   CCDS; CCDS20851.1; -.
DR   RefSeq; NP_766327.3; NM_172739.4.
DR   RefSeq; XP_006539872.1; XM_006539809.3.
DR   RefSeq; XP_011248814.1; XM_011250512.2.
DR   SMR; Q91YM2; -.
DR   BioGrid; 231317; 1.
DR   CORUM; Q91YM2; -.
DR   IntAct; Q91YM2; 2.
DR   MINT; Q91YM2; -.
DR   STRING; 10090.ENSMUSP00000075242; -.
DR   iPTMnet; Q91YM2; -.
DR   PhosphoSitePlus; Q91YM2; -.
DR   jPOST; Q91YM2; -.
DR   MaxQB; Q91YM2; -.
DR   PaxDb; Q91YM2; -.
DR   PRIDE; Q91YM2; -.
DR   Ensembl; ENSMUST00000075845; ENSMUSP00000075242; ENSMUSG00000058230.
DR   Ensembl; ENSMUST00000171937; ENSMUSP00000127379; ENSMUSG00000058230.
DR   GeneID; 232906; -.
DR   KEGG; mmu:232906; -.
DR   UCSC; uc009fhw.1; mouse.
DR   CTD; 2909; -.
DR   MGI; MGI:1929494; Arhgap35.
DR   eggNOG; KOG4271; Eukaryota.
DR   eggNOG; ENOG410XR4E; LUCA.
DR   GeneTree; ENSGT00950000182819; -.
DR   InParanoid; Q91YM2; -.
DR   KO; K05732; -.
DR   OMA; WAPGSDG; -.
DR   OrthoDB; 110157at2759; -.
DR   PhylomeDB; Q91YM2; -.
DR   TreeFam; TF324451; -.
DR   Reactome; R-MMU-194840; Rho GTPase cycle.
DR   Reactome; R-MMU-416550; Sema4D mediated inhibition of cell attachment and migration.
DR   Reactome; R-MMU-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR   ChiTaRS; Arhgap35; mouse.
DR   PRO; PR:Q91YM2; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000058230; Expressed in 285 organ(s), highest expression level in ear vesicle.
DR   ExpressionAtlas; Q91YM2; baseline and differential.
DR   Genevisible; Q91YM2; MM.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR   GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0032794; F:GTPase activating protein binding; ISO:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0007411; P:axon guidance; IDA:UniProtKB.
DR   GO; GO:0007413; P:axonal fasciculation; IMP:UniProtKB.
DR   GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR   GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR   GO; GO:0031668; P:cellular response to extracellular stimulus; IMP:UniProtKB.
DR   GO; GO:0021955; P:central nervous system neuron axonogenesis; IMP:UniProtKB.
DR   GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:UniProtKB.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; TAS:MGI.
DR   GO; GO:0030879; P:mammary gland development; IMP:UniProtKB.
DR   GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IDA:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR   GO; GO:0043116; P:negative regulation of vascular permeability; IMP:MGI.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0097485; P:neuron projection guidance; IMP:UniProtKB.
DR   GO; GO:0045724; P:positive regulation of cilium assembly; IMP:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0008064; P:regulation of actin polymerization or depolymerization; IMP:UniProtKB.
DR   GO; GO:0050770; P:regulation of axonogenesis; IMP:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
DR   GO; GO:0044319; P:wound healing, spreading of cells; IMP:UniProtKB.
DR   Gene3D; 1.10.10.440; -; 2.
DR   Gene3D; 1.10.555.10; -; 1.
DR   InterPro; IPR002713; FF_domain.
DR   InterPro; IPR036517; FF_domain_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039007; pG1.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR032835; RhoGAP-FF1.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR039006; RhoGAP_pG2.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF01846; FF; 1.
DR   Pfam; PF00071; Ras; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF16512; RhoGAP-FF1; 1.
DR   SMART; SM00441; FF; 4.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF81698; SSF81698; 1.
DR   PROSITE; PS51676; FF; 4.
DR   PROSITE; PS51852; PG1; 1.
DR   PROSITE; PS51853; PG2; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Complete proteome; Cytoplasm;
KW   Cytoskeleton; DNA-binding; GTP-binding; GTPase activation;
KW   Lipid-binding; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1499       Rho GTPase-activating protein 35.
FT                                /FTId=PRO_0000056731.
FT   DOMAIN      270    327       FF 1.
FT   DOMAIN      368    422       FF 2.
FT   DOMAIN      429    483       FF 3.
FT   DOMAIN      485    550       FF 4.
FT   DOMAIN      592    767       pG1 pseudoGTPase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01199}.
FT   DOMAIN      783    947       pG2 pseudoGTPase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01200}.
FT   DOMAIN     1249   1436       Rho-GAP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00172}.
FT   NP_BIND      33     37       GTP. {ECO:0000250|UniProtKB:Q9NRY4}.
FT   NP_BIND      95     97       GTP. {ECO:0000250|UniProtKB:Q9NRY4}.
FT   NP_BIND     201    203       GTP. {ECO:0000250|UniProtKB:Q9NRY4}.
FT   NP_BIND     229    231       GTP. {ECO:0000250|UniProtKB:Q9NRY4}.
FT   REGION        1    266       Has GTPase activity, required for proper
FT                                localization.
FT                                {ECO:0000269|PubMed:11044403}.
FT   REGION     1213   1236       Required for phospholipid binding and
FT                                regulation of the substrate preference.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   COMPBIAS   1440   1487       Pro-rich.
FT   BINDING      28     28       GTP. {ECO:0000250|UniProtKB:Q9NRY4}.
FT   BINDING      52     52       GTP; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   BINDING      56     56       GTP. {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES     308    308       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES     589    589       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     770    770       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES     773    773       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     970    970       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     975    975       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     985    985       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1072   1072       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES    1087   1087       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1105   1105       Phosphotyrosine; by ABL2 and PTK6.
FT                                {ECO:0000244|PubMed:17947660,
FT                                ECO:0000244|PubMed:18034455,
FT                                ECO:0000244|PubMed:21183079,
FT                                ECO:0000269|PubMed:16971514}.
FT   MOD_RES    1134   1134       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1142   1142       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1150   1150       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES    1176   1176       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES    1179   1179       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1221   1221       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES    1226   1226       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES    1236   1236       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NRY4}.
FT   MOD_RES    1472   1472       Phosphoserine.
FT                                {ECO:0000269|PubMed:18502760}.
FT   MOD_RES    1476   1476       Phosphoserine.
FT                                {ECO:0000269|PubMed:18502760}.
FT   MOD_RES    1480   1480       Phosphothreonine.
FT                                {ECO:0000269|PubMed:18502760}.
FT   MOD_RES    1483   1483       Phosphoserine.
FT                                {ECO:0000269|PubMed:18502760}.
FT   MUTAGEN    1396   1396       L->Q: In ENU mutant Arhgap35-D34; mutant
FT                                animals show hypodysplastic kidneys and
FT                                neural tube closure defects; the number
FT                                of ciliated cells and cilia average
FT                                length are drastically reduced in the
FT                                proximal tubules. Results in loss of
FT                                activation of GTP hydrolysis.
FT                                {ECO:0000269|PubMed:26859289}.
FT   MUTAGEN    1472   1472       S->A: Reduces phosphorylation by GSK3B by
FT                                50%. No effect on polarized cell
FT                                migration. {ECO:0000269|PubMed:18502760}.
FT   MUTAGEN    1476   1476       S->A: Abolishes phosphorylation by GSK3B.
FT                                Reduces phosphorylation by MAPK. Affects
FT                                polarized cell migration. Increases
FT                                RhoGAP catalytic activity.
FT                                {ECO:0000269|PubMed:18502760}.
FT   MUTAGEN    1480   1480       T->A: Abolishes phosphorylation by GSK3B.
FT                                Reduces phosphorylation by MAPK. Affects
FT                                polarized cell migration. Increases
FT                                RhoGAP catalytic activity.
FT                                {ECO:0000269|PubMed:18502760}.
FT   MUTAGEN    1483   1483       S->A: Abolishes phosphorylation by GSK3B.
FT                                Reduces phosphorylation by MAPK. No
FT                                effect on polarized cell migration.
FT                                {ECO:0000269|PubMed:18502760}.
SQ   SEQUENCE   1499 AA;  170393 MW;  7E13EC38257CE950 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 NWPSVSRKMQ
     ASPEYQDYVY LEGTQKAKKL FLQHIHRLKH EHIERRRKLY LAALPLAFEA LIPNLDEVDH
     LSCIKAKKLL ETKPEFLKWF VVLEETPWDA TSHIDNMENE RIPFDLMDTV PAEQLYETHL
     EKLRNERKRA EMRRAFKENL ETSPFITPGK PWEEARSFIM NEDFYQWLEE SVYMDIYGKH
     QKQIIDRAKE EFQELLLEYS ELFYELELDA KPSKEKMGVI QDVLGEEQRF KALQKLQAER
     DALILKHIHF VYHPTKETCP SCPACVDAKI EHLISSRFIR PSDRNQKNSL SDLNIDRINL
     VILGKDGLAR ELANEIRALC TNDDKYVIDG KMYELSLRPI EGNVRLPVNS FQTPTFQPHG
     CLCLYNSKES LSYVVESIEK SRESTLGRRD NHLVHLPLTL ILVNKRGDTS GETLHSLIQQ
     GQQIASKLQC VFLDPASAGI GYGRNINEKQ ISQVLKGLLD SKRNLNLVSS TASIKDLADV
     DLRIVMCLMC GDPFSADDVL SPVLQSQTCK SSHCGSSNSV LLELPIGLHK KRIELSVLSY
     HSSFSIRKSR LVHGYIVFYS AKRKASLAML RAFLCEVQDI IPIQLVALTD GAIDVLDNDL
     SREQLTEGEE IAQEIDGRFT SIPCSQPQHK LELFHPFFKD VVEKKNIIEA THMYDNVAEA
     CSTTEEVFNS PRAGSPLCNS NLQDSEEDVE PPSYHLFRED ATLPSLSKDH SKFSMELEGN
     DGLSFIMSNF ESKLNNKVPP PVKPKPPVHF DITKDLSYLD QGHREGQRKS MSSSPWMPQD
     GFDPSDYAEP MDAVVKPRNE EENIYSVPHD STQGKIITIR NINKAQSNGS GNGSDSEMDT
     SSLERGRKVS AVSKPVLYRT RCTRLGRFAS YRTSFSVGSD DELGPIRKKE EDQASQGYKG
     DNAVIPYETD EDPRRRNILR SLRRNTKKPK PKPRPSITKA TWESNYFGVP LTTVVTPEKP
     IPIFIERCIE YIEATGLSTE GIYRVSGNKS EMESLQRQFD QDHNLDLAEK DFTVNTVAGA
     MKSFFSELPD PLVPYSMQID LVEAHKINDR EQKLHALKEV LKKFPKENHE VFKYVISHLN
     KVSHNNKVNL MTSENLSICF WPTLMRPDFS SMDALTATRS YQTIIELFIQ QCPFFFYNRP
     ISEPPGAAPG SPSAMAPTVP FLTSTPATSQ PSPPQSPPPT PQSPMQPLLS SQLQAEHTL
//
DBGET integrated database retrieval system