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Protein

Rho GTPase-activating protein 35

Gene

Arhgap35

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'. May participate in the regulation of retinal development and degeneration. May transduce signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP). May also act as a tumor suppressor (By similarity).By similarity

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. GTPase activator activity Source: MGI
  3. GTP binding Source: InterPro

GO - Biological processi

  1. camera-type eye development Source: MGI
  2. forebrain development Source: MGI
  3. integrin-mediated signaling pathway Source: MGI
  4. negative regulation of Rho protein signal transduction Source: MGI
  5. negative regulation of transcription, DNA-templated Source: Ensembl
  6. negative regulation of vascular permeability Source: MGI
  7. neural tube closure Source: MGI
  8. positive regulation of GTPase activity Source: GOC
  9. positive regulation of neuron projection development Source: MGI
  10. regulation of cell shape Source: MGI
  11. small GTPase mediated signal transduction Source: InterPro
  12. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_295273. Sema4D mediated inhibition of cell attachment and migration.
REACT_297947. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GTPase-activating protein 35
Alternative name(s):
Glucocorticoid receptor DNA-binding factor 1
Gene namesi
Name:Arhgap35
Synonyms:Grlf1,Kiaa1722
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1929494. Arhgap35.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. actin cytoskeleton Source: MGI
  2. cytoplasm Source: MGI
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14991499Rho GTPase-activating protein 35PRO_0000056731Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei308 – 3081PhosphotyrosineBy similarity
Modified residuei589 – 5891PhosphoserineBy similarity
Modified residuei773 – 7731PhosphoserineBy similarity
Modified residuei970 – 9701PhosphoserineBy similarity
Modified residuei975 – 9751PhosphoserineBy similarity
Modified residuei1072 – 10721PhosphoserineBy similarity
Modified residuei1087 – 10871PhosphotyrosineBy similarity
Modified residuei1105 – 11051Phosphotyrosine; by ABL2 and PTK63 Publications
Modified residuei1134 – 11341PhosphoserineBy similarity
Modified residuei1150 – 11501PhosphoserineBy similarity
Modified residuei1179 – 11791PhosphoserineBy similarity

Post-translational modificationi

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 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ91YM2.
PaxDbiQ91YM2.
PRIDEiQ91YM2.

PTM databases

PhosphoSiteiQ91YM2.

Expressioni

Gene expression databases

BgeeiQ91YM2.
CleanExiMM_GRLF1.
ExpressionAtlasiQ91YM2. baseline and differential.
GenevestigatoriQ91YM2.

Interactioni

Subunit structurei

Interacts with the general transcription factor GTF2I, the interaction sequesters GTF2I in the cytoplasm (By similarity). Interacts with RASA1.By similarity1 Publication

Protein-protein interaction databases

BioGridi231317. 2 interactions.
IntActiQ91YM2. 1 interaction.
MINTiMINT-4096884.
STRINGi10090.ENSMUSP00000075242.

Structurei

3D structure databases

ProteinModelPortaliQ91YM2.
SMRiQ91YM2. Positions 13-249, 267-331, 1242-1437.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini270 – 32758FF 1Add
BLAST
Domaini368 – 42255FF 2Add
BLAST
Domaini429 – 48355FF 3Add
BLAST
Domaini485 – 55066FF 4Add
BLAST
Domaini1249 – 1436188Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1440 – 148748Pro-richAdd
BLAST

Sequence similaritiesi

Contains 4 FF domains.Curated
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG241832.
GeneTreeiENSGT00760000118863.
HOVERGENiHBG051844.
InParanoidiQ91YM2.
KOiK05732.
OMAiPITEPPG.
OrthoDBiEOG779NWX.
PhylomeDBiQ91YM2.
TreeFamiTF324451.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR002713. FF_domain.
IPR027417. P-loop_NTPase.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF01846. FF. 1 hit.
PF00071. Ras. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00441. FF. 4 hits.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF81698. SSF81698. 1 hit.
PROSITEiPS51676. FF. 4 hits.
PS50238. RHOGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91YM2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMMARKQDVR IPTYNISVVG LSGTEKEKGQ CGIGKSCLCN RFVRPSADEF
60 70 80 90 100
HLDHTSVLST SDFGGRVVNN DHFLYWGEVS RSLEDCVECK MHIVEQTEFI
110 120 130 140 150
DDQTFQPHRS TALQPYIKRA AATKLASAEK LMYFCTDQLG LEQDFEQKQM
160 170 180 190 200
PDGKLLVDGF LLGIDVSRGM NRNFDDQLKF VSNLYNQLAK TKKPIVVVLT
210 220 230 240 250
KCDEGVERYI RDAHTFALSK KNLQVVETSA RSNVNVDLAF STLVQLIDKS
260 270 280 290 300
RGKTKIIPYF EALKQQSQQI ATAKDKYEWL VSRIVKNHNE NWPSVSRKMQ
310 320 330 340 350
ASPEYQDYVY LEGTQKAKKL FLQHIHRLKH EHIERRRKLY LAALPLAFEA
360 370 380 390 400
LIPNLDEVDH LSCIKAKKLL ETKPEFLKWF VVLEETPWDA TSHIDNMENE
410 420 430 440 450
RIPFDLMDTV PAEQLYETHL EKLRNERKRA EMRRAFKENL ETSPFITPGK
460 470 480 490 500
PWEEARSFIM NEDFYQWLEE SVYMDIYGKH QKQIIDRAKE EFQELLLEYS
510 520 530 540 550
ELFYELELDA KPSKEKMGVI QDVLGEEQRF KALQKLQAER DALILKHIHF
560 570 580 590 600
VYHPTKETCP SCPACVDAKI EHLISSRFIR PSDRNQKNSL SDLNIDRINL
610 620 630 640 650
VILGKDGLAR ELANEIRALC TNDDKYVIDG KMYELSLRPI EGNVRLPVNS
660 670 680 690 700
FQTPTFQPHG CLCLYNSKES LSYVVESIEK SRESTLGRRD NHLVHLPLTL
710 720 730 740 750
ILVNKRGDTS GETLHSLIQQ GQQIASKLQC VFLDPASAGI GYGRNINEKQ
760 770 780 790 800
ISQVLKGLLD SKRNLNLVSS TASIKDLADV DLRIVMCLMC GDPFSADDVL
810 820 830 840 850
SPVLQSQTCK SSHCGSSNSV LLELPIGLHK KRIELSVLSY HSSFSIRKSR
860 870 880 890 900
LVHGYIVFYS AKRKASLAML RAFLCEVQDI IPIQLVALTD GAIDVLDNDL
910 920 930 940 950
SREQLTEGEE IAQEIDGRFT SIPCSQPQHK LELFHPFFKD VVEKKNIIEA
960 970 980 990 1000
THMYDNVAEA CSTTEEVFNS PRAGSPLCNS NLQDSEEDVE PPSYHLFRED
1010 1020 1030 1040 1050
ATLPSLSKDH SKFSMELEGN DGLSFIMSNF ESKLNNKVPP PVKPKPPVHF
1060 1070 1080 1090 1100
DITKDLSYLD QGHREGQRKS MSSSPWMPQD GFDPSDYAEP MDAVVKPRNE
1110 1120 1130 1140 1150
EENIYSVPHD STQGKIITIR NINKAQSNGS GNGSDSEMDT SSLERGRKVS
1160 1170 1180 1190 1200
AVSKPVLYRT RCTRLGRFAS YRTSFSVGSD DELGPIRKKE EDQASQGYKG
1210 1220 1230 1240 1250
DNAVIPYETD EDPRRRNILR SLRRNTKKPK PKPRPSITKA TWESNYFGVP
1260 1270 1280 1290 1300
LTTVVTPEKP IPIFIERCIE YIEATGLSTE GIYRVSGNKS EMESLQRQFD
1310 1320 1330 1340 1350
QDHNLDLAEK DFTVNTVAGA MKSFFSELPD PLVPYSMQID LVEAHKINDR
1360 1370 1380 1390 1400
EQKLHALKEV LKKFPKENHE VFKYVISHLN KVSHNNKVNL MTSENLSICF
1410 1420 1430 1440 1450
WPTLMRPDFS SMDALTATRS YQTIIELFIQ QCPFFFYNRP ISEPPGAAPG
1460 1470 1480 1490
SPSAMAPTVP FLTSTPATSQ PSPPQSPPPT PQSPMQPLLS SQLQAEHTL
Length:1,499
Mass (Da):170,393
Last modified:January 9, 2007 - v3
Checksum:i7E13EC38257CE950
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK147326 mRNA. Translation: BAE27848.1.
AK147688 mRNA. Translation: BAE28076.1.
AK173242 Transcribed RNA. Translation: BAD32520.1.
CCDSiCCDS20851.1.
RefSeqiNP_766327.3. NM_172739.4.
XP_006539872.1. XM_006539809.2.
UniGeneiMm.28646.
Mm.400358.

Genome annotation databases

EnsembliENSMUST00000075845; ENSMUSP00000075242; ENSMUSG00000058230.
ENSMUST00000171937; ENSMUSP00000127379; ENSMUSG00000058230.
GeneIDi232906.
KEGGimmu:232906.
UCSCiuc009fhw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK147326 mRNA. Translation: BAE27848.1.
AK147688 mRNA. Translation: BAE28076.1.
AK173242 Transcribed RNA. Translation: BAD32520.1.
CCDSiCCDS20851.1.
RefSeqiNP_766327.3. NM_172739.4.
XP_006539872.1. XM_006539809.2.
UniGeneiMm.28646.
Mm.400358.

3D structure databases

ProteinModelPortaliQ91YM2.
SMRiQ91YM2. Positions 13-249, 267-331, 1242-1437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231317. 2 interactions.
IntActiQ91YM2. 1 interaction.
MINTiMINT-4096884.
STRINGi10090.ENSMUSP00000075242.

PTM databases

PhosphoSiteiQ91YM2.

Proteomic databases

MaxQBiQ91YM2.
PaxDbiQ91YM2.
PRIDEiQ91YM2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000075845; ENSMUSP00000075242; ENSMUSG00000058230.
ENSMUST00000171937; ENSMUSP00000127379; ENSMUSG00000058230.
GeneIDi232906.
KEGGimmu:232906.
UCSCiuc009fhw.1. mouse.

Organism-specific databases

CTDi2909.
MGIiMGI:1929494. Arhgap35.

Phylogenomic databases

eggNOGiNOG241832.
GeneTreeiENSGT00760000118863.
HOVERGENiHBG051844.
InParanoidiQ91YM2.
KOiK05732.
OMAiPITEPPG.
OrthoDBiEOG779NWX.
PhylomeDBiQ91YM2.
TreeFamiTF324451.

Enzyme and pathway databases

ReactomeiREACT_295273. Sema4D mediated inhibition of cell attachment and migration.
REACT_297947. Rho GTPase cycle.

Miscellaneous databases

NextBioi381321.
PROiQ91YM2.
SOURCEiSearch...

Gene expression databases

BgeeiQ91YM2.
CleanExiMM_GRLF1.
ExpressionAtlasiQ91YM2. baseline and differential.
GenevestigatoriQ91YM2.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR002713. FF_domain.
IPR027417. P-loop_NTPase.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF01846. FF. 1 hit.
PF00071. Ras. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00441. FF. 4 hits.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF81698. SSF81698. 1 hit.
PROSITEiPS51676. FF. 4 hits.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 163-1499.
    Tissue: Brain.
  3. "Integrin signaling through Arg activates p190RhoGAP by promoting its binding to p120RasGAP and recruitment to the membrane."
    Bradley W.D., Hernandez S.E., Settleman J., Koleske A.J.
    Mol. Biol. Cell 17:4827-4836(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-1105, INTERACTION WITH RASA1, FUNCTION.
  4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiRHG35_MOUSE
AccessioniPrimary (citable) accession number: Q91YM2
Secondary accession number(s): Q3UGY1, Q69ZC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2003
Last sequence update: January 9, 2007
Last modified: April 1, 2015
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.