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Q91YM2 (RHG35_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho GTPase-activating protein 35
Alternative name(s):
Glucocorticoid receptor DNA-binding factor 1
Gene names
Name:Arhgap35
Synonyms:Grlf1,Kiaa1722
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1499 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3

Subunit structure

Interacts with the general transcription factor GTF2I, the interaction sequesters GTF2I in the cytoplasm By similarity. Interacts with RASA1. Ref.3

Subcellular location

Nucleus Potential.

Post-translational modification

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.

Sequence similarities

Contains 4 FF domains.

Contains 1 Rho-GAP domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DiseaseTumor suppressor
   DomainRepeat
   LigandDNA-binding
   Molecular functionGTPase activation
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcamera-type eye development

Inferred from mutant phenotype PubMed 11044403. Source: MGI

forebrain development

Inferred from mutant phenotype PubMed 11044403. Source: MGI

integrin-mediated signaling pathway

Traceable author statement PubMed 11044403. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

negative regulation of vascular permeability

Inferred from mutant phenotype PubMed 17562701. Source: MGI

neural tube closure

Inferred from mutant phenotype PubMed 11044403. Source: MGI

positive regulation of GTPase activity

Traceable author statement PubMed 11044403. Source: GOC

regulation of cell shape

Inferred from direct assay PubMed 11044403. Source: MGI

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentactin cytoskeleton

Inferred from direct assay PubMed 11044403. Source: MGI

cytoplasm

Inferred from direct assay PubMed 11044403. Source: MGI

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTP binding

Inferred from electronic annotation. Source: InterPro

GTPase activator activity

Traceable author statement PubMed 11044403. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14991499Rho GTPase-activating protein 35
PRO_0000056731

Regions

Domain270 – 32758FF 1
Domain368 – 42255FF 2
Domain429 – 48355FF 3
Domain485 – 55066FF 4
Domain1249 – 1436188Rho-GAP
Compositional bias1440 – 148748Pro-rich

Amino acid modifications

Modified residue3081Phosphotyrosine By similarity
Modified residue5891Phosphoserine By similarity
Modified residue7731Phosphoserine By similarity
Modified residue9701Phosphoserine By similarity
Modified residue9751Phosphoserine By similarity
Modified residue10721Phosphoserine By similarity
Modified residue10871Phosphotyrosine By similarity
Modified residue11051Phosphotyrosine; by ABL2 and PTK6 Ref.3 Ref.5 Ref.7
Modified residue11341Phosphoserine By similarity
Modified residue11501Phosphoserine By similarity
Modified residue11791Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q91YM2 [UniParc].

Last modified January 9, 2007. Version 3.
Checksum: 7E13EC38257CE950

FASTA1,499170,393
        10         20         30         40         50         60 
MMMARKQDVR IPTYNISVVG LSGTEKEKGQ CGIGKSCLCN RFVRPSADEF HLDHTSVLST 

        70         80         90        100        110        120 
SDFGGRVVNN DHFLYWGEVS RSLEDCVECK MHIVEQTEFI DDQTFQPHRS TALQPYIKRA 

       130        140        150        160        170        180 
AATKLASAEK LMYFCTDQLG LEQDFEQKQM PDGKLLVDGF LLGIDVSRGM NRNFDDQLKF 

       190        200        210        220        230        240 
VSNLYNQLAK TKKPIVVVLT KCDEGVERYI RDAHTFALSK KNLQVVETSA RSNVNVDLAF 

       250        260        270        280        290        300 
STLVQLIDKS RGKTKIIPYF EALKQQSQQI ATAKDKYEWL VSRIVKNHNE NWPSVSRKMQ 

       310        320        330        340        350        360 
ASPEYQDYVY LEGTQKAKKL FLQHIHRLKH EHIERRRKLY LAALPLAFEA LIPNLDEVDH 

       370        380        390        400        410        420 
LSCIKAKKLL ETKPEFLKWF VVLEETPWDA TSHIDNMENE RIPFDLMDTV PAEQLYETHL 

       430        440        450        460        470        480 
EKLRNERKRA EMRRAFKENL ETSPFITPGK PWEEARSFIM NEDFYQWLEE SVYMDIYGKH 

       490        500        510        520        530        540 
QKQIIDRAKE EFQELLLEYS ELFYELELDA KPSKEKMGVI QDVLGEEQRF KALQKLQAER 

       550        560        570        580        590        600 
DALILKHIHF VYHPTKETCP SCPACVDAKI EHLISSRFIR PSDRNQKNSL SDLNIDRINL 

       610        620        630        640        650        660 
VILGKDGLAR ELANEIRALC TNDDKYVIDG KMYELSLRPI EGNVRLPVNS FQTPTFQPHG 

       670        680        690        700        710        720 
CLCLYNSKES LSYVVESIEK SRESTLGRRD NHLVHLPLTL ILVNKRGDTS GETLHSLIQQ 

       730        740        750        760        770        780 
GQQIASKLQC VFLDPASAGI GYGRNINEKQ ISQVLKGLLD SKRNLNLVSS TASIKDLADV 

       790        800        810        820        830        840 
DLRIVMCLMC GDPFSADDVL SPVLQSQTCK SSHCGSSNSV LLELPIGLHK KRIELSVLSY 

       850        860        870        880        890        900 
HSSFSIRKSR LVHGYIVFYS AKRKASLAML RAFLCEVQDI IPIQLVALTD GAIDVLDNDL 

       910        920        930        940        950        960 
SREQLTEGEE IAQEIDGRFT SIPCSQPQHK LELFHPFFKD VVEKKNIIEA THMYDNVAEA 

       970        980        990       1000       1010       1020 
CSTTEEVFNS PRAGSPLCNS NLQDSEEDVE PPSYHLFRED ATLPSLSKDH SKFSMELEGN 

      1030       1040       1050       1060       1070       1080 
DGLSFIMSNF ESKLNNKVPP PVKPKPPVHF DITKDLSYLD QGHREGQRKS MSSSPWMPQD 

      1090       1100       1110       1120       1130       1140 
GFDPSDYAEP MDAVVKPRNE EENIYSVPHD STQGKIITIR NINKAQSNGS GNGSDSEMDT 

      1150       1160       1170       1180       1190       1200 
SSLERGRKVS AVSKPVLYRT RCTRLGRFAS YRTSFSVGSD DELGPIRKKE EDQASQGYKG 

      1210       1220       1230       1240       1250       1260 
DNAVIPYETD EDPRRRNILR SLRRNTKKPK PKPRPSITKA TWESNYFGVP LTTVVTPEKP 

      1270       1280       1290       1300       1310       1320 
IPIFIERCIE YIEATGLSTE GIYRVSGNKS EMESLQRQFD QDHNLDLAEK DFTVNTVAGA 

      1330       1340       1350       1360       1370       1380 
MKSFFSELPD PLVPYSMQID LVEAHKINDR EQKLHALKEV LKKFPKENHE VFKYVISHLN 

      1390       1400       1410       1420       1430       1440 
KVSHNNKVNL MTSENLSICF WPTLMRPDFS SMDALTATRS YQTIIELFIQ QCPFFFYNRP 

      1450       1460       1470       1480       1490 
ISEPPGAAPG SPSAMAPTVP FLTSTPATSQ PSPPQSPPPT PQSPMQPLLS SQLQAEHTL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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(2005) [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(2004) [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(2006) [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(2006) [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(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK147326 mRNA. Translation: BAE27848.1.
AK147688 mRNA. Translation: BAE28076.1.
AK173242 Transcribed RNA. Translation: BAD32520.1.
RefSeqNP_766327.3. NM_172739.4.
XP_006539871.1. XM_006539808.1.
XP_006539872.1. XM_006539809.1.
XP_006539873.1. XM_006539810.1.
UniGeneMm.28646.
Mm.400358.

3D structure databases

ProteinModelPortalQ91YM2.
SMRQ91YM2. Positions 13-249, 267-331, 1242-1437.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid231317. 2 interactions.
IntActQ91YM2. 1 interaction.
MINTMINT-4096884.
STRING10090.ENSMUSP00000075242.

PTM databases

PhosphoSiteQ91YM2.

Proteomic databases

PaxDbQ91YM2.
PRIDEQ91YM2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000075845; ENSMUSP00000075242; ENSMUSG00000058230.
ENSMUST00000171937; ENSMUSP00000127379; ENSMUSG00000058230.
GeneID232906.
KEGGmmu:232906.
UCSCuc009fhw.1. mouse.

Organism-specific databases

CTD232906.
MGIMGI:1929494. Grlf1.

Phylogenomic databases

eggNOGNOG241832.
GeneTreeENSGT00740000114884.
HOVERGENHBG051844.
InParanoidQ91YM2.
KOK05732.
OMAVLYRTRC.
OrthoDBEOG779NWX.
PhylomeDBQ91YM2.
TreeFamTF324451.

Gene expression databases

ArrayExpressQ91YM2.
BgeeQ91YM2.
CleanExMM_GRLF1.
GenevestigatorQ91YM2.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR002713. FF_domain.
IPR027417. P-loop_NTPase.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamPF01846. FF. 1 hit.
PF00071. Ras. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTSM00441. FF. 4 hits.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF81698. SSF81698. 1 hit.
PROSITEPS51676. FF. 4 hits.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio381321.
PROQ91YM2.
SOURCESearch...

Entry information

Entry nameRHG35_MOUSE
AccessionPrimary (citable) accession number: Q91YM2
Secondary accession number(s): Q3UGY1, Q69ZC4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2003
Last sequence update: January 9, 2007
Last modified: April 16, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot