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Protein

Rho GTPase-activating protein 18

Gene

Arhgap18

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Rho GTPase activating protein that suppresses F-actin polymerization by inhibiting Rho. Rho GTPase activating proteins act by converting Rho-type GTPases to an inactive GDP-bound state. Plays a key role in tissue tension and 3D tissue shape by regulating cortical actomyosin network formation. Acts downstream of YAP1 and inhibits actin polymerization, which in turn reduces nuclear localization of YAP1. Regulates cell shape, spreading, and migration (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiR-MMU-194840. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GTPase-activating protein 18
Alternative name(s):
Rho-type GTPase-activating protein 18
Gene namesi
Name:Arhgap18Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1921160. Arhgap18.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 663663Rho GTPase-activating protein 18PRO_0000245790Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651PhosphoserineCombined sources
Modified residuei68 – 681PhosphoserineCombined sources
Modified residuei260 – 2601PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8K0Q5.
MaxQBiQ8K0Q5.
PaxDbiQ8K0Q5.
PRIDEiQ8K0Q5.

PTM databases

iPTMnetiQ8K0Q5.
PhosphoSiteiQ8K0Q5.

Expressioni

Tissue specificityi

Widely expressed: expressed in most organs, except small intestine.1 Publication

Gene expression databases

BgeeiQ8K0Q5.
CleanExiMM_ARHGAP18.
ExpressionAtlasiQ8K0Q5. baseline and differential.
GenevisibleiQ8K0Q5. MM.

Interactioni

Subunit structurei

Interacts with MPHOSPH6.By similarity

Protein-protein interaction databases

IntActiQ8K0Q5. 1 interaction.
STRINGi10090.ENSMUSP00000044834.

Structurei

3D structure databases

ProteinModelPortaliQ8K0Q5.
SMRiQ8K0Q5. Positions 321-533.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini324 – 523200Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2200. Eukaryota.
ENOG410XQ10. LUCA.
GeneTreeiENSGT00760000119123.
HOGENOMiHOG000015106.
HOVERGENiHBG072023.
InParanoidiQ8K0Q5.
OMAiTANTMHL.
OrthoDBiEOG7ZGX3J.
PhylomeDBiQ8K0Q5.
TreeFamiTF314044.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K0Q5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNWLSSSSGV VLTAYHPSGK DQVAGDSHVK GGDEATSSRR YGQYTINQEG
60 70 80 90 100
STKVPERPPF DRSSSQDSLD ESMEAYWTEL ENIKRSNENR QEGQEAIVVK
110 120 130 140 150
EPDEGELEEE WLKEAGLSNL FGESIDDPQE SILFLSTLTR TQAAAVQKRV
160 170 180 190 200
ETVSQTLRKK NKQHHIRDVR DIFAQQREAQ EKPPDDSDLR SVRTNENKGQ
210 220 230 240 250
GKDDQPSSGA VDSKEQISRV PEDTPASETD INLEVSFAEQ AVNQKEFSKE
260 270 280 290 300
RTQKISSNDS LPSFRLPKDK TGTTRIGDLA PQDMKKVCSL SLIELTALYD
310 320 330 340 350
VLGLEFKQQK AVKIKTRDSG LFGIPLTILL EQDQRKVPGT RIPLIFQKLI
360 370 380 390 400
SRIEEGSLET EGLLRIPGAA MRIKNLCQEL EAKFYEGTFN WESVKQHDAA
410 420 430 440 450
SLLKLFLREL PQPLLSMEYL KAFQAVQNLP TRKEQLQALN LLVILLPDAN
460 470 480 490 500
RDTLKALLEF LQRVIDNKEK NKMTAGNVAM VMAPNLFMCH TLGLKSSEQR
510 520 530 540 550
EFEMAAGTAN VMHLLIRYQK ILWTIPKFIV IQVRKQNIEN QKKERKAMKK
560 570 580 590 600
LLKKMAYDRE KHEKQDKTAN GADVPQGVIR VQAPHLSKVS MAIQLTEELK
610 620 630 640 650
ASDVLARFLS QESGVAQTLK KGEVFLYEIG GNIGERCLDD DTHMKDLYQL
660
NPNAEWVIKS KPV
Length:663
Mass (Da):74,930
Last modified:October 1, 2002 - v1
Checksum:iBB9ED06B850FEF41
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti293 – 2931I → F in BAC37322 (PubMed:16141072).Curated
Sequence conflicti518 – 5192YQ → FN in AAH25004 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC025004 mRNA. Translation: AAH25004.1.
BC030858 mRNA. Translation: AAH30858.1.
AK078522 mRNA. Translation: BAC37322.1.
CCDSiCCDS23757.1.
RefSeqiNP_789807.1. NM_176837.2.
UniGeneiMm.356496.

Genome annotation databases

EnsembliENSMUST00000039557; ENSMUSP00000044834; ENSMUSG00000039031.
GeneIDi73910.
KEGGimmu:73910.
UCSCiuc007ese.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC025004 mRNA. Translation: AAH25004.1.
BC030858 mRNA. Translation: AAH30858.1.
AK078522 mRNA. Translation: BAC37322.1.
CCDSiCCDS23757.1.
RefSeqiNP_789807.1. NM_176837.2.
UniGeneiMm.356496.

3D structure databases

ProteinModelPortaliQ8K0Q5.
SMRiQ8K0Q5. Positions 321-533.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8K0Q5. 1 interaction.
STRINGi10090.ENSMUSP00000044834.

PTM databases

iPTMnetiQ8K0Q5.
PhosphoSiteiQ8K0Q5.

Proteomic databases

EPDiQ8K0Q5.
MaxQBiQ8K0Q5.
PaxDbiQ8K0Q5.
PRIDEiQ8K0Q5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000039557; ENSMUSP00000044834; ENSMUSG00000039031.
GeneIDi73910.
KEGGimmu:73910.
UCSCiuc007ese.1. mouse.

Organism-specific databases

CTDi93663.
MGIiMGI:1921160. Arhgap18.

Phylogenomic databases

eggNOGiKOG2200. Eukaryota.
ENOG410XQ10. LUCA.
GeneTreeiENSGT00760000119123.
HOGENOMiHOG000015106.
HOVERGENiHBG072023.
InParanoidiQ8K0Q5.
OMAiTANTMHL.
OrthoDBiEOG7ZGX3J.
PhylomeDBiQ8K0Q5.
TreeFamiTF314044.

Enzyme and pathway databases

ReactomeiR-MMU-194840. Rho GTPase cycle.

Miscellaneous databases

PROiQ8K0Q5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K0Q5.
CleanExiMM_ARHGAP18.
ExpressionAtlasiQ8K0Q5. baseline and differential.
GenevisibleiQ8K0Q5. MM.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/NImported.
    Tissue: KidneyImported and LiverImported.
  2. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 293-663.
    Strain: C57BL/6J.
    Tissue: Muellerian duct.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68 AND SER-260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Liver, Lung, Spleen and Testis.
  4. "ARHGAP18, a GTPase-activating protein for RhoA, controls cell shape, spreading, and motility."
    Maeda M., Hasegawa H., Hyodo T., Ito S., Asano E., Yuang H., Funasaka K., Shimokata K., Hasegawa Y., Hamaguchi M., Senga T.
    Mol. Biol. Cell 22:3840-3852(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiRHG18_MOUSE
AccessioniPrimary (citable) accession number: Q8K0Q5
Secondary accession number(s): Q8BP03, Q8R196
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 93 of the entry and version 1 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

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 one 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.