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Protein

Rho GTPase-activating protein 18

Gene

ARHGAP18

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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 (PubMed:21865595). 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 (PubMed:25778702). Regulates cell shape, spreading, and migration (PubMed:21865595).2 Publications

GO - Molecular functioni

  • GTPase activator activity Source: UniProtKB

GO - Biological processi

  • positive regulation of GTPase activity Source: GOC
  • regulation of actin cytoskeleton organization Source: UniProtKB
  • regulation of actin filament polymerization Source: UniProtKB
  • regulation of cell motility Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • regulation of small GTPase mediated signal transduction Source: UniProtKB
  • small GTPase mediated signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiR-HSA-194840. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GTPase-activating protein 18
Alternative name(s):
MacGAP1 Publication
Rho-type GTPase-activating protein 18
Gene namesi
Name:ARHGAP18Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21035. ARHGAP18.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi365 – 3651R → A: Abolishes GTPase activation activity. 1 Publication

Organism-specific databases

PharmGKBiPA134884487.

Polymorphism and mutation databases

BioMutaiARHGAP18.
DMDMi296452981.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 663663Rho GTPase-activating protein 18PRO_0000245789Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661PhosphoserineBy similarity
Modified residuei69 – 691PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8N392.
MaxQBiQ8N392.
PaxDbiQ8N392.
PRIDEiQ8N392.

PTM databases

iPTMnetiQ8N392.
PhosphoSiteiQ8N392.
SwissPalmiQ8N392.

Expressioni

Gene expression databases

BgeeiQ8N392.
CleanExiHS_ARHGAP18.
GenevisibleiQ8N392. HS.

Organism-specific databases

HPAiHPA031595.

Interactioni

Subunit structurei

Interacts with MPHOSPH6.1 Publication

Protein-protein interaction databases

BioGridi125050. 1 interaction.
IntActiQ8N392. 2 interactions.
STRINGi9606.ENSP00000275189.

Structurei

3D structure databases

ProteinModelPortaliQ8N392.
SMRiQ8N392. Positions 320-533.
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.
InParanoidiQ8N392.
OMAiTANTMHL.
OrthoDBiEOG7ZGX3J.
PhylomeDBiQ8N392.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8N392-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSWLSSSQGV VLTAYHPSGK DQTVGNSHAK AGEEATSSRR YGQYTMNQES
60 70 80 90 100
TTIKVMEKPP FDRSISQDSL DELSMEDYWI ELENIKKSSE NSQEDQEVVV
110 120 130 140 150
VKEPDEGELE EEWLKEAGLS NLFGESAGDP QESIVFLSTL TRTQAAAVQK
160 170 180 190 200
RVETVSQTLR KKNKQYQIPD VRDIFAQQRE SKETAPGGTE SQSLRTNENK
210 220 230 240 250
YQGRDDEASN LVGEEKLIPP EETPAPETDI NLEVSFAEQA LNQKESSKEK
260 270 280 290 300
IQKSKGDDAT LPSFRLPKDK TGTTRIGDLA PQDMKKVCHL ALIELTALYD
310 320 330 340 350
VLGIELKQQK AVKIKTKDSG LFCVPLTALL EQDQRKVPGM RIPLIFQKLI
360 370 380 390 400
SRIEERGLET EGLLRIPGAA IRIKNLCQEL EAKFYEGTFN WESVKQHDAA
410 420 430 440 450
SLLKLFIREL PQPLLSVEYL KAFQAVQNLP TKKQQLQALN LLVILLPDAN
460 470 480 490 500
RDTLKALLEF LQRVIDNKEK NKMTVMNVAM VMAPNLFMCH ALGLKSSEQR
510 520 530 540 550
EFVMAAGTAN TMHLLIKYQK LLWTIPKFIV NQVRKQNTEN HKKDKRAMKK
560 570 580 590 600
LLKKMAYDRE KYEKQDKSTN DADVPQGVIR VQAPHLSKVS MAIQLTEELK
610 620 630 640 650
ASDVLARFLS QESGVAQTLK KGEVFLYEIG GNIGERCLDD DTYMKDLYQL
660
NPNAEWVIKS KPL
Length:663
Mass (Da):74,977
Last modified:May 18, 2010 - v3
Checksum:i2DD127301026928D
GO
Isoform 2 (identifier: Q8N392-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:618
Mass (Da):70,164
Checksum:i12A738DABAFE2ABB
GO

Sequence cautioni

The sequence AAH17223.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH39611.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH62417.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAB61887.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti307 – 3071K → E in AAH17223 (PubMed:15489334).Curated
Sequence conflicti467 – 4671N → K in AAH62417 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231T → A.3 Publications
Corresponds to variant rs3752536 [ dbSNP | Ensembl ].
VAR_060460
Natural varianti91 – 911N → S.
Corresponds to variant rs11544371 [ dbSNP | Ensembl ].
VAR_060461
Natural varianti165 – 1651Q → H.
Corresponds to variant rs11544372 [ dbSNP | Ensembl ].
VAR_060462

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4545Missing in isoform 2. 1 PublicationVSP_052092Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL834511 mRNA. Translation: CAD39167.2.
AL450310 Genomic DNA. Translation: CAH72298.1.
CH471051 Genomic DNA. Translation: EAW48076.1.
CH471051 Genomic DNA. Translation: EAW48077.1.
BC017223 mRNA. Translation: AAH17223.1. Sequence problems.
BC039611 mRNA. Translation: AAH39611.1. Sequence problems.
BC062417 mRNA. Translation: AAH62417.1. Sequence problems.
BC101708 mRNA. Translation: AAI01709.1.
BC107416 mRNA. Translation: AAI07417.1.
BC111940 mRNA. Translation: AAI11941.1.
AB053293 mRNA. Translation: BAB61887.1. Different initiation.
CCDSiCCDS34535.1. [Q8N392-1]
PIRiG59432.
RefSeqiNP_277050.2. NM_033515.2. [Q8N392-1]
XP_005267269.1. XM_005267212.1. [Q8N392-2]
UniGeneiHs.486458.

Genome annotation databases

EnsembliENST00000368149; ENSP00000357131; ENSG00000146376. [Q8N392-1]
GeneIDi93663.
KEGGihsa:93663.
UCSCiuc003qbr.4. human. [Q8N392-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL834511 mRNA. Translation: CAD39167.2.
AL450310 Genomic DNA. Translation: CAH72298.1.
CH471051 Genomic DNA. Translation: EAW48076.1.
CH471051 Genomic DNA. Translation: EAW48077.1.
BC017223 mRNA. Translation: AAH17223.1. Sequence problems.
BC039611 mRNA. Translation: AAH39611.1. Sequence problems.
BC062417 mRNA. Translation: AAH62417.1. Sequence problems.
BC101708 mRNA. Translation: AAI01709.1.
BC107416 mRNA. Translation: AAI07417.1.
BC111940 mRNA. Translation: AAI11941.1.
AB053293 mRNA. Translation: BAB61887.1. Different initiation.
CCDSiCCDS34535.1. [Q8N392-1]
PIRiG59432.
RefSeqiNP_277050.2. NM_033515.2. [Q8N392-1]
XP_005267269.1. XM_005267212.1. [Q8N392-2]
UniGeneiHs.486458.

3D structure databases

ProteinModelPortaliQ8N392.
SMRiQ8N392. Positions 320-533.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125050. 1 interaction.
IntActiQ8N392. 2 interactions.
STRINGi9606.ENSP00000275189.

PTM databases

iPTMnetiQ8N392.
PhosphoSiteiQ8N392.
SwissPalmiQ8N392.

Polymorphism and mutation databases

BioMutaiARHGAP18.
DMDMi296452981.

Proteomic databases

EPDiQ8N392.
MaxQBiQ8N392.
PaxDbiQ8N392.
PRIDEiQ8N392.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368149; ENSP00000357131; ENSG00000146376. [Q8N392-1]
GeneIDi93663.
KEGGihsa:93663.
UCSCiuc003qbr.4. human. [Q8N392-1]

Organism-specific databases

CTDi93663.
GeneCardsiARHGAP18.
H-InvDBHIX0006211.
HGNCiHGNC:21035. ARHGAP18.
HPAiHPA031595.
MIMi613351. gene.
neXtProtiNX_Q8N392.
PharmGKBiPA134884487.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2200. Eukaryota.
ENOG410XQ10. LUCA.
GeneTreeiENSGT00760000119123.
HOGENOMiHOG000015106.
HOVERGENiHBG072023.
InParanoidiQ8N392.
OMAiTANTMHL.
OrthoDBiEOG7ZGX3J.
PhylomeDBiQ8N392.
TreeFamiTF314044.

Enzyme and pathway databases

ReactomeiR-HSA-194840. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSiARHGAP18. human.
GenomeRNAii93663.
NextBioi78204.
PROiQ8N392.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N392.
CleanExiHS_ARHGAP18.
GenevisibleiQ8N392. HS.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-23.
    Tissue: Melanoma.
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-23.
  4. "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] (ISOFORM 1), VARIANT ALA-23.
    Tissue: BrainImported and UterusImported.
  5. "Molecular cloning and characterization of a novel GTPase activating Protein that regulated mast cell degranulation."
    Uchida T., Kuramasu A., Okumura K., Nakao A., Ogawa H., Ra C.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 39-663 (ISOFORM 1).
    Tissue: Mast cell.
  6. "A protein interaction framework for human mRNA degradation."
    Lehner B., Sanderson C.M.
    Genome Res. 14:1315-1323(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MPHOSPH6.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-365.
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. Cited for: FUNCTION.

Entry informationi

Entry nameiRHG18_HUMAN
AccessioniPrimary (citable) accession number: Q8N392
Secondary accession number(s): E1P575
, Q58EZ3, Q6P679, Q6PJD7, Q96S64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: May 18, 2010
Last modified: March 16, 2016
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.