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Reviewed, UniProtKB/Swiss-Prot Q8N392 (RHG18_HUMAN)

Last modified November 24, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Rho GTPase-activating protein 18
Alternative name(s):
    Rho-type GTPase-activating protein 18
    MacGAP
Gene names
Name: ARHGAP18
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length663 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state By similarity. UniProtKB Q9BRR9

Subunit structure

Interacts with MPHOSPH6. Ref.5

Sequence similarities

Contains 1 Rho-GAP domain.

Sequence caution

The sequence AAH39611.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

The sequence AAH62417.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionGTPase activation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processsignal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentintracellular

Inferred from electronic annotation. Source: InterPro

   Molecular functionGTPase activator activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding Ref.5

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MPHOSPH6Q995471EBI-372814,EBI-373187

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.5 Ref.3 Ref.4 (identifier: Q8N392-1)

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.
Isoform 2 Ref.2 (identifier: Q8N392-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 663663Rho GTPase-activating protein 18
PRO_0000245789

Regions

Domain324 – 523200Rho-GAP

Natural variations

Alternative sequence1 – 4545Missing in isoform 2. Ref.2
VSP_052092
Natural variant231A → T: dbSNP rs3752536.
VAR_060460
Natural variant911N → S: dbSNP rs11544371.
VAR_060461
Natural variant1651Q → H: dbSNP rs11544372.
VAR_060462

Experimental info

Sequence conflict3071K → E in AAH17223. Ref.3
Sequence conflict4671N → K in AAH62417. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 25, 2004. Version 2.
Checksum: E490D7B78E56971B

FASTA66374,947
        10         20         30         40         50         60 
MSWLSSSQGV VLTAYHPSGK DQAVGNSHAK AGEEATSSRR YGQYTMNQES TTIKVMEKPP 

        70         80         90        100        110        120 
FDRSISQDSL DELSMEDYWI ELENIKKSSE NSQEDQEVVV VKEPDEGELE EEWLKEAGLS 

       130        140        150        160        170        180 
NLFGESAGDP QESIVFLSTL TRTQAAAVQK RVETVSQTLR KKNKQYQIPD VRDIFAQQRE 

       190        200        210        220        230        240 
SKETAPGGTE SQSLRTNENK YQGRDDEASN LVGEEKLIPP EETPAPETDI NLEVSFAEQA 

       250        260        270        280        290        300 
LNQKESSKEK IQKSKGDDAT LPSFRLPKDK TGTTRIGDLA PQDMKKVCHL ALIELTALYD 

       310        320        330        340        350        360 
VLGIELKQQK AVKIKTKDSG LFCVPLTALL EQDQRKVPGM RIPLIFQKLI SRIEERGLET 

       370        380        390        400        410        420 
EGLLRIPGAA IRIKNLCQEL EAKFYEGTFN WESVKQHDAA SLLKLFIREL PQPLLSVEYL 

       430        440        450        460        470        480 
KAFQAVQNLP TKKQQLQALN LLVILLPDAN RDTLKALLEF LQRVIDNKEK NKMTVMNVAM 

       490        500        510        520        530        540 
VMAPNLFMCH ALGLKSSEQR EFVMAAGTAN TMHLLIKYQK LLWTIPKFIV NQVRKQNTEN 

       550        560        570        580        590        600 
HKKDKRAMKK LLKKMAYDRE KYEKQDKSTN DADVPQGVIR VQAPHLSKVS MAIQLTEELK 

       610        620        630        640        650        660 
ASDVLARFLS QESGVAQTLK KGEVFLYEIG GNIGERCLDD DTYMKDLYQL NPNAEWVIKS 


KPL 

« Hide

Isoform 2.

Checksum: 12A738DABAFE2ABB
Show »

FASTA61870,164

References

« Hide 'large scale' references
[1]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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. expand/collapse author list , 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: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2).
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain and Uterus.
[4]"Moleculer 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.
[5]"A protein interaction framework for human mRNA degradation."
Lehner B., Sanderson C.M.
Genome Res. 14:1315-1323(2004) [PubMed: 15231747] [Abstract]
Cited for: INTERACTION WITH MPHOSPH6.
[6]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AL834511 mRNA. Translation: CAD39167.2.
AL450310 Genomic DNA. Translation: CAH72298.1.
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.
IPIIPI00296353.
IPI00760924.
PIRG59432.
RefSeqNP_277050.2.
UniGeneHs.486458

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ8N392. 1 interaction.
STRINGQ8N392.

PTM databases

PhosphoSiteQ8N392.

Proteomic databases

PRIDEQ8N392.

Genome annotation databases

EnsemblENST00000275189; ENSP00000275189; ENSG00000146376; Homo sapiens. [Genome view]
GeneID93663.
KEGGhsa:93663.
UCSCuc003qbr.1. human.

Organism-specific databases

CTD93663.
GeneCardsGC06M129939.
HGNCHGNC:21035. ARHGAP18.
PharmGKBPA134884487.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ8N392.
HOVERGENQ8N392.

Enzyme and pathway databases

ReactomeREACT_11044. Signaling by Rho GTPases.

Gene expression databases

ArrayExpressQ8N392.
BgeeQ8N392.
CleanExHS_ARHGAP18.
GenevestigatorQ8N392.
GermOnlineENSG00000146376. Homo sapiens.

Family and domain databases

InterProIPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP.
[Graphical view]
Gene3DG3DSA:1.10.555.10. RhoGAP. 1 hit.
PfamPF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTSM00324. RhoGAP. 1 hit.
[Graphical view]
PROSITEPS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio78204.

Entry information

Entry nameRHG18_HUMAN
AccessionPrimary (citable) accession number: Q8N392
Secondary accession number(s): Q58EZ3 expand/collapse secondary AC list , Q6P679, Q6PJD7, Q96S64
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: October 25, 2004
Last modified: November 24, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents