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UniProtKB/Swiss-Prot entry O43307


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ARHG9_HUMAN
Primary accession number O43307
Secondary accession number Q5JSL6
Integrated into Swiss-Prot on October 17, 2006
Sequence was last modified on October 17, 2006 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 63)
Name and origin of the protein
Protein name Rho guanine nucleotide exchange factor 9
Synonyms Rac/Cdc42 guanine nucleotide exchange factor 9
Collybistin
PEM-2 homolog
Gene name
Name: ARHGEF9
Synonyms: KIAA0424
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1093/dnares/4.5.307; PubMed=9455477 [NCBI, ExPASy, EBI, Israel, Japan]
Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro.";
DNA Res. 4:307-313(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03440; PubMed=15772651 [NCBI, ExPASy, EBI, Israel, Japan]
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1074/jbc.274.47.33587; PubMed=10559246 [NCBI, ExPASy, EBI, Israel, Japan]
Reid T., Bathoorn A., Ahmadian M.R., Collard J.G.;
"Identification and characterization of hPEM-2, a guanine nucleotide exchange factor specific for Cdc42.";
J. Biol. Chem. 274:33587-33593(1999).
[5]
VARIANT STHEE ALA-55, CHARACTERIZATION OF VARIANT STHEE ALA-55, AND ALTERNATIVE SPLICING.
DOI=10.1523/JNEUROSCI.1184-04.2004; PubMed=15215304 [NCBI, ExPASy, EBI, Israel, Japan]
Harvey K., Duguid I.C., Alldred M.J., Beatty S.E., Ward H., Keep N.H., Lingenfelter S.E., Pearce B.R., Lundgren J., Owen M.J., Smart T.G., Luescher B., Rees M.I., Harvey R.J.;
"The GDP-GTP exchange factor collybistin: an essential determinant of neuronal gephyrin clustering.";
J. Neurosci. 24:5816-5826(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB007884; BAA24854.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL451106; CAI39550.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL355142; CAI39550.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391277; CAI39550.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391277; CAI40401.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL355142; CAI40401.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL451106; CAI40401.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL355142; CAI41195.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391277; CAI41195.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL451106; CAI41195.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC117406; AAI17407.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00552489; -.
RefSeq NP_056000.1; -.
UniGene Hs.54697
3D structure databases
PDB
2YSQ; NMR; -; A=7-75.[ExPASy / RCSB / EBI]
PDBsum 2YSQ; -.
SMR O43307; 90-454.
ModBase O43307.
Enzyme and pathway databases
Reactome REACT_11044; Signaling by Rho GTPases.
Organism-specific databases
GeneCards GC0XM062771; -.
HGNC HGNC:14561; ARHGEF9.
GenAtlas ARHGEF9.
MIM 300429; gene. [NCBI / EBI]
300607; phenotype. [NCBI / EBI]
Orphanet 163985; Hyperekplexia - epilepsy.
98465; X-linked neuromuscular intellectual deficit.
PharmGKB PA24978; -.
HUGE KIAA0424.
Gene expression databases
ArrayExpress O43307; -.
Bgee O43307; -.
CleanEx HS_ARHGEF9; -.
GermOnline ENSG00000131089; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005089; Molecular function: Rho guanyl-nucleotide exchange factor activity (inferred from electronic annotation from InterPro).
GO:0035023; Biological process: regulation of Rho protein signal transduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000219; DH-domain.
IPR001331; GDS_CDC24_CS.
IPR001849; Pleckstrin_homology.
IPR001452; SH3_domain.
Graphical view of domain structure.
Gene3D G3DSA:1.20.900.10; RhoGEF; 1.
Pfam PF00169; PH; 1.
PF00621; RhoGEF; 1.
PF00018; SH3_1; 1.
Pfam graphical view of domain structure.
ProDom PD000066; SH3; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00233; PH; 1.
SM00325; RhoGEF; 1.
SM00326; SH3; 1.
SMART graphical view of domain structure.
PROSITE PS00741; DH_1; FALSE_NEG.
PS50010; DH_2; 1.
PS50003; PH_DOMAIN; 1.
PS50002; SH3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE O43307; -.
Genome annotation databases
Ensembl ENSG00000131089; Homo sapiens. [Contig view]
GeneID 23229; -.
KEGG hsa:23229; -.
Phylogenomic databases
HOVERGEN O43307; -.
Other
NextBio 44841; -.
SOURCE ARHGEF9; Homo sapiens.
ProtoNet O43307.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Disease mutation; Epilepsy; Guanine-nucleotide releasing factor; SH3 domain.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   516  516     Rho guanine nucleotide exchange factor 9. PRO_0000253895
DOMAIN   8    67  60     SH3. 
DOMAIN   103   287  185     DH. 
DOMAIN   318   425  108     PH. 
REGION   100   110  11     Interaction with GPHN (By similarity). 
VARIANT   55    55  1     G -> A (in STHEE; affects dendritic gephrin clustering and trafficking of GABA-A receptors to synapses). VAR_028752 
Sequence information
Length: 516 AA [This is the length of the unprocessed precursor] Molecular weight: 60982 Da [This is the MW of the unprocessed precursor] CRC64: AAEE17366B46B707 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTLLITGDSI VSAEAVWDHV TMANRELAFK AGDVIKVLDA SNKDWWWGQI DDEEGWFPAS 

        70         80         90        100        110        120 
FVRLWVNQED EVEEGPSDVQ NGHLDPNSDC LCLGRPLQNR DQMRANVINE IMSTERHYIK 

       130        140        150        160        170        180 
HLKDICEGYL KQCRKRRDMF SDEQLKVIFG NIEDIYRFQM GFVRDLEKQY NNDDPHLSEI 

       190        200        210        220        230        240 
GPCFLEHQDG FWIYSEYCNN HLDACMELSK LMKDSRYQHF FEACRLLQQM IDIAIDGFLL 

       250        260        270        280        290        300 
TPVQKICKYP LQLAELLKYT AQDHSDYRYV AAALAVMRNV TQQINERKRR LENIDKIAQW 

       310        320        330        340        350        360 
QASVLDWEGE DILDRSSELI YTGEMAWIYQ PYGRNQQRVF FLFDHQMVLC KKDLIRRDIL 

       370        380        390        400        410        420 
YYKGRIDMDK YEVVDIEDGR DDDFNVSMKN AFKLHNKETE EIHLFFAKKL EEKIRWLRAF 

       430        440        450        460        470        480 
REERKMVQED EKIGFEISEN QKRQAAMTVR KVPKQKGVNS ARSVPPSYPP PQDPLNHGQY 

       490        500        510 
LVPDGIAQSQ VFEFTEPKRS QSPFWQNFSR LTPFKK 

O43307 in FASTA format

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