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O43307

- ARHG9_HUMAN

UniProt

O43307 - ARHG9_HUMAN

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Protein

Rho guanine nucleotide exchange factor 9

Gene
ARHGEF9, ARHDH9, KIAA0424
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Acts as guanine nucleotide exchange factor (GEF) for CDC42. Promotes formation of GPHN clusters.1 Publication

GO - Molecular functioni

  1. Rho guanyl-nucleotide exchange factor activity Source: InterPro

GO - Biological processi

  1. apoptotic signaling pathway Source: Reactome
  2. ion transmembrane transport Source: Reactome
  3. neurotrophin TRK receptor signaling pathway Source: Reactome
  4. positive regulation of apoptotic process Source: Reactome
  5. regulation of small GTPase mediated signal transduction Source: Reactome
  6. small GTPase mediated signal transduction Source: Reactome
  7. synaptic transmission Source: Reactome
  8. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.
REACT_24987. GABA A receptor activation.
REACT_25387. Ligand-gated ion channel transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho guanine nucleotide exchange factor 9
Alternative name(s):
Collybistin
PEM-2 homolog
Rac/Cdc42 guanine nucleotide exchange factor 9
Gene namesi
Name:ARHGEF9
Synonyms:ARHDH9, KIAA0424
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:14561. ARHGEF9.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Epileptic encephalopathy, early infantile, 8 (EIEE8) [MIM:300607]: A disorder characterized by hyperekplexia and early infantile epileptic encephalopathy. Neurologic features include exaggerated startle response, seizures, impaired psychomotor development, and mental retardation. Seizures can be provoked by tactile stimulation or extreme emotion.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti55 – 551G → A in EIEE8; affects dendritic gephrin clustering and trafficking of GABA-A receptors to synapses. 1 Publication
VAR_028752

Keywords - Diseasei

Disease mutation, Epilepsy

Organism-specific databases

MIMi300607. phenotype.
Orphaneti163985. Hyperekplexia - epilepsy.
PharmGKBiPA24978.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 516516Rho guanine nucleotide exchange factor 9PRO_0000253895Add
BLAST

Proteomic databases

PaxDbiO43307.
PRIDEiO43307.

PTM databases

PhosphoSiteiO43307.

Expressioni

Tissue specificityi

Detected in brain. Detected at low levels in heart.1 Publication

Gene expression databases

ArrayExpressiO43307.
BgeeiO43307.
CleanExiHS_ARHGEF9.
GenevestigatoriO43307.

Organism-specific databases

HPAiHPA035419.

Interactioni

Subunit structurei

Interacts with GPHN.

Protein-protein interaction databases

BioGridi116834. 5 interactions.
IntActiO43307. 1 interaction.
STRINGi9606.ENSP00000253401.

Structurei

Secondary structure

1
516
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 177
Beta strandi22 – 265
Beta strandi34 – 396
Beta strandi42 – 498
Beta strandi54 – 585
Helixi59 – 613
Beta strandi62 – 665

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YSQNMR-A7-75[»]
ProteinModelPortaliO43307.
SMRiO43307. Positions 4-450.

Miscellaneous databases

EvolutionaryTraceiO43307.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 6760SH3Add
BLAST
Domaini103 – 287185DHAdd
BLAST
Domaini318 – 425108PHAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni100 – 11011Interaction with GPHN By similarityAdd
BLAST

Sequence similaritiesi

Contains 1 PH domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiCOG5422.
HOGENOMiHOG000237363.
HOVERGENiHBG050568.
OMAiKVTKQKG.
PhylomeDBiO43307.
TreeFamiTF316832.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR000219. DH-domain.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O43307-1) [UniParc]FASTAAdd to Basket

Also known as: CB3(SH3+)

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

MTLLITGDSI VSAEAVWDHV TMANRELAFK AGDVIKVLDA SNKDWWWGQI    50
DDEEGWFPAS FVRLWVNQED EVEEGPSDVQ NGHLDPNSDC LCLGRPLQNR 100
DQMRANVINE IMSTERHYIK HLKDICEGYL KQCRKRRDMF SDEQLKVIFG 150
NIEDIYRFQM GFVRDLEKQY NNDDPHLSEI GPCFLEHQDG FWIYSEYCNN 200
HLDACMELSK LMKDSRYQHF FEACRLLQQM IDIAIDGFLL TPVQKICKYP 250
LQLAELLKYT AQDHSDYRYV AAALAVMRNV TQQINERKRR LENIDKIAQW 300
QASVLDWEGE DILDRSSELI YTGEMAWIYQ PYGRNQQRVF FLFDHQMVLC 350
KKDLIRRDIL YYKGRIDMDK YEVVDIEDGR DDDFNVSMKN AFKLHNKETE 400
EIHLFFAKKL EEKIRWLRAF REERKMVQED EKIGFEISEN QKRQAAMTVR 450
KVPKQKGVNS ARSVPPSYPP PQDPLNHGQY LVPDGIAQSQ VFEFTEPKRS 500
QSPFWQNFSR LTPFKK 516
Length:516
Mass (Da):60,982
Last modified:October 17, 2006 - v3
Checksum:iAAEE17366B46B707
GO
Isoform 2 (identifier: O43307-2) [UniParc]FASTAAdd to Basket

Also known as: CB3(SH3-)

The sequence of this isoform differs from the canonical sequence as follows:
     1-10: MTLLITGDSI → MQWIRGGSGM
     11-63: Missing.

Show »
Length:463
Mass (Da):54,965
Checksum:i046F5EC27274EC71
GO
Isoform 3 (identifier: O43307-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-102: Missing.

Show »
Length:414
Mass (Da):49,458
Checksum:i65A0F069D8E0A009
GO

Sequence cautioni

The sequence BAA24854.2 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti55 – 551G → A in EIEE8; affects dendritic gephrin clustering and trafficking of GABA-A receptors to synapses. 1 Publication
VAR_028752
Natural varianti401 – 4011E → K Probable disease-associated mutation found in a patient with moderate mental retardation, speech delay and sleep disturbances. 1 Publication
VAR_069370

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 102102Missing in isoform 3. VSP_044555Add
BLAST
Alternative sequencei1 – 1010MTLLITGDSI → MQWIRGGSGM in isoform 2. VSP_042920
Alternative sequencei11 – 6353Missing in isoform 2. VSP_042921Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091N → D in BAF82682. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB007884 mRNA. Translation: BAA24854.2. Different initiation.
AK289993 mRNA. Translation: BAF82682.1.
AK295033 mRNA. Translation: BAG58088.1.
AL451106, AL355142, AL391277 Genomic DNA. Translation: CAI39550.1.
AL391277, AL355142, AL451106 Genomic DNA. Translation: CAI40401.1.
AL355142, AL391277, AL451106 Genomic DNA. Translation: CAI41195.1.
BC056892 mRNA. No translation available.
BC117406 mRNA. Translation: AAI17407.1.
CCDSiCCDS35315.1. [O43307-1]
CCDS55429.1. [O43307-3]
CCDS55430.1. [O43307-2]
RefSeqiNP_001166950.1. NM_001173479.1. [O43307-2]
NP_001166951.1. NM_001173480.1. [O43307-3]
NP_056000.1. NM_015185.2. [O43307-1]
UniGeneiHs.54697.

Genome annotation databases

EnsembliENST00000253401; ENSP00000253401; ENSG00000131089. [O43307-1]
ENST00000374870; ENSP00000364004; ENSG00000131089. [O43307-3]
ENST00000437457; ENSP00000399994; ENSG00000131089. [O43307-2]
ENST00000601443; ENSP00000469587; ENSG00000268229. [O43307-1]
ENST00000601864; ENSP00000471377; ENSG00000268229. [O43307-2]
ENST00000602267; ENSP00000469767; ENSG00000268229. [O43307-3]
GeneIDi23229.
KEGGihsa:23229.
UCSCiuc004dvj.2. human. [O43307-1]
uc011mot.2. human. [O43307-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB007884 mRNA. Translation: BAA24854.2 . Different initiation.
AK289993 mRNA. Translation: BAF82682.1 .
AK295033 mRNA. Translation: BAG58088.1 .
AL451106 , AL355142 , AL391277 Genomic DNA. Translation: CAI39550.1 .
AL391277 , AL355142 , AL451106 Genomic DNA. Translation: CAI40401.1 .
AL355142 , AL391277 , AL451106 Genomic DNA. Translation: CAI41195.1 .
BC056892 mRNA. No translation available.
BC117406 mRNA. Translation: AAI17407.1 .
CCDSi CCDS35315.1. [O43307-1 ]
CCDS55429.1. [O43307-3 ]
CCDS55430.1. [O43307-2 ]
RefSeqi NP_001166950.1. NM_001173479.1. [O43307-2 ]
NP_001166951.1. NM_001173480.1. [O43307-3 ]
NP_056000.1. NM_015185.2. [O43307-1 ]
UniGenei Hs.54697.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YSQ NMR - A 7-75 [» ]
ProteinModelPortali O43307.
SMRi O43307. Positions 4-450.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116834. 5 interactions.
IntActi O43307. 1 interaction.
STRINGi 9606.ENSP00000253401.

PTM databases

PhosphoSitei O43307.

Proteomic databases

PaxDbi O43307.
PRIDEi O43307.

Protocols and materials databases

DNASUi 23229.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000253401 ; ENSP00000253401 ; ENSG00000131089 . [O43307-1 ]
ENST00000374870 ; ENSP00000364004 ; ENSG00000131089 . [O43307-3 ]
ENST00000437457 ; ENSP00000399994 ; ENSG00000131089 . [O43307-2 ]
ENST00000601443 ; ENSP00000469587 ; ENSG00000268229 . [O43307-1 ]
ENST00000601864 ; ENSP00000471377 ; ENSG00000268229 . [O43307-2 ]
ENST00000602267 ; ENSP00000469767 ; ENSG00000268229 . [O43307-3 ]
GeneIDi 23229.
KEGGi hsa:23229.
UCSCi uc004dvj.2. human. [O43307-1 ]
uc011mot.2. human. [O43307-2 ]

Organism-specific databases

CTDi 23229.
GeneCardsi GC0XM062771.
GeneReviewsi ARHGEF9.
HGNCi HGNC:14561. ARHGEF9.
HPAi HPA035419.
MIMi 300429. gene.
300607. phenotype.
neXtProti NX_O43307.
Orphaneti 163985. Hyperekplexia - epilepsy.
PharmGKBi PA24978.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5422.
HOGENOMi HOG000237363.
HOVERGENi HBG050568.
OMAi KVTKQKG.
PhylomeDBi O43307.
TreeFami TF316832.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.
REACT_24987. GABA A receptor activation.
REACT_25387. Ligand-gated ion channel transport.

Miscellaneous databases

EvolutionaryTracei O43307.
GeneWikii ARHGEF9.
GenomeRNAii 23229.
NextBioi 44841.
PROi O43307.
SOURCEi Search...

Gene expression databases

ArrayExpressi O43307.
Bgeei O43307.
CleanExi HS_ARHGEF9.
Genevestigatori O43307.

Family and domain databases

Gene3Di 1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProi IPR000219. DH-domain.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEi PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
    Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain and Hippocampus.
  3. "The DNA sequence of the human X chromosome."
    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.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 1 AND 3).
    Tissue: Brain and Uterus.
  5. "Identification and characterization of hPEM-2, a guanine nucleotide exchange factor specific for Cdc42."
    Reid T., Bathoorn A., Ahmadian M.R., Collard J.G.
    J. Biol. Chem. 274:33587-33593(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Solution structure of the SH3 domain from Rho guanine nucleotide exchange factor 9."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 7-75.
  7. Cited for: VARIANT EIEE8 ALA-55, CHARACTERIZATION OF VARIANT EIEE8 ALA-55, ALTERNATIVE SPLICING.
  8. Cited for: VARIANT LYS-401.

Entry informationi

Entry nameiARHG9_HUMAN
AccessioniPrimary (citable) accession number: O43307
Secondary accession number(s): A8K1S8
, B4DHC7, F8W7P8, Q5JSL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: September 3, 2014
This is version 114 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi