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Protein
Submitted name:

Rho GTPase-activating protein 4

Gene

ARHGAP4

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Protein predictedi

Functioni

GO - Molecular functioni

  1. Rho GTPase activator activity Source: Ensembl

GO - Biological processi

  1. negative regulation of axon extension Source: Ensembl
  2. negative regulation of fibroblast migration Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Rho GTPase-activating protein 4Imported
Gene namesi
Name:ARHGAP4Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:674. ARHGAP4.

Subcellular locationi

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. growth cone Source: Ensembl
  3. microtubule Source: Ensembl
Complete GO annotation...

PTM / Processingi

Proteomic databases

PRIDEiC9J5M2.

Expressioni

Gene expression databases

BgeeiC9J5M2.
ExpressionAtlasiC9J5M2. baseline and differential.

Family & Domainsi

Phylogenomic databases

GeneTreeiENSGT00760000118863.
HOGENOMiHOG000039980.

Family and domain databases

InterProiIPR001060. FCH_dom.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
[Graphical view]
PROSITEiPS50133. FCH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

C9J5M2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRWQLSEQLR CLELQGELRR ELLQELAEFM RRRAEVELEY SRGLEKLAER
60 70 80 90 100
FSSRGGRLGS SREHQSFRKE PSLLSPLHCW AVLLQHTRQQ SRESAALSEV
110 120 130 140 150
LAGPLAQRLS HIAEDVGRLV KKSRDLEQQL QDELLEVVSE LQTAKKTYQA
160 170
YHMESVNAEA KLREAERQEE KRAGRS
Length:176
Mass (Da):20,479
Last modified:February 4, 2015 - v4
Checksum:i1CD4862571CB681F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei176 – 1761Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KF510182 Genomic DNA. No translation available.
KF510654 Genomic DNA. No translation available.
KF510656 Genomic DNA. No translation available.
U52112 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000442262; ENSP00000398259; ENSG00000089820.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KF510182 Genomic DNA. No translation available.
KF510654 Genomic DNA. No translation available.
KF510656 Genomic DNA. No translation available.
U52112 Genomic DNA. No translation available.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiC9J5M2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000442262; ENSP00000398259; ENSG00000089820.

Organism-specific databases

HGNCiHGNC:674. ARHGAP4.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000118863.
HOGENOMiHOG000039980.

Miscellaneous databases

ChiTaRSiARHGAP4. human.
NextBioi35485086.

Gene expression databases

BgeeiC9J5M2.
ExpressionAtlasiC9J5M2. baseline and differential.

Family and domain databases

InterProiIPR001060. FCH_dom.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
[Graphical view]
PROSITEiPS50133. FCH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiC9J5M2_HUMAN
AccessioniPrimary (citable) accession number: C9J5M2
Entry historyi
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: February 4, 2015
Last modified: February 4, 2015
This is version 35 of the entry and version 4 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.