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Protein
Submitted name:

GTP-binding protein

Gene

cRhoB

Organism
Gallus gallus (Chicken)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-GGA-114604. GPVI-mediated activation cascade.
R-GGA-194840. Rho GTPase cycle.
R-GGA-416482. G alpha (12/13) signalling events.
R-GGA-416572. Sema4D induced cell migration and growth-cone collapse.
R-GGA-5625740. RHO GTPases activate PKNs.
R-GGA-5625900. RHO GTPases activate CIT.
R-GGA-5627117. RHO GTPases Activate ROCKs.
R-GGA-5663220. RHO GTPases Activate Formins.

Names & Taxonomyi

Protein namesi
Submitted name:
GTP-binding proteinImported
Submitted name:
GTPase cRhoBImported
Submitted name:
Uncharacterized proteinImported
Gene namesi
Name:cRhoBImported
Synonyms:RHOBImported, rhoBImported
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 3

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000026544.

Family & Domainsi

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
KOiK07856.
OMAiGKKHHCV.
OrthoDBiEOG73FQPD.
TreeFamiTF300837.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.

Sequencei

Sequence statusi: Complete.

O93468-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAIRKKLVV VGDGACGKTC LLIVFSKDEF PEVYVPTVFE NYVADIEVDG
60 70 80 90 100
KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSVDSPD SLENIPEKWV
110 120 130 140 150
PEVKHFCPNV PIILVANKKD LRNDEHVRNE LARMKQEPVR TEDGRAMAIR
160 170 180 190
IQAYDYLECS AKTKEGVREV FETATRAALQ KRYGTQNGCI NCCKVL
Length:196
Mass (Da):22,205
Last modified:November 1, 1998 - v1
Checksum:iD5906EB99AD3F0A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AADN03003241 Genomic DNA. No translation available.
U79758 mRNA. Translation: AAC18963.1.
AF098515 mRNA. Translation: AAD12257.1.
RefSeqiNP_990240.1. NM_204909.1.
UniGeneiGga.3852.

Genome annotation databases

EnsembliENSGALT00000026595; ENSGALP00000026544; ENSGALG00000016485.
GeneIDi395734.
KEGGigga:395734.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AADN03003241 Genomic DNA. No translation available.
U79758 mRNA. Translation: AAC18963.1.
AF098515 mRNA. Translation: AAD12257.1.
RefSeqiNP_990240.1. NM_204909.1.
UniGeneiGga.3852.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000026544.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000026595; ENSGALP00000026544; ENSGALG00000016485.
GeneIDi395734.
KEGGigga:395734.

Organism-specific databases

CTDi388.

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
KOiK07856.
OMAiGKKHHCV.
OrthoDBiEOG73FQPD.
TreeFamiTF300837.

Enzyme and pathway databases

ReactomeiR-GGA-114604. GPVI-mediated activation cascade.
R-GGA-194840. Rho GTPase cycle.
R-GGA-416482. G alpha (12/13) signalling events.
R-GGA-416572. Sema4D induced cell migration and growth-cone collapse.
R-GGA-5625740. RHO GTPases activate PKNs.
R-GGA-5625900. RHO GTPases activate CIT.
R-GGA-5627117. RHO GTPases Activate ROCKs.
R-GGA-5663220. RHO GTPases Activate Formins.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Differential expression of distinct members of Rho family GTP-binding proteins during neuronal development: identification of Rac1B, a new neural-specific member of the family."
    Malosio M.L., Gilardelli D., Paris S., Albertinazzi C., de Curtis I.
    J. Neurosci. 17:6717-6728(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: Neural retinaImported.
  2. "A role for rhoB in the delamination of neural crest cells from the dorsal neural tube."
    Liu J.-P., Jessell T.M.
    Development 0:0-0(1999)
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution."
    International Chicken Genome Sequencing Consortium
    Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A.
    , Kremitzki C., Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., Wilson R.K.
    Nature 432:695-716(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Red jungle fowlImported.
  4. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Red jungle fowlImported.

Entry informationi

Entry nameiO93468_CHICK
AccessioniPrimary (citable) accession number: O93468
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1998
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.