Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Rho-related GTP-binding protein RhoB

Gene

RHOB

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

Functioni

Mediates apoptosis in neoplastically transformed cells after DNA damage. Not essential for development but affects cell adhesion and growth factor signaling in transformed cells. Plays a negative role in tumorigenesis as deletion causes tumor formation. Involved in intracellular protein trafficking of a number of proteins. Targets PKN1 to endosomes and is involved in trafficking of the EGF receptor from late endosomes to lysosomes. Also required for stability and nuclear trafficking of AKT1/AKT which promotes endothelial cell survival during vascular development. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Required for genotoxic stress-induced cell death in breast cancer cells.5 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 198GTPBy similarity
Nucleotide bindingi59 – 635GTPBy similarity
Nucleotide bindingi117 – 1204GTPBy similarity

GO - Molecular functioni

  1. GDP binding Source: Ensembl
  2. GTPase activity Source: UniProtKB
  3. GTP binding Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. apoptotic process Source: UniProtKB
  3. axon guidance Source: Reactome
  4. blood coagulation Source: Reactome
  5. cell adhesion Source: UniProtKB
  6. cellular response to hydrogen peroxide Source: UniProtKB
  7. cellular response to ionizing radiation Source: UniProtKB
  8. cytokinesis Source: UniProtKB
  9. endosome to lysosome transport Source: UniProtKB
  10. intracellular protein transport Source: Ensembl
  11. metabolic process Source: GOC
  12. negative regulation of cell cycle Source: UniProtKB
  13. platelet activation Source: Reactome
  14. positive regulation of angiogenesis Source: UniProtKB
  15. positive regulation of apoptotic process Source: UniProtKB
  16. regulation of small GTPase mediated signal transduction Source: Reactome
  17. Rho protein signal transduction Source: UniProtKB
  18. small GTPase mediated signal transduction Source: Reactome
  19. transformed cell apoptotic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Angiogenesis, Apoptosis, Cell adhesion, Differentiation, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_1695. GPVI-mediated activation cascade.
REACT_18407. G alpha (12/13) signalling events.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
SignaLinkiP62745.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho-related GTP-binding protein RhoB
Alternative name(s):
Rho cDNA clone 6
Short name:
h6
Gene namesi
Name:RHOB
Synonyms:ARH6, ARHB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:668. RHOB.

Subcellular locationi

Late endosome membrane; Lipid-anchor. Cell membrane; Lipid-anchor. Nucleus. Cleavage furrow
Note: Late endosomal membrane (geranylgeranylated form). Plasma membrane (farnesylated form). Also detected at the nuclear margin and in the nucleus. Translocates to the equatorial region before furrow formation in a ECT2-dependent manner.

GO - Cellular componenti

  1. cleavage furrow Source: UniProtKB
  2. cytosol Source: Reactome
  3. early endosome Source: Ensembl
  4. endosome membrane Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProtKB
  6. focal adhesion Source: UniProtKB
  7. late endosome membrane Source: UniProtKB-SubCell
  8. nucleus Source: UniProtKB
  9. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141G → V: No effect on internalization of EGF receptor but decreases trafficking of receptor to the lysosome with associated accumulation in late endosomes. 1 Publication
Mutagenesisi39 – 391F → G: Abolishes binding to PKN1 and trafficking of EGF receptor. 1 Publication
Mutagenesisi189 – 1891C → S: No effect on prenylation. Reduced palmitoylation. Abolishes palmitoylation; when associated with S-192. 1 Publication
Mutagenesisi192 – 1921C → S: Reduced geranylgeranylation but no effect on farnesylation. Reduced palmitoylation. Abolishes palmitoylation; when associated with S-189. 2 Publications
Mutagenesisi193 – 1931C → S: Abolishes methylation, palmitoylation and prenylation. 2 Publications
Mutagenesisi194 – 1941K → L: No effect on palmitoylation or prenylation. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA24950.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 193193Rho-related GTP-binding protein RhoBPRO_0000030417Add
BLAST
Propeptidei194 – 1963Removed in mature formPRO_0000030418

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411ADP-ribosylasparagine; by botulinum toxinBy similarity
Modified residuei154 – 1541PhosphotyrosineBy similarity
Lipidationi189 – 1891S-palmitoyl cysteine1 Publication
Lipidationi192 – 1921S-palmitoyl cysteine1 Publication
Modified residuei193 – 1931Cysteine methyl ester1 Publication
Lipidationi193 – 1931S-farnesyl cysteine; in plasma membrane form2 Publications
Lipidationi193 – 1931S-geranylgeranyl cysteine; in endosomal form2 Publications

Post-translational modificationi

Prenylation specifies the subcellular location of RHOB. The farnesylated form is localized to the plasma membrane while the geranylgeranylated form is localized to the endosome.2 Publications

Keywords - PTMi

ADP-ribosylation, Lipoprotein, Methylation, Palmitate, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP62745.
PaxDbiP62745.
PeptideAtlasiP62745.
PRIDEiP62745.

PTM databases

PhosphoSiteiP62745.

Expressioni

Inductioni

Up-regulated by DNA damaging agents like H2O2 or ionizing radiation (IR).1 Publication

Gene expression databases

BgeeiP62745.
CleanExiHS_RHOB.
ExpressionAtlasiP62745. baseline and differential.
GenevestigatoriP62745.

Organism-specific databases

HPAiCAB004560.

Interactioni

Subunit structurei

Binds ROCK1 and ROCK2. Also binds PKN1/PRK1. Interacts with ARGGEF3, RTKN and AKAP13.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SMURF1Q9HCE7-23EBI-602647,EBI-9845742
TNFAIP1Q138295EBI-602647,EBI-2505861

Protein-protein interaction databases

BioGridi106881. 16 interactions.
IntActiP62745. 23 interactions.
MINTiMINT-4824810.
STRINGi9606.ENSP00000272233.

Structurei

Secondary structure

1
196
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 129Combined sources
Helixi18 – 2710Combined sources
Beta strandi41 – 488Combined sources
Beta strandi51 – 599Combined sources
Turni67 – 693Combined sources
Helixi70 – 734Combined sources
Beta strandi79 – 857Combined sources
Helixi89 – 979Combined sources
Helixi99 – 1068Combined sources
Beta strandi112 – 1176Combined sources
Helixi119 – 1235Combined sources
Helixi125 – 1339Combined sources
Helixi141 – 15010Combined sources
Beta strandi154 – 1585Combined sources
Turni161 – 1633Combined sources
Helixi167 – 17913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FV8X-ray1.90A4-187[»]
ProteinModelPortaliP62745.
SMRiP62745. Positions 2-185.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62745.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi34 – 429Effector regionSequence Analysis

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP62745.
KOiK07856.
OMAiVRINAFE.
OrthoDBiEOG73FQPD.
PhylomeDBiP62745.
TreeFamiTF300837.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62745-1 [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 LRSDEHVRTE LARMKQEPVR TDDGRAMAVR
160 170 180 190
IQAYDYLECS AKTKEGVREV FETATRAALQ KRYGSQNGCI NCCKVL
Length:196
Mass (Da):22,123
Last modified:July 31, 1988 - v1
Checksum:iCCE6FD53AE00CD83
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06820 mRNA. Translation: CAA29968.1.
AF498971 mRNA. Translation: AAM21118.1.
CR542272 mRNA. Translation: CAG47068.1.
AK124398 mRNA. Translation: BAG54035.1.
AK312487 mRNA. Translation: BAG35389.1.
BT019546 mRNA. Translation: AAV38353.1.
BT019547 mRNA. Translation: AAV38354.1.
AC023137 Genomic DNA. Translation: AAY24345.1.
CH471053 Genomic DNA. Translation: EAX00819.1.
CH471053 Genomic DNA. Translation: EAX00820.1.
BC066954 mRNA. Translation: AAH66954.1.
M12174 mRNA. Translation: AAA36565.1.
BK001232 mRNA. Translation: DAA01138.1.
BK001671 Genomic DNA. Translation: DAA01912.1.
CCDSiCCDS1699.1.
PIRiA01372. TVHURH.
RefSeqiNP_004031.1. NM_004040.3.
UniGeneiHs.502876.

Genome annotation databases

EnsembliENST00000272233; ENSP00000272233; ENSG00000143878.
GeneIDi388.
KEGGihsa:388.
UCSCiuc002rdv.3. human.

Polymorphism databases

DMDMi51338601.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06820 mRNA. Translation: CAA29968.1.
AF498971 mRNA. Translation: AAM21118.1.
CR542272 mRNA. Translation: CAG47068.1.
AK124398 mRNA. Translation: BAG54035.1.
AK312487 mRNA. Translation: BAG35389.1.
BT019546 mRNA. Translation: AAV38353.1.
BT019547 mRNA. Translation: AAV38354.1.
AC023137 Genomic DNA. Translation: AAY24345.1.
CH471053 Genomic DNA. Translation: EAX00819.1.
CH471053 Genomic DNA. Translation: EAX00820.1.
BC066954 mRNA. Translation: AAH66954.1.
M12174 mRNA. Translation: AAA36565.1.
BK001232 mRNA. Translation: DAA01138.1.
BK001671 Genomic DNA. Translation: DAA01912.1.
CCDSiCCDS1699.1.
PIRiA01372. TVHURH.
RefSeqiNP_004031.1. NM_004040.3.
UniGeneiHs.502876.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FV8X-ray1.90A4-187[»]
ProteinModelPortaliP62745.
SMRiP62745. Positions 2-185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106881. 16 interactions.
IntActiP62745. 23 interactions.
MINTiMINT-4824810.
STRINGi9606.ENSP00000272233.

Chemistry

ChEMBLiCHEMBL1795102.
DrugBankiDB00083. Botulinum Toxin Type A.

PTM databases

PhosphoSiteiP62745.

Polymorphism databases

DMDMi51338601.

Proteomic databases

MaxQBiP62745.
PaxDbiP62745.
PeptideAtlasiP62745.
PRIDEiP62745.

Protocols and materials databases

DNASUi388.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272233; ENSP00000272233; ENSG00000143878.
GeneIDi388.
KEGGihsa:388.
UCSCiuc002rdv.3. human.

Organism-specific databases

CTDi388.
GeneCardsiGC02P020646.
HGNCiHGNC:668. RHOB.
HPAiCAB004560.
MIMi165370. gene.
neXtProtiNX_P62745.
PharmGKBiPA24950.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP62745.
KOiK07856.
OMAiVRINAFE.
OrthoDBiEOG73FQPD.
PhylomeDBiP62745.
TreeFamiTF300837.

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_1695. GPVI-mediated activation cascade.
REACT_18407. G alpha (12/13) signalling events.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
SignaLinkiP62745.

Miscellaneous databases

ChiTaRSiRHOB. human.
EvolutionaryTraceiP62745.
GeneWikiiRHOB.
GenomeRNAii388.
NextBioi1615.
PROiP62745.
SOURCEiSearch...

Gene expression databases

BgeeiP62745.
CleanExiHS_RHOB.
ExpressionAtlasiP62745. baseline and differential.
GenevestigatoriP62745.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Coding sequence of human rho cDNAs clone 6 and clone 9."
    Chardin P., Madaule P., Tavitian A.
    Nucleic Acids Res. 16:2717-2717(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Hippocampus.
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  9. Lubec G., Chen W.-Q., Sun Y.
    Submitted (NOV-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 8-27; 52-68; 105-118 AND 151-162, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  10. "A novel ras-related gene family."
    Madaule P., Axel R.
    Cell 41:31-40(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-196.
  11. "PRK1 is targeted to endosomes by the small GTPase, RhoB."
    Mellor H., Flynn P., Nobes C.D., Hall A., Parker P.J.
    J. Biol. Chem. 273:4811-4814(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PKN1.
  12. "Regulation of epidermal growth factor receptor traffic by the small GTPase rhoB."
    Gampel A., Parker P.J., Mellor H.
    Curr. Biol. 9:955-958(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF PHE-39.
  13. "Farnesyltransferase inhibitors disrupt EGF receptor traffic through modulation of the RhoB GTPase."
    Wherlock M., Gampel A., Futter C., Mellor H.
    J. Cell Sci. 117:3221-3231(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-14.
  14. "Ultrastructural localization of ras-related proteins using epitope-tagged plasmids."
    Robertson D., Paterson H.F., Adamson P., Hall A., Monaghan P.
    J. Histochem. Cytochem. 43:471-480(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  15. "Post-translational modifications of p21rho proteins."
    Adamson P., Marshall C.J., Hall A., Tilbrook P.A.
    J. Biol. Chem. 267:20033-20038(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-189 AND CYS-192, ISOPRENYLATION AT CYS-193, METHYLATION AT CYS-193, MUTAGENESIS OF CYS-189; CYS-192; CYS-193 AND LYS-194.
  16. "CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB."
    Armstrong S.A., Hannah V.C., Goldstein J.L., Brown M.S.
    J. Biol. Chem. 270:7864-7868(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-193, MUTAGENESIS OF CYS-192 AND CYS-193.
  17. "AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation."
    Diviani D., Soderling J., Scott J.D.
    J. Biol. Chem. 276:44247-44257(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AKAP13.
  18. "XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC."
    Arthur W.T., Ellerbroek S.M., Der C.J., Burridge K., Wennerberg K.
    J. Biol. Chem. 277:42964-42972(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGEF3.
  19. "Dissecting the role of Rho-mediated signaling in contractile ring formation."
    Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S., Miki T.
    Mol. Biol. Cell 17:43-55(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "The nuclear guanine nucleotide exchange factors Ect2 and Net1 regulate RhoB-mediated cell death after DNA damage."
    Srougi M.C., Burridge K.
    PLoS ONE 6:E17108-E17108(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.

Entry informationi

Entry nameiRHOB_HUMAN
AccessioniPrimary (citable) accession number: P62745
Secondary accession number(s): B2R692
, P01121, Q5U0H6, Q7RTN5, Q7RTR9, Q9CUV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 20, 1986
Last sequence update: July 31, 1988
Last modified: March 31, 2015
This is version 133 of the entry and version 1 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

Miscellaneous

RHOB is one of the targets of farnesyltransferase inhibitors which are currently under investigation as cancer therapeutics. These elevate the levels of geranylgeranylated RHOB and cause mislocalization, leading to apoptosis and antineoplastic effects.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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.