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P62745

- RHOB_HUMAN

UniProt

P62745 - RHOB_HUMAN

Protein

Rho-related GTP-binding protein RhoB

Gene

RHOB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    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
    4. protein binding Source: IntAct

    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. GTP catabolic process Source: GOC
    11. negative regulation of cell cycle Source: UniProtKB
    12. platelet activation Source: Reactome
    13. positive regulation of angiogenesis Source: UniProtKB
    14. positive regulation of apoptotic process Source: UniProtKB
    15. protein transport Source: UniProtKB-KW
    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

    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: 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. endosome membrane Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. late endosome membrane Source: UniProtKB-SubCell
    6. nucleus Source: UniProtKB
    7. plasma membrane Source: UniProtKB

    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

    ArrayExpressiP62745.
    BgeeiP62745.
    CleanExiHS_RHOB.
    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
    TNFAIP1Q138295EBI-602647,EBI-2505861

    Protein-protein interaction databases

    BioGridi106881. 13 interactions.
    IntActiP62745. 22 interactions.
    MINTiMINT-4824810.
    STRINGi9606.ENSP00000272233.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000233974.
    HOVERGENiHBG009351.
    InParanoidiP62745.
    KOiK07856.
    OMAiVWEVFET.
    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

    MAAIRKKLVV VGDGACGKTC LLIVFSKDEF PEVYVPTVFE NYVADIEVDG    50
    KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSVDSPD SLENIPEKWV 100
    PEVKHFCPNV PIILVANKKD LRSDEHVRTE LARMKQEPVR TDDGRAMAVR 150
    IQAYDYLECS AKTKEGVREV FETATRAALQ KRYGSQNGCI NCCKVL 196
    Length:196
    Mass (Da):22,123
    Last modified:August 1, 1988 - v1
    Checksum:iCCE6FD53AE00CD83
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_004040.2.
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS1699.1.
    PIRi A01372. TVHURH.
    RefSeqi NP_004031.1. NM_004040.2.
    UniGenei Hs.502876.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FV8 X-ray 1.90 A 4-187 [» ]
    ProteinModelPortali P62745.
    SMRi P62745. Positions 2-185.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106881. 13 interactions.
    IntActi P62745. 22 interactions.
    MINTi MINT-4824810.
    STRINGi 9606.ENSP00000272233.

    Chemistry

    ChEMBLi CHEMBL1795102.

    PTM databases

    PhosphoSitei P62745.

    Polymorphism databases

    DMDMi 51338601.

    Proteomic databases

    MaxQBi P62745.
    PaxDbi P62745.
    PeptideAtlasi P62745.
    PRIDEi P62745.

    Protocols and materials databases

    DNASUi 388.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000272233 ; ENSP00000272233 ; ENSG00000143878 .
    GeneIDi 388.
    KEGGi hsa:388.
    UCSCi uc002rdv.3. human.

    Organism-specific databases

    CTDi 388.
    GeneCardsi GC02P020568.
    HGNCi HGNC:668. RHOB.
    HPAi CAB004560.
    MIMi 165370. gene.
    neXtProti NX_P62745.
    PharmGKBi PA24950.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233974.
    HOVERGENi HBG009351.
    InParanoidi P62745.
    KOi K07856.
    OMAi VWEVFET.
    OrthoDBi EOG73FQPD.
    PhylomeDBi P62745.
    TreeFami TF300837.

    Enzyme and pathway databases

    Reactomei REACT_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.
    SignaLinki P62745.

    Miscellaneous databases

    ChiTaRSi RHOB. human.
    EvolutionaryTracei P62745.
    GeneWikii RHOB.
    GenomeRNAii 388.
    NextBioi 1615.
    PROi P62745.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62745.
    Bgeei P62745.
    CleanExi HS_RHOB.
    Genevestigatori P62745.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003578. Small_GTPase_Rho.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00174. RHO. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51420. RHO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Coding sequence of human rho cDNAs clone 6 and clone 9."
      Chardin P., Madaule P., Tavitian A.
      Nucleic Acids Res. 16:2717-2717(1988) [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 (APR-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 (JUN-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(2004) [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 (OCT-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(2005) [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(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    9. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-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(1985) [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(1998) [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(1999) [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(2004) [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(1995) [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(1992) [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(1995) [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(2001) [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(2002) [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(2006) [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(2011) [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 21, 1986
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 128 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