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Q9ULC3

- RAB23_HUMAN

UniProt

Q9ULC3 - RAB23_HUMAN

Protein

Ras-related protein Rab-23

Gene

RAB23

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Together with SUFU, prevents nuclear import of GLI1, and thereby inhibits GLI1 transcription factor activity. Regulates GLI1 in differentiating chondrocytes. Likewise, regulates GLI3 proteolytic processing and modulates GLI2 and GLI3 transcription factor activity. Plays a role in autophagic vacuole assembly, and mediates defense against pathogens, such as S.aureus, by promoting their capture by autophagosomes that then merge with lysosomes.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi16 – 238GTPBy similarity
    Nucleotide bindingi64 – 685GTPBy similarity
    Nucleotide bindingi121 – 1244GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: UniProtKB
    2. GTP binding Source: UniProtKB-KW

    GO - Biological processi

    1. autophagic vacuole assembly Source: UniProtKB
    2. cellular defense response Source: UniProtKB
    3. craniofacial suture morphogenesis Source: UniProtKB
    4. embryonic digit morphogenesis Source: Ensembl
    5. GTP catabolic process Source: UniProtKB
    6. negative regulation of proteolysis Source: Ensembl
    7. negative regulation of transcription factor import into nucleus Source: UniProtKB
    8. protein transport Source: UniProtKB-KW
    9. regulation of smoothened signaling pathway Source: Ensembl
    10. small GTPase mediated signal transduction Source: InterPro
    11. spinal cord dorsal/ventral patterning Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ9ULC3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Rab-23
    Gene namesi
    Name:RAB23
    ORF Names:HSPC137
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:14263. RAB23.

    Subcellular locationi

    Cell membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Cell membrane. Cytoplasm. Cytoplasmic vesicleautophagosome. Endosome membrane By similarity. Cytoplasmic vesiclephagosome. Cytoplasmic vesiclephagosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
    Note: Recruited to phagosomes containing S.aureus or M.tuberculosis.

    GO - Cellular componenti

    1. autophagic vacuole Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. endosome membrane Source: UniProtKB-SubCell
    4. extracellular vesicular exosome Source: UniProt
    5. phagocytic vesicle Source: UniProtKB
    6. phagocytic vesicle membrane Source: UniProtKB-SubCell
    7. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Carpenter syndrome 1 (CRPT1) [MIM:201000]: A rare autosomal recessive disorder characterized by acrocephaly with variable synostosis of the sagittal, lambdoid, and coronal sutures; peculiar facies; brachydactyly of the hands with syndactyly; preaxial polydactyly and syndactyly of the feet; congenital heart defects; growth retardation; mental retardation; hypogenitalism; and obesity. In addition, cerebral malformations, oral and dental abnormalities, coxa valga, genu valgum, hydronephrosis, precocious puberty, and hearing loss may be observed.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121M → K in CRPT1. 1 Publication
    VAR_065294
    Natural varianti79 – 791Missing in CRPT1. 1 Publication
    VAR_065295
    Natural varianti85 – 851C → R in CRPT1. 1 Publication
    VAR_034902

    Keywords - Diseasei

    Craniosynostosis, Disease mutation

    Organism-specific databases

    MIMi201000. phenotype.
    Orphaneti65759. Carpenter syndrome.
    PharmGKBiPA34113.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 234234Ras-related protein Rab-23PRO_0000121211Add
    BLAST
    Propeptidei235 – 2373Removed in mature formSequence AnalysisPRO_0000370771

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei234 – 2341Cysteine methyl esterSequence Analysis
    Lipidationi234 – 2341S-geranylgeranyl cysteineBy similarity

    Keywords - PTMi

    Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiQ9ULC3.
    PaxDbiQ9ULC3.
    PRIDEiQ9ULC3.

    PTM databases

    PhosphoSiteiQ9ULC3.

    Expressioni

    Gene expression databases

    BgeeiQ9ULC3.
    CleanExiHS_RAB23.
    GenevestigatoriQ9ULC3.

    Organism-specific databases

    HPAiHPA029135.
    HPA029136.

    Interactioni

    Subunit structurei

    Interacts with SUFU.1 Publication

    Protein-protein interaction databases

    BioGridi119694. 3 interactions.
    IntActiQ9ULC3. 3 interactions.
    MINTiMINT-6783510.
    STRINGi9606.ENSP00000320413.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ULC3.
    SMRiQ9ULC3. Positions 8-171.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi38 – 469Effector regionBy similarity

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233968.
    HOVERGENiHBG100144.
    InParanoidiQ9ULC3.
    KOiK06234.
    OMAiVTEVFKY.
    OrthoDBiEOG72C51B.
    PhylomeDBiQ9ULC3.
    TreeFamiTF317494.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003579. Small_GTPase_Rab_type.
    [Graphical view]
    PfamiPF00071. Ras. 1 hit.
    [Graphical view]
    PRINTSiPR00449. RASTRNSFRMNG.
    SMARTiSM00175. RAB. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51419. RAB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9ULC3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLEEDMEVAI KMVVVGNGAV GKSSMIQRYC KGIFTKDYKK TIGVDFLERQ    50
    IQVNDEDVRL MLWDTAGQEE FDAITKAYYR GAQACVLVFS TTDRESFEAV 100
    SSWREKVVAE VGDIPTVLVQ NKIDLLDDSC IKNEEAEALA KRLKLRFYRT 150
    SVKEDLNVNE VFKYLAEKYL QKLKQQIAED PELTHSSSNK IGVFNTSGGS 200
    HSGQNSGTLN GGDVINLRPN KQRTKKNRNP FSSCSIP 237
    Length:237
    Mass (Da):26,659
    Last modified:May 1, 2000 - v1
    Checksum:iB9CB96E94DDF6036
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti95 – 951E → G in AAF29101. (PubMed:11042152)Curated
    Sequence conflicti144 – 1441K → R in AAF29101. (PubMed:11042152)Curated
    Sequence conflicti225 – 2251K → N in AAF29101. (PubMed:11042152)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121M → K in CRPT1. 1 Publication
    VAR_065294
    Natural varianti13 – 131Missing.1 Publication
    VAR_034900
    Natural varianti40 – 401K → R.1 Publication
    Corresponds to variant rs45442500 [ dbSNP | Ensembl ].
    VAR_034901
    Natural varianti79 – 791Missing in CRPT1. 1 Publication
    VAR_065295
    Natural varianti85 – 851C → R in CRPT1. 1 Publication
    VAR_034902
    Natural varianti101 – 1011S → A.1 Publication
    Corresponds to variant rs45479896 [ dbSNP | Ensembl ].
    VAR_034903
    Natural varianti207 – 2071G → S.2 Publications
    Corresponds to variant rs1040461 [ dbSNP | Ensembl ].
    VAR_017159

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB034244 mRNA. Translation: BAA87324.1.
    AB025427 mRNA. Translation: BAB40309.1.
    AF161486 mRNA. Translation: AAF29101.1.
    AF498951 mRNA. Translation: AAM21099.1.
    AK313796 mRNA. Translation: BAG36532.1.
    AY585189 mRNA. Translation: AAT79492.1.
    CR749371 mRNA. Translation: CAH18224.1.
    AL031321 Genomic DNA. Translation: CAI21564.1.
    CH471081 Genomic DNA. Translation: EAX04476.1.
    BC015021 mRNA. Translation: AAH15021.1.
    CCDSiCCDS4962.1.
    RefSeqiNP_001265595.1. NM_001278666.1.
    NP_001265596.1. NM_001278667.1.
    NP_001265597.1. NM_001278668.1.
    NP_057361.3. NM_016277.4.
    NP_899050.1. NM_183227.2.
    UniGeneiHs.555016.

    Genome annotation databases

    EnsembliENST00000317483; ENSP00000320413; ENSG00000112210.
    ENST00000468148; ENSP00000417610; ENSG00000112210.
    GeneIDi51715.
    KEGGihsa:51715.
    UCSCiuc003pds.3. human.

    Polymorphism databases

    DMDMi12643897.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB034244 mRNA. Translation: BAA87324.1 .
    AB025427 mRNA. Translation: BAB40309.1 .
    AF161486 mRNA. Translation: AAF29101.1 .
    AF498951 mRNA. Translation: AAM21099.1 .
    AK313796 mRNA. Translation: BAG36532.1 .
    AY585189 mRNA. Translation: AAT79492.1 .
    CR749371 mRNA. Translation: CAH18224.1 .
    AL031321 Genomic DNA. Translation: CAI21564.1 .
    CH471081 Genomic DNA. Translation: EAX04476.1 .
    BC015021 mRNA. Translation: AAH15021.1 .
    CCDSi CCDS4962.1.
    RefSeqi NP_001265595.1. NM_001278666.1.
    NP_001265596.1. NM_001278667.1.
    NP_001265597.1. NM_001278668.1.
    NP_057361.3. NM_016277.4.
    NP_899050.1. NM_183227.2.
    UniGenei Hs.555016.

    3D structure databases

    ProteinModelPortali Q9ULC3.
    SMRi Q9ULC3. Positions 8-171.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119694. 3 interactions.
    IntActi Q9ULC3. 3 interactions.
    MINTi MINT-6783510.
    STRINGi 9606.ENSP00000320413.

    PTM databases

    PhosphoSitei Q9ULC3.

    Polymorphism databases

    DMDMi 12643897.

    Proteomic databases

    MaxQBi Q9ULC3.
    PaxDbi Q9ULC3.
    PRIDEi Q9ULC3.

    Protocols and materials databases

    DNASUi 51715.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000317483 ; ENSP00000320413 ; ENSG00000112210 .
    ENST00000468148 ; ENSP00000417610 ; ENSG00000112210 .
    GeneIDi 51715.
    KEGGi hsa:51715.
    UCSCi uc003pds.3. human.

    Organism-specific databases

    CTDi 51715.
    GeneCardsi GC06M057100.
    HGNCi HGNC:14263. RAB23.
    HPAi HPA029135.
    HPA029136.
    MIMi 201000. phenotype.
    606144. gene.
    neXtProti NX_Q9ULC3.
    Orphaneti 65759. Carpenter syndrome.
    PharmGKBi PA34113.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233968.
    HOVERGENi HBG100144.
    InParanoidi Q9ULC3.
    KOi K06234.
    OMAi VTEVFKY.
    OrthoDBi EOG72C51B.
    PhylomeDBi Q9ULC3.
    TreeFami TF317494.

    Enzyme and pathway databases

    SignaLinki Q9ULC3.

    Miscellaneous databases

    GeneWikii RAB23.
    GenomeRNAii 51715.
    NextBioi 55759.
    PROi Q9ULC3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9ULC3.
    CleanExi HS_RAB23.
    Genevestigatori Q9ULC3.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003579. Small_GTPase_Rab_type.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00175. RAB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51419. RAB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human mRNA for RAB23 protein."
      Seki N., Yoshikawa T., Azuma T., Saito T., Muramatsu M.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal brain.
    2. "Expression of RAB-23 in human hair follicle."
      Ikeda A., Yamashita M.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Hair follicle.
    3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Umbilical cord blood.
    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], VARIANT SER-207.
    5. "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-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-207.
      Tissue: Brain.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon carcinoma.
    7. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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: Uterus.
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes."
      Seto S., Tsujimura K., Koide Y.
      Traffic 12:407-420(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "The small GTPases Rab9A and Rab23 function at distinct steps in autophagy during group A Streptococcus infection."
      Nozawa T., Aikawa C., Goda A., Maruyama F., Hamada S., Nakagawa I.
      Cell. Microbiol. 14:1149-1165(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Rab23 negatively regulates Gli1 transcriptional factor in a Su(Fu)-dependent manner."
      Chi S., Xie G., Liu H., Chen K., Zhang X., Li C., Xie J.
      Cell. Signal. 24:1222-1228(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUFU, FUNCTION, GTPASE ACTIVITY, SUBCELLULAR LOCATION.
    16. Cited for: VARIANTS VAL-13 DEL; ARG-40 AND ALA-101, VARIANT CRPT1 ARG-85.
    17. "Carpenter syndrome: extended RAB23 mutation spectrum and analysis of nonsense-mediated mRNA decay."
      Jenkins D., Baynam G., De Catte L., Elcioglu N., Gabbett M.T., Hudgins L., Hurst J.A., Jehee F.S., Oley C., Wilkie A.O.
      Hum. Mutat. 32:E2069-E2078(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CRPT1 LYS-12 AND TYR-79 DEL.

    Entry informationi

    Entry nameiRAB23_HUMAN
    AccessioniPrimary (citable) accession number: Q9ULC3
    Secondary accession number(s): B2R9I5
    , Q68DJ6, Q8NI06, Q9P023
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 138 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3