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P36405

- ARL3_HUMAN

UniProt

P36405 - ARL3_HUMAN

Protein

ADP-ribosylation factor-like protein 3

Gene

ARL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). Required for normal cytokinesis and cilia signaling. Requires assistance from GTPase-activating proteins (GAPs) like RP2 and PDE6D, in order to cycle between inactive GDP-bound and active GTP-bound forms. Required for targeting proteins such as NPHP3 to the ciliary membrane by releasing myristoylated NPHP3 from UNC119B cargo adapter into the cilium. Does not act as an allosteric activator of the cholera toxin catalytic subunit.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi31 – 311MagnesiumBy similarity
    Metal bindingi48 – 481MagnesiumBy similarity
    Binding sitei48 – 481GTPBy similarity
    Binding sitei70 – 701GTP; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi24 – 318GTPBy similarity
    Nucleotide bindingi67 – 715GTPBy similarity
    Nucleotide bindingi126 – 1294GTPBy similarity
    Nucleotide bindingi159 – 1613GTPBy similarity

    GO - Molecular functioni

    1. GDP binding Source: UniProtKB
    2. GTPase activity Source: Ensembl
    3. GTP binding Source: UniProtKB
    4. metal ion binding Source: UniProtKB-KW
    5. microtubule binding Source: UniProtKB
    6. protein binding Source: UniProtKB

    GO - Biological processi

    1. cilium morphogenesis Source: UniProtKB
    2. cytokinesis Source: UniProtKB
    3. intraciliary transport Source: Ensembl
    4. kidney development Source: UniProtKB
    5. photoreceptor cell development Source: UniProtKB
    6. post-Golgi vesicle-mediated transport Source: MGI
    7. protein transport Source: UniProtKB-KW
    8. small GTPase mediated signal transduction Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ADP-ribosylation factor-like protein 3
    Gene namesi
    Name:ARL3
    Synonyms:ARFL3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:694. ARL3.

    Subcellular locationi

    Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeletonspindle. Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasm. Cell projectioncilium
    Note: Detected predominantly in the photoreceptor connecting cilium. Present on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasmic microtubule Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. Golgi apparatus Source: UniProtKB
    5. Golgi membrane Source: UniProtKB-SubCell
    6. midbody Source: UniProtKB
    7. nucleus Source: UniProtKB
    8. photoreceptor connecting cilium Source: UniProtKB
    9. primary cilium Source: UniProtKB
    10. spindle microtubule Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi31 – 311T → N: Enhances the interaction with RP2. 2 Publications
    Mutagenesisi71 – 711Q → L: Enhances the interaction with RP2. Does not induce a mitotic arrest resulting from the loss of the microtubule-based mitotic spindle. Induces release of myristoylated proteins from UNC119. Interacts with ARL2BP, GOLGA4, PDE6D and UNC119. 4 Publications

    Organism-specific databases

    PharmGKBiPA24987.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedSequence Analysis
    Chaini2 – 182181ADP-ribosylation factor-like protein 3PRO_0000207456Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineSequence Analysis
    Modified residuei5 – 51Phosphoserine1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein

    Proteomic databases

    MaxQBiP36405.
    PaxDbiP36405.
    PeptideAtlasiP36405.
    PRIDEiP36405.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00003327.
    UCD-2DPAGEP36405.

    PTM databases

    PhosphoSiteiP36405.

    Expressioni

    Tissue specificityi

    Expressed in the retina. Strongly expressed in connecting cilium, the myoid region of the inner segments (IS) and in cone photoreceptors (at protein level).1 Publication

    Gene expression databases

    BgeeiP36405.
    CleanExiHS_ARL3.
    GenevestigatoriP36405.

    Organism-specific databases

    HPAiHPA036292.

    Interactioni

    Subunit structurei

    Interacts with RP2. The GTP-bound form interacts with PDE6D. Found in a complex with ARL3, RP2 and UNC119 (or UNC119B); RP2 induces hydrolysis of GTP ARL3 in the complex, leading to the release of UNC119 (or UNC119B). Interacts with SYS1. The GTP-bound form interacts with ARL2BP and PDE6D. Interacts with RP2; interaction is direct and stimulated with the activated GTP-bound form of ARL3. Microtubule-associated protein. Does not interact with TBCC. May interact with GOLGA4.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PDE6DO439242EBI-712710,EBI-712685
    UNC119Q134325EBI-712710,EBI-711260

    Protein-protein interaction databases

    BioGridi106896. 11 interactions.
    IntActiP36405. 10 interactions.
    MINTiMINT-1368863.
    STRINGi9606.ENSP00000260746.

    Structurei

    3D structure databases

    ProteinModelPortaliP36405.
    SMRiP36405. Positions 2-177.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Arf family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000163691.
    HOVERGENiHBG002073.
    InParanoidiP36405.
    KOiK07944.
    OMAiLECEEFQ.
    OrthoDBiEOG7M98HG.
    PhylomeDBiP36405.
    TreeFamiTF105463.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR024156. Small_GTPase_ARF.
    IPR006689. Small_GTPase_ARF/SAR.
    [Graphical view]
    PfamiPF00025. Arf. 1 hit.
    [Graphical view]
    PRINTSiPR00328. SAR1GTPBP.
    SMARTiSM00177. ARF. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51417. ARF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P36405-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLLSILRKL KSAPDQEVRI LLLGLDNAGK TTLLKQLASE DISHITPTQG    50
    FNIKSVQSQG FKLNVWDIGG QRKIRPYWKN YFENTDILIY VIDSADRKRF 100
    EETGQELAEL LEEEKLSCVP VLIFANKQDL LTAAPASEIA EGLNLHTIRD 150
    RVWQIQSCSA LTGEGVQDGM NWVCKNVNAK KK 182
    Length:182
    Mass (Da):20,456
    Last modified:February 1, 1995 - v2
    Checksum:iE5C1ACAD0BD55537
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti34 – 341L → M.1 Publication
    Corresponds to variant rs1141895 [ dbSNP | Ensembl ].
    VAR_014869

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07151 mRNA. Translation: AAA21654.1.
    AF493889 mRNA. Translation: AAM12603.1.
    AK312525 mRNA. Translation: BAG35424.1.
    CR407637 mRNA. Translation: CAG28565.1.
    AL391121 Genomic DNA. Translation: CAI40862.1.
    BC009841 mRNA. Translation: AAH09841.1.
    CCDSiCCDS7538.1.
    PIRiA54869.
    RefSeqiNP_004302.1. NM_004311.3.
    UniGeneiHs.182215.

    Genome annotation databases

    EnsembliENST00000260746; ENSP00000260746; ENSG00000138175.
    GeneIDi403.
    KEGGihsa:403.
    UCSCiuc001kwa.3. human.

    Polymorphism databases

    DMDMi543851.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07151 mRNA. Translation: AAA21654.1 .
    AF493889 mRNA. Translation: AAM12603.1 .
    AK312525 mRNA. Translation: BAG35424.1 .
    CR407637 mRNA. Translation: CAG28565.1 .
    AL391121 Genomic DNA. Translation: CAI40862.1 .
    BC009841 mRNA. Translation: AAH09841.1 .
    CCDSi CCDS7538.1.
    PIRi A54869.
    RefSeqi NP_004302.1. NM_004311.3.
    UniGenei Hs.182215.

    3D structure databases

    ProteinModelPortali P36405.
    SMRi P36405. Positions 2-177.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106896. 11 interactions.
    IntActi P36405. 10 interactions.
    MINTi MINT-1368863.
    STRINGi 9606.ENSP00000260746.

    PTM databases

    PhosphoSitei P36405.

    Polymorphism databases

    DMDMi 543851.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00003327.
    UCD-2DPAGE P36405.

    Proteomic databases

    MaxQBi P36405.
    PaxDbi P36405.
    PeptideAtlasi P36405.
    PRIDEi P36405.

    Protocols and materials databases

    DNASUi 403.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260746 ; ENSP00000260746 ; ENSG00000138175 .
    GeneIDi 403.
    KEGGi hsa:403.
    UCSCi uc001kwa.3. human.

    Organism-specific databases

    CTDi 403.
    GeneCardsi GC10M104423.
    HGNCi HGNC:694. ARL3.
    HPAi HPA036292.
    MIMi 604695. gene.
    neXtProti NX_P36405.
    PharmGKBi PA24987.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000163691.
    HOVERGENi HBG002073.
    InParanoidi P36405.
    KOi K07944.
    OMAi LECEEFQ.
    OrthoDBi EOG7M98HG.
    PhylomeDBi P36405.
    TreeFami TF105463.

    Miscellaneous databases

    GeneWikii ARL3.
    GenomeRNAii 403.
    NextBioi 1689.
    PROi P36405.
    SOURCEi Search...

    Gene expression databases

    Bgeei P36405.
    CleanExi HS_ARL3.
    Genevestigatori P36405.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR024156. Small_GTPase_ARF.
    IPR006689. Small_GTPase_ARF/SAR.
    [Graphical view ]
    Pfami PF00025. Arf. 1 hit.
    [Graphical view ]
    PRINTSi PR00328. SAR1GTPBP.
    SMARTi SM00177. ARF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51417. ARF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ADP-ribosylation factor (ARF)-like 3, a new member of the ARF family of GTP-binding proteins cloned from human and rat tissues."
      Cavenagh M.A., Breiner M., Schurmann A., Rosenwald A.G., Terui T., Zhang C.-J., Randoazzo P.A., Adams M., Joost H.-G., Kahn R.A.
      J. Biol. Chem. 269:18937-18942(1994) [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. "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: Thalamus.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-34.
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Skin.
    7. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 80-97 AND 128-149, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    8. "ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin."
      Bhamidipati A., Lewis S.A., Cowan N.J.
      J. Cell Biol. 149:1087-1096(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ABSENCE OF INTERACTION WITH TBCC.
    9. "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1-binding proteins."
      Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.
      J. Biol. Chem. 276:22826-22837(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARL2BP; GOLGA4; PDE6D AND UNC119, MUTAGENESIS OF GLN-71.
    10. "Localization in the human retina of the X-linked retinitis pigmentosa protein RP2, its homologue cofactor C and the RP2 interacting protein Arl3."
      Grayson C., Bartolini F., Chapple J.P., Willison K.R., Bhamidipati A., Lewis S.A., Luthert P.J., Hardcastle A.J., Cowan N.J., Cheetham M.E.
      Hum. Mol. Genet. 11:3065-3074(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH MICROTUBULES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    11. "Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C."
      Bartolini F., Bhamidipati A., Thomas S., Schwahn U., Lewis S.A., Cowan N.J.
      J. Biol. Chem. 277:14629-14634(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RP2 AND ARL2BP, MUTAGENESIS OF THR-31 AND GLN-71.
    12. "Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p."
      Behnia R., Panic B., Whyte J.R.C., Munro S.
      Nat. Cell Biol. 6:405-413(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SYS1, SUBCELLULAR LOCATION.
    13. "Arl2 and Arl3 regulate different microtubule-dependent processes."
      Zhou C., Cunningham L., Marcus A.I., Li Y., Kahn R.A.
      Mol. Biol. Cell 17:2476-2487(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLN-71, SUBCELLULAR LOCATION.
    14. "Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3."
      Kuehnel K., Veltel S., Schlichting I., Wittinghofer A.
      Structure 14:367-378(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RP2.
    15. "Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3-effector-GAP complex."
      Veltel S., Kravchenko A., Ismail S., Wittinghofer A.
      FEBS Lett. 582:2501-2507(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, GTP/GDP BINDING, IDENTIFICATION IN A COMPLEX WITH UNC119 AND RP2, SUBCELLULAR LOCATION.
    16. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: FUNCTION, MUTAGENESIS OF THR-31 AND GLN-71.

    Entry informationi

    Entry nameiARL3_HUMAN
    AccessioniPrimary (citable) accession number: P36405
    Secondary accession number(s): B2R6C7, Q53X83, Q5JSM2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 145 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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