Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P35293

- RAB18_MOUSE

UniProt

P35293 - RAB18_MOUSE

Protein

Ras-related protein Rab-18

Gene

Rab18

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Plays a role in apical endocytosis/recycling. May be implicated in transport between the plasma membrane and early endosomes. Plays a key role in eye and brain development and neurodegeneration By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 239GTPBy similarity
    Nucleotide bindingi63 – 675GTPBy similarity
    Nucleotide bindingi122 – 1254GTPBy similarity
    Nucleotide bindingi151 – 1533GTPBy similarity

    GO - Molecular functioni

    1. GDP binding Source: UniProtKB
    2. GTP binding Source: UniProtKB-KW

    GO - Biological processi

    1. brain development Source: UniProtKB
    2. eye development Source: UniProtKB
    3. lipid particle organization Source: MGI
    4. protein transport Source: UniProtKB-KW
    5. small GTPase mediated signal transduction Source: InterPro

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Rab-18
    Gene namesi
    Name:Rab18
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:102790. Rab18.

    Subcellular locationi

    Apical cell membrane Curated; Lipid-anchor Curated. Basal cell membrane Curated; Lipid-anchor Curated
    Note: Highly enriched on apical endocytic structures in polarized epithelial cells of kidney proximal tubules. Detected on both the apical and basolateral domains in epithelial cells of the intestine.

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB-SubCell
    2. basal plasma membrane Source: UniProtKB-SubCell
    3. intracellular Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 203203Ras-related protein Rab-18PRO_0000121194Add
    BLAST
    Propeptidei204 – 2063Removed in mature formSequence AnalysisPRO_0000370762

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Lipidationi199 – 1991S-palmitoyl cysteineSequence Analysis
    Modified residuei203 – 2031Cysteine methyl esterSequence Analysis
    Lipidationi203 – 2031S-geranylgeranyl cysteineBy similarity

    Keywords - PTMi

    Acetylation, Lipoprotein, Methylation, Palmitate, Prenylation

    Proteomic databases

    MaxQBiP35293.
    PaxDbiP35293.
    PRIDEiP35293.

    PTM databases

    PhosphoSiteiP35293.

    Expressioni

    Tissue specificityi

    Expression is high in the brain, moderate in the pituitary, and low in the liver. Detected in all tissues.

    Gene expression databases

    ArrayExpressiP35293.
    BgeeiP35293.
    CleanExiMM_RAB18.
    GenevestigatoriP35293.

    Interactioni

    Protein-protein interaction databases

    BioGridi202536. 1 interaction.
    IntActiP35293. 1 interaction.
    MINTiMINT-1864434.

    Structurei

    3D structure databases

    ProteinModelPortaliP35293.
    SMRiP35293. Positions 2-178.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi37 – 459Effector regionBy similarity

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233968.
    HOVERGENiHBG009351.
    InParanoidiP35293.
    KOiK07910.
    OMAiTYTTRND.
    OrthoDBiEOG7CVQ04.
    PhylomeDBiP35293.
    TreeFamiTF313448.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR025662. Sigma_54_int_dom_ATP-bd_1.
    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.

    P35293-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDEDVLTTLK ILIIGESGVG KSSLLLRFTD DTFDPELAAT IGVDFKVKTI    50
    SVDGNKAKLA IWDTAGQERF RTLTPSYYRG AQGVILVYDV TRRDTFVKLD 100
    NWLNELETYC TRNDIVNMLV GNKIDKENRE VDRNEGLKFA RKHSMLFIEA 150
    SAKTCDGVQC AFEELVEKII QTPGLWESEN QNKGVKLSHR EESRGGGACG 200
    GYCSVL 206
    Length:206
    Mass (Da):23,035
    Last modified:October 1, 1996 - v2
    Checksum:iD1B0F48666999B77
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80333 mRNA. Translation: CAA56583.1.
    L04966 mRNA. Translation: AAC37632.1.
    AK045514 mRNA. Translation: BAC32402.1.
    AK140901 mRNA. Translation: BAE24512.1.
    AK143673 mRNA. Translation: BAE25489.1.
    AK146177 mRNA. Translation: BAE26955.1.
    AK146397 mRNA. Translation: BAE27140.1.
    AK154920 mRNA. Translation: BAE32926.1.
    BC056351 mRNA. Translation: AAH56351.1.
    M79308 mRNA. Translation: AAK14832.1.
    CCDSiCCDS29044.1.
    PIRiJN0874.
    RefSeqiNP_851415.1. NM_181070.6.
    UniGeneiMm.132802.

    Genome annotation databases

    EnsembliENSMUST00000097680; ENSMUSP00000095285; ENSMUSG00000073639.
    GeneIDi19330.
    KEGGimmu:19330.
    UCSCiuc008dzo.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80333 mRNA. Translation: CAA56583.1 .
    L04966 mRNA. Translation: AAC37632.1 .
    AK045514 mRNA. Translation: BAC32402.1 .
    AK140901 mRNA. Translation: BAE24512.1 .
    AK143673 mRNA. Translation: BAE25489.1 .
    AK146177 mRNA. Translation: BAE26955.1 .
    AK146397 mRNA. Translation: BAE27140.1 .
    AK154920 mRNA. Translation: BAE32926.1 .
    BC056351 mRNA. Translation: AAH56351.1 .
    M79308 mRNA. Translation: AAK14832.1 .
    CCDSi CCDS29044.1.
    PIRi JN0874.
    RefSeqi NP_851415.1. NM_181070.6.
    UniGenei Mm.132802.

    3D structure databases

    ProteinModelPortali P35293.
    SMRi P35293. Positions 2-178.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202536. 1 interaction.
    IntActi P35293. 1 interaction.
    MINTi MINT-1864434.

    PTM databases

    PhosphoSitei P35293.

    Proteomic databases

    MaxQBi P35293.
    PaxDbi P35293.
    PRIDEi P35293.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000097680 ; ENSMUSP00000095285 ; ENSMUSG00000073639 .
    GeneIDi 19330.
    KEGGi mmu:19330.
    UCSCi uc008dzo.1. mouse.

    Organism-specific databases

    CTDi 22931.
    MGIi MGI:102790. Rab18.

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233968.
    HOVERGENi HBG009351.
    InParanoidi P35293.
    KOi K07910.
    OMAi TYTTRND.
    OrthoDBi EOG7CVQ04.
    PhylomeDBi P35293.
    TreeFami TF313448.

    Miscellaneous databases

    NextBioi 296305.
    PROi P35293.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35293.
    Bgeei P35293.
    CleanExi MM_RAB18.
    Genevestigatori P35293.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR025662. Sigma_54_int_dom_ATP-bd_1.
    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. "Cloning and subcellular localization of novel rab proteins reveals polarized and cell type-specific expression."
      Luetcke A., Parton R.G., Murphy C., Olkkonen V.M., Dupree P., Valencia A., Simons K., Zerial M.
      J. Cell Sci. 107:3437-3448(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    2. "Gene cloning and characterization of a GTP-binding Rab protein from mouse pituitary AtT-20 cells."
      Yu H., Leaf D.S., Moore H.P.
      Gene 132:273-278(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: LAF1.
      Tissue: Pituitary.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J, DBA/2 and NOD.
      Tissue: Corpora quadrigemina, Head and Spleen.
    4. "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].
      Strain: C57BL/6.
      Tissue: Brain.
    5. "The complexity of the Rab and Rho GTP-binding protein subfamilies revealed by a PCR cloning approach."
      Chavrier P., Simons K., Zerial M.
      Gene 112:261-264(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-68.
      Tissue: Kidney.

    Entry informationi

    Entry nameiRAB18_MOUSE
    AccessioniPrimary (citable) accession number: P35293
    Secondary accession number(s): Q543V0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 131 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3