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Q14088

- RB33A_HUMAN

UniProt

Q14088 - RB33A_HUMAN

Protein

Ras-related protein Rab-33A

Gene

RAB33A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (01 May 1997)
      Previous versions | rss
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    Functioni

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi43 – 508GTPBy similarity
    Nucleotide bindingi91 – 955GTPBy similarity
    Nucleotide bindingi151 – 1544GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: ProtInc
    2. GTP binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. antigen processing and presentation Source: UniProt
    2. GTP catabolic process Source: GOC
    3. protein transport Source: InterPro
    4. small GTPase mediated signal transduction Source: InterPro

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Rab-33A
    Alternative name(s):
    Small GTP-binding protein S10
    Gene namesi
    Name:RAB33A
    Synonyms:RABS10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:9773. RAB33A.

    Subcellular locationi

    Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated

    GO - Cellular componenti

    1. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34124.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 237237Ras-related protein Rab-33APRO_0000121237Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi235 – 2351S-geranylgeranyl cysteineBy similarity
    Modified residuei237 – 2371Cysteine methyl esterBy similarity
    Lipidationi237 – 2371S-geranylgeranyl cysteineBy similarity

    Keywords - PTMi

    Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiQ14088.
    PaxDbiQ14088.
    PRIDEiQ14088.

    PTM databases

    PhosphoSiteiQ14088.

    Expressioni

    Tissue specificityi

    Expressed only in lymphoid cell lines.

    Gene expression databases

    BgeeiQ14088.
    CleanExiHS_RAB33A.
    GenevestigatoriQ14088.

    Organism-specific databases

    HPAiHPA059737.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Hoxa1P090223EBI-744685,EBI-3957603From a different organism.
    RABAC1Q9UI143EBI-744685,EBI-712367

    Protein-protein interaction databases

    BioGridi114764. 6 interactions.
    IntActiQ14088. 4 interactions.
    MINTiMINT-1455156.
    STRINGi9606.ENSP00000257017.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14088.
    SMRiQ14088. Positions 35-199.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233968.
    HOVERGENiHBG009351.
    InParanoidiQ14088.
    KOiK07919.
    OMAiFMSLACR.
    OrthoDBiEOG78PVB5.
    PhylomeDBiQ14088.
    TreeFamiTF300097.

    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.

    Q14088-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQPILGHGS LQPASAAGLA SLELDSSLDQ YVQIRIFKII VIGDSNVGKT    50
    CLTFRFCGGT FPDKTEATIG VDFREKTVEI EGEKIKVQVW DTAGQERFRK 100
    SMVEHYYRNV HAVVFVYDVT KMTSFTNLKM WIQECNGHAV PPLVPKVLVG 150
    NKCDLREQIQ VPSNLALKFA DAHNMLLFET SAKDPKESQN VESIFMCLAC 200
    RLKAQKSLLY RDAERQQGKV QKLEFPQEAN SKTSCPC 237
    Length:237
    Mass (Da):26,593
    Last modified:May 1, 1997 - v2
    Checksum:i2EE23B8237225F4A
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti102 – 1021M → T.
    VAR_006849

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14889 mRNA. Translation: BAA03606.1.
    AF498959 mRNA. Translation: AAM21107.1.
    BT007038 mRNA. Translation: AAP35687.1.
    AL139234 Genomic DNA. Translation: CAI42781.1.
    BC001157 mRNA. Translation: AAH01157.1.
    BC009996 mRNA. Translation: AAH09996.1.
    CCDSiCCDS14621.1.
    PIRiS35058.
    RefSeqiNP_004785.1. NM_004794.2.
    UniGeneiHs.654356.

    Genome annotation databases

    EnsembliENST00000257017; ENSP00000257017; ENSG00000134594.
    GeneIDi9363.
    KEGGihsa:9363.
    UCSCiuc004evl.3. human.

    Polymorphism databases

    DMDMi2500071.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14889 mRNA. Translation: BAA03606.1 .
    AF498959 mRNA. Translation: AAM21107.1 .
    BT007038 mRNA. Translation: AAP35687.1 .
    AL139234 Genomic DNA. Translation: CAI42781.1 .
    BC001157 mRNA. Translation: AAH01157.1 .
    BC009996 mRNA. Translation: AAH09996.1 .
    CCDSi CCDS14621.1.
    PIRi S35058.
    RefSeqi NP_004785.1. NM_004794.2.
    UniGenei Hs.654356.

    3D structure databases

    ProteinModelPortali Q14088.
    SMRi Q14088. Positions 35-199.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114764. 6 interactions.
    IntActi Q14088. 4 interactions.
    MINTi MINT-1455156.
    STRINGi 9606.ENSP00000257017.

    PTM databases

    PhosphoSitei Q14088.

    Polymorphism databases

    DMDMi 2500071.

    Proteomic databases

    MaxQBi Q14088.
    PaxDbi Q14088.
    PRIDEi Q14088.

    Protocols and materials databases

    DNASUi 9363.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257017 ; ENSP00000257017 ; ENSG00000134594 .
    GeneIDi 9363.
    KEGGi hsa:9363.
    UCSCi uc004evl.3. human.

    Organism-specific databases

    CTDi 9363.
    GeneCardsi GC0XP129305.
    HGNCi HGNC:9773. RAB33A.
    HPAi HPA059737.
    MIMi 300333. gene.
    neXtProti NX_Q14088.
    PharmGKBi PA34124.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233968.
    HOVERGENi HBG009351.
    InParanoidi Q14088.
    KOi K07919.
    OMAi FMSLACR.
    OrthoDBi EOG78PVB5.
    PhylomeDBi Q14088.
    TreeFami TF300097.

    Miscellaneous databases

    GeneWikii RAB33A.
    GenomeRNAii 9363.
    NextBioi 35063.
    PROi Q14088.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q14088.
    CleanExi HS_RAB33A.
    Genevestigatori Q14088.

    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. "Molecular cloning of a cDNA encoding a novel small GTP-binding protein."
      Koda T., Kakinuma M.
      FEBS Lett. 328:21-24(1993) [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-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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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.

    Entry informationi

    Entry nameiRB33A_HUMAN
    AccessioniPrimary (citable) accession number: Q14088
    Secondary accession number(s): Q5JUZ6, Q92465
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 134 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, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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