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Q6IQ22

- RAB12_HUMAN

UniProt

Q6IQ22 - RAB12_HUMAN

Protein

Ras-related protein Rab-12

Gene

RAB12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 3 (09 Jan 2007)
      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. That Rab may play a role in protein transport from recycling endosomes to lysosomes regulating, for instance, the degradation of the transferrin receptor. Involved in autophagy By similarity.By similarity

    Enzyme regulationi

    Rab activation is generally mediated by a guanine exchange factor (GEF), while inactivation through hydrolysis of bound GTP is catalyzed by a GTPase activating protein (GAP) By similarity. That Rab is activated by DENND3, a guanine exchange factor.By similarity1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi49 – 579GTP
    Nucleotide bindingi97 – 1015GTPBy similarity
    Nucleotide bindingi155 – 1595GTP
    Nucleotide bindingi187 – 1882GTP

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular protein catabolic process Source: UniProtKB
    2. endosome to lysosome transport Source: UniProtKB
    3. protein transport Source: UniProtKB-KW
    4. small GTPase mediated signal transduction Source: InterPro

    Keywords - Biological processi

    Autophagy, Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Rab-12
    Gene namesi
    Name:RAB12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:31332. RAB12.

    Subcellular locationi

    Recycling endosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Lysosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Golgi apparatus membrane By similarity. Cytoplasmic vesicleautophagosome By similarity

    GO - Cellular componenti

    1. Golgi membrane Source: UniProtKB-SubCell
    2. lysosomal membrane Source: UniProtKB-SubCell
    3. lysosome Source: UniProtKB
    4. recycling endosome membrane Source: UniProtKB
    5. secretory granule Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Endosome, Golgi apparatus, Lysosome, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671102.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 244244Ras-related protein Rab-12PRO_0000271377Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei21 – 211PhosphoserineBy similarity
    Modified residuei106 – 1061PhosphoserineBy similarity
    Lipidationi243 – 2431S-geranylgeranyl cysteineBy similarity
    Lipidationi244 – 2441S-geranylgeranyl cysteineBy similarity

    Keywords - PTMi

    Acetylation, Lipoprotein, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiQ6IQ22.
    PaxDbiQ6IQ22.
    PRIDEiQ6IQ22.

    PTM databases

    PhosphoSiteiQ6IQ22.

    Expressioni

    Gene expression databases

    BgeeiQ6IQ22.
    CleanExiHS_RAB12.
    GenevestigatoriQ6IQ22.

    Organism-specific databases

    HPAiHPA040727.

    Interactioni

    Subunit structurei

    Interacts with RABIF and OPTN.2 Publications

    Protein-protein interaction databases

    BioGridi128387. 4 interactions.
    STRINGi9606.ENSP00000331748.

    Structurei

    Secondary structure

    1
    244
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 489
    Helixi55 – 628
    Beta strandi77 – 8610
    Beta strandi89 – 9810
    Helixi102 – 1043
    Helixi105 – 11410
    Beta strandi116 – 1238
    Helixi127 – 1315
    Helixi133 – 14311
    Beta strandi149 – 1557
    Helixi157 – 1626
    Helixi167 – 1759
    Beta strandi181 – 1844
    Turni187 – 1904
    Helixi193 – 20614

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IL1X-ray2.10A36-208[»]
    ProteinModelPortaliQ6IQ22.
    SMRiQ6IQ22. Positions 38-208.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6IQ22.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi71 – 799Effector regionBy similarity

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233968.
    HOVERGENiHBG009351.
    InParanoidiQ6IQ22.
    KOiK07907.
    OMAiPPRMRCC.
    OrthoDBiEOG769ZKM.
    PhylomeDBiQ6IQ22.
    TreeFamiTF314097.

    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.

    Q6IQ22-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDPGAALQRR AGGGGGLGAG SPALSGGQGR RRKQPPRPAD FKLQVIIIGS    50
    RGVGKTSLME RFTDDTFCEA CKSTVGVDFK IKTVELRGKK IRLQIWDTAG 100
    QERFNSITSA YYRSAKGIIL VYDITKKETF DDLPKWMKMI DKYASEDAEL 150
    LLVGNKLDCE TDREITRQQG EKFAQQITGM RFCEASAKDN FNVDEIFLKL 200
    VDDILKKMPL DILRNELSNS ILSLQPEPEI PPELPPPRPH VRCC 244
    Length:244
    Mass (Da):27,248
    Last modified:January 9, 2007 - v3
    Checksum:iB4DC65DD0DCB45C4
    GO

    Sequence cautioni

    The sequence AAH71600.2 differs from that shown. Reason: Intron retention.
    The sequence AAH98407.1 differs from that shown. Reason: Intron retention.
    The sequence BC050338 differs from that shown. Reason: Frameshift at position 195.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP001793 Genomic DNA. No translation available.
    CH471113 Genomic DNA. Translation: EAX01616.1.
    BC050338 mRNA. No translation available.
    BC071600 mRNA. Translation: AAH71600.2. Sequence problems.
    BC098407 mRNA. Translation: AAH98407.1. Sequence problems.
    CCDSiCCDS42410.1.
    RefSeqiNP_001020471.2. NM_001025300.2.
    UniGeneiHs.270074.

    Genome annotation databases

    EnsembliENST00000329286; ENSP00000331748; ENSG00000206418.
    GeneIDi201475.
    KEGGihsa:201475.
    UCSCiuc002knp.3. human.

    Polymorphism databases

    DMDMi122064944.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP001793 Genomic DNA. No translation available.
    CH471113 Genomic DNA. Translation: EAX01616.1 .
    BC050338 mRNA. No translation available.
    BC071600 mRNA. Translation: AAH71600.2 . Sequence problems.
    BC098407 mRNA. Translation: AAH98407.1 . Sequence problems.
    CCDSi CCDS42410.1.
    RefSeqi NP_001020471.2. NM_001025300.2.
    UniGenei Hs.270074.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IL1 X-ray 2.10 A 36-208 [» ]
    ProteinModelPortali Q6IQ22.
    SMRi Q6IQ22. Positions 38-208.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128387. 4 interactions.
    STRINGi 9606.ENSP00000331748.

    PTM databases

    PhosphoSitei Q6IQ22.

    Polymorphism databases

    DMDMi 122064944.

    Proteomic databases

    MaxQBi Q6IQ22.
    PaxDbi Q6IQ22.
    PRIDEi Q6IQ22.

    Protocols and materials databases

    DNASUi 201475.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000329286 ; ENSP00000331748 ; ENSG00000206418 .
    GeneIDi 201475.
    KEGGi hsa:201475.
    UCSCi uc002knp.3. human.

    Organism-specific databases

    CTDi 201475.
    GeneCardsi GC18P008600.
    HGNCi HGNC:31332. RAB12.
    HPAi HPA040727.
    neXtProti NX_Q6IQ22.
    PharmGKBi PA142671102.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233968.
    HOVERGENi HBG009351.
    InParanoidi Q6IQ22.
    KOi K07907.
    OMAi PPRMRCC.
    OrthoDBi EOG769ZKM.
    PhylomeDBi Q6IQ22.
    TreeFami TF314097.

    Miscellaneous databases

    ChiTaRSi RAB12. human.
    EvolutionaryTracei Q6IQ22.
    GenomeRNAii 201475.
    NextBioi 90147.
    PROi Q6IQ22.

    Gene expression databases

    Bgeei Q6IQ22.
    CleanExi HS_RAB12.
    Genevestigatori Q6IQ22.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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: Placenta.
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors."
      Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.
      J. Cell Biol. 191:367-381(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Identification and characterisation of novel Mss4-binding Rab GTPases."
      Wixler V., Wixler L., Altenfeld A., Ludwig S., Goody R.S., Itzen A.
      Biol. Chem. 392:239-248(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RABIF.
    9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Crystal structure of a predicted human GTPase in complex with GDP."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 36-208 IN COMPLEX WITH MAGNESIUM AND GDP.

    Entry informationi

    Entry nameiRAB12_HUMAN
    AccessioniPrimary (citable) accession number: Q6IQ22
    Secondary accession number(s): A6NEF5, Q4KMQ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 103 of the entry and version 3 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3