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P24386

- RAE1_HUMAN

UniProt

P24386 - RAE1_HUMAN

Protein

Rab proteins geranylgeranyltransferase component A 1

Gene

CHM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 3 (06 Jun 2002)
      Previous versions | rss
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    Functioni

    Substrate-binding subunit of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B composed of RABGGTA and RABGGTB, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Besides, a pre-formed complex consisting of CHM and the Rab GGTase dimer (RGGT or component B) can bind to and prenylate Rab proteins; this alternative pathway is proposed to be the predominant pathway for Rab protein geranylgeranylation.2 Publications

    GO - Molecular functioni

    1. GTPase activator activity Source: UniProtKB-KW
    2. Rab geranylgeranyltransferase activity Source: ProtInc
    3. Rab GTPase binding Source: UniProtKB

    GO - Biological processi

    1. blood vessel development Source: Ensembl
    2. protein geranylgeranylation Source: UniProtKB
    3. protein targeting to membrane Source: UniProtKB
    4. response to stimulus Source: UniProtKB-KW
    5. visual perception Source: ProtInc

    Keywords - Molecular functioni

    GTPase activation

    Keywords - Biological processi

    Sensory transduction, Vision

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rab proteins geranylgeranyltransferase component A 1
    Alternative name(s):
    Choroideremia protein
    Rab escort protein 1
    Short name:
    REP-1
    TCD protein
    Gene namesi
    Name:CHM
    Synonyms:REP1, TCD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:1940. CHM.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. Rab-protein geranylgeranyltransferase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Choroideremia (CHM) [MIM:303100]: An X-linked recessive disease characterized by a slowly progressive degeneration of the choroid, photoreceptors, and retinal pigment epithelium. Affected males develop night blindness in their teenage years followed by loss of peripheral vision and complete blindness at middle age. Carrier females are generally asymptomatic but funduscopic examination often shows patchy areas of chorioretinal atrophy.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti471 – 4711Q → L in CHM; may affect splicing. 1 Publication
    VAR_008273
    Natural varianti507 – 5071H → R in CHM; impairs the interaction with RABGGTA. 1 Publication
    VAR_066847
    Natural varianti550 – 5501L → P in CHM. 1 Publication
    VAR_066848

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi282 – 2821F → L: Abolishes prenylation of RAB1A and association with RGGT. 1 Publication
    Mutagenesisi290 – 2901V → F: Impairs prenylation of RAB1A and abolishes association with RGGT. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi303100. phenotype.
    Orphaneti180. Choroideremia.
    PharmGKBiPA26471.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 653653Rab proteins geranylgeranyltransferase component A 1PRO_0000056686Add
    BLAST

    Proteomic databases

    MaxQBiP24386.
    PaxDbiP24386.
    PRIDEiP24386.

    PTM databases

    PhosphoSiteiP24386.

    Expressioni

    Gene expression databases

    ArrayExpressiP24386.
    BgeeiP24386.
    CleanExiHS_CHM.
    GenevestigatoriP24386.

    Organism-specific databases

    HPAiCAB016171.
    HPA003231.

    Interactioni

    Subunit structurei

    Monomer. Heterotrimer composed of RABGGTA, RABGGTB and CHM; within this trimer, RABGGTA and RABGGTB form the catalytic component B, while CHM (component A) mediates Rab protein binding. Can associate with the Rab GGTase dimer (RGGT or component B) prior to Rab protein binding; the association is stabilized by geranylgeranyl pyrophosphate (GGpp). The CHM:RGGT:Rab complex is destabilized by GGpp. Interacts with RAB1A, RAB1B, RAB5A, RAB7A and RAB27A and mediates their prenylation.3 Publications

    Protein-protein interaction databases

    BioGridi107545. 7 interactions.
    IntActiP24386. 47 interactions.
    STRINGi9606.ENSP00000350386.

    Structurei

    3D structure databases

    ProteinModelPortaliP24386.
    SMRiP24386. Positions 3-107, 178-617.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Rab GDI family.Curated

    Phylogenomic databases

    eggNOGiCOG5044.
    HOGENOMiHOG000220905.
    HOVERGENiHBG004961.
    InParanoidiP24386.
    OMAiQKNHASV.
    OrthoDBiEOG7Q5HCQ.
    PhylomeDBiP24386.
    TreeFamiTF320813.

    Family and domain databases

    InterProiIPR018203. GDP_dissociation_inhibitor.
    IPR001738. Rab_escort.
    IPR016664. Rab_geranylTrfase_A_euk.
    [Graphical view]
    PfamiPF00996. GDI. 2 hits.
    [Graphical view]
    PIRSFiPIRSF016550. Rab_ger_ger_transf_A_euk. 1 hit.
    PRINTSiPR00893. RABESCORT.
    PR00891. RABGDIREP.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P24386-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MADTLPSEFD VIVIGTGLPE SIIAAACSRS GRRVLHVDSR SYYGGNWASF    50
    SFSGLLSWLK EYQENSDIVS DSPVWQDQIL ENEEAIALSR KDKTIQHVEV 100
    FCYASQDLHE DVEEAGALQK NHALVTSANS TEAADSAFLP TEDESLSTMS 150
    CEMLTEQTPS SDPENALEVN GAEVTGEKEN HCDDKTCVPS TSAEDMSENV 200
    PIAEDTTEQP KKNRITYSQI IKEGRRFNID LVSKLLYSRG LLIDLLIKSN 250
    VSRYAEFKNI TRILAFREGR VEQVPCSRAD VFNSKQLTMV EKRMLMKFLT 300
    FCMEYEKYPD EYKGYEEITF YEYLKTQKLT PNLQYIVMHS IAMTSETASS 350
    TIDGLKATKN FLHCLGRYGN TPFLFPLYGQ GELPQCFCRM CAVFGGIYCL 400
    RHSVQCLVVD KESRKCKAII DQFGQRIISE HFLVEDSYFP ENMCSRVQYR 450
    QISRAVLITD RSVLKTDSDQ QISILTVPAE EPGTFAVRVI ELCSSTMTCM 500
    KGTYLVHLTC TSSKTAREDL ESVVQKLFVP YTEMEIENEQ VEKPRILWAL 550
    YFNMRDSSDI SRSCYNDLPS NVYVCSGPDC GLGNDNAVKQ AETLFQEICP 600
    NEDFCPPPPN PEDIILDGDS LQPEASESSA IPEANSETFK ESTNLGNLEE 650
    SSE 653
    Length:653
    Mass (Da):73,476
    Last modified:June 6, 2002 - v3
    Checksum:i7CFFAECE7BA1F3AF
    GO
    Isoform 2 (identifier: P24386-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         105-110: SQDLHE → RSTLLL
         111-653: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:110
    Mass (Da):12,301
    Checksum:iAD591A7B415DFD18
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti625 – 6262AS → RA in AAA61032. (PubMed:2215697)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti471 – 4711Q → L in CHM; may affect splicing. 1 Publication
    VAR_008273
    Natural varianti507 – 5071H → R in CHM; impairs the interaction with RABGGTA. 1 Publication
    VAR_066847
    Natural varianti550 – 5501L → P in CHM. 1 Publication
    VAR_066848

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei105 – 1106SQDLHE → RSTLLL in isoform 2. 1 PublicationVSP_042817
    Alternative sequencei111 – 653543Missing in isoform 2. 1 PublicationVSP_042818Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78121 mRNA. Translation: CAA55011.1.
    AL009175, AL022401, AL035451 Genomic DNA. Translation: CAI42098.1.
    AL022401, AL009175, AL035451 Genomic DNA. Translation: CAI43163.1.
    AL035451, AL009175 Genomic DNA. Translation: CAI42042.1.
    AL035451, AL009175, AL022401 Genomic DNA. Translation: CAI42043.1.
    AL009175, AL035451 Genomic DNA. Translation: CAI42097.1.
    AL138748 Genomic DNA. No translation available.
    BC130494 mRNA. Translation: AAI30495.1.
    BC130496 mRNA. Translation: AAI30497.1.
    M83773 mRNA. Translation: AAA61032.1.
    X57637 mRNA. Translation: CAA40855.1.
    S37423
    , S37416, S37417, S37422 Genomic DNA. Translation: AAD13814.1.
    CCDSiCCDS14454.1. [P24386-1]
    CCDS48139.1. [P24386-2]
    PIRiI37234.
    RefSeqiNP_000381.1. NM_000390.2. [P24386-1]
    NP_001138886.1. NM_001145414.2.
    UniGeneiHs.496449.

    Genome annotation databases

    EnsembliENST00000357749; ENSP00000350386; ENSG00000188419. [P24386-1]
    GeneIDi1121.
    KEGGihsa:1121.
    UCSCiuc004eet.3. human. [P24386-1]
    uc004eev.4. human. [P24386-2]

    Polymorphism databases

    DMDMi21431807.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Mutations of the REP1 gene

    Retina International's Scientific Newsletter

    Retinal and hearing impairment genetic mutation database choroideremia (Rab escort protein 1) (CHM)

    Leiden Open Variation Database (LOVD)

    NGRL, Manchester LOVD choroideremia (Rab escort protein 1) (CHM)

    Leiden Open Variation Database (LOVD)

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78121 mRNA. Translation: CAA55011.1 .
    AL009175 , AL022401 , AL035451 Genomic DNA. Translation: CAI42098.1 .
    AL022401 , AL009175 , AL035451 Genomic DNA. Translation: CAI43163.1 .
    AL035451 , AL009175 Genomic DNA. Translation: CAI42042.1 .
    AL035451 , AL009175 , AL022401 Genomic DNA. Translation: CAI42043.1 .
    AL009175 , AL035451 Genomic DNA. Translation: CAI42097.1 .
    AL138748 Genomic DNA. No translation available.
    BC130494 mRNA. Translation: AAI30495.1 .
    BC130496 mRNA. Translation: AAI30497.1 .
    M83773 mRNA. Translation: AAA61032.1 .
    X57637 mRNA. Translation: CAA40855.1 .
    S37423
    , S37416 , S37417 , S37422 Genomic DNA. Translation: AAD13814.1 .
    CCDSi CCDS14454.1. [P24386-1 ]
    CCDS48139.1. [P24386-2 ]
    PIRi I37234.
    RefSeqi NP_000381.1. NM_000390.2. [P24386-1 ]
    NP_001138886.1. NM_001145414.2.
    UniGenei Hs.496449.

    3D structure databases

    ProteinModelPortali P24386.
    SMRi P24386. Positions 3-107, 178-617.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107545. 7 interactions.
    IntActi P24386. 47 interactions.
    STRINGi 9606.ENSP00000350386.

    PTM databases

    PhosphoSitei P24386.

    Polymorphism databases

    DMDMi 21431807.

    Proteomic databases

    MaxQBi P24386.
    PaxDbi P24386.
    PRIDEi P24386.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357749 ; ENSP00000350386 ; ENSG00000188419 . [P24386-1 ]
    GeneIDi 1121.
    KEGGi hsa:1121.
    UCSCi uc004eet.3. human. [P24386-1 ]
    uc004eev.4. human. [P24386-2 ]

    Organism-specific databases

    CTDi 1121.
    GeneCardsi GC0XM085116.
    GeneReviewsi CHM.
    HGNCi HGNC:1940. CHM.
    HPAi CAB016171.
    HPA003231.
    MIMi 300390. gene.
    303100. phenotype.
    neXtProti NX_P24386.
    Orphaneti 180. Choroideremia.
    PharmGKBi PA26471.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5044.
    HOGENOMi HOG000220905.
    HOVERGENi HBG004961.
    InParanoidi P24386.
    OMAi QKNHASV.
    OrthoDBi EOG7Q5HCQ.
    PhylomeDBi P24386.
    TreeFami TF320813.

    Miscellaneous databases

    GeneWikii Rab_escort_protein.
    GenomeRNAii 1121.
    NextBioi 4654.
    PROi P24386.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P24386.
    Bgeei P24386.
    CleanExi HS_CHM.
    Genevestigatori P24386.

    Family and domain databases

    InterProi IPR018203. GDP_dissociation_inhibitor.
    IPR001738. Rab_escort.
    IPR016664. Rab_geranylTrfase_A_euk.
    [Graphical view ]
    Pfami PF00996. GDI. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF016550. Rab_ger_ger_transf_A_euk. 1 hit.
    PRINTSi PR00893. RABESCORT.
    PR00891. RABGDIREP.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Retina.
    2. "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].
    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] (ISOFORM 2).
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 289-653 (ISOFORM 1).
      Tissue: Retina.
    5. "Cloning of a gene that is rearranged in patients with choroideraemia."
      Cremers F.P.M., van de Pol D.J.R., van Kerkhoff L.P.M., Wieringa B., Ropers H.-H.
      Nature 347:674-677(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 338-653 (ISOFORM 1).
    6. "Detection and characterization of point mutations in the choroideremia candidate gene by PCR-SSCP analysis and direct DNA sequencing."
      van den Hurk J.A.J.M., van de Pol T.J.R., Molloy C.M., Brunsmann F., Ruther K., Zrenner E., Pinckers A.J.L.G., Pawlowitzki I.H., Bleeker-Wagemakers E.M., Wieringa B., Ropers H.-H., Cremers F.P.M.
      Am. J. Hum. Genet. 50:1195-1202(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 451-590.
    7. Cited for: SIMILARITY TO SMG P25A GDI.
    8. "Rab escort protein-1 is a multifunctional protein that accompanies newly prenylated rab proteins to their target membranes."
      Alexandrov K., Horiuchi H., Steele-Mortimer O., Seabra M.C., Zerial M.
      EMBO J. 13:5262-5273(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH RAB5A AND RAB7A.
    9. "Rab geranylgeranylation occurs preferentially via the pre-formed REP-RGGT complex and is regulated by geranylgeranyl pyrophosphate."
      Baron R.A., Seabra M.C.
      Biochem. J. 415:67-75(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF PHE-282 AND VAL-290.
    10. "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].
    11. "Comprehensive mutation analysis (20 families) of the choroideremia gene reveals a missense variant that prevents the binding of REP1 with rab geranylgeranyl transferase."
      Esposito G., De Falco F., Tinto N., Testa F., Vitagliano L., Tandurella I.C., Iannone L., Rossi S., Rinaldi E., Simonelli F., Zagari A., Salvatore F.
      Hum. Mutat. 32:1460-1469(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RABGGTA, VARIANT CHM ARG-507, CHARACTERIZATION OF VARIANT CHM ARG-507.
    12. Cited for: VARIANT CHM LEU-471.
    13. "The functional effect of pathogenic mutations in Rab escort protein 1."
      Sergeev Y.V., Smaoui N., Sui R., Stiles D., Gordiyenko N., Strunnikova N., Macdonald I.M.
      Mutat. Res. 665:44-50(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CHM PRO-550.

    Entry informationi

    Entry nameiRAE1_HUMAN
    AccessioniPrimary (citable) accession number: P24386
    Secondary accession number(s): A1L4D2, O43732
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: June 6, 2002
    Last modified: October 1, 2014
    This is version 134 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

    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