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P15303

- SEC23_YEAST

UniProt

P15303 - SEC23_YEAST

Protein

Protein transport protein SEC23

Gene

SEC23

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC23 interacts with BET3 in order to target TRAPPI complex to COPII involved in internalisation of plasma membrane proteins like the maltose transporter.22 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi56 – 561Zinc1 Publication
    Metal bindingi61 – 611Zinc1 Publication
    Metal bindingi80 – 801Zinc1 Publication
    Metal bindingi83 – 831Zinc1 Publication

    GO - Molecular functioni

    1. GTPase activator activity Source: SGD
    2. protein binding Source: IntAct
    3. Sar GTPase activator activity Source: FlyBase
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. ER to Golgi vesicle-mediated transport Source: InterPro
    2. intracellular protein transport Source: InterPro
    3. positive regulation of Ras GTPase activity Source: FlyBase
    4. regulation of COPII vesicle coating Source: SGD

    Keywords - Biological processi

    ER-Golgi transport, Protein transport, Transport

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-34306-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein transport protein SEC23
    Gene namesi
    Name:SEC23
    Ordered Locus Names:YPR181C
    ORF Names:P9705.14
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XVI

    Organism-specific databases

    CYGDiYPR181c.
    SGDiS000006385. SEC23.

    Subcellular locationi

    GO - Cellular componenti

    1. COPII vesicle coat Source: SGD
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. Golgi membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 768768Protein transport protein SEC23PRO_0000205145Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Post-translational modificationi

    Ubiquitinated. Ubiquitination is required for the formation of the SEC23/24 complex. Deubiquitinated by the UBP3/BRE5 complex.1 Publication

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    MaxQBiP15303.
    PaxDbiP15303.
    PeptideAtlasiP15303.

    Expressioni

    Gene expression databases

    GenevestigatoriP15303.

    Interactioni

    Subunit structurei

    The COPII coat is composed of at least 7 proteins: the SEC23/24 complex, the SEC13/31 complex, SFB2, SFB3 and the protein SAR1. Forms two other heterodimeric complexes with SFB3 and PDR17. Interacts with BET1, BET3, BOS1, EMP24, GRH1, SEC16, SEC22 and SYS1.18 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SEC16P484155EBI-16584,EBI-16551
    SEC24P404824EBI-16584,EBI-16592
    SEC31P389684EBI-16584,EBI-20524
    SFB2P539535EBI-16584,EBI-17006

    Protein-protein interaction databases

    BioGridi36353. 77 interactions.
    DIPiDIP-2232N.
    IntActiP15303. 34 interactions.
    MINTiMINT-540233.
    STRINGi4932.YPR181C.

    Structurei

    Secondary structure

    1
    768
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 108
    Beta strandi11 – 2212
    Helixi23 – 286
    Beta strandi33 – 375
    Beta strandi48 – 514
    Turni59 – 613
    Beta strandi69 – 724
    Turni73 – 764
    Beta strandi77 – 793
    Turni81 – 833
    Beta strandi86 – 883
    Helixi91 – 933
    Beta strandi98 – 1003
    Helixi103 – 1053
    Beta strandi108 – 1136
    Beta strandi123 – 1297
    Helixi134 – 14916
    Beta strandi156 – 16813
    Beta strandi172 – 18312
    Helixi190 – 1989
    Beta strandi221 – 2233
    Helixi224 – 2274
    Beta strandi228 – 2303
    Helixi231 – 24313
    Helixi262 – 27615
    Beta strandi283 – 2908
    Beta strandi294 – 2974
    Helixi311 – 3155
    Helixi322 – 33918
    Beta strandi342 – 3487
    Helixi355 – 36511
    Beta strandi369 – 3735
    Helixi378 – 3869
    Beta strandi394 – 3974
    Beta strandi399 – 40810
    Beta strandi412 – 4209
    Beta strandi437 – 4393
    Beta strandi443 – 4508
    Beta strandi456 – 4627
    Beta strandi484 – 49512
    Turni496 – 4983
    Beta strandi499 – 51214
    Helixi517 – 5215
    Helixi525 – 53915
    Helixi545 – 56319
    Beta strandi564 – 5674
    Helixi571 – 5733
    Turni578 – 5814
    Helixi582 – 59211
    Turni594 – 5963
    Helixi603 – 61311
    Helixi618 – 6258
    Beta strandi628 – 6325
    Beta strandi634 – 6363
    Helixi645 – 6473
    Beta strandi653 – 6575
    Beta strandi659 – 6668
    Helixi668 – 6769
    Helixi678 – 6803
    Helixi682 – 6843
    Helixi685 – 70319
    Beta strandi710 – 7156
    Helixi719 – 7213
    Helixi722 – 7254
    Beta strandi740 – 7423
    Helixi752 – 76312

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M2OX-ray2.50A/C1-768[»]
    1M2VX-ray2.75A1-768[»]
    2QTVX-ray2.50A2-768[»]
    4BZIelectron microscopy23.00A/D/G1-768[»]
    ProteinModelPortaliP15303.
    SMRiP15303. Positions 2-768.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15303.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SEC23/SEC24 family. SEC23 subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG5047.
    GeneTreeiENSGT00390000006916.
    HOGENOMiHOG000231690.
    KOiK14006.
    OMAiTSIQPTH.
    OrthoDBiEOG7MPRPC.

    Family and domain databases

    Gene3Di3.40.20.10. 1 hit.
    3.40.50.410. 1 hit.
    InterProiIPR029006. ADF-H/Gelsolin-like_dom.
    IPR007123. Gelsolin-like_dom.
    IPR006900. Sec23/24_helical_dom.
    IPR006896. Sec23/24_trunk_dom.
    IPR012990. Sec23_24_beta_S.
    IPR002035. VWF_A.
    IPR006895. Znf_Sec23_Sec24.
    [Graphical view]
    PfamiPF00626. Gelsolin. 1 hit.
    PF08033. Sec23_BS. 1 hit.
    PF04815. Sec23_helical. 1 hit.
    PF04811. Sec23_trunk. 1 hit.
    PF04810. zf-Sec23_Sec24. 1 hit.
    [Graphical view]
    SMARTiSM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF53300. SSF53300. 1 hit.
    SSF81811. SSF81811. 1 hit.
    SSF82919. SSF82919. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P15303-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDFETNEDIN GVRFTWNVFP STRSDANSNV VPVGCLYTPL KEYDELNVAP    50
    YNPVVCSGPH CKSILNPYCV IDPRNSSWSC PICNSRNHLP PQYTNLSQEN 100
    MPLELQSTTI EYITNKPVTV PPIFFFVVDL TSETENLDSL KESIITSLSL 150
    LPPNALIGLI TYGNVVQLHD LSSETIDRCN VFRGDREYQL EALTEMLTGQ 200
    KPTGPGGAAS HLPNAMNKVT PFSLNRFFLP LEQVEFKLNQ LLENLSPDQW 250
    SVPAGHRPLR ATGSALNIAS LLLQGCYKNI PARIILFASG PGTVAPGLIV 300
    NSELKDPLRS HHDIDSDHAQ HYKKACKFYN QIAQRVAANG HTVDIFAGCY 350
    DQIGMSEMKQ LTDSTGGVLL LTDAFSTAIF KQSYLRLFAK DEEGYLKMAF 400
    NGNMAVKTSK DLKVQGLIGH ASAVKKTDAN NISESEIGIG ATSTWKMASL 450
    SPYHSYAIFF EIANTAANSN PMMSAPGSAD RPHLAYTQFI TTYQHSSGTN 500
    RIRVTTVANQ LLPFGTPAIA ASFDQEAAAV LMARIAVHKA ETDDGADVIR 550
    WLDRTLIKLC QKYADYNKDD PQSFRLAPNF SLYPQFTYYL RRSQFLSVFN 600
    NSPDETAFYR HIFTREDTTN SLIMIQPTLT SFSMEDDPQP VLLDSISVKP 650
    NTILLLDTFF FILIYHGEQI AQWRKAGYQD DPQYADFKAL LEEPKLEAAE 700
    LLVDRFPLPR FIDTEAGGSQ ARFLLSKLNP SDNYQDMARG GSTIVLTDDV 750
    SLQNFMTHLQ QVAVSGQA 768
    Length:768
    Mass (Da):85,385
    Last modified:April 1, 1990 - v1
    Checksum:i69811913848265FB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15474 Genomic DNA. Translation: CAA33501.1.
    U25842 Genomic DNA. Translation: AAB68114.1.
    BK006949 Genomic DNA. Translation: DAA11597.1.
    PIRiS05742. BVBY23.
    RefSeqiNP_015507.1. NM_001184278.1.

    Genome annotation databases

    EnsemblFungiiYPR181C; YPR181C; YPR181C.
    GeneIDi856311.
    KEGGisce:YPR181C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15474 Genomic DNA. Translation: CAA33501.1 .
    U25842 Genomic DNA. Translation: AAB68114.1 .
    BK006949 Genomic DNA. Translation: DAA11597.1 .
    PIRi S05742. BVBY23.
    RefSeqi NP_015507.1. NM_001184278.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M2O X-ray 2.50 A/C 1-768 [» ]
    1M2V X-ray 2.75 A 1-768 [» ]
    2QTV X-ray 2.50 A 2-768 [» ]
    4BZI electron microscopy 23.00 A/D/G 1-768 [» ]
    ProteinModelPortali P15303.
    SMRi P15303. Positions 2-768.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36353. 77 interactions.
    DIPi DIP-2232N.
    IntActi P15303. 34 interactions.
    MINTi MINT-540233.
    STRINGi 4932.YPR181C.

    Proteomic databases

    MaxQBi P15303.
    PaxDbi P15303.
    PeptideAtlasi P15303.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YPR181C ; YPR181C ; YPR181C .
    GeneIDi 856311.
    KEGGi sce:YPR181C.

    Organism-specific databases

    CYGDi YPR181c.
    SGDi S000006385. SEC23.

    Phylogenomic databases

    eggNOGi COG5047.
    GeneTreei ENSGT00390000006916.
    HOGENOMi HOG000231690.
    KOi K14006.
    OMAi TSIQPTH.
    OrthoDBi EOG7MPRPC.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-34306-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P15303.
    NextBioi 981685.

    Gene expression databases

    Genevestigatori P15303.

    Family and domain databases

    Gene3Di 3.40.20.10. 1 hit.
    3.40.50.410. 1 hit.
    InterProi IPR029006. ADF-H/Gelsolin-like_dom.
    IPR007123. Gelsolin-like_dom.
    IPR006900. Sec23/24_helical_dom.
    IPR006896. Sec23/24_trunk_dom.
    IPR012990. Sec23_24_beta_S.
    IPR002035. VWF_A.
    IPR006895. Znf_Sec23_Sec24.
    [Graphical view ]
    Pfami PF00626. Gelsolin. 1 hit.
    PF08033. Sec23_BS. 1 hit.
    PF04815. Sec23_helical. 1 hit.
    PF04811. Sec23_trunk. 1 hit.
    PF04810. zf-Sec23_Sec24. 1 hit.
    [Graphical view ]
    SMARTi SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53300. SSF53300. 1 hit.
    SSF81811. SSF81811. 1 hit.
    SSF82919. SSF82919. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Yeast Sec23p acts in the cytoplasm to promote protein transport from the endoplasmic reticulum to the Golgi complex in vivo and in vitro."
      Hicke L., Schekman R.W.
      EMBO J. 8:1677-1684(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: MBY8-20C.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
      Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
      , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
      Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway."
      Novick P., Field C., Schekman R.W.
      Cell 21:205-215(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Order of events in the yeast secretory pathway."
      Novick P., Ferro S., Schekman R.W.
      Cell 25:461-469(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Reconstitution of SEC gene product-dependent intercompartmental protein transport."
      Baker D., Hicke L., Rexach M.F., Schleyer M., Schekman R.W.
      Cell 54:335-344(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Reconstitution of protein transport from the endoplasmic reticulum to the Golgi complex in yeast: the acceptor Golgi compartment is defective in the sec23 mutant."
      Ruohola H., Kabcenell A.K., Ferro-Novick S.
      J. Cell Biol. 107:1465-1476(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway."
      Kaiser C.A., Schekman R.W.
      Cell 61:723-733(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Sec23p and a novel 105-kDa protein function as a multimeric complex to promote vesicle budding and protein transport from the endoplasmic reticulum."
      Hicke L., Yoshihisa T., Schekman R.W.
      Mol. Biol. Cell 3:667-676(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    10. "Multicopy STS1 restores both protein transport and ribosomal RNA stability in a new yeast sec23 mutant allele."
      Liang S., Lacroute F., Kepes F.
      Eur. J. Cell Biol. 62:270-281(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum."
      Yoshihisa T., Barlowe C., Schekman R.W.
      Science 259:1466-1468(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast."
      Bednarek S.Y., Ravazzola M., Hosobuchi M., Amherdt M., Perrelet A., Schekman R.W., Orci L.
      Cell 83:1183-1196(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p."
      Espenshade P.J., Gimeno R.E., Holzmacher E., Teung P., Kaiser C.A.
      J. Cell Biol. 131:311-324(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEC16.
    14. "Amino acid permeases require COPII components and the ER resident membrane protein Shr3p for packaging into transport vesicles in vitro."
      Kuehn M.J., Schekman R.W., Ljungdahl P.O.
      J. Cell Biol. 135:585-595(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent regions of Sec16p."
      Gimeno R.E., Espenshade P.J., Kaiser C.A.
      Mol. Biol. Cell 7:1815-1823(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEC16.
    16. "COPII subunit interactions in the assembly of the vesicle coat."
      Shaywitz D.A., Espenshade P.J., Gimeno R.E., Kaiser C.A.
      J. Biol. Chem. 272:25413-25416(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE COPII COAT, INTERACTION WITH SEC16.
    17. "Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast."
      Suetterlin C., Doering T.L., Schimmoeller F., Schroeder S., Riezman H.
      J. Cell Sci. 110:2703-2714(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Selective packaging of cargo molecules into endoplasmic reticulum-derived COPII vesicles."
      Campbell J.L., Schekman R.W.
      Proc. Natl. Acad. Sci. U.S.A. 94:837-842(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Role of endoplasmic reticulum-derived vesicles in the formation of Golgi elements in sec23 and sec18 Saccharomyces Cerevisiae mutants."
      Morin-Ganet M.N., Rambourg A., Clermont Y., Kepes F.
      Anat. Rec. 251:256-264(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes."
      Matsuoka K., Orci L., Amherdt M., Bednarek S.Y., Hamamoto S., Schekman R.W., Yeung T.
      Cell 93:263-275(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    21. "COPII-cargo interactions direct protein sorting into ER-derived transport vesicles."
      Kuehn M.J., Herrmann J.M., Schekman R.W.
      Nature 391:187-190(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE SEC23/24 COMPLEX.
    22. "Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs."
      Springer S., Schekman R.W.
      Science 281:698-700(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BET1; BOS1; SAR1 AND SEC24.
    23. "Clathrin and two components of the COPII complex, Sec23p and Sec24p, could be involved in endocytosis of the Saccharomyces cerevisiae maltose transporter."
      Penalver E., Lucero P., Moreno E., Lagunas R.
      J. Bacteriol. 181:2555-2563(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE SEC23/24 COMPLEX.
    24. "Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesicles."
      Gilstring C.F., Melin-Larsson M., Ljungdahl P.O.
      Mol. Biol. Cell 10:3549-3565(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHR3.
    25. "Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae."
      Shimoni Y., Kurihara T., Ravazzola M., Amherdt M., Orci L., Schekman R.W.
      J. Cell Biol. 151:973-984(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SFB3.
    26. "The use of liposomes to study COPII- and COPI-coated vesicle formation and membrane protein sorting."
      Matsuoka K., Schekman R.W.
      Methods 20:417-428(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    27. "Sec24p and Iss1p function interchangeably in transport vesicle formation from the endoplasmic reticulum in Saccharomyces cerevisiae."
      Kurihara T., Hamamoto S., Gimeno R.E., Kaiser C.A., Schekman R.W., Yoshihisa T.
      Mol. Biol. Cell 11:983-998(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDR17.
    28. "An acidic sequence of a putative yeast Golgi membrane protein binds COPII and facilitates ER export."
      Votsmeier C., Gallwitz D.
      EMBO J. 20:6742-6750(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SYS1.
    29. "Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in transport between the endoplasmic reticulum and Golgi complex."
      Belden W.J., Barlowe C.
      J. Biol. Chem. 276:43040-43048(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EMP24 AND ERV25.
    30. "Dynamics of the COPII coat with GTP and stable analogues."
      Antonny B., Madden D.T., Hamamoto S., Orci L., Schekman R.W.
      Nat. Cell Biol. 3:531-537(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE COPII COAT.
    31. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. Cited for: ELECTRON MICROSCOPY OF THE SEC23/24 COMPLEX.
    34. Cited for: ELECTRON MICROSCOPY OF THE SEC23/24 COMPLEX.
    35. "Sec16p potentiates the action of COPII proteins to bud transport vesicles."
      Supek F., Madden D.T., Hamamoto S., Orci L., Schekman R.W.
      J. Cell Biol. 158:1029-1038(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    36. Cited for: FUNCTION OF THE SEC23/24 COMPLEX, INTERACTION WITH BET1; SEC22 AND SED5.
    37. Cited for: STRUCTURE OF THE COPII COMPLEX.
    38. "Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23."
      Cohen M., Stutz F., Belgareh N., Haguenauer-Tsapis R., Dargemont C.
      Nat. Cell Biol. 5:661-667(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH SEC24.
    39. "Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting."
      Sato K., Nakano A.
      J. Biol. Chem. 279:1330-1335(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: COPII COMPLEX ASSEMBLY, FUNCTION OF THE COPII COMPLEX.
    40. "Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile."
      Schuldiner M., Collins S.R., Thompson N.J., Denic V., Bhamidipati A., Punna T., Ihmels J., Andrews B., Boone C., Greenblatt J.F., Weissman J.S., Krogan N.J.
      Cell 123:507-519(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GRH1.
    41. "The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein that contributes to ER to Golgi traffic."
      Behnia R., Barr F.A., Flanagan J.J., Barlowe C., Munro S.
      J. Cell Biol. 176:255-261(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GHR1.
    42. "TRAPPI tethers COPII vesicles by binding the coat subunit Sec23."
      Cai H., Yu S., Menon S., Cai Y., Lazarova D., Fu C., Reinisch K., Hay J.C., Ferro-Novick S.
      Nature 445:941-944(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BET3.
    43. "Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat."
      Bi X., Corpina R.A., Goldberg J.
      Nature 419:271-277(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SAR1 AND ZINC.

    Entry informationi

    Entry nameiSEC23_YEAST
    AccessioniPrimary (citable) accession number: P15303
    Secondary accession number(s): D6W4I1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 144 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

    External Data

    Dasty 3