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P40482

- SEC24_YEAST

UniProt

P40482 - SEC24_YEAST

Protein

Protein transport protein SEC24

Gene

SEC24

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 137 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      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. SEC24 specifically recruits cargo proteins like BET1 or SYS1 to the COPII vesicles. The SEC23/24 complex is also involved in internalisation of plasma membrane proteins like the maltose transporter.13 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi231 – 2311Zinc2 Publications
    Metal bindingi234 – 2341Zinc2 Publications
    Metal bindingi253 – 2531Zinc2 Publications
    Metal bindingi256 – 2561Zinc2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. signal sequence binding Source: SGD
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cargo loading into COPII-coated vesicle Source: SGD
    2. intracellular protein transport Source: InterPro

    Keywords - Biological processi

    ER-Golgi transport, Protein transport, Transport

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31364-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein transport protein SEC24
    Alternative name(s):
    Abnormal nuclear morphology 1
    Gene namesi
    Name:SEC24
    Synonyms:ANU1
    Ordered Locus Names:YIL109C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IX

    Organism-specific databases

    CYGDiYIL109c.
    SGDiS000001371. SEC24.

    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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi230 – 2301R → A: Abolishes binding to and packaging of cargo protein BET1. 1 Publication
    Mutagenesisi231 – 2311C → S: Lethal. 1 Publication
    Mutagenesisi235 – 2351R → A: Abolishes binding to and packaging of cargo protein BET1. 1 Publication
    Mutagenesisi559 – 5591R → M: Abolishes binding to and packaging of cargo protein BET1. 1 Publication
    Mutagenesisi561 – 5611R → M: Abolishes binding to and packaging of cargo protein BET1. 1 Publication
    Mutagenesisi616 – 6161L → W: Abolishes binding to and packaging of cargo protein BET1. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 926926Protein transport protein SEC24PRO_0000205150Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei178 – 1781Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP40482.
    PaxDbiP40482.
    PeptideAtlasiP40482.

    Expressioni

    Gene expression databases

    GenevestigatoriP40482.

    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. Interacts with BET1, EMP24, GRH1, SEC22, SED5 and SYS1.16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GRH1Q044103EBI-16592,EBI-32083
    SEC23P153034EBI-16592,EBI-16584
    SEC31P389684EBI-16592,EBI-20524

    Protein-protein interaction databases

    BioGridi34882. 71 interactions.
    DIPiDIP-2233N.
    IntActiP40482. 22 interactions.
    MINTiMINT-476513.
    STRINGi4932.YIL109C.

    Structurei

    Secondary structure

    1
    926
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi64 – 729
    Beta strandi140 – 1423
    Helixi143 – 1453
    Helixi151 – 1555
    Helixi165 – 1673
    Beta strandi168 – 1703
    Helixi173 – 1753
    Turni179 – 1813
    Beta strandi182 – 19211
    Helixi193 – 1997
    Beta strandi204 – 2074
    Beta strandi212 – 2143
    Turni232 – 2343
    Beta strandi243 – 2453
    Turni246 – 2494
    Beta strandi250 – 2523
    Turni254 – 2563
    Beta strandi259 – 2613
    Helixi264 – 2674
    Helixi277 – 2793
    Helixi281 – 2844
    Beta strandi286 – 2916
    Helixi294 – 2963
    Beta strandi305 – 3117
    Helixi314 – 3196
    Helixi321 – 33212
    Turni333 – 3353
    Beta strandi344 – 35815
    Helixi362 – 3643
    Beta strandi374 – 3763
    Turni390 – 3923
    Beta strandi393 – 3953
    Turni396 – 3994
    Helixi400 – 41314
    Turni414 – 4163
    Helixi424 – 43512
    Turni436 – 4383
    Beta strandi440 – 4489
    Helixi471 – 4755
    Helixi482 – 49211
    Beta strandi495 – 50511
    Helixi509 – 5179
    Turni518 – 5203
    Beta strandi523 – 5275
    Helixi534 – 54916
    Beta strandi554 – 5629
    Beta strandi566 – 57611
    Beta strandi578 – 58710
    Beta strandi594 – 6007
    Beta strandi606 – 61813
    Turni620 – 6223
    Beta strandi624 – 63714
    Helixi639 – 6446
    Helixi648 – 66518
    Helixi668 – 68922
    Beta strandi696 – 6994
    Beta strandi702 – 7043
    Helixi705 – 7073
    Helixi710 – 7189
    Turni721 – 7233
    Helixi730 – 74213
    Helixi745 – 7528
    Beta strandi755 – 7584
    Turni759 – 7613
    Helixi791 – 7933
    Beta strandi799 – 8035
    Beta strandi805 – 8128
    Helixi818 – 8258
    Helixi830 – 8323
    Helixi847 – 86014
    Beta strandi870 – 8756
    Helixi885 – 89915
    Helixi913 – 92311

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M2VX-ray2.75B1-926[»]
    1PCXX-ray2.50A117-926[»]
    1PD0X-ray2.60A117-926[»]
    1PD1X-ray2.60A117-926[»]
    4BZIelectron microscopy23.00E/F/L/M/N/O1-926[»]
    ProteinModelPortaliP40482.
    SMRiP40482. Positions 133-926.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP40482.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni231 – 25626Zinc finger-likeAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi110 – 1145Poly-Gln
    Compositional biasi157 – 1604Poly-Pro

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5028.
    GeneTreeiENSGT00590000082962.
    HOGENOMiHOG000196365.
    KOiK14007.
    OMAiIDETIND.
    OrthoDBiEOG71K6BX.

    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]
    SUPFAMiSSF53300. SSF53300. 1 hit.
    SSF81811. SSF81811. 1 hit.
    SSF82919. SSF82919. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P40482-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHHKKRVYP QAQLQYGQNA TPLQQPAQFM PPQDPAAAGM SYGQMGMPPQ    50
    GAVPSMGQQQ FLTPAQEQLH QQIDQATTSM NDMHLHNVPL VDPNAYMQPQ 100
    VPVQMGTPLQ QQQQPMAAPA YGQPSAAMGQ NMRPMNQLYP IDLLTELPPP 150
    ITDLTLPPPP LVIPPERMLV PSELSNASPD YIRSTLNAVP KNSSLLKKSK 200
    LPFGLVIRPY QHLYDDIDPP PLNEDGLIVR CRRCRSYMNP FVTFIEQGRR 250
    WRCNFCRLAN DVPMQMDQSD PNDPKSRYDR NEIKCAVMEY MAPKEYTLRQ 300
    PPPATYCFLI DVSQSSIKSG LLATTINTLL QNLDSIPNHD ERTRISILCV 350
    DNAIHYFKIP LDSENNEESA DQINMMDIAD LEEPFLPRPN SMVVSLKACR 400
    QNIETLLTKI PQIFQSNLIT NFALGPALKS AYHLIGGVGG KIIVVSGTLP 450
    NLGIGKLQRR NESGVVNTSK ETAQLLSCQD SFYKNFTIDC SKVQITVDLF 500
    LASEDYMDVA SLSNLSRFTA GQTHFYPGFS GKNPNDIVKF STEFAKHISM 550
    DFCMETVMRA RGSTGLRMSR FYGHFFNRSS DLCAFSTMPR DQSYLFEVNV 600
    DESIMADYCY VQVAVLLSLN NSQRRIRIIT LAMPTTESLA EVYASADQLA 650
    IASFYNSKAV EKALNSSLDD ARVLINKSVQ DILATYKKEI VVSNTAGGAP 700
    LRLCANLRMF PLLMHSLTKH MAFRSGIVPS DHRASALNNL ESLPLKYLIK 750
    NIYPDVYSLH DMADEAGLPV QTEDGEATGT IVLPQPINAT SSLFERYGLY 800
    LIDNGNELFL WMGGDAVPAL VFDVFGTQDI FDIPIGKQEI PVVENSEFNQ 850
    RVRNIINQLR NHDDVITYQS LYIVRGASLS EPVNHASARE VATLRLWASS 900
    TLVEDKILNN ESYREFLQIM KARISK 926
    Length:926
    Mass (Da):103,636
    Last modified:February 1, 1995 - v1
    Checksum:i35E2BDD24CC75899
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z38125 Genomic DNA. Translation: CAA86271.1.
    AY692888 Genomic DNA. Translation: AAT92907.1.
    BK006942 Genomic DNA. Translation: DAA08444.1.
    PIRiS48463.
    RefSeqiNP_012157.3. NM_001179457.3.

    Genome annotation databases

    EnsemblFungiiYIL109C; YIL109C; YIL109C.
    GeneIDi854697.
    KEGGisce:YIL109C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z38125 Genomic DNA. Translation: CAA86271.1 .
    AY692888 Genomic DNA. Translation: AAT92907.1 .
    BK006942 Genomic DNA. Translation: DAA08444.1 .
    PIRi S48463.
    RefSeqi NP_012157.3. NM_001179457.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M2V X-ray 2.75 B 1-926 [» ]
    1PCX X-ray 2.50 A 117-926 [» ]
    1PD0 X-ray 2.60 A 117-926 [» ]
    1PD1 X-ray 2.60 A 117-926 [» ]
    4BZI electron microscopy 23.00 E/F/L/M/N/O 1-926 [» ]
    ProteinModelPortali P40482.
    SMRi P40482. Positions 133-926.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34882. 71 interactions.
    DIPi DIP-2233N.
    IntActi P40482. 22 interactions.
    MINTi MINT-476513.
    STRINGi 4932.YIL109C.

    Proteomic databases

    MaxQBi P40482.
    PaxDbi P40482.
    PeptideAtlasi P40482.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YIL109C ; YIL109C ; YIL109C .
    GeneIDi 854697.
    KEGGi sce:YIL109C.

    Organism-specific databases

    CYGDi YIL109c.
    SGDi S000001371. SEC24.

    Phylogenomic databases

    eggNOGi COG5028.
    GeneTreei ENSGT00590000082962.
    HOGENOMi HOG000196365.
    KOi K14007.
    OMAi IDETIND.
    OrthoDBi EOG71K6BX.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31364-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P40482.
    NextBioi 977337.

    Gene expression databases

    Genevestigatori P40482.

    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 ]
    SUPFAMi SSF53300. SSF53300. 1 hit.
    SSF81811. SSF81811. 1 hit.
    SSF82919. SSF82919. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "Specific interaction of the yeast cis-Golgi syntaxin Sed5p and the coat protein complex II component Sec24p of endoplasmic reticulum-derived transport vesicles."
      Peng R., Grabowski R., De Antoni A., Gallwitz D.
      Proc. Natl. Acad. Sci. U.S.A. 96:3751-3756(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 731-740 AND 774-793, INTERACTION WITH SED5, MUTAGENESIS OF CYS-231.
    5. "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.
    6. "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.
    7. "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.
    8. "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.
    9. "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.
    10. "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.
    11. "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 SEC23.
    12. "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.
    13. "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.
    14. "Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members."
      Peng R., De Antoni A., Gallwitz D.
      J. Biol. Chem. 275:11521-11528(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    15. "Sfb2p, a yeast protein related to Sec24p, can function as a constituent of COPII coats required for vesicle budding from the endoplasmic reticulum."
      Higashio H., Kimata Y., Kiriyama T., Hirata A., Kohno K.
      J. Biol. Chem. 275:17900-17908(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "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 PMA1.
    17. "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.
    18. "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: FUNCTION, SUBCELLULAR LOCATION.
    19. "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.
    20. "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.
    21. "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.
    22. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    23. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. Cited for: ELECTRON MICROSCOPY OF THE SEC23/24 COMPLEX.
    25. Cited for: ELECTRON MICROSCOPY OF THE SEC23/24 COMPLEX.
    26. "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.
    27. Cited for: STRUCTURE OF THE COPII COMPLEX.
    28. "Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles."
      Miller E.A., Beilharz T.H., Malkus P.N., Lee M.C.S., Hamamoto S., Orci L., Schekman R.W.
      Cell 114:497-509(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BET1 AND SYS1, MUTAGENESIS OF ARG-230; ARG-235; ARG-559; ARG-561 AND LEU-616.
    29. "The early secretory pathway contributes to autophagy in yeast."
      Hamasaki M., Noda T., Ohsumi Y.
      Cell Struct. Funct. 28:49-54(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    30. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    31. "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: INTERACTION WITH SEC23.
    32. "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.
    33. "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.
    34. "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.
    35. "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 SEC23 AND ZINC.
    36. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 117-926 IN COMPLEX WITH SED5; SYS1; BET1 AND ZINC, INTERACTION WITH SEC22.

    Entry informationi

    Entry nameiSEC24_YEAST
    AccessioniPrimary (citable) accession number: P40482
    Secondary accession number(s): D6VVH8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 137 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, Direct protein sequencing, 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 IX
      Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

    External Data

    Dasty 3