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Q04491

- SEC13_YEAST

UniProt

Q04491 - SEC13_YEAST

Protein

Protein transport protein SEC13

Gene

SEC13

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 139 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Functions as a component of the nuclear pore complex (NPC) and the COPII coat. It is one of 5 proteins constituting the COPII coat, which is involved in anterograde (ER to Golgi) double-membrane transport vesicle formation. First the small GTPase SAR1, activated by and binding to the integral ER membrane protein SEC12, exchanges GDP for GTP and recruits the heterodimer SEC23/24, which in turn recruits the heterotetramer SEC13-SEC31. The polymerization of COPII coat complexes then causes physically the deformation (budding) of the membrane, leading to the creation of a transport vesicle. The COPII complex is dissociated upon SAR1-GTP hydrolysis to SAR1-GDP. SEC23 functions as the SAR1 GTPase activating protein, whose activity is stimulated in the presence of SEC13/31. SEC13 is directly or indirectly required for normal ER membrane and nuclear envelope morphology. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution. Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis.19 Publications

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: IntAct
    3. structural molecule activity Source: SGD

    GO - Biological processi

    1. COPII-coated vesicle budding Source: SGD
    2. ER-associated ubiquitin-dependent protein catabolic process Source: SGD
    3. mRNA transport Source: UniProtKB-KW
    4. nuclear pore distribution Source: SGD
    5. positive regulation of GTPase activity Source: SGD
    6. positive regulation of transcription, DNA-templated Source: SGD
    7. protein transport Source: UniProtKB-KW

    Keywords - Biological processi

    ER-Golgi transport, mRNA transport, Protein transport, Translocation, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32326-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein transport protein SEC13
    Gene namesi
    Name:SEC13
    Synonyms:ANU3
    Ordered Locus Names:YLR208W
    ORF Names:L8167.4
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLR208w.
    SGDiS000004198. SEC13.

    Subcellular locationi

    GO - Cellular componenti

    1. COPII vesicle coat Source: SGD
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. Golgi membrane Source: GOC
    4. nuclear pore outer ring Source: SGD
    5. Seh1-associated complex Source: SGD
    6. vacuolar membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Endoplasmic reticulum, Membrane, Nuclear pore complex, Nucleus, Vacuole

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi176 – 1761G → R: Leads to mislocalization of NPCs and overproliferation of the nuclear and ER membranes at 34 degree Celsius. 1 Publication
    Mutagenesisi224 – 2241S → K: Growth inhibited above 30 degrees Celsius. 1 Publication
    Mutagenesisi262 – 2621W → R: Growth inhibited above 30 degrees Celsius. 1 Publication
    Mutagenesisi266 – 2661G → D: Growth inhibited above 34 degrees Celsius. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 297297Protein transport protein SEC13PRO_0000051206Add
    BLAST

    Proteomic databases

    MaxQBiQ04491.
    PaxDbiQ04491.
    PeptideAtlasiQ04491.

    Expressioni

    Gene expression databases

    GenevestigatoriQ04491.

    Interactioni

    Subunit structurei

    The basic repeat unit of a COPII coated vesicle is composed of 5 proteins: the small GTPase SAR1, the heterodimeric SEC23-SEC24 complex, and the heterotetrameric SEC13-SEC31 complex. This repeat unit polymerizes to induce membrane deformation into a transport vesicle. The nuclear pore complex (NPC) constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. The 55-60 MDa NPC is composed of at least 31 different subunits: ASM4, CDC31, GLE1, GLE2, NDC1, NIC96, NSP1, NUP1, NUP2, NUP100, NUP116, NUP120, NUP133, NUP145, NUP157, NUP159, NUP170, NUP188, NUP192, NUP42, NUP49, NUP53, NUP57, NUP60, NUP82, NUP84, NUP85, POM152, POM34, SEH1 and SEC1. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. SEC13 is part of the heptameric 0.5 MDa autoassembling NUP84 NPC subcomplex (NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1). Component of the SEA complex composed of at least IML1/SEA1, RTC1/SEA2, MTC5/SEA3, NPR2, NPR3, SEA4, SEC13 and SEH1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-16529,EBI-16529
    NUP145P496878EBI-16529,EBI-11730
    SEC31P389688EBI-16529,EBI-20524

    Protein-protein interaction databases

    BioGridi31476. 103 interactions.
    DIPiDIP-1826N.
    IntActiQ04491. 22 interactions.
    MINTiMINT-402427.
    STRINGi4932.YLR208W.

    Structurei

    Secondary structure

    1
    297
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 43
    Beta strandi5 – 73
    Beta strandi12 – 176
    Beta strandi21 – 288
    Beta strandi33 – 386
    Beta strandi47 – 493
    Beta strandi56 – 616
    Helixi64 – 663
    Beta strandi68 – 747
    Beta strandi79 – 879
    Beta strandi93 – 953
    Beta strandi98 – 1003
    Beta strandi102 – 1076
    Helixi110 – 1123
    Beta strandi114 – 1207
    Beta strandi123 – 1308
    Beta strandi132 – 1343
    Beta strandi139 – 1424
    Beta strandi148 – 1536
    Beta strandi157 – 1615
    Turni162 – 1654
    Beta strandi166 – 1705
    Beta strandi172 – 1776
    Beta strandi182 – 1887
    Turni189 – 1924
    Beta strandi193 – 2008
    Beta strandi207 – 2126
    Beta strandi217 – 22610
    Beta strandi227 – 2293
    Beta strandi231 – 2388
    Beta strandi244 – 2518
    Beta strandi257 – 2626
    Beta strandi264 – 2663
    Beta strandi269 – 2735
    Beta strandi274 – 2763
    Beta strandi278 – 2836
    Beta strandi285 – 2873
    Beta strandi289 – 2913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PM6X-ray2.45B/D1-297[»]
    2PM7X-ray2.35B/D1-297[»]
    2PM9X-ray3.30B1-297[»]
    3IKOX-ray3.20A/D/G1-297[»]
    3JROX-ray4.00A1-297[»]
    3JRPX-ray2.60A1-297[»]
    3MZKX-ray2.69A/D1-297[»]
    3MZLX-ray2.80A/C/E/G1-297[»]
    4BZJelectron microscopy40.00B/F2-292[»]
    4BZKelectron microscopy40.00B/F1-292[»]
    ProteinModelPortaliQ04491.
    SMRiQ04491. Positions 1-297.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04491.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati7 – 4640WD 1Add
    BLAST
    Repeati51 – 9242WD 2Add
    BLAST
    Repeati97 – 13842WD 3Add
    BLAST
    Repeati143 – 19553WD 4Add
    BLAST
    Repeati202 – 24443WD 5Add
    BLAST
    Repeati252 – 29140WD 6Add
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat SEC13 family.Curated
    Contains 6 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    GeneTreeiENSGT00550000075049.
    HOGENOMiHOG000216895.
    KOiK14004.
    OMAiRACAGKD.
    OrthoDBiEOG7WQ83P.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF00400. WD40. 5 hits.
    [Graphical view]
    SMARTiSM00320. WD40. 6 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS50082. WD_REPEATS_2. 3 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q04491-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVVIANAHNE LIHDAVLDYY GKRLATCSSD KTIKIFEVEG ETHKLIDTLT    50
    GHEGPVWRVD WAHPKFGTIL ASCSYDGKVL IWKEENGRWS QIAVHAVHSA 100
    SVNSVQWAPH EYGPLLLVAS SDGKVSVVEF KENGTTSPII IDAHAIGVNS 150
    ASWAPATIEE DGEHNGTKES RKFVTGGADN LVKIWKYNSD AQTYVLESTL 200
    EGHSDWVRDV AWSPTVLLRS YLASVSQDRT CIIWTQDNEQ GPWKKTLLKE 250
    EKFPDVLWRA SWSLSGNVLA LSGGDNKVTL WKENLEGKWE PAGEVHQ 297
    Length:297
    Mass (Da):33,043
    Last modified:October 1, 1993 - v1
    Checksum:iA94388B4B9CB77FE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05929 Genomic DNA. Translation: AAA35028.1.
    U14913 Genomic DNA. Translation: AAB67426.1.
    BK006945 Genomic DNA. Translation: DAA09525.1.
    PIRiA45442.
    RefSeqiNP_013309.1. NM_001182095.1.

    Genome annotation databases

    EnsemblFungiiYLR208W; YLR208W; YLR208W.
    GeneIDi850905.
    KEGGisce:YLR208W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05929 Genomic DNA. Translation: AAA35028.1 .
    U14913 Genomic DNA. Translation: AAB67426.1 .
    BK006945 Genomic DNA. Translation: DAA09525.1 .
    PIRi A45442.
    RefSeqi NP_013309.1. NM_001182095.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PM6 X-ray 2.45 B/D 1-297 [» ]
    2PM7 X-ray 2.35 B/D 1-297 [» ]
    2PM9 X-ray 3.30 B 1-297 [» ]
    3IKO X-ray 3.20 A/D/G 1-297 [» ]
    3JRO X-ray 4.00 A 1-297 [» ]
    3JRP X-ray 2.60 A 1-297 [» ]
    3MZK X-ray 2.69 A/D 1-297 [» ]
    3MZL X-ray 2.80 A/C/E/G 1-297 [» ]
    4BZJ electron microscopy 40.00 B/F 2-292 [» ]
    4BZK electron microscopy 40.00 B/F 1-292 [» ]
    ProteinModelPortali Q04491.
    SMRi Q04491. Positions 1-297.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31476. 103 interactions.
    DIPi DIP-1826N.
    IntActi Q04491. 22 interactions.
    MINTi MINT-402427.
    STRINGi 4932.YLR208W.

    Proteomic databases

    MaxQBi Q04491.
    PaxDbi Q04491.
    PeptideAtlasi Q04491.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR208W ; YLR208W ; YLR208W .
    GeneIDi 850905.
    KEGGi sce:YLR208W.

    Organism-specific databases

    CYGDi YLR208w.
    SGDi S000004198. SEC13.

    Phylogenomic databases

    eggNOGi COG2319.
    GeneTreei ENSGT00550000075049.
    HOGENOMi HOG000216895.
    KOi K14004.
    OMAi RACAGKD.
    OrthoDBi EOG7WQ83P.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32326-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q04491.
    NextBioi 967299.
    PROi Q04491.

    Gene expression databases

    Genevestigatori Q04491.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF00400. WD40. 5 hits.
    [Graphical view ]
    SMARTi SM00320. WD40. 6 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS50082. WD_REPEATS_2. 3 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cytosolic Sec13p complex is required for vesicle formation from the endoplasmic reticulum in vitro."
      Pryer N.K., Salama N.R., Schekman R.W., Kaiser C.A.
      J. Cell Biol. 120:865-875(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF SER-224; TRP-262 AND GLY-266.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(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. "A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores."
      Siniossoglou S., Wimmer C., Rieger M., Doye V., Tekotte H., Weise C., Emig S., Segref A., Hurt E.C.
      Cell 84:265-275(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 35-39; 79-83; 125-131; 278-282 AND 289-293, FUNCTION IN NUCLEAR MRNA EXPORT.
    5. "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.
    6. "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.
    7. "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.
    8. "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.
    9. "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.
    10. "Control of amino acid permease sorting in the late secretory pathway of Saccharomyces cerevisiae by SEC13, LST4, LST7 and LST8."
      Roberg K.J., Bickel S., Rowley N., Kaiser C.A.
      Genetics 147:1569-1584(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "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.
    12. "Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae."
      Roberg K.J., Rowley N., Kaiser C.A.
      J. Cell Biol. 137:1469-1482(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "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.
    14. "Sec31 encodes an essential component of the COPII coat required for transport vesicle budding from the endoplasmic reticulum."
      Salama N.R., Chuang J.S., Schekman R.W.
      Mol. Biol. Cell 8:205-217(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEC31.
    15. "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.
    16. "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.
    17. "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.
    18. "The yeast nuclear pore complex: composition, architecture, and transport mechanism."
      Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.
      J. Cell Biol. 148:635-651(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, NPC SUBUNIT LOCATION.
    19. "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.
    20. Cited for: FUNCTION, LOCALIZATION AT NPC, ROLE IN NPC BIOGENESIS.
    21. "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.
    22. "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.
    23. Cited for: FUNCTION, HETEROTETRAMERIC COMPLEX WITH SEC31.
    24. Cited for: FUNCTION, COPII FORMATION AND STRUCTURE.
    25. "Isolation and characterization of new Saccharomyces cerevisiae mutants perturbed in nuclear pore complex assembly."
      Ryan K.J., Wente S.R.
      BMC Genet. 3:17-17(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ER MEMBRANE AND NUCLEAR ENVELOPE MORPHOLOGY, NPC ASSEMBLY AND DISTRIBUTION, MUTAGENESIS OF GLY-176.
    26. "Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins."
      Lutzmann M., Kunze R., Buerer A., Aebi U., Hurt E.C.
      EMBO J. 21:387-397(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, NUP84 NPC SUBCOMPLEX ASSEMBLY/STRUCTURE.
    27. "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.
    28. "Selective protein exit from yeast endoplasmic reticulum in absence of functional COPII coat component Sec13p."
      Fatal N., Suntio T., Makarow M.
      Mol. Biol. Cell 13:4130-4140(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    29. Cited for: STRUCTURE OF THE COPII COMPLEX.
    30. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    31. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    32. Cited for: REVIEW.
    33. "Signals for COPII-dependent export from the ER: what's the ticket out?"
      Barlowe C.
      Trends Cell Biol. 13:295-300(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    34. "Peering through the pore: nuclear pore complex structure, assembly, and function."
      Suntharalingam M., Wente S.R.
      Dev. Cell 4:775-789(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    35. "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.
    36. "A conserved coatomer-related complex containing Sec13 and Seh1 dynamically associates with the vacuole in Saccharomyces cerevisiae."
      Dokudovskaya S., Waharte F., Schlessinger A., Pieper U., Devos D.P., Cristea I.M., Williams R., Salamero J., Chait B.T., Sali A., Field M.C., Rout M.P., Dargemont C.
      Mol. Cell. Proteomics 10:M110.006478.1-M110.006478.17(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE SEA COMPLEX, FUNCTION.
    37. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSEC13_YEAST
    AccessioniPrimary (citable) accession number: Q04491
    Secondary accession number(s): D6VYK9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 21400 molecules/cell in log phase SD medium.1 Publication

    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 XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3