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Q04491

- SEC13_YEAST

UniProt

Q04491 - SEC13_YEAST

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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

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. 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
Complete GO annotation...

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 Source: UniProtKB-KW
  3. Golgi membrane Source: GOC
  4. nuclear pore outer ring Source: SGD
  5. Seh1-associated complex Source: SGD
  6. vacuole Source: UniProtKB-KW
Complete GO annotation...

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. 104 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.
InParanoidiQ04491.
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

        10         20         30         40         50
MVVIANAHNE LIHDAVLDYY GKRLATCSSD KTIKIFEVEG ETHKLIDTLT
60 70 80 90 100
GHEGPVWRVD WAHPKFGTIL ASCSYDGKVL IWKEENGRWS QIAVHAVHSA
110 120 130 140 150
SVNSVQWAPH EYGPLLLVAS SDGKVSVVEF KENGTTSPII IDAHAIGVNS
160 170 180 190 200
ASWAPATIEE DGEHNGTKES RKFVTGGADN LVKIWKYNSD AQTYVLESTL
210 220 230 240 250
EGHSDWVRDV AWSPTVLLRS YLASVSQDRT CIIWTQDNEQ GPWKKTLLKE
260 270 280 290
EKFPDVLWRA SWSLSGNVLA LSGGDNKVTL WKENLEGKWE PAGEVHQ
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. 104 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.
InParanoidi Q04491.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 140 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