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P15303

- SEC23_YEAST

UniProt

P15303 - SEC23_YEAST

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Protein
Protein transport protein SEC23
Gene
SEC23, YPR181C, P9705.14
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 561Zinc
Metal bindingi61 – 611Zinc
Metal bindingi80 – 801Zinc
Metal bindingi83 – 831Zinc

GO - Molecular functioni

  1. GTPase activator activity Source: SGD
  2. Sar GTPase activator activity Source: FlyBase
  3. protein binding Source: IntAct
  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
Complete GO annotation...

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

Cytoplasm. Cytoplasmic vesicleCOPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction 5 Publications

GO - Cellular componenti

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

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 SEC23
PRO_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 SYS1.17 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

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.

Miscellaneous databases

EvolutionaryTraceiP15303.

Family & Domainsi

Sequence similaritiesi

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 143 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

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