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P40482

- SEC24_YEAST

UniProt

P40482 - SEC24_YEAST

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Protein
Protein transport protein SEC24
Gene
SEC24, ANU1, YIL109C
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. 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 – 2311Zinc
Metal bindingi234 – 2341Zinc
Metal bindingi253 – 2531Zinc
Metal bindingi256 – 2561Zinc

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
Complete GO annotation...

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

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 8 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

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 SEC24
PRO_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 SYS1.15 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

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.

Miscellaneous databases

EvolutionaryTraceiP40482.

Family & Domainsi

Region

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

Compositional bias

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

Sequence similaritiesi

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 136 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

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