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P15303 (SEC23_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein transport protein SEC23
Gene names
Name:SEC23
Ordered Locus Names:YPR181C
ORF Names:P9705.14
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length768 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.17 Ref.18 Ref.19 Ref.21 Ref.23 Ref.25 Ref.26 Ref.36 Ref.39 Ref.40 Ref.42

Subunit structure

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. Ref.9 Ref.13 Ref.15 Ref.16 Ref.20 Ref.22 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.36 Ref.38 Ref.40 Ref.41 Ref.42

Subcellular location

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 Potential Ref.12 Ref.20 Ref.25 Ref.26 Ref.35.

Post-translational modification

Ubiquitinated. Ubiquitination is required for the formation of the SEC23/24 complex. Deubiquitinated by the UBP3/BRE5 complex. Ref.38

Sequence similarities

Belongs to the SEC23/SEC24 family. SEC23 subfamily.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 768768Protein transport protein SEC23
PRO_0000205145

Sites

Metal binding561Zinc
Metal binding611Zinc
Metal binding801Zinc
Metal binding831Zinc

Amino acid modifications

Modified residue11N-acetylmethionine Ref.32

Secondary structure

........................................................................................................................ 768
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15303 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 69811913848265FB

FASTA76885,385
        10         20         30         40         50         60 
MDFETNEDIN GVRFTWNVFP STRSDANSNV VPVGCLYTPL KEYDELNVAP YNPVVCSGPH 

        70         80         90        100        110        120 
CKSILNPYCV IDPRNSSWSC PICNSRNHLP PQYTNLSQEN MPLELQSTTI EYITNKPVTV 

       130        140        150        160        170        180 
PPIFFFVVDL TSETENLDSL KESIITSLSL LPPNALIGLI TYGNVVQLHD LSSETIDRCN 

       190        200        210        220        230        240 
VFRGDREYQL EALTEMLTGQ KPTGPGGAAS HLPNAMNKVT PFSLNRFFLP LEQVEFKLNQ 

       250        260        270        280        290        300 
LLENLSPDQW SVPAGHRPLR ATGSALNIAS LLLQGCYKNI PARIILFASG PGTVAPGLIV 

       310        320        330        340        350        360 
NSELKDPLRS HHDIDSDHAQ HYKKACKFYN QIAQRVAANG HTVDIFAGCY DQIGMSEMKQ 

       370        380        390        400        410        420 
LTDSTGGVLL LTDAFSTAIF KQSYLRLFAK DEEGYLKMAF NGNMAVKTSK DLKVQGLIGH 

       430        440        450        460        470        480 
ASAVKKTDAN NISESEIGIG ATSTWKMASL SPYHSYAIFF EIANTAANSN PMMSAPGSAD 

       490        500        510        520        530        540 
RPHLAYTQFI TTYQHSSGTN RIRVTTVANQ LLPFGTPAIA ASFDQEAAAV LMARIAVHKA 

       550        560        570        580        590        600 
ETDDGADVIR WLDRTLIKLC QKYADYNKDD PQSFRLAPNF SLYPQFTYYL RRSQFLSVFN 

       610        620        630        640        650        660 
NSPDETAFYR HIFTREDTTN SLIMIQPTLT SFSMEDDPQP VLLDSISVKP NTILLLDTFF 

       670        680        690        700        710        720 
FILIYHGEQI AQWRKAGYQD DPQYADFKAL LEEPKLEAAE LLVDRFPLPR FIDTEAGGSQ 

       730        740        750        760 
ARFLLSKLNP SDNYQDMARG GSTIVLTDDV SLQNFMTHLQ QVAVSGQA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"Structure of the Sec23p/24p and Sec13p/31p complexes of COPII."
Lederkremer G.Z., Cheng Y., Petre B.M., Vogan E., Springer S., Schekman R.W., Walz T., Kirchhausen T.
Proc. Natl. Acad. Sci. U.S.A. 98:10704-10709(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ELECTRON MICROSCOPY OF THE SEC23/24 COMPLEX.
[34]"Surface structure of the COPII-coated vesicle."
Matsuoka K., Schekman R.W., Orci L., Heuser J.E.
Proc. Natl. Acad. Sci. U.S.A. 98:13705-13709(2001) [PubMed] [Europe PMC] [Abstract]
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]"SNARE selectivity of the COPII coat."
Mossessova E., Bickford L.C., Goldberg J.
Cell 114:483-495(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE SEC23/24 COMPLEX, INTERACTION WITH BET1; SEC22 AND SED5.
[37]"Self-assembly of minimal COPII cages."
Antonny B., Gounon P., Schekman R.W., Orci L.
EMBO Rep. 4:419-424(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15474 Genomic DNA. Translation: CAA33501.1.
U25842 Genomic DNA. Translation: AAB68114.1.
BK006949 Genomic DNA. Translation: DAA11597.1.
PIRBVBY23. S05742.
RefSeqNP_015507.1. NM_001184278.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M2OX-ray2.50A/C1-768[»]
1M2VX-ray2.75A1-768[»]
2QTVX-ray2.50A2-768[»]
4BZIelectron microscopy23.00A/D/G1-768[»]
ProteinModelPortalP15303.
SMRP15303. Positions 2-768.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36353. 77 interactions.
DIPDIP-2232N.
IntActP15303. 34 interactions.
MINTMINT-540233.
STRING4932.YPR181C.

Proteomic databases

MaxQBP15303.
PaxDbP15303.
PeptideAtlasP15303.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPR181C; YPR181C; YPR181C.
GeneID856311.
KEGGsce:YPR181C.

Organism-specific databases

CYGDYPR181c.
SGDS000006385. SEC23.

Phylogenomic databases

eggNOGCOG5047.
GeneTreeENSGT00390000006916.
HOGENOMHOG000231690.
KOK14006.
OMATSIQPTH.
OrthoDBEOG7MPRPC.

Enzyme and pathway databases

BioCycYEAST:G3O-34306-MONOMER.

Gene expression databases

GenevestigatorP15303.

Family and domain databases

Gene3D3.40.20.10. 1 hit.
3.40.50.410. 1 hit.
InterProIPR029006. 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]
PfamPF00626. 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]
SMARTSM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF53300. SSF53300. 1 hit.
SSF81811. SSF81811. 1 hit.
SSF82919. SSF82919. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP15303.
NextBio981685.

Entry information

Entry nameSEC23_YEAST
AccessionPrimary (citable) accession number: P15303
Secondary accession number(s): D6W4I1
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references