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Q04491 (SEC13_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 138. 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 SEC13
Gene names
Name:SEC13
Synonyms:ANU3
Ordered Locus Names:YLR208W
ORF Names:L8167.4
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.15 Ref.19 Ref.20 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.35 Ref.36

Subunit structure

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. Ref.11 Ref.16 Ref.18 Ref.22 Ref.36

Subcellular location

Cytoplasmic vesicleCOPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleusnuclear pore complex. Vacuole membrane; Peripheral membrane protein Ref.8 Ref.16 Ref.19 Ref.27 Ref.30 Ref.36.

Miscellaneous

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

Sequence similarities

Belongs to the WD repeat SEC13 family.

Contains 6 WD repeats.

Ontologies

Keywords
   Biological processER-Golgi transport
mRNA transport
Protein transport
Translocation
Transport
   Cellular componentCytoplasmic vesicle
Endoplasmic reticulum
Membrane
Nuclear pore complex
Nucleus
Vacuole
   DomainRepeat
WD repeat
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCOPII-coated vesicle budding

Inferred from mutant phenotype PubMed 8223424Ref.1. Source: SGD

ER-associated ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 12538638. Source: SGD

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear pore distribution

Inferred from mutant phenotype Ref.20. Source: SGD

positive regulation of GTPase activity

Inferred from direct assay Ref.22. Source: SGD

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15817685. Source: SGD

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCOPII vesicle coat

Inferred from direct assay Ref.24PubMed 8004676. Source: SGD

Golgi membrane

Inferred from mutant phenotype PubMed 8223424Ref.1. Source: GOC

Seh1-associated complex

Inferred from direct assay Ref.36. Source: SGD

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear pore outer ring

Inferred from direct assay Ref.26PubMed 18046406. Source: SGD

vacuolar membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 11805826PubMed 18160040. Source: IntAct

protein binding

Inferred from physical interaction PubMed 11283351PubMed 11805826PubMed 16429126PubMed 18160040PubMed 18719252PubMed 21784248Ref.11. Source: IntAct

structural molecule activity

Inferred from direct assay Ref.29PubMed 17604721. Source: SGD

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297Protein transport protein SEC13
PRO_0000051206

Regions

Repeat7 – 4640WD 1
Repeat51 – 9242WD 2
Repeat97 – 13842WD 3
Repeat143 – 19553WD 4
Repeat202 – 24443WD 5
Repeat252 – 29140WD 6

Experimental info

Mutagenesis1761G → R: Leads to mislocalization of NPCs and overproliferation of the nuclear and ER membranes at 34 degree Celsius. Ref.25
Mutagenesis2241S → K: Growth inhibited above 30 degrees Celsius. Ref.1
Mutagenesis2621W → R: Growth inhibited above 30 degrees Celsius. Ref.1
Mutagenesis2661G → D: Growth inhibited above 34 degrees Celsius. Ref.1

Secondary structure

...................................................................... 297
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q04491 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: A94388B4B9CB77FE

FASTA29733,043
        10         20         30         40         50         60 
MVVIANAHNE LIHDAVLDYY GKRLATCSSD KTIKIFEVEG ETHKLIDTLT GHEGPVWRVD 

        70         80         90        100        110        120 
WAHPKFGTIL ASCSYDGKVL IWKEENGRWS QIAVHAVHSA SVNSVQWAPH EYGPLLLVAS 

       130        140        150        160        170        180 
SDGKVSVVEF KENGTTSPII IDAHAIGVNS ASWAPATIEE DGEHNGTKES RKFVTGGADN 

       190        200        210        220        230        240 
LVKIWKYNSD AQTYVLESTL EGHSDWVRDV AWSPTVLLRS YLASVSQDRT CIIWTQDNEQ 

       250        260        270        280        290 
GPWKKTLLKE EKFPDVLWRA SWSLSGNVLA LSGGDNKVTL WKENLEGKWE PAGEVHQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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]"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]"Structure and assembly of the Nup84p complex."
Siniossoglou S., Lutzmann M., Santos-Rosa H., Leonard K., Mueller S., Aebi U., Hurt E.C.
J. Cell Biol. 149:41-54(2000) [PubMed] [Europe PMC] [Abstract]
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]"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: FUNCTION, HETEROTETRAMERIC COMPLEX WITH SEC31.
[24]"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: 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]"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.
[30]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[31]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[32]"Intracellular sorting and transport of proteins."
van Vliet C., Thomas E.C., Merino-Trigo A., Teasdale R.D., Gleeson P.A.
Prog. Biophys. Mol. Biol. 83:1-45(2003) [PubMed] [Europe PMC] [Abstract]
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]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L05929 Genomic DNA. Translation: AAA35028.1.
U14913 Genomic DNA. Translation: AAB67426.1.
BK006945 Genomic DNA. Translation: DAA09525.1.
PIRA45442.
RefSeqNP_013309.1. NM_001182095.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ04491.
SMRQ04491. Positions 1-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31476. 103 interactions.
DIPDIP-1826N.
IntActQ04491. 22 interactions.
MINTMINT-402427.
STRING4932.YLR208W.

Proteomic databases

MaxQBQ04491.
PaxDbQ04491.
PeptideAtlasQ04491.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR208W; YLR208W; YLR208W.
GeneID850905.
KEGGsce:YLR208W.

Organism-specific databases

CYGDYLR208w.
SGDS000004198. SEC13.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00550000075049.
HOGENOMHOG000216895.
KOK14004.
OMARACAGKD.
OrthoDBEOG7WQ83P.

Enzyme and pathway databases

BioCycYEAST:G3O-32326-MONOMER.

Gene expression databases

GenevestigatorQ04491.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00400. WD40. 5 hits.
[Graphical view]
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ04491.
NextBio967299.
PROQ04491.

Entry information

Entry nameSEC13_YEAST
AccessionPrimary (citable) accession number: Q04491
Secondary accession number(s): D6VYK9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 11, 2014
This is version 138 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 XII

Yeast (Saccharomyces cerevisiae) chromosome XII: 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