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P53011 (SEH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. 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:
Nucleoporin SEH1
Alternative name(s):
Nuclear pore protein SEH1
SEC13 homolog 1
Gene names
Name:SEH1
Ordered Locus Names:YGL100W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Involved in nuclear poly(A)+ RNA export and NPC biogenesis. It is also required for normal nuclear morphology. 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.1 Ref.6 Ref.7 Ref.12

Subunit structure

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. SEH1 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.5 Ref.12

Subcellular location

Nucleusnuclear pore complex. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Vacuole membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein; Nucleoplasmic side. Note: Symmetric distribution. Ref.12

Miscellaneous

Present with 952 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the WD repeat SEC13 family.

Contains 6 WD repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NUP85P466733EBI-16940,EBI-12345

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 349349Nucleoporin SEH1
PRO_0000051215

Regions

Repeat7 – 4640WD 1
Repeat53 – 9442WD 2
Repeat106 – 14742WD 3
Repeat153 – 19240WD 4
Repeat210 – 25344WD 5
Repeat302 – 34140WD 6

Amino acid modifications

Modified residue2571Phosphoserine Ref.10

Secondary structure

............................................................ 349
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53011 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: EAF75B9DE074106B

FASTA34939,123
        10         20         30         40         50         60 
MQPFDSGHDD LVHDVVYDFY GRHVATCSSD QHIKVFKLDK DTSNWELSDS WRAHDSSIVA 

        70         80         90        100        110        120 
IDWASPEYGR IIASASYDKT VKLWEEDPDQ EECSGRRWNK LCTLNDSKGS LYSVKFAPAH 

       130        140        150        160        170        180 
LGLKLACLGN DGILRLYDAL EPSDLRSWTL TSEMKVLSIP PANHLQSDFC LSWCPSRFSP 

       190        200        210        220        230        240 
EKLAVSALEQ AIIYQRGKDG KLHVAAKLPG HKSLIRSISW APSIGRWYQL IATGCKDGRI 

       250        260        270        280        290        300 
RIFKITEKLS PLASEESLTN SNMFDNSADV DMDAQGRSDS NTEEKAELQS NLQVELLSEH 

       310        320        330        340 
DDHNGEVWSV SWNLTGTILS SAGDDGKVRL WKATYSNEFK CMSVITAQQ 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 116-121 AND 136-146, FUNCTION IN NUCLEAR MRNA EXPORT.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"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.
[6]"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.
[7]"Genome-wide nuclear morphology screen identifies novel genes involved in nuclear architecture and gene-silencing in Saccharomyces cerevisiae."
Teixeira M.T., Dujon B., Fabre E.
J. Mol. Biol. 321:551-561(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, NUCLEAR MORPHOLOGY.
[8]"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.
[9]"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].
[10]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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].
[12]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X90994 Genomic DNA. Translation: CAA62480.1.
Z72622 Genomic DNA. Translation: CAA96806.1.
AY558497 Genomic DNA. Translation: AAS56823.1.
BK006941 Genomic DNA. Translation: DAA08006.1.
PIRS62137.
RefSeqNP_011415.1. NM_001180965.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EWEX-ray3.50A/C1-349[»]
3F3FX-ray2.90A/B/E/F1-349[»]
3F3GX-ray3.75A/B/E/F1-349[»]
3F3PX-ray3.20A/B/E/F/I/J1-349[»]
ProteinModelPortalP53011.
SMRP53011. Positions 1-349.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33149. 213 interactions.
DIPDIP-4193N.
IntActP53011. 21 interactions.
MINTMINT-547303.
STRING4932.YGL100W.

Protein family/group databases

TCDB1.I.1.1.1. the nuclear pore complex (npc) family.

Proteomic databases

PaxDbP53011.
PeptideAtlasP53011.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL100W; YGL100W; YGL100W.
GeneID852778.
KEGGsce:YGL100W.

Organism-specific databases

CYGDYGL100w.
SGDS000003068. SEH1.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00550000074999.
HOGENOMHOG000216896.
KOK14299.
OMAYEAPDIM.
OrthoDBEOG7TQVBP.

Enzyme and pathway databases

BioCycYEAST:G3O-30600-MONOMER.

Gene expression databases

GenevestigatorP53011.

Family and domain databases

Gene3D2.130.10.10. 3 hits.
InterProIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00400. WD40. 5 hits.
[Graphical view]
SMARTSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 2 hits.
PROSITEPS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP53011.
NextBio972254.
PROP53011.

Entry information

Entry nameSEH1_YEAST
AccessionPrimary (citable) accession number: P53011
Secondary accession number(s): D6VU45
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 132 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 VII

Yeast (Saccharomyces cerevisiae) chromosome VII: 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