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Protein

Nucleoporin POM34

Gene

POM34

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • structural constituent of nuclear pore Source: SGD

GO - Biological processi

  • mRNA transport Source: UniProtKB-KW
  • nuclear pore organization Source: SGD
  • protein import into nucleus Source: SGD
  • spindle pole body duplication Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-32179-MONOMER.

Protein family/group databases

TCDBi1.I.1.1.1. the nuclear pore complex (npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin POM34
Alternative name(s):
Nuclear pore protein POM34
Pore membrane protein POM34
Gene namesi
Name:POM34
Ordered Locus Names:YLR018C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLR018c.
EuPathDBiFungiDB:YLR018C.
SGDiS000004008. POM34.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei64 – 8421HelicalSequence AnalysisAdd
BLAST
Transmembranei133 – 15321HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • integral component of nuclear outer membrane Source: SGD
  • nuclear pore Source: SGD
  • nuclear pore transmembrane ring Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299Nucleoporin POM34PRO_0000204911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei270 – 2701Phosphoserine1 Publication
Modified residuei273 – 2731Phosphothreonine1 Publication
Modified residuei292 – 2921Phosphoserine1 Publication
Modified residuei294 – 2941Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12445.
PaxDbiQ12445.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi31292. 98 interactions.
DIPiDIP-8961N.
IntActiQ12445. 6 interactions.
MINTiMINT-1362914.

Structurei

3D structure databases

ProteinModelPortaliQ12445.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG45366.
InParanoidiQ12445.
KOiK18724.
OMAiPSSKYAY.
OrthoDBiEOG71VT5V.

Family and domain databases

InterProiIPR012578. Nucl_pore_cmplx.
[Graphical view]
PfamiPF08058. NPCC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12445-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIQAGQLGL DDNDVPGPLP DTDSKPSSQS QNDTPMFKLG NFESPVLKEL
60 70 80 90 100
SRRTVNKEME TQRIMTNVIA FAFWNLLVKF IKFFWNNTHV GRQFCNRLSR
110 120 130 140 150
IHLYMLTFHT LKKANIIYHT TFSWLNAELL DYLFHLLISL NILFSLWKLL
160 170 180 190 200
STVKVSDLNL TDRQKKLLGV DMQSSVDTGL QPQHPHYVST SKISQMAQNK
210 220 230 240 250
THIPQTNLKN HPAYLFKGLE TPLKARQREM AEEQTKLQSQ SLHTKNVFGT
260 270 280 290
LQRHSGISST LVSANNDNNS PHTPVTRKGY IPSSKYAYMM NSQSPRGKI
Length:299
Mass (Da):34,232
Last modified:November 1, 1996 - v1
Checksum:iEEDB5BEFF5BEDF6A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911S → P in AAS56272 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90564 Genomic DNA. Translation: CAA62155.1.
Z73191 Genomic DNA. Translation: CAA97542.1.
Z73190 Genomic DNA. Translation: CAA97540.1.
AY557946 Genomic DNA. Translation: AAS56272.1.
BK006945 Genomic DNA. Translation: DAA09336.1.
PIRiS64840.
RefSeqiNP_013118.1. NM_001181905.1.

Genome annotation databases

EnsemblFungiiYLR018C; YLR018C; YLR018C.
GeneIDi850705.
KEGGisce:YLR018C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90564 Genomic DNA. Translation: CAA62155.1.
Z73191 Genomic DNA. Translation: CAA97542.1.
Z73190 Genomic DNA. Translation: CAA97540.1.
AY557946 Genomic DNA. Translation: AAS56272.1.
BK006945 Genomic DNA. Translation: DAA09336.1.
PIRiS64840.
RefSeqiNP_013118.1. NM_001181905.1.

3D structure databases

ProteinModelPortaliQ12445.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31292. 98 interactions.
DIPiDIP-8961N.
IntActiQ12445. 6 interactions.
MINTiMINT-1362914.

Protein family/group databases

TCDBi1.I.1.1.1. the nuclear pore complex (npc) family.

Proteomic databases

MaxQBiQ12445.
PaxDbiQ12445.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR018C; YLR018C; YLR018C.
GeneIDi850705.
KEGGisce:YLR018C.

Organism-specific databases

CYGDiYLR018c.
EuPathDBiFungiDB:YLR018C.
SGDiS000004008. POM34.

Phylogenomic databases

eggNOGiNOG45366.
InParanoidiQ12445.
KOiK18724.
OMAiPSSKYAY.
OrthoDBiEOG71VT5V.

Enzyme and pathway databases

BioCyciYEAST:G3O-32179-MONOMER.

Miscellaneous databases

NextBioi966751.
PROiQ12445.

Family and domain databases

InterProiIPR012578. Nucl_pore_cmplx.
[Graphical view]
PfamiPF08058. NPCC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A 7.8kb fragment from chromosome XII of Saccharomyces cerevisiae does not harbour PKC2."
    Saville S.P., Atkinson S., Jamieson L., Pocklington M.J., Orr E.
    Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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. "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.
  7. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  9. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294, IDENTIFICATION BY MASS SPECTROMETRY [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-294, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270; THR-273; SER-292 AND SER-294, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPOM34_YEAST
AccessioniPrimary (citable) accession number: Q12445
Secondary accession number(s): D6VY20, E9P8U3, Q7LGY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 112 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

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.