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P39685 (PO152_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Nucleoporin POM152
Alternative name(s):
Nuclear pore protein POM152
P150
Pore membrane protein POM152
Gene names
Name:POM152
Ordered Locus Names:YMR129W
ORF Names:YM9553.05
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1337 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. POM152 is important for the de novo assembly of NPCs. Ref.4 Ref.5 Ref.7

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. Interacts with NUP188. Ref.4 Ref.6

Subcellular location

Nucleusnuclear pore complex. Nucleus membrane; Multi-pass membrane protein. Note: Central core structure of the nuclear pore complex.

Post-translational modification

The N-terminus is blocked.

Phosphorylated by CDC28. Ref.10 Ref.12 Ref.13 Ref.14 Ref.15

Miscellaneous

Present with 3410 molecules/cell in log phase SD medium. Ref.9

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13371337Nucleoporin POM152
PRO_0000204910

Regions

Topological domain1 – 110110Cytoplasmic Potential
Transmembrane111 – 13121Helical; Potential
Topological domain132 – 14817Perinuclear space Potential
Transmembrane149 – 16921Helical; Potential
Topological domain170 – 1723Cytoplasmic Potential
Transmembrane173 – 19321Helical; Potential
Topological domain194 – 13371144Perinuclear space Potential
Repeat390 – 413241
Repeat626 – 650252
Repeat732 – 755243
Repeat836 – 859244
Repeat943 – 966245
Repeat1058 – 1077206
Repeat1157 – 1178227
Repeat1253 – 1276248
Region1 – 175175Pore side Probable
Region196 – 13371142Cisternal side Probable
Region390 – 12768878 X 24 AA approximate repeats

Amino acid modifications

Modified residue451Phosphoserine Ref.12 Ref.14 Ref.15
Modified residue601Phosphoserine Ref.13
Modified residue7871Phosphothreonine Ref.15
Modified residue7971Phosphoserine Ref.15
Glycosylation2801N-linked (GlcNAc...) Probable

Sequences

Sequence LengthMass (Da)Tools
P39685 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: A024A42069193898

FASTA1,337151,653
        10         20         30         40         50         60 
MEHRYNVFND TPRGNHWMGS SVSGSPRPSY SSRPNVNTTR RFQYSDDEPA EKIRPLRSRS 

        70         80         90        100        110        120 
FKSTESNISD EKSRISERDS KDRYINGDKK VDIYSLPLIS TDVLEISKQR TFAVILFLII 

       130        140        150        160        170        180 
QCYKIYDLVI LKSGLPLSGL LFKNYRFNFI SKYFIIDSFF LYVLPSFNIP RLTFKPWVVY 

       190        200        210        220        230        240 
LQILAMLLLN IFISSDHEFV LISLIMTTWR KLYTKELSVT GSAINHHRIF DSSAHFKGAL 

       250        260        270        280        290        300 
TIKILPENTA MFNPLHESYC LPMDTNLFKI NSIDVPIRIN STEEIEYIEL EYRDLYTNSV 

       310        320        330        340        350        360 
ELRSLSKKDF KIIDNPKSFL KKDQSVLKSH SNDFEEGSTI RYLAVTLQDI GFYQIKKIVD 

       370        380        390        400        410        420 
SKKLNLKIHQ SHLVVPYCPI ASITGTGSND RCIGDSDNVS FEIQGVPPMK LAYSKIVNGQ 

       430        440        450        460        470        480 
TFSYVDSSLQ PEYFESPLQS SKSKQSFTQG ELNDLKWGRN QPVNINLDSS ITQDGKFAYK 

       490        500        510        520        530        540 
IDKITDGLGN VVDFTSLPEE LKKRYDLSYN FNVHEVPRAA LEERFDPKSP TKRSIAIVFE 

       550        560        570        580        590        600 
EIKNWISDIP YVISLSYTDA QDKSKKIMNV TTDSLTKVLQ ADLPGSYNLE YIESKFCPGE 

       610        620        630        640        650        660 
IVGKSNVLVT MPVAPTMEVK SFPILDQCVG QVGLNFELSF TGAPPYYYNT KIYKLENGER 

       670        680        690        700        710        720 
KLYDAKRYTS EGTRNRFSYS PPKEGNYEIV FDTVSNKLFT EPIKLEPVKE YTFKTSMRVK 

       730        740        750        760        770        780 
PSASLKLHHD LKLCLGDHSS VPVALKGQGP FTLTYDIIET FSSKRKTFEI KEIKTNEYVI 

       790        800        810        820        830        840 
KTPVFTTGGD YILSLVSIKD STGCVVGLSQ PDAKIQVRRD IPSAAFNFFE PIKEAKIKHG 

       850        860        870        880        890        900 
SVTEIPLKLS GEGPFTVKFK HMDYDGNIVK EFENKFQNSY KPALKVSKEG LYQLVDIRDS 

       910        920        930        940        950        960 
SCQGNVIYRN SLYKVSFLEK PKFAIQDNHH ITKVTENLFS KEEVCQGMEG TVDLALFGSP 

       970        980        990       1000       1010       1020 
PFILEYDLMA PNGHISTKKI QVATKYASLK LPNQIPGEYI TTIKAIFDGN YGESDIHFRE 

      1030       1040       1050       1060       1070       1080 
HQSELIIKQT VHPIPDVAFA DGGKTLRACA ANVDQISFLE PINLKFLQGE SPFSITFSVY 

      1090       1100       1110       1120       1130       1140 
HESTSRTDQY TIDNIDSENF SFEKLYEGMK LGNHAITIDS VVDANGCVNS LISGPRNQIL 

      1150       1160       1170       1180       1190       1200 
VSITDAPKIH ILDPSTEYCV GDYVAYQLNG VAPFMIKYEF NGIPLKSKER SSQFVRLASE 

      1210       1220       1230       1240       1250       1260 
PGIISITSLQ DSSSQCIVDF TNPKLKSEFD DLSLNIHPIP SVTVSQGNYV TEDIREGDQA 

      1270       1280       1290       1300       1310       1320 
EVIFSFEGTP PFSLTYVRTE ETDGKHGKRR SQVVETHKVT DIYSHEYKVI TSLQGTYEAI 

      1330 
EITDAYCFAK NDLFFNN 

« Hide

References

« Hide 'large scale' references
[1]"POM152 is an integral protein of the pore membrane domain of the yeast nuclear envelope."
Wozniak R.W., Blobel G., Rout M.P.
J. Cell Biol. 125:31-42(1994) [PubMed: 8138573] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION, REPEATS.
Strain: ATCC 200060 / W303.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed: 9169872] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"The yeast nucleoporin Nup188p interacts genetically and physically with the core structures of the nuclear pore complex."
Nehrbass U., Rout M.P., Maguire S., Blobel G., Wozniak R.W.
J. Cell Biol. 133:1153-1162(1996) [PubMed: 8682855] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NUP188.
[5]"Topology and functional domains of the yeast pore membrane protein Pom152p."
Tcheperegine S.E., Marelli M., Wozniak R.W.
J. Biol. Chem. 274:5252-5258(1999) [PubMed: 9988776] [Abstract]
Cited for: FUNCTION, TOPOLOGY.
[6]"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: 10684247] [Abstract]
Cited for: CHARACTERIZATION, NPC SUBUNIT LOCATION.
[7]"A link between the synthesis of nucleoporins and the biogenesis of the nuclear envelope."
Marelli M., Lusk C.P., Chan H., Aitchison J.D., Wozniak R.W.
J. Cell Biol. 153:709-724(2001) [PubMed: 11352933] [Abstract]
Cited for: FUNCTION, DE NOVO NPC ASSEMBLY.
[8]"Peering through the pore: nuclear pore complex structure, assembly, and function."
Suntharalingam M., Wente S.R.
Dev. Cell 4:775-789(2003) [PubMed: 12791264] [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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]"Targets of the cyclin-dependent kinase Cdk1."
Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K., Shokat K.M., Morgan D.O.
Nature 425:859-864(2003) [PubMed: 14574415] [Abstract]
Cited for: PHOSPHORYLATION BY CDC28.
[11]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed: 16847258] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[12]"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: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, MASS SPECTROMETRY.
Strain: ADR376.
[13]"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: 17287358] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, MASS SPECTROMETRY.
[14]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, MASS SPECTROMETRY.
[15]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-787 AND SER-797, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z31592 Genomic DNA. Translation: CAA83469.1.
Z48622 Genomic DNA. Translation: CAA88554.1.
BK006946 Genomic DNA. Translation: DAA10026.1.
PIRA53824.
RefSeqNP_013848.1. NM_001182630.1.

3D structure databases

ProteinModelPortalP39685.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1520N.
IntActP39685. 5 interactions.
MINTMINT-389828.
STRINGP39685.

Protein family/group databases

TCDB9.A.14.1.1. nuclear pore complex (NPC) family.

Proteomic databases

PeptideAtlasP39685.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR129W; YMR129W; YMR129W.
GeneID855159.
KEGGsce:YMR129W.
NMPDRfig|4932.3.peg.4897.

Organism-specific databases

CYGDYMR129w.
SGDS000004736. POM152.

Phylogenomic databases

eggNOGfuNOG05029.
GeneTreeEFGT00050000003458.
HOGENOMHBG203438.
OMATPPFEFT.
OrthoDBEOG4GBBF8.

Gene expression databases

ArrayExpressP39685.
GenevestigatorP39685.
GermOnlineYMR129W. Saccharomyces cerevisiae.

Family and domain databases

ProtoNetSearch...

Other

NextBio978578.

Entry information

Entry namePO152_YEAST
AccessionPrimary (citable) accession number: P39685
Secondary accession number(s): D6VZV2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: December 14, 2011
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIII

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