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Protein

Nucleoporin POM152

Gene

POM152

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. POM152 is important for the de novo assembly of NPCs.3 Publications

GO - Molecular functioni

  • protein anchor Source: SGD
  • structural constituent of nuclear pore Source: SGD

GO - Biological processi

  • mRNA transport Source: UniProtKB-KW
  • nuclear pore organization Source: SGD
  • nucleocytoplasmic transport 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-32822-MONOMER.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin POM152
Alternative name(s):
Nuclear pore protein POM152
P150
Pore membrane protein POM152
Gene namesi
Name:POM152
Ordered Locus Names:YMR129W
ORF Names:YM9553.05
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR129W.
SGDiS000004736. POM152.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 110110Cytoplasmic2 PublicationsAdd
BLAST
Transmembranei111 – 13121HelicalSequence analysisAdd
BLAST
Topological domaini132 – 14817Perinuclear space2 PublicationsAdd
BLAST
Transmembranei149 – 16921HelicalSequence analysisAdd
BLAST
Topological domaini170 – 1723Cytoplasmic2 Publications
Transmembranei173 – 19321HelicalSequence analysisAdd
BLAST
Topological domaini194 – 13371144Perinuclear space1 Publication1 PublicationAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • nuclear envelope lumen Source: SGD
  • nuclear membrane Source: UniProtKB-SubCell
  • 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 – 13371337Nucleoporin POM152PRO_0000204910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei45 – 451PhosphoserineCombined sources
Modified residuei60 – 601PhosphoserineCombined sources
Glycosylationi280 – 2801N-linked (GlcNAc...)1 Publication

Post-translational modificationi

The N-terminus is blocked.
Phosphorylated by CDC28.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP39685.
PeptideAtlasiP39685.

PTM databases

iPTMnetiP39685.

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. Interacts with NUP188.1 Publication

GO - Molecular functioni

  • protein anchor Source: SGD

Protein-protein interaction databases

BioGridi35306. 89 interactions.
DIPiDIP-1520N.
IntActiP39685. 5 interactions.
MINTiMINT-389828.

Structurei

3D structure databases

ProteinModelPortaliP39685.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati390 – 4132411 PublicationAdd
BLAST
Repeati626 – 6502521 PublicationAdd
BLAST
Repeati732 – 7552431 PublicationAdd
BLAST
Repeati836 – 8592441 PublicationAdd
BLAST
Repeati943 – 9662451 PublicationAdd
BLAST
Repeati1058 – 10772061 PublicationAdd
BLAST
Repeati1157 – 11782271 PublicationAdd
BLAST
Repeati1253 – 12762481 PublicationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 175175Pore sideCuratedAdd
BLAST
Regioni196 – 13371142Cisternal sideCuratedAdd
BLAST
Regioni390 – 12768878 X 24 AA approximate repeatsAdd
BLAST

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000115596.
InParanoidiP39685.
KOiK18725.
OMAiIHECSGD.
OrthoDBiEOG7D2FNZ.

Sequencei

Sequence statusi: Complete.

P39685-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEHRYNVFND TPRGNHWMGS SVSGSPRPSY SSRPNVNTTR RFQYSDDEPA
60 70 80 90 100
EKIRPLRSRS FKSTESNISD EKSRISERDS KDRYINGDKK VDIYSLPLIS
110 120 130 140 150
TDVLEISKQR TFAVILFLII QCYKIYDLVI LKSGLPLSGL LFKNYRFNFI
160 170 180 190 200
SKYFIIDSFF LYVLPSFNIP RLTFKPWVVY LQILAMLLLN IFISSDHEFV
210 220 230 240 250
LISLIMTTWR KLYTKELSVT GSAINHHRIF DSSAHFKGAL TIKILPENTA
260 270 280 290 300
MFNPLHESYC LPMDTNLFKI NSIDVPIRIN STEEIEYIEL EYRDLYTNSV
310 320 330 340 350
ELRSLSKKDF KIIDNPKSFL KKDQSVLKSH SNDFEEGSTI RYLAVTLQDI
360 370 380 390 400
GFYQIKKIVD SKKLNLKIHQ SHLVVPYCPI ASITGTGSND RCIGDSDNVS
410 420 430 440 450
FEIQGVPPMK LAYSKIVNGQ TFSYVDSSLQ PEYFESPLQS SKSKQSFTQG
460 470 480 490 500
ELNDLKWGRN QPVNINLDSS ITQDGKFAYK IDKITDGLGN VVDFTSLPEE
510 520 530 540 550
LKKRYDLSYN FNVHEVPRAA LEERFDPKSP TKRSIAIVFE EIKNWISDIP
560 570 580 590 600
YVISLSYTDA QDKSKKIMNV TTDSLTKVLQ ADLPGSYNLE YIESKFCPGE
610 620 630 640 650
IVGKSNVLVT MPVAPTMEVK SFPILDQCVG QVGLNFELSF TGAPPYYYNT
660 670 680 690 700
KIYKLENGER KLYDAKRYTS EGTRNRFSYS PPKEGNYEIV FDTVSNKLFT
710 720 730 740 750
EPIKLEPVKE YTFKTSMRVK PSASLKLHHD LKLCLGDHSS VPVALKGQGP
760 770 780 790 800
FTLTYDIIET FSSKRKTFEI KEIKTNEYVI KTPVFTTGGD YILSLVSIKD
810 820 830 840 850
STGCVVGLSQ PDAKIQVRRD IPSAAFNFFE PIKEAKIKHG SVTEIPLKLS
860 870 880 890 900
GEGPFTVKFK HMDYDGNIVK EFENKFQNSY KPALKVSKEG LYQLVDIRDS
910 920 930 940 950
SCQGNVIYRN SLYKVSFLEK PKFAIQDNHH ITKVTENLFS KEEVCQGMEG
960 970 980 990 1000
TVDLALFGSP PFILEYDLMA PNGHISTKKI QVATKYASLK LPNQIPGEYI
1010 1020 1030 1040 1050
TTIKAIFDGN YGESDIHFRE HQSELIIKQT VHPIPDVAFA DGGKTLRACA
1060 1070 1080 1090 1100
ANVDQISFLE PINLKFLQGE SPFSITFSVY HESTSRTDQY TIDNIDSENF
1110 1120 1130 1140 1150
SFEKLYEGMK LGNHAITIDS VVDANGCVNS LISGPRNQIL VSITDAPKIH
1160 1170 1180 1190 1200
ILDPSTEYCV GDYVAYQLNG VAPFMIKYEF NGIPLKSKER SSQFVRLASE
1210 1220 1230 1240 1250
PGIISITSLQ DSSSQCIVDF TNPKLKSEFD DLSLNIHPIP SVTVSQGNYV
1260 1270 1280 1290 1300
TEDIREGDQA EVIFSFEGTP PFSLTYVRTE ETDGKHGKRR SQVVETHKVT
1310 1320 1330
DIYSHEYKVI TSLQGTYEAI EITDAYCFAK NDLFFNN
Length:1,337
Mass (Da):151,653
Last modified:February 1, 1995 - v1
Checksum:iA024A42069193898
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z31592 Genomic DNA. Translation: CAA83469.1.
Z48622 Genomic DNA. Translation: CAA88554.1.
BK006946 Genomic DNA. Translation: DAA10026.1.
PIRiA53824.
RefSeqiNP_013848.1. NM_001182630.1.

Genome annotation databases

EnsemblFungiiYMR129W; YMR129W; YMR129W.
GeneIDi855159.
KEGGisce:YMR129W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z31592 Genomic DNA. Translation: CAA83469.1.
Z48622 Genomic DNA. Translation: CAA88554.1.
BK006946 Genomic DNA. Translation: DAA10026.1.
PIRiA53824.
RefSeqiNP_013848.1. NM_001182630.1.

3D structure databases

ProteinModelPortaliP39685.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35306. 89 interactions.
DIPiDIP-1520N.
IntActiP39685. 5 interactions.
MINTiMINT-389828.

Protein family/group databases

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

PTM databases

iPTMnetiP39685.

Proteomic databases

MaxQBiP39685.
PeptideAtlasiP39685.

Protocols and materials databases

DNASUi855159.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR129W; YMR129W; YMR129W.
GeneIDi855159.
KEGGisce:YMR129W.

Organism-specific databases

EuPathDBiFungiDB:YMR129W.
SGDiS000004736. POM152.

Phylogenomic databases

HOGENOMiHOG000115596.
InParanoidiP39685.
KOiK18725.
OMAiIHECSGD.
OrthoDBiEOG7D2FNZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-32822-MONOMER.

Miscellaneous databases

NextBioi978578.
PROiP39685.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION, REPEATS.
    Strain: ATCC 200060 / W303.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-45, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPO152_YEAST
AccessioniPrimary (citable) accession number: P39685
Secondary accession number(s): D6VZV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3410 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

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 one 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.