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Protein

Nuclear envelope pore membrane protein POM 121

Gene

Pom121

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL).

GO - Molecular functioni

  • structural constituent of nuclear pore Source: RGD

GO - Biological processi

  • mRNA transport Source: UniProtKB-KW
  • nuclear pore organization Source: RGD
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear envelope pore membrane protein POM 121
Alternative name(s):
Nucleoporin Nup121
Pore membrane protein of 121 kDa
p145
Gene namesi
Name:Pom121
Synonyms:Nup121
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620680. Pom121.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei57 – 7721HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi531 – 5311D → A: Abolishes cleavage. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11991199Nuclear envelope pore membrane protein POM 121PRO_0000204908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei83 – 831PhosphoserineBy similarity
Modified residuei244 – 2441PhosphoserineBy similarity
Modified residuei319 – 3191PhosphoserineBy similarity
Modified residuei322 – 3221PhosphoserineBy similarity
Modified residuei325 – 3251PhosphoserineBy similarity
Modified residuei345 – 3451PhosphoserineBy similarity
Modified residuei355 – 3551PhosphoserineCombined sources
Modified residuei367 – 3671PhosphoserineBy similarity
Modified residuei370 – 3701PhosphoserineBy similarity
Modified residuei408 – 4081PhosphoserineBy similarity
Modified residuei409 – 4091PhosphoserineBy similarity
Modified residuei412 – 4121PhosphoserineBy similarity
Modified residuei413 – 4131PhosphoserineBy similarity
Modified residuei416 – 4161PhosphoserineBy similarity
Modified residuei417 – 4171PhosphoserineBy similarity

Post-translational modificationi

Proteolytically cleaved by caspase-3 during apoptosis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei531 – 5322Cleavage; by caspase-3

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP52591.
PRIDEiP52591.

PTM databases

iPTMnetiP52591.
PhosphoSiteiP52591.

Miscellaneous databases

PMAP-CutDBP52591.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001968.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YI0X-ray1.81A291-320[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 5656Cisternal sideSequence analysisAdd
BLAST
Regioni76 – 11991124Pore sideSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 85Poly-Ala
Compositional biasi53 – 586Poly-Ala
Compositional biasi438 – 4414Poly-Ser
Compositional biasi497 – 5004Poly-Pro
Compositional biasi684 – 6874Poly-Ser
Compositional biasi1023 – 10264Poly-Ala
Compositional biasi1033 – 10386Poly-Ser
Compositional biasi1058 – 10636Poly-Gly

Domaini

Contains F-X-F-G repeats.

Sequence similaritiesi

Belongs to the POM121 family.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IM0V. Eukaryota.
ENOG4112BJY. LUCA.
HOGENOMiHOG000015364.
HOVERGENiHBG053628.
InParanoidiP52591.
KOiK14316.
PhylomeDBiP52591.

Family and domain databases

InterProiIPR026090. POM121.
[Graphical view]
PANTHERiPTHR23193:SF5. PTHR23193:SF5. 1 hit.

Sequencei

Sequence statusi: Complete.

P52591-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPAAAAADG GERRRPPLGV REGRGRTRGC GGPAGAAALG LALLGLALYL
60 70 80 90 100
VPAAAALAWL AVGASAAWWG LSREPRGPRG LSSFVRESRR HPRPALTASP
110 120 130 140 150
LPAKSPVNGS LCEPRSPLGG PDPAELLLMG SYLGKPGPPE PALPQDPRDR
160 170 180 190 200
PGRRPPSRSP PSSSTAQRVH HVYPALPTPL LRPSRRPPHR DCGPLSSRFV
210 220 230 240 250
ITPRRRYPIQ QAQYSLLGAL PTVCWNGGHK KAVLSARNSR MVCSPVTVRI
260 270 280 290 300
APPDSKLFRS PMPEQILSTT LSSPSSNAPD PCAKETVLNA LKEKKKRTVA
310 320 330 340 350
EEDQLHLDGQ ENKRRRHDSS GSGHSAFEPL VANGVPAAFV PKPGSLKRSL
360 370 380 390 400
ASQSSDDHLN KRSRTSSVSS LTSTCTGGIP SSSRNAITSS YSSTRGVSQL
410 420 430 440 450
WKRSGPTSSP FSSPASSRSQ TPERPAKKTR EEEPCHQSSS SAPLVTDKES
460 470 480 490 500
PGEKVTDPAT GKQQSLWTSP PTPGSSGQRK RKIQLLPSRR GDQLTLPPPP
510 520 530 540 550
ELGYSITAED LDMERRASLQ WFNKVLEDKT DDASTPATDT SPATSPPFTL
560 570 580 590 600
TLPTVGPAAS PASLPAPSSN PLLESLKKMQ ESPAPSSSEP PEAATVAAPS
610 620 630 640 650
PPKTPSLLAP LVSPLTGPLA STSSDSKPTT TFLGLASASS ATPLTDTKAP
660 670 680 690 700
GVSQAQLCVS TPAATAPSPT PASTLFGMLS PPASSSSLAT PGPACASPMF
710 720 730 740 750
KPIFPATPKS ESDNPLPTSS SAATTTPAST ALPTTATATA HTFKPIFESV
760 770 780 790 800
EPFAAMPLSP PFSLKQTTAP ATTAATSAPL LTGLGTATST VATGTTASAS
810 820 830 840 850
KPVFGFGVTT AASTASTIAS TSQSILFGGA PPVTASSSAP ALASIFQFGK
860 870 880 890 900
PLAPAASVAG TSFSQSLASS AQTAASNSSG GFSGFGGTLT TSTSAPATTS
910 920 930 940 950
QPTLTFSNTV TPTFNIPFSA SAKPALPTYP GANSQPTFGA TDGATKPALA
960 970 980 990 1000
PSFGSSFTFG NSVASAPSAA PAPAAFGGAA QPAFGGLKAS ASTFGTPAST
1010 1020 1030 1040 1050
QPAFGSTTSV FSFGSATTSG FGAAAATTQT THSGSSSSLF GSSTPSPFTF
1060 1070 1080 1090 1100
GGSAAPAGGG GFGLSATPGT GSTSGTFSFG SGQSGTTGTT TSFGGSLSQN
1110 1120 1130 1140 1150
TLGAPSQSSP FAFSVGSTPE SKPVFGGTST PTFGQSAPAP GVGTTGSSLS
1160 1170 1180 1190
FGAPSTPAQG FVGVGPFGSG APSFSIGAGS KTPGARQRLQ ARRQHTRKK
Length:1,199
Mass (Da):120,785
Last modified:October 1, 1996 - v1
Checksum:i6DC4451B91D5B907
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z21513 mRNA. Translation: CAA79725.1.
Z21514 Genomic DNA. Translation: CAA79726.1.
PIRiA40670.
RefSeqiNP_446074.1. NM_053622.1.
UniGeneiRn.10474.

Genome annotation databases

GeneIDi113975.
KEGGirno:113975.
UCSCiRGD:620680. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z21513 mRNA. Translation: CAA79725.1.
Z21514 Genomic DNA. Translation: CAA79726.1.
PIRiA40670.
RefSeqiNP_446074.1. NM_053622.1.
UniGeneiRn.10474.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YI0X-ray1.81A291-320[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001968.

PTM databases

iPTMnetiP52591.
PhosphoSiteiP52591.

Proteomic databases

PaxDbiP52591.
PRIDEiP52591.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi113975.
KEGGirno:113975.
UCSCiRGD:620680. rat.

Organism-specific databases

CTDi9883.
RGDi620680. Pom121.

Phylogenomic databases

eggNOGiENOG410IM0V. Eukaryota.
ENOG4112BJY. LUCA.
HOGENOMiHOG000015364.
HOVERGENiHBG053628.
InParanoidiP52591.
KOiK14316.
PhylomeDBiP52591.

Miscellaneous databases

PMAP-CutDBP52591.
PROiP52591.

Family and domain databases

InterProiIPR026090. POM121.
[Graphical view]
PANTHERiPTHR23193:SF5. PTHR23193:SF5. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region."
    Hallberg E., Wozniak R.W., Blobel G.
    J. Cell Biol. 122:513-521(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. Lubec G., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 250-256; 365-384 AND 578-603, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. "Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells."
    Daigle N., Beaudouin J., Hartnell L., Imreh G., Hallberg E., Lippincott-Schwartz J., Ellenberg J.
    J. Cell Biol. 154:71-84(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  4. "Correlation between nucleocytoplasmic transport and caspase-3-dependent dismantling of nuclear pores during apoptosis."
    Kihlmark M., Rustum C., Eriksson C., Beckman M., Iverfeldt K., Hallberg E.
    Exp. Cell Res. 293:346-356(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-531.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPO121_RAT
AccessioniPrimary (citable) accession number: P52591
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.