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P37199

- NU155_RAT

UniProt

P37199 - NU155_RAT

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Protein
Nuclear pore complex protein Nup155
Gene
Nup155
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Essential component of nuclear pore complex. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport.

GO - Molecular functioni

  1. protein binding Source: RGD
  2. structural constituent of nuclear pore Source: InterPro

GO - Biological processi

  1. mRNA transport Source: UniProtKB-KW
  2. nucleocytoplasmic transport Source: InterPro
  3. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear pore complex protein Nup155
Alternative name(s):
155 kDa nucleoporin
Nucleoporin Nup155
P140
Gene namesi
Name:Nup155
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621199. Nup155.

Subcellular locationi

Nucleusnuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side
Note: In mitosis, assumes a diffuse cytoplasmic distribution probably as a monomer, before reversing back into a punctate nuclear surface localization at the end of mitosis.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. nuclear envelope Source: RGD
  3. nuclear membrane Source: UniProtKB-SubCell
  4. nuclear pore Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13901390Nuclear pore complex protein Nup155
PRO_0000204846Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi525 – 5251O-linked (GlcNAc)1 Publication

Post-translational modificationi

Phosphorylated. Phosphorylation and dephosphorylation may be important for the function of NUP155 and may play a role in the reversible disassembly of the nuclear pore complex during mitosis.
Disulfide-linked to NUP62. The the inner channel of the NPC has a different redox environment from the cytoplasm and allows the formation of interchain disulfide bonds between some nucleoporins, the significant increase of these linkages upon oxidative stress reduces the permeability of the NPC By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP37199.
PRIDEiP37199.

PTM databases

PhosphoSiteiP37199.

Expressioni

Gene expression databases

GenevestigatoriP37199.

Interactioni

Subunit structurei

Interacts with GLE1. Able to form a heterotrimer with GLE1 and NUPL2 in vitro By similarity. Forms a complex with NUP53, NUP93, NUP205 and lamin B.1 Publication

Protein-protein interaction databases

BioGridi250622. 1 interaction.
STRINGi10116.ENSRNOP00000019606.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi584 – 65471Pro-rich
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5308.
HOGENOMiHOG000043927.
HOVERGENiHBG052680.
KOiK14312.
PhylomeDBiP37199.

Family and domain databases

InterProiIPR007187. Nucleoporin_Nup133/Nup155_C.
IPR014908. Nucleoporin_Nup133/Nup155_N.
IPR004870. Nucleoporin_Nup155.
[Graphical view]
PANTHERiPTHR10350. PTHR10350. 1 hit.
PfamiPF03177. Nucleoporin_C. 1 hit.
PF08801. Nucleoporin_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37199-1 [UniParc]FASTAAdd to Basket

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MPSMLGSMMV ASTSAPSLQE ALENAGRLID RQLQEDRMYP DLSELLMVSA     50
PNSPTVSGMS DMDYPLQGPG LLSVPSLPEI STIRRVPLRL SWLNSLDTCS 100
VTAMMGVFPP ISRAWLTIDS DIFMWNYEDG GDLAYFDGLS ETILAVGLVK 150
PKAGIFQPHV RHLLVLATPV DIVILGLSYA NVQTGSGILN DSVCGGLQLL 200
PDPLYSLPTD NTYLLTITST DNGRIFLAGK DGCLYEVAYQ AEAGWFSQRC 250
RKINHSKSSL SFLVPSLLQF TFSEDDPIVQ IEIDNSRNIL YTRSEKGVIQ 300
VYDLGHDGQG MSRVASVSQN AIVCAAGNIA RTIDRSVFKP IVQIAVIENS 350
ESLDCQLLAV THAGVRLYFS TCPFRQPLAR PNTLTLVHVR LPPGFSASST 400
VEKPSKVHKA LYSKGILLMT ASENEDNDIL WCVNHDTFPF QKPMMETQMT 450
TRVDGHSWAL SAIDELKVDK IITPLNKDHI PITDSPVVVQ QHMLPPKKFV 500
LLSAQGSLMF HKLRPVDQLR HLLVSNVGGD GEEIERFFKL HQEDQACATC 550
LILACSTAAC DREVSAWATR AFFRYGGEAQ MRFPATLPTP SNVGPILGSP 600
MYSSSPVPTG SPYPNPSSLG TPSHGAQPPT MSTPMSAVGN PAMQAASLSG 650
LTGPEIVYSG KHNGICIYFS RIMGNIWDAS LVVERVFKSS NREITAIESS 700
VPIQLLESVL QELKGLQEFL DRNSQFSGGP LGNPNTTAKV QQRLLGVMRP 750
ENGNTQQMQQ ELQRKFHEAQ LSEKISLQAI QQLVRKSYQA LALWKLLCEH 800
QFTVIVGELQ KEFQEQLKIT TFKDLVIREK EVTGALIASL INCYIRDNAA 850
VDGISLHLQD TCPLLYSTDD AVCSKANELL QRSRQVQSKS ERERMLRESL 900
KEYQKISNQV DLPSVCAQYR QVRFYEGVVE LSLTAAEKKD PQGLGLHFYK 950
HGEPEEDVVG LQTFQERLNS YKCITDTLQE LVNQSKAAPQ SPSVPKKPGP 1000
PVLSSDPNML SNEEAGHHFE QMLKLAQRSK DELFSIALYN WLIQADLADK 1050
LLQIASPFLE PHLVRMAKVD QNRVRYMDLL WRYYEKNRSF SSAARVLSKL 1100
ADMHSTEISL QQRLEYIARA ILSAKSSTAI SSIAADGEFL HELEEKMEVA 1150
RIQLQIQETL QRQYSHHSSV QDAISQLDSE LMDITKLYGE FADPFKLAEC 1200
KLAIIHCAGY SDPILVHTLW QDIIEKELSD SVTLSSSDRM HALSLKLVLL 1250
GKIYAGTPRF FPLDFIVQFL EQQVCTLNWD VGFVIQTMNE IGVPLPRLLE 1300
VYDQLFKSRD PFWNRVKSPL HLLDCIHVLL TRYVENPSLV LNCERRRFTN 1350
LCLDAVCGYL VELQSMSSSV AVQAITGNFK SLQAKLERLH 1390
Length:1,390
Mass (Da):155,003
Last modified:October 1, 1994 - v1
Checksum:i1B51716043BF9CCF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z21780 mRNA. Translation: CAA79848.1.
PIRiA45455.
RefSeqiNP_446404.1. NM_053952.1.
UniGeneiRn.11328.

Genome annotation databases

GeneIDi117021.
KEGGirno:117021.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z21780 mRNA. Translation: CAA79848.1 .
PIRi A45455.
RefSeqi NP_446404.1. NM_053952.1.
UniGenei Rn.11328.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 250622. 1 interaction.
STRINGi 10116.ENSRNOP00000019606.

PTM databases

PhosphoSitei P37199.

Proteomic databases

PaxDbi P37199.
PRIDEi P37199.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 117021.
KEGGi rno:117021.

Organism-specific databases

CTDi 9631.
RGDi 621199. Nup155.

Phylogenomic databases

eggNOGi COG5308.
HOGENOMi HOG000043927.
HOVERGENi HBG052680.
KOi K14312.
PhylomeDBi P37199.

Miscellaneous databases

NextBioi 619775.
PROi P37199.

Gene expression databases

Genevestigatori P37199.

Family and domain databases

InterProi IPR007187. Nucleoporin_Nup133/Nup155_C.
IPR014908. Nucleoporin_Nup133/Nup155_N.
IPR004870. Nucleoporin_Nup155.
[Graphical view ]
PANTHERi PTHR10350. PTHR10350. 1 hit.
Pfami PF03177. Nucleoporin_C. 1 hit.
PF08801. Nucleoporin_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nup155 is a novel nuclear pore complex protein that contains neither repetitive sequence motifs nor reacts with WGA."
    Radu A., Blobel G., Wozniak R.W.
    J. Cell Biol. 121:1-9(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications."
    Wells L., Vosseller K., Cole R.N., Cronshaw J.M., Matunis M.J., Hart G.W.
    Mol. Cell. Proteomics 1:791-804(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-525.
  3. "Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex."
    Hawryluk-Gara L.A., Shibuya E.K., Wozniak R.W.
    Mol. Biol. Cell 16:2382-2394(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH LAMIN B; NUP53; NUP93 AND NUP155.

Entry informationi

Entry nameiNU155_RAT
AccessioniPrimary (citable) accession number: P37199
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 11, 2014
This is version 96 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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