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Protein

Nuclear pore complex protein Nup155

Gene

Nup155

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

  • atrial cardiac muscle cell action potential Source: MGI
  • mRNA export from nucleus Source: MGI
  • nuclear envelope organization Source: MGI
  • protein import into nucleus Source: MGI
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

ReactomeiR-MMU-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-MMU-4570464. SUMOylation of RNA binding proteins.
R-MMU-4615885. SUMOylation of DNA replication proteins.
R-MMU-5578749. Transcriptional regulation by small RNAs.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear pore complex protein Nup155
Alternative name(s):
155 kDa nucleoporin
Nucleoporin Nup155
Gene namesi
Name:Nup155
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:2181182. Nup155.

Subcellular locationi

  • Nucleusnuclear pore complex By similarity
  • Nucleus membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Nucleus membrane By similarity; Peripheral membrane protein By similarity; Nucleoplasmic side By similarity

  • 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.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Disruption phenotypei

Homozygous null mice die before embryonic day 8.5.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 13911390Nuclear pore complex protein Nup155PRO_0000204845Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi526 – 5261O-linked (GlcNAc)By similarity

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 (By similarity).By similarity
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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ99P88.
MaxQBiQ99P88.
PaxDbiQ99P88.
PRIDEiQ99P88.

PTM databases

iPTMnetiQ99P88.
PhosphoSiteiQ99P88.
SwissPalmiQ99P88.

Expressioni

Gene expression databases

BgeeiQ99P88.
CleanExiMM_NUP155.
GenevisibleiQ99P88. MM.

Interactioni

Subunit structurei

Interacts with GLE1 and NUP35/NUP53. Able to form a heterotrimer with GLE1 and NUPL2 in vitro (By similarity). Forms a complex with NUP53, NUP93, NUP205 and lamin B (By similarity).By similarity

Protein-protein interaction databases

BioGridi228424. 25 interactions.
IntActiQ99P88. 24 interactions.
MINTiMINT-4104214.
STRINGi10090.ENSMUSP00000128819.

Structurei

3D structure databases

ProteinModelPortaliQ99P88.
SMRiQ99P88. Positions 89-598, 893-1311.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi585 – 65571Pro-richAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1900. Eukaryota.
COG5308. LUCA.
GeneTreeiENSGT00390000016532.
HOVERGENiHBG052680.
InParanoidiQ99P88.
KOiK14312.
OMAiDRCFPDL.
OrthoDBiEOG7JQBMH.
PhylomeDBiQ99P88.
TreeFamiTF105951.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99P88-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSVLGSMMV ASTSAAASLQ EALENAGRLI DRQLQEDRMY PDLSELLMVS
60 70 80 90 100
APNSPTVSGM SDMDYPLQGP GLLSVPSLPE ISTIRRVPLP PELVEQFGHM
110 120 130 140 150
QCNCMMGVFP PISRAWLTID SDIFMWNYED GGDLAYFDGL SETILAVGLV
160 170 180 190 200
KPKAGIFQPH VRHLLVLATP VDIVILGLSY ANVQTGSGIL NDSMCGGMQL
210 220 230 240 250
LPDPLYSLPT DNTYLLTITS TDNGRIFLAG KDGCLYEVAY QAEAGWFSQR
260 270 280 290 300
CRKINHSKSS LSFLVPSLLQ FTFSEDDPIV QIEIDNSRNI LYTRSEKGVI
310 320 330 340 350
QVYDLGHDGQ GMSRVASVSQ NAIVSAAGNI ARTIDRSVFK PIVQIAVIES
360 370 380 390 400
SESLDCQLLA VTHAGVRLYF STCPFRQPLA RPNTLTLVHV RLPPGFSASS
410 420 430 440 450
TVEKPSKVHK ALYSKGILLM TASENEDNDI LWCVNHDTFP FQKPMMETQM
460 470 480 490 500
TTRVDGHSWA LSAIDELKVD KIITPLNKDH IPITDSPVVV QQHMLPPKKF
510 520 530 540 550
VLLSAQGSLM FHKLRPVDQL RHLLVSNVGG DGEEIERFFK LHQEDQACAT
560 570 580 590 600
CLILACSTAA CDREVSAWAT RAFFRYGGEA QMRFPATLPT PSNVGPILGS
610 620 630 640 650
PMYSSSPVPS GSPYPNPSSL GTPSHGAQPP TMSTPMCAVG SPAMQAASMS
660 670 680 690 700
GLTGPEIVYS GKHNGICIYF SRIMGNIWDA SLVVERVFKS SNREITAIES
710 720 730 740 750
SVPVQLLESV LQELKGLQEF LDRNSQFSGG PLGNPNTTAR VQQRLVGFMR
760 770 780 790 800
PENGNTQQMQ QELQRKFQEA QLSEKISLQA IQQLVRKSYQ ALALWKLLCE
810 820 830 840 850
HQFSVIVGEL QKEFQEQLKI TTFKDLVIRD KEVTGALIAS LINCYIRDNA
860 870 880 890 900
AVDGISLHLQ DTCPLLYSTD DAVCSKANEL LQRSRQVQSK TERERMLRES
910 920 930 940 950
LKEYQKISNQ VDLPSVCAQY RQVRFYEGVV ELSLTAAEKK DPQGLGLHFY
960 970 980 990 1000
KHGEPEEDVV GLQTFQERLN SYKCITDTLQ ELVNQSKAAP QSPSVPKKPG
1010 1020 1030 1040 1050
PPVLSSDPNM LSNEEAGHHF EQMLKLAQRS KDELFSIALY NWLIQADLAD
1060 1070 1080 1090 1100
KLLQIASPFL EPHLVRMARV DQNRVRYMDL LWRYYEKNRS FSSAARVLSK
1110 1120 1130 1140 1150
LADMHSTEIS LQQRLEYIAR AILSAKSSTA ISSIAADGEF LHELEEKMEV
1160 1170 1180 1190 1200
ARIQLQIQET LQRQYSHHSS VQDAISQLDS ELMDITKLYG EFADPFKLAE
1210 1220 1230 1240 1250
CKLAVIHCAG YSDPILVHTL WQDIIEKELN DSVALSSSDR MHALSLKLVL
1260 1270 1280 1290 1300
LGKIYAGTPR FFPLDFIVQF LEQQVCTLNW DVGFVIQTMN EIGVPLPRLL
1310 1320 1330 1340 1350
EVYDQLFKSR DPFWNRVKSP LHLLDCIHVL LTRYVENPSL VLNCERRRFT
1360 1370 1380 1390
NLCLDAVCGY LVELQSMSSS VAVQAITGNF KSLQAKLERL H
Length:1,391
Mass (Da):155,118
Last modified:June 1, 2001 - v1
Checksum:iA8F9BE2E25653F32
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF322375 mRNA. Translation: AAK11317.1.
CCDSiCCDS37034.1.
RefSeqiNP_573490.3. NM_133227.3.
UniGeneiMm.295168.

Genome annotation databases

EnsembliENSMUST00000163765; ENSMUSP00000128819; ENSMUSG00000022142.
GeneIDi170762.
KEGGimmu:170762.
UCSCiuc007vei.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF322375 mRNA. Translation: AAK11317.1.
CCDSiCCDS37034.1.
RefSeqiNP_573490.3. NM_133227.3.
UniGeneiMm.295168.

3D structure databases

ProteinModelPortaliQ99P88.
SMRiQ99P88. Positions 89-598, 893-1311.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228424. 25 interactions.
IntActiQ99P88. 24 interactions.
MINTiMINT-4104214.
STRINGi10090.ENSMUSP00000128819.

PTM databases

iPTMnetiQ99P88.
PhosphoSiteiQ99P88.
SwissPalmiQ99P88.

Proteomic databases

EPDiQ99P88.
MaxQBiQ99P88.
PaxDbiQ99P88.
PRIDEiQ99P88.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000163765; ENSMUSP00000128819; ENSMUSG00000022142.
GeneIDi170762.
KEGGimmu:170762.
UCSCiuc007vei.1. mouse.

Organism-specific databases

CTDi9631.
MGIiMGI:2181182. Nup155.

Phylogenomic databases

eggNOGiKOG1900. Eukaryota.
COG5308. LUCA.
GeneTreeiENSGT00390000016532.
HOVERGENiHBG052680.
InParanoidiQ99P88.
KOiK14312.
OMAiDRCFPDL.
OrthoDBiEOG7JQBMH.
PhylomeDBiQ99P88.
TreeFamiTF105951.

Enzyme and pathway databases

ReactomeiR-MMU-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-MMU-4570464. SUMOylation of RNA binding proteins.
R-MMU-4615885. SUMOylation of DNA replication proteins.
R-MMU-5578749. Transcriptional regulation by small RNAs.

Miscellaneous databases

NextBioi370370.
PROiQ99P88.
SOURCEiSearch...

Gene expression databases

BgeeiQ99P88.
CleanExiMM_NUP155.
GenevisibleiQ99P88. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genomic organization, alternative splicing and comparative analysis of the human nucleoporin 155 (NUP155) gene."
    Zhang X., Li Z., Yang H., Bolund L.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Mutation in nuclear pore component NUP155 leads to atrial fibrillation and early sudden cardiac death."
    Zhang X., Chen S., Yoo S., Chakrabarti S., Zhang T., Ke T., Oberti C., Yong S.L., Fang F., Li L., de la Fuente R., Wang L., Chen Q., Wang Q.K.
    Cell 135:1017-1027(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "Intermolecular disulfide bonds between nucleoporins regulate karyopherin-dependent nuclear transport."
    Yoshimura S.H., Otsuka S., Kumeta M., Taga M., Takeyasu K.
    J. Cell Sci. 126:3141-3150(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BOND.

Entry informationi

Entry nameiNU155_MOUSE
AccessioniPrimary (citable) accession number: Q99P88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: June 1, 2001
Last modified: April 13, 2016
This is version 121 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.