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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. Could be essessential for embryogenesis (By similarity). Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport.By similarity

GO - Molecular functioni

  1. 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 1 Publication. Nucleus membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Nucleus membrane 1 Publication; Peripheral membrane protein 1 Publication; Nucleoplasmic side 1 Publication
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.

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. nuclear envelope Source: RGD
  3. nuclear pore Source: UniProtKB-KW
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 Nup155PRO_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).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.By similarity1 Publication

Protein-protein interaction databases

BioGridi250622. 1 interaction.
STRINGi10116.ENSRNOP00000019606.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5308.
HOGENOMiHOG000043927.
HOVERGENiHBG052680.
InParanoidiP37199.
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

« Hide

        10         20         30         40         50
MPSMLGSMMV ASTSAPSLQE ALENAGRLID RQLQEDRMYP DLSELLMVSA
60 70 80 90 100
PNSPTVSGMS DMDYPLQGPG LLSVPSLPEI STIRRVPLRL SWLNSLDTCS
110 120 130 140 150
VTAMMGVFPP ISRAWLTIDS DIFMWNYEDG GDLAYFDGLS ETILAVGLVK
160 170 180 190 200
PKAGIFQPHV RHLLVLATPV DIVILGLSYA NVQTGSGILN DSVCGGLQLL
210 220 230 240 250
PDPLYSLPTD NTYLLTITST DNGRIFLAGK DGCLYEVAYQ AEAGWFSQRC
260 270 280 290 300
RKINHSKSSL SFLVPSLLQF TFSEDDPIVQ IEIDNSRNIL YTRSEKGVIQ
310 320 330 340 350
VYDLGHDGQG MSRVASVSQN AIVCAAGNIA RTIDRSVFKP IVQIAVIENS
360 370 380 390 400
ESLDCQLLAV THAGVRLYFS TCPFRQPLAR PNTLTLVHVR LPPGFSASST
410 420 430 440 450
VEKPSKVHKA LYSKGILLMT ASENEDNDIL WCVNHDTFPF QKPMMETQMT
460 470 480 490 500
TRVDGHSWAL SAIDELKVDK IITPLNKDHI PITDSPVVVQ QHMLPPKKFV
510 520 530 540 550
LLSAQGSLMF HKLRPVDQLR HLLVSNVGGD GEEIERFFKL HQEDQACATC
560 570 580 590 600
LILACSTAAC DREVSAWATR AFFRYGGEAQ MRFPATLPTP SNVGPILGSP
610 620 630 640 650
MYSSSPVPTG SPYPNPSSLG TPSHGAQPPT MSTPMSAVGN PAMQAASLSG
660 670 680 690 700
LTGPEIVYSG KHNGICIYFS RIMGNIWDAS LVVERVFKSS NREITAIESS
710 720 730 740 750
VPIQLLESVL QELKGLQEFL DRNSQFSGGP LGNPNTTAKV QQRLLGVMRP
760 770 780 790 800
ENGNTQQMQQ ELQRKFHEAQ LSEKISLQAI QQLVRKSYQA LALWKLLCEH
810 820 830 840 850
QFTVIVGELQ KEFQEQLKIT TFKDLVIREK EVTGALIASL INCYIRDNAA
860 870 880 890 900
VDGISLHLQD TCPLLYSTDD AVCSKANELL QRSRQVQSKS ERERMLRESL
910 920 930 940 950
KEYQKISNQV DLPSVCAQYR QVRFYEGVVE LSLTAAEKKD PQGLGLHFYK
960 970 980 990 1000
HGEPEEDVVG LQTFQERLNS YKCITDTLQE LVNQSKAAPQ SPSVPKKPGP
1010 1020 1030 1040 1050
PVLSSDPNML SNEEAGHHFE QMLKLAQRSK DELFSIALYN WLIQADLADK
1060 1070 1080 1090 1100
LLQIASPFLE PHLVRMAKVD QNRVRYMDLL WRYYEKNRSF SSAARVLSKL
1110 1120 1130 1140 1150
ADMHSTEISL QQRLEYIARA ILSAKSSTAI SSIAADGEFL HELEEKMEVA
1160 1170 1180 1190 1200
RIQLQIQETL QRQYSHHSSV QDAISQLDSE LMDITKLYGE FADPFKLAEC
1210 1220 1230 1240 1250
KLAIIHCAGY SDPILVHTLW QDIIEKELSD SVTLSSSDRM HALSLKLVLL
1260 1270 1280 1290 1300
GKIYAGTPRF FPLDFIVQFL EQQVCTLNWD VGFVIQTMNE IGVPLPRLLE
1310 1320 1330 1340 1350
VYDQLFKSRD PFWNRVKSPL HLLDCIHVLL TRYVENPSLV LNCERRRFTN
1360 1370 1380 1390
LCLDAVCGYL VELQSMSSSV AVQAITGNFK SLQAKLERLH
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.
InParanoidi P37199.
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: October 29, 2014
This is version 98 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