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Protein

Nucleoporin p58/p45

Gene

Nup58

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

Functioni

Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane.By similarity

GO - Molecular functioni

GO - Biological processi

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:
Nucleoporin p58/p45Curated
Alternative name(s):
58 kDa nucleoporinBy similarity
Nucleoporin-like protein 1
Gene namesi
Name:Nup58By similarity
Synonyms:Nupl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1919094. Nupl1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 587587Nucleoporin p58/p45PRO_0000204893Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei319 – 3191PhosphothreonineBy similarity

Post-translational modificationi

O-glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ8R332.
MaxQBiQ8R332.
PaxDbiQ8R332.
PRIDEiQ8R332.

PTM databases

iPTMnetiQ8R332.
PhosphoSiteiQ8R332.

Expressioni

Gene expression databases

BgeeiQ8R332.
CleanExiMM_NUPL1.
GenevisibleiQ8R332. MM.

Interactioni

Subunit structurei

Component of the p62 complex, a complex at least composed of NUP62, NUP54, and NUP58. Interacts with NUTF2. Interacts with SRP1-alpha and Importin p97 proteins when they are together, but not with SRP1-alpha protein alone (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Mapk1P630853EBI-646962,EBI-397697

Protein-protein interaction databases

IntActiQ8R332. 3 interactions.
MINTiMINT-4104404.
STRINGi10090.ENSMUSP00000038716.

Structurei

3D structure databases

ProteinModelPortaliQ8R332.
SMRiQ8R332. Positions 238-415.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati7 – 821
Repeati30 – 3122
Repeati44 – 4523
Repeati63 – 6424
Repeati68 – 6925
Repeati476 – 47726
Repeati480 – 48127
Repeati501 – 50228
Repeati507 – 50829
Repeati517 – 518210
Repeati519 – 520211
Repeati533 – 534212
Repeati556 – 557213
Repeati566 – 567214

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 56756114 X 2 AA repeats of F-GAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili244 – 26421Sequence analysisAdd
BLAST
Coiled coili302 – 36968Sequence analysisAdd
BLAST

Domaini

Contains FG repeats.

Sequence similaritiesi

Belongs to the NUP58 family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG410IIR3. Eukaryota.
ENOG410ZJAM. LUCA.
GeneTreeiENSGT00730000111111.
HOGENOMiHOG000273874.
HOVERGENiHBG052703.
InParanoidiQ8R332.
KOiK14307.
OMAiSKVQDDI.
OrthoDBiEOG7H1JN7.
PhylomeDBiQ8R332.
TreeFamiTF106502.

Family and domain databases

InterProiIPR024882. Nucleoporin_p58/p45.
[Graphical view]
PANTHERiPTHR13437. PTHR13437. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8R332-1) [UniParc]FASTAAdd to basket

Also known as: p58

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATGFSFGSG TLGSTTVAPG GTGAGSGFSF GTVASSTPSV GLNFGSLGSS
60 70 80 90 100
VTPASTSASA GGFGTGLFGS KPATGFTLGG TSAGTAATTS ASTTGFSLGF
110 120 130 140 150
SKPAASATPF ALPVTSTSAS GLTLSSALTS TPAASTGFTL NNLGATPATT
160 170 180 190 200
TTASTGLSLG GALAGLGGSL FQSGNTATSG LGQNALSLSL GTTAPTSAAS
210 220 230 240 250
NEGLGGIDFS TSSDKKSDKT GTRPEDSKAL KDENLPPVIC QDVENLQKFV
260 270 280 290 300
KEQKQVQEEI SRMSSKAMLK VQEDIKALKQ LLSLAASGLQ RNTLNIDKLK
310 320 330 340 350
LETAQELKNA EIALRTQKTP PGLQHENTAP ADYFRILVQQ FEVQLQQYRQ
360 370 380 390 400
QIEELENHLA TQASNSHITP QDLSMAMQKI YQTFVALAAQ LQSIHENVKV
410 420 430 440 450
LKEQYLGYRK MFLGDAVDVF EARRTEAKKW QNAPRVTTGP TPFSTMPNAA
460 470 480 490 500
AVAMAATLTQ QQQPATGPQP SLGVSFGTPF GSGIGTGLQS SGLGSSNLGG
510 520 530 540 550
FGTSSGFGCG TTGASTFGFG TTDKPSGSLS AGFGSSSTSG FNFSNPGITA
560 570 580
SAGLTFGVSN PASAGFGTGG QLLQLKRPPA GNKRGKR
Length:587
Mass (Da):59,445
Last modified:June 1, 2002 - v1
Checksum:i697E22078331BF0A
GO
Isoform 2 (identifier: Q8R332-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     533-587: FGSSSTSGFN...PPAGNKRGKR → QKSHVLTGFRKPSVMETNELGRKIQF

Note: No experimental confirmation available.
Show »
Length:558
Mass (Da):57,020
Checksum:i8FCD7AFB782EC2C9
GO
Isoform 3 (identifier: Q8R332-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     533-587: FGSSSTSGFNFSNPGITASAGLTFGVSNPASAGFGTGGQLLQLKRPPAGNKRGKR → LCASA

Note: No experimental confirmation available.
Show »
Length:537
Mass (Da):54,452
Checksum:iE09C0B801C2B37BB
GO
Isoform 4 (identifier: Q8R332-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     533-587: Missing.

Note: No experimental confirmation available.
Show »
Length:532
Mass (Da):54,006
Checksum:i2B37BBEB0F3C160C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551S → Y in BAC26564 (PubMed:16141072).Curated
Sequence conflicti78 – 781L → V in BAC26564 (PubMed:16141072).Curated
Sequence conflicti117 – 1171T → A in BAC39663 (PubMed:16141072).Curated
Sequence conflicti143 – 1431L → F in BAC37200 (PubMed:16141072).Curated
Sequence conflicti513 – 5131G → E in BAC26564 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei533 – 58755FGSSS…KRGKR → QKSHVLTGFRKPSVMETNEL GRKIQF in isoform 2. 1 PublicationVSP_008573Add
BLAST
Alternative sequencei533 – 58755FGSSS…KRGKR → LCASA in isoform 3. 1 PublicationVSP_008574Add
BLAST
Alternative sequencei533 – 58755Missing in isoform 4. 1 PublicationVSP_008575Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029688 mRNA. Translation: BAC26564.1.
AK078279 mRNA. Translation: BAC37200.1.
AK086412 mRNA. Translation: BAC39663.1.
AK146477 mRNA. Translation: BAE27201.1.
BC026743 mRNA. Translation: AAH26743.1.
CCDSiCCDS27175.1. [Q8R332-1]
RefSeqiNP_733479.1. NM_170591.1. [Q8R332-1]
XP_006519650.1. XM_006519587.1. [Q8R332-2]
UniGeneiMm.258051.

Genome annotation databases

EnsembliENSMUST00000041905; ENSMUSP00000038716; ENSMUSG00000063895. [Q8R332-1]
GeneIDi71844.
KEGGimmu:71844.
UCSCiuc007uex.1. mouse. [Q8R332-2]
uc007uey.1. mouse. [Q8R332-3]
uc007uez.1. mouse. [Q8R332-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029688 mRNA. Translation: BAC26564.1.
AK078279 mRNA. Translation: BAC37200.1.
AK086412 mRNA. Translation: BAC39663.1.
AK146477 mRNA. Translation: BAE27201.1.
BC026743 mRNA. Translation: AAH26743.1.
CCDSiCCDS27175.1. [Q8R332-1]
RefSeqiNP_733479.1. NM_170591.1. [Q8R332-1]
XP_006519650.1. XM_006519587.1. [Q8R332-2]
UniGeneiMm.258051.

3D structure databases

ProteinModelPortaliQ8R332.
SMRiQ8R332. Positions 238-415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R332. 3 interactions.
MINTiMINT-4104404.
STRINGi10090.ENSMUSP00000038716.

PTM databases

iPTMnetiQ8R332.
PhosphoSiteiQ8R332.

Proteomic databases

EPDiQ8R332.
MaxQBiQ8R332.
PaxDbiQ8R332.
PRIDEiQ8R332.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041905; ENSMUSP00000038716; ENSMUSG00000063895. [Q8R332-1]
GeneIDi71844.
KEGGimmu:71844.
UCSCiuc007uex.1. mouse. [Q8R332-2]
uc007uey.1. mouse. [Q8R332-3]
uc007uez.1. mouse. [Q8R332-1]

Organism-specific databases

CTDi71844.
MGIiMGI:1919094. Nupl1.

Phylogenomic databases

eggNOGiENOG410IIR3. Eukaryota.
ENOG410ZJAM. LUCA.
GeneTreeiENSGT00730000111111.
HOGENOMiHOG000273874.
HOVERGENiHBG052703.
InParanoidiQ8R332.
KOiK14307.
OMAiSKVQDDI.
OrthoDBiEOG7H1JN7.
PhylomeDBiQ8R332.
TreeFamiTF106502.

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

NextBioi334706.
PROiQ8R332.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R332.
CleanExiMM_NUPL1.
GenevisibleiQ8R332. MM.

Family and domain databases

InterProiIPR024882. Nucleoporin_p58/p45.
[Graphical view]
PANTHERiPTHR13437. PTHR13437. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Heart, Olfactory bulb and Testis.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.

Entry informationi

Entry nameiNUP58_MOUSE
AccessioniPrimary (citable) accession number: Q8R332
Secondary accession number(s): Q3UJF4
, Q8BUA7, Q8BVG7, Q8C0W3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: June 1, 2002
Last modified: March 16, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

In rat, the p62 complex contains two different isoforms of NUP58. Isoform p45 has however not been isolated in mouse so far.

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.