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Q9JIH2 (NUP50_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear pore complex protein Nup50
Alternative name(s):
50 kDa nucleoporin
Nuclear pore-associated protein 60 kDa-like
Nucleoporin Nup50
Gene names
Name:Nup50
Synonyms:Npap60
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the nuclear pore complex that has a direct role in nuclear protein import. Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta-cargo complex and importin recycling. Interacts with multiple transport receptor proteins including CDKN1B. This interaction is required for correct intracellular transport and degradation of CDKN1B. Ref.6

Subunit structure

Does not interact with TPR By similarity. Interacts with Importin alpha-2, Importin beta, Importin beta-2, NUP153, Ran binding protein 7, CDKN1B and itself.

Subcellular location

Nucleusnuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side By similarity. Note: Localizes to the nucleoplasmic fibrils of the nuclear pore complex. Dissociates from the NPC structure early during prophase of mitosis. Associates to the newly formed nuclear membrane during telophase By similarity.

Tissue specificity

Widely expressed at low levels. Highest in the developing neural tube and adult testes.

Domain

Contains FG repeats.

Involvement in disease

Defects in Nup50 are the cause of neural tube defects, exencephaly and intrauterine growth retardation.

Sequence similarities

Contains 1 RanBD1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Nuclear pore complex protein Nup50
PRO_0000204869

Regions

Repeat76 – 7721
Repeat112 – 11322
Repeat225 – 22623
Repeat271 – 27224
Repeat301 – 30225
Domain333 – 466134RanBD1
Region76 – 3022275 X 2 AA repeats of F-G
Region143 – 20563Binding to CDKN1B
Compositional bias55 – 9036Gly-rich
Compositional bias266 – 32964Ser-rich

Amino acid modifications

Modified residue81N6-acetyllysine Ref.5
Modified residue821N6-acetyllysine By similarity
Modified residue1261N6-acetyllysine Ref.5
Modified residue2461Phosphothreonine By similarity
Modified residue2941Phosphoserine By similarity
Modified residue4481N6-acetyllysine Ref.5

Experimental info

Sequence conflict127 – 1359KISSPKCNN → VSNPKTNGD in AAF70057. Ref.2
Sequence conflict1581Q → H in BAE40705. Ref.3
Sequence conflict3141L → P in AAF34721. Ref.1
Sequence conflict3211E → D in AAH60234. Ref.3
Sequence conflict3241A → P in AAF34721. Ref.1
Sequence conflict439 – 4413LPA → IKV in BAB31500. Ref.3
Sequence conflict4511E → K in BAB31500. Ref.3
Sequence conflict462 – 4643EKK → QKT in BAB31500. Ref.3

Secondary structure

..... 466
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9JIH2 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 8B9216CBB613661A

FASTA46649,485
        10         20         30         40         50         60 
MAKRVAEKEL TDRNWDEEDE VEEMGTFSVA SEEVMKNRAV KKAKRRNVGF ESDSGGAFKG 

        70         80         90        100        110        120 
FKGLVVPSGG GGFSGFGGSG GKPLEGLTNG NSTDNATPFS NVKTAAEPKA AFGSFAVNGP 

       130        140        150        160        170        180 
TTLVDKKISS PKCNNSNQPP SSGPASSTAC PGNAYHKQLA GLNCSVRDWI VKHVNTNPLC 

       190        200        210        220        230        240 
DLTPIFKDYE RYLATIEKQL ENGGGSSSES QTDRATAGME PPSLFGSTKL QQESPFSFHG 

       250        260        270        280        290        300 
NKAEDTSEKV EFTAEKKSDA AQGATSASFS FGKKIESSAL GSLSSGSLTG FSFSAGSSSL 

       310        320        330        340        350        360 
FGKDAAQSKA ASSLFSAKAS ESPAGGGSSE CRDGEEEEND EPPKVVVTEV KEEDAFYSKK 

       370        380        390        400        410        420 
CKLFYKKDNE FKEKGVGTLH LKPTATQKTQ LLVRADTNLG NILLNVLIAP NMPCTRTGKN 

       430        440        450        460 
NVLIVCVPNP PLDEKQPTLP ATMLIRVKTS EDADELHKIL LEKKDA 

« Hide

References

« Hide 'large scale' references
[1]"Characterization and targeted disruption of murine nup50, a p27(Kip1)-interacting component of the nuclear pore complex."
Smitherman M., Lee K., Swanger J., Kapur R., Clurman B.E.
Mol. Cell. Biol. 20:5631-5642(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Embryo.
[2]"Cyclin E-mediated elimination of p27 requires its interaction with the nuclear pore-associated protein mNPAP60."
Mueller D., Thieke K., Buergin A., Dickmanns A., Eilers M.
EMBO J. 19:2168-2180(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[3]"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. expand/collapse author list , 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].
Strain: C57BL/6J.
Tissue: Amnion, Bone marrow, Ovary, Pituitary, Testis and Thymus.
[4]"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].
Strain: C57BL/6.
Tissue: Brain.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-126 AND LYS-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[6]"Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling."
Matsuura Y., Stewart M.
EMBO J. 24:3681-3689(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-46 IN COMPLEX WITH KPNA2, FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF229256 mRNA. Translation: AAF34721.1.
AF251799 mRNA. Translation: AAF70057.1.
AK018983 mRNA. Translation: BAB31500.1.
AK087706 mRNA. Translation: BAC39975.1.
AK133371 mRNA. Translation: BAE21620.1.
AK133562 mRNA. Translation: BAE21727.1.
AK141750 mRNA. Translation: BAE24822.1.
AK151947 mRNA. Translation: BAE30821.1.
AK152309 mRNA. Translation: BAE31115.1.
AK161713 mRNA. Translation: BAE36546.1.
AK165581 mRNA. Translation: BAE38272.1.
AK168888 mRNA. Translation: BAE40705.1.
CH466550 Genomic DNA. Translation: EDL04446.1.
BC059239 mRNA. Translation: AAH59239.1.
BC060234 mRNA. Translation: AAH60234.1.
BC065102 mRNA. Translation: AAH65102.1.
CCDSCCDS27714.1.
RefSeqNP_057923.2. NM_016714.2.
UniGeneMm.28379.
Mm.391486.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C1MX-ray2.20B1-46[»]
ProteinModelPortalQ9JIH2.
SMRQ9JIH2. Positions 1-46, 349-466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201817. 2 interactions.
DIPDIP-46130N.
IntActQ9JIH2. 2 interactions.
MINTMINT-4104287.

PTM databases

PhosphoSiteQ9JIH2.

Proteomic databases

MaxQBQ9JIH2.
PaxDbQ9JIH2.
PRIDEQ9JIH2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000165443; ENSMUSP00000131457; ENSMUSG00000016619.
GeneID18141.
KEGGmmu:18141.
UCSCuc007xcq.1. mouse.

Organism-specific databases

CTD10762.
MGIMGI:1351502. Nup50.

Phylogenomic databases

eggNOGNOG255247.
GeneTreeENSGT00440000035348.
HOVERGENHBG052697.
InParanoidQ6P1F4.
KOK14295.
OMAANIEQQH.
OrthoDBEOG7CRTR9.
TreeFamTF106504.

Gene expression databases

BgeeQ9JIH2.
GenevestigatorQ9JIH2.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR015007. NUP2/50/61.
IPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
[Graphical view]
PfamPF08911. NUP50. 1 hit.
PF00638. Ran_BP1. 1 hit.
[Graphical view]
SMARTSM00160. RanBD. 1 hit.
[Graphical view]
PROSITEPS50196. RANBD1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNUP50. mouse.
EvolutionaryTraceQ9JIH2.
NextBio293388.
PROQ9JIH2.
SOURCESearch...

Entry information

Entry nameNUP50_MOUSE
AccessionPrimary (citable) accession number: Q9JIH2
Secondary accession number(s): Q3TG43 expand/collapse secondary AC list , Q3TN17, Q6P1F4, Q6PAL4, Q8C2Y6, Q9CU02, Q9JK85
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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