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Protein

Nucleoporin NUP53

Gene

Nup35

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. May play a role in the association of MAD1 with the NPC (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

ReactomeiREACT_272921. Regulation of HSF1-mediated heat shock response.
REACT_280637. Transcriptional regulation by small RNAs.
REACT_329153. Nuclear Pore Complex (NPC) Disassembly.
REACT_341634. Regulation of Glucokinase by Glucokinase Regulatory Protein.
REACT_360954. SUMOylation of DNA damage response and repair proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin NUP53
Alternative name(s):
35 kDa nucleoporin
Mitotic phosphoprotein 44
Short name:
MP-44
Nuclear pore complex protein Nup53
Nucleoporin Nup35
Gene namesi
Name:Nup35
Synonyms:Mp44, Nup53
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componentsi: Chromosome 2, Chromosome 7

Organism-specific databases

MGIiMGI:1916732. Nup35.

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 – 325325Nucleoporin NUP53PRO_0000234295Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661PhosphoserineBy similarity
Modified residuei73 – 731PhosphoserineBy similarity
Modified residuei99 – 991PhosphoserineBy similarity
Modified residuei100 – 1001PhosphoserineBy similarity
Modified residuei106 – 1061PhosphothreonineBy similarity
Modified residuei121 – 1211PhosphoserineBy similarity
Modified residuei128 – 1281PhosphothreonineBy similarity
Modified residuei137 – 1371PhosphoserineBy similarity
Modified residuei258 – 2581Phosphoserine1 Publication
Modified residuei264 – 2641PhosphothreonineBy similarity
Modified residuei272 – 2721PhosphothreonineBy similarity
Modified residuei274 – 2741PhosphothreonineBy similarity
Modified residuei278 – 2781PhosphoserineBy similarity
Modified residuei279 – 2791PhosphothreonineBy similarity
Modified residuei307 – 3071PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8R4R6.
PaxDbiQ8R4R6.
PRIDEiQ8R4R6.

PTM databases

PhosphoSiteiQ8R4R6.

Expressioni

Gene expression databases

BgeeiQ8R4R6.
CleanExiMM_NUP35.
ExpressionAtlasiQ8R4R6. baseline.
GenevisibleiQ8R4R6. MM.

Interactioni

Subunit structurei

Interacts with TMEM48/NDC1. Forms a complex with NUP93, NUP155, NUP205 and lamin B; The interaction with NUP93 is direct.By similarity

Protein-protein interaction databases

IntActiQ8R4R6. 2 interactions.
MINTiMINT-4127456.
STRINGi10090.ENSMUSP00000107385.

Structurei

Secondary structure

1
325
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi170 – 1734Combined sources
Beta strandi174 – 1785Combined sources
Helixi182 – 1843Combined sources
Helixi185 – 1939Combined sources
Beta strandi198 – 2036Combined sources
Beta strandi205 – 21612Combined sources
Helixi217 – 2248Combined sources
Turni225 – 2284Combined sources
Turni232 – 2343Combined sources
Beta strandi238 – 2414Combined sources
Helixi245 – 2484Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WWHX-ray2.70A/B/C/D156-261[»]
ProteinModelPortaliQ8R4R6.
SMRiQ8R4R6. Positions 169-249.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8R4R6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini169 – 24981RRM Nup35-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the Nup53 family.Curated
Contains 1 RRM Nup35-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG253574.
GeneTreeiENSGT00390000005923.
HOGENOMiHOG000231921.
HOVERGENiHBG060396.
InParanoidiQ8R4R6.
KOiK14313.
OMAiSIYDELS.
OrthoDBiEOG79KPFQ.
PhylomeDBiQ8R4R6.
TreeFamiTF325369.

Family and domain databases

InterProiIPR017389. Nucleoporin_NUP53.
IPR007846. RRM_NUP35_dom.
[Graphical view]
PfamiPF05172. Nup35_RRM. 1 hit.
[Graphical view]
PIRSFiPIRSF038119. Nucleoporin_NUP53. 1 hit.
PROSITEiPS51472. RRM_NUP35. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R4R6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAFAVDPQA PTLGSEPMML GSPTSPKTGA NAQFLPGFLM GDLPAPVTPQ
60 70 80 90 100
PRSISGPSVG VMEMRSPLLA GGSPPQPVVP AHKDKSGAPP VRSIYDDISS
110 120 130 140 150
PGLGSTPLTS RRQANISLLQ SPLVGATTPV PGQSMFSPAN IGQPRKTTLS
160 170 180 190 200
PAQLDPFYTQ GDSLTSEDHL DDTWVTVFGF PQASASYILL QFAQYGNILK
210 220 230 240 250
HVMSNTGNWM HIRYQSKLQA RKALSKDGRI FGESIMIGVK PCIDKNVMEN
260 270 280 290 300
SDRGVLSSPS LAFTTPIRTL GTPTQSGSTP RVSTMRPLAT AYKASTSDYQ
310 320
VISDRQTPKK DESLVSRAME YMFGW
Length:325
Mass (Da):34,786
Last modified:May 16, 2006 - v2
Checksum:iA8994CBDF25A3C84
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131L → V in AAL86380 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF411517 mRNA. Translation: AAL86380.1.
AK009187 mRNA. Translation: BAB26128.1.
AK089997 mRNA. Translation: BAC41034.1.
AK136109 mRNA. Translation: BAE22825.1.
AK145775 mRNA. Translation: BAE26644.1.
AL928869 Genomic DNA. Translation: CAM23081.1.
BC048814 mRNA. Translation: AAH48814.1.
CCDSiCCDS16179.1.
RefSeqiNP_001177108.1. NM_001190179.1.
NP_081367.1. NM_027091.4.
UniGeneiMm.29200.

Genome annotation databases

EnsembliENSMUST00000028382; ENSMUSP00000028382; ENSMUSG00000026999.
ENSMUST00000111755; ENSMUSP00000107385; ENSMUSG00000091900.
GeneIDi69482.
KEGGimmu:69482.
UCSCiuc008khs.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF411517 mRNA. Translation: AAL86380.1.
AK009187 mRNA. Translation: BAB26128.1.
AK089997 mRNA. Translation: BAC41034.1.
AK136109 mRNA. Translation: BAE22825.1.
AK145775 mRNA. Translation: BAE26644.1.
AL928869 Genomic DNA. Translation: CAM23081.1.
BC048814 mRNA. Translation: AAH48814.1.
CCDSiCCDS16179.1.
RefSeqiNP_001177108.1. NM_001190179.1.
NP_081367.1. NM_027091.4.
UniGeneiMm.29200.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WWHX-ray2.70A/B/C/D156-261[»]
ProteinModelPortaliQ8R4R6.
SMRiQ8R4R6. Positions 169-249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R4R6. 2 interactions.
MINTiMINT-4127456.
STRINGi10090.ENSMUSP00000107385.

PTM databases

PhosphoSiteiQ8R4R6.

Proteomic databases

MaxQBiQ8R4R6.
PaxDbiQ8R4R6.
PRIDEiQ8R4R6.

Protocols and materials databases

DNASUi69482.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028382; ENSMUSP00000028382; ENSMUSG00000026999.
ENSMUST00000111755; ENSMUSP00000107385; ENSMUSG00000091900.
GeneIDi69482.
KEGGimmu:69482.
UCSCiuc008khs.2. mouse.

Organism-specific databases

CTDi129401.
MGIiMGI:1916732. Nup35.

Phylogenomic databases

eggNOGiNOG253574.
GeneTreeiENSGT00390000005923.
HOGENOMiHOG000231921.
HOVERGENiHBG060396.
InParanoidiQ8R4R6.
KOiK14313.
OMAiSIYDELS.
OrthoDBiEOG79KPFQ.
PhylomeDBiQ8R4R6.
TreeFamiTF325369.

Enzyme and pathway databases

ReactomeiREACT_272921. Regulation of HSF1-mediated heat shock response.
REACT_280637. Transcriptional regulation by small RNAs.
REACT_329153. Nuclear Pore Complex (NPC) Disassembly.
REACT_341634. Regulation of Glucokinase by Glucokinase Regulatory Protein.
REACT_360954. SUMOylation of DNA damage response and repair proteins.

Miscellaneous databases

EvolutionaryTraceiQ8R4R6.
NextBioi329578.
PROiQ8R4R6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R4R6.
CleanExiMM_NUP35.
ExpressionAtlasiQ8R4R6. baseline.
GenevisibleiQ8R4R6. MM.

Family and domain databases

InterProiIPR017389. Nucleoporin_NUP53.
IPR007846. RRM_NUP35_dom.
[Graphical view]
PfamiPF05172. Nup35_RRM. 1 hit.
[Graphical view]
PIRSFiPIRSF038119. Nucleoporin_NUP53. 1 hit.
PROSITEiPS51472. RRM_NUP35. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression analysis of human mitotic phosphoprotein 44 gene."
    Guo J.H., Yu L.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/c.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Egg, Submandibular gland and Tongue.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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: FVB/N.
    Tissue: Mammary tumor.
  5. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 214-221, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Crystal structure of the mppn domain of mouse nup35."
    Handa N., Murayama K., Kukimoto M., Hamana H., Uchikubo T., Takemoto C., Terada T., Shirouzu M., Yokoyama S.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 156-261.

Entry informationi

Entry nameiNUP53_MOUSE
AccessioniPrimary (citable) accession number: Q8R4R6
Secondary accession number(s): A2ATJ3, Q9D7J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: June 24, 2015
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.