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Q8NFH5 (NUP53_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Nucleoporin NUP53
Alternative name(s):
35 kDa nucleoporin
Mitotic phosphoprotein 44
Short name=MP-44
Nuclear pore complex protein Nup53
Nucleoporin Nup35
Gene names
Name:NUP35
Synonyms:MP44, NUP53
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Subunit structure

Interacts with TMEM48/NDC1. Forms a complex with NUP93, NUP155, NUP205 and lamin B; the interaction with NUP93 is direct. Ref.5 Ref.7

Subcellular location

Nucleusnuclear pore complex. Nucleus membrane; Peripheral membrane protein. Note: Tightly associated with the nuclear membrane and lamina. Ref.1 Ref.5

Sequence similarities

Belongs to the Nup53 family.

Contains 1 RRM Nup35-type domain.

Ontologies

Keywords
   Biological processmRNA transport
Protein transport
Translocation
Transport
   Cellular componentMembrane
Nuclear pore complex
Nucleus
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

glucose transport

Traceable author statement. Source: Reactome

hexose transport

Traceable author statement. Source: Reactome

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear envelope disassembly

Traceable author statement. Source: Reactome

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of glucose transport

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentintermediate filament cytoskeleton

Inferred from direct assay. Source: HPA

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nuclear envelope

Traceable author statement. Source: Reactome

nuclear membrane

Inferred from direct assay. Source: HPA

nuclear pore

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 326326Nucleoporin NUP53
PRO_0000234294

Regions

Domain170 – 25081RRM Nup35-type

Amino acid modifications

Modified residue661Phosphoserine Ref.12
Modified residue731Phosphoserine Ref.6 Ref.12 Ref.14
Modified residue991Phosphoserine Ref.9
Modified residue1001Phosphoserine Ref.9 Ref.11 Ref.12
Modified residue1061Phosphothreonine Ref.9 Ref.12
Modified residue1211Phosphoserine Ref.12
Modified residue1291Phosphothreonine Ref.9
Modified residue1381Phosphoserine Ref.9
Modified residue2591Phosphoserine By similarity
Modified residue2651Phosphothreonine Ref.9
Modified residue2731Phosphothreonine Ref.9 Ref.12
Modified residue2791Phosphoserine Ref.9 Ref.12
Modified residue2801Phosphothreonine Ref.9 Ref.12
Modified residue3081Phosphothreonine Ref.9

Experimental info

Sequence conflict3131E → G in AAL86379. Ref.2
Sequence conflict3181K → Q in AAL86379. Ref.2

Secondary structure

.................. 326
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8NFH5 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 6420B0EF1AE31013

FASTA32634,774
        10         20         30         40         50         60 
MAAFAVEPQG PALGSEPMML GSPTSPKPGV NAQFLPGFLM GDLPAPVTPQ PRSISGPSVG 

        70         80         90        100        110        120 
VMEMRSPLLA GGSPPQPVVP AHKDKSGAPP VRSIYDDISS PGLGSTPLTS RRQPNISVMQ 

       130        140        150        160        170        180 
SPLVGVTSTP GTGQSMFSPA SIGQPRKTTL SPAQLDPFYT QGDSLTSEDH LDDSWVTVFG 

       190        200        210        220        230        240 
FPQASASYIL LQFAQYGNIL KHVMSNTGNW MHIRYQSKLQ ARKALSKDGR IFGESIMIGV 

       250        260        270        280        290        300 
KPCIDKSVME SSDRCALSSP SLAFTPPIKT LGTPTQPGST PRISTMRPLA TAYKASTSDY 

       310        320 
QVISDRQTPK KDESLVSKAM EYMFGW 

« Hide

References

« Hide 'large scale' references
[1]"Proteomic analysis of the mammalian nuclear pore complex."
Cronshaw J.M., Krutchinsky A.N., Zhang W., Chait B.T., Matunis M.J.
J. Cell Biol. 158:915-927(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[2]"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].
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Bone marrow and Skin.
[5]"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: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NUP93, IDENTIFICATION IN A COMPLEX WITH LAMIN B; NUP155 AND NUP205.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"The conserved transmembrane nucleoporin NDC1 is required for nuclear pore complex assembly in vertebrate cells."
Mansfeld J., Guettinger S., Hawryluk-Gara L.A., Pante N., Mall M., Galy V., Haselmann U., Muehlhaeusser P., Wozniak R.W., Mattaj I.W., Kutay U., Antonin W.
Mol. Cell 22:93-103(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMEM48.
[8]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-100; THR-106; THR-129; SER-138; THR-265; THR-273; SER-279; THR-280 AND THR-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-73; SER-100; THR-106; SER-121; THR-273; SER-279 AND THR-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF514993 mRNA. Translation: AAM76704.1.
AF411516 mRNA. Translation: AAL86379.1.
AC064871 Genomic DNA. Translation: AAY24198.1.
AC079249 Genomic DNA. Translation: AAX88896.1.
BC047029 mRNA. Translation: AAH47029.1.
BC061698 mRNA. Translation: AAH61698.1.
CCDSCCDS2290.1.
RefSeqNP_001274514.1. NM_001287585.1.
NP_612142.2. NM_138285.4.
UniGeneHs.180591.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4LIRX-ray2.46A/B151-266[»]
ProteinModelPortalQ8NFH5.
SMRQ8NFH5. Positions 169-252.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126190. 4 interactions.
DIPDIP-47308N.
IntActQ8NFH5. 1 interaction.
MINTMINT-4301788.
STRING9606.ENSP00000295119.

PTM databases

PhosphoSiteQ8NFH5.

Polymorphism databases

DMDM74730292.

Proteomic databases

MaxQBQ8NFH5.
PaxDbQ8NFH5.
PeptideAtlasQ8NFH5.
PRIDEQ8NFH5.

Protocols and materials databases

DNASU129401.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295119; ENSP00000295119; ENSG00000163002.
GeneID129401.
KEGGhsa:129401.
UCSCuc002upf.3. human.

Organism-specific databases

CTD129401.
GeneCardsGC02P183982.
HGNCHGNC:29797. NUP35.
HPAHPA018401.
HPA018410.
HPA018441.
MIM608140. gene.
neXtProtNX_Q8NFH5.
PharmGKBPA134861481.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253574.
HOGENOMHOG000231921.
HOVERGENHBG060396.
InParanoidQ8NFH5.
KOK14313.
OMAANISVMQ.
PhylomeDBQ8NFH5.
TreeFamTF325369.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ8NFH5.
BgeeQ8NFH5.
CleanExHS_NUP35.
GenevestigatorQ8NFH5.

Family and domain databases

InterProIPR017389. Nucleoporin_NUP53.
IPR007846. RRM_NUP35_dom.
[Graphical view]
PfamPF05172. Nup35_RRM. 1 hit.
[Graphical view]
PIRSFPIRSF038119. Nucleoporin_NUP53. 1 hit.
PROSITEPS51472. RRM_NUP35. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNUP35.
GenomeRNAi129401.
NextBio82574.
PROQ8NFH5.
SOURCESearch...

Entry information

Entry nameNUP53_HUMAN
AccessionPrimary (citable) accession number: Q8NFH5
Secondary accession number(s): Q4ZFZ9, Q53S95, Q8TDJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM