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Q8WUM0 (NU133_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear pore complex protein Nup133
Alternative name(s):
133 kDa nucleoporin
Nucleoporin Nup133
Gene names
Name:NUP133
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1156 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in poly(A)+ RNA transport. Ref.5

Subunit structure

Forms part of the Nup160 subcomplex in the nuclear pore which is composed of NUP160, NUP133, NUP107 and Nup96. This complex plays a role in RNA export and in tethering Nup98 and NUP153 to the nucleus. Ref.4 Ref.5

Subcellular location

Nucleusnuclear pore complex. Chromosomecentromerekinetochore. Note: Located on both the cytoplasmic and nuclear sides of the nuclear pore. During mitosis, localizes to the kinetochores. Ref.4 Ref.5

Sequence similarities

Belongs to the nucleoporin Nup133 family.

Sequence caution

The sequence BAA91885.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB14106.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processmRNA transport
Protein transport
Translocation
Transport
   Cellular componentCentromere
Chromosome
Kinetochore
Nuclear pore complex
Nucleus
   Coding sequence diversityPolymorphism
   PTMAcetylation
Phosphoprotein
   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 export from nucleus

Inferred from direct assay Ref.5. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear envelope disassembly

Traceable author statement. Source: Reactome

nuclear pore organization

Inferred from mutant phenotype PubMed 15146057. Source: UniProtKB

paraxial mesoderm development

Inferred from electronic annotation. Source: Ensembl

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_componentcondensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

nuclear envelope

Traceable author statement. Source: Reactome

nuclear pore

Inferred from direct assay Ref.4Ref.5PubMed 17098863. Source: UniProtKB

nuclear pore outer ring

Inferred from direct assay PubMed 15146057PubMed 17360435. Source: UniProtKB

   Molecular_functionnucleocytoplasmic transporter activity

Inferred from direct assay Ref.5. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CENPFP494542EBI-295695,EBI-968343
NUP107P577406EBI-295695,EBI-295687

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11561156Nuclear pore complex protein Nup133
PRO_0000204838

Amino acid modifications

Modified residue11N-acetylmethionine Ref.13 Ref.15 Ref.16
Modified residue71Phosphoserine Ref.13
Modified residue271Phosphoserine Ref.10 Ref.13
Modified residue281Phosphothreonine Ref.10 Ref.13
Modified residue411Phosphoserine Ref.10
Modified residue451Phosphoserine Ref.7 Ref.10 Ref.12 Ref.13
Modified residue501Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13
Modified residue4801Phosphoserine Ref.12
Modified residue7871N6-acetyllysine By similarity

Natural variations

Natural variant1061T → P.
Corresponds to variant rs428231 [ dbSNP | Ensembl ].
VAR_030829
Natural variant2941I → V.
Corresponds to variant rs11805194 [ dbSNP | Ensembl ].
VAR_030830
Natural variant3261G → V in a breast cancer sample; somatic mutation. Ref.18
VAR_035854
Natural variant4061Q → R.
Corresponds to variant rs1065674 [ dbSNP | Ensembl ].
VAR_030831
Natural variant4481G → R in a breast cancer sample; somatic mutation. Ref.18
VAR_035855

Experimental info

Sequence conflict611R → G in BAA91829. Ref.1
Sequence conflict1461P → S in BAA91829. Ref.1
Sequence conflict3451L → F in AAH20107. Ref.3
Sequence conflict6261S → N in BAA91829. Ref.1
Sequence conflict9281F → L in BAA91885. Ref.1

Secondary structure

.............................................................................................. 1156
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8WUM0 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: 78B733E353824577

FASTA1,156128,979
        10         20         30         40         50         60 
MFPAAPSPRT PGTGSRRGPL AGLGPGSTPR TASRKGLPLG SAVSSPVLFS PVGRRSSLSS 

        70         80         90        100        110        120 
RGTPTRMFPH HSITESVNYD VKTFGSSLPV KVMEALTLAE VDDQLTINID EGGWACLVCK 

       130        140        150        160        170        180 
EKLIIWKIAL SPITKLSVCK ELQLPPSDFH WSADLVALSY SSPSGEAHST QAVAVMVATR 

       190        200        210        220        230        240 
EGSIRYWPSL AGEDTYTEAF VDSGGDKTYS FLTAVQGGSF ILSSSGSQLI RLIPESSGKI 

       250        260        270        280        290        300 
HQHILPQGQG MLSGIGRKVS SLFGILSPSS DLTLSSVLWD RERSSFYSLT SSNISKWELD 

       310        320        330        340        350        360 
DSSEKHAYSW DINRALKENI TDAIWGSESN YEAIKEGVNI RYLDLKQNCD GLVILAAAWH 

       370        380        390        400        410        420 
SADNPCLIYY SLITIEDNGC QMSDAVTVEV TQYNPPFQSE DLILCQLTVP NFSNQTAYLY 

       430        440        450        460        470        480 
NESAVYVCST GTGKFSLPQE KIVFNAQGDS VLGAGACGGV PIIFSRNSGL VSITSRENVS 

       490        500        510        520        530        540 
ILAEDLEGSL ASSVAGPNSE SMIFETTTKN ETIAQEDKIK LLKAAFLQYC RKDLGHAQMV 

       550        560        570        580        590        600 
VDELFSSHSD LDSDSELDRA VTQISVDLMD DYPASDPRWA ESVPEEAPGF SNTSLIILHQ 

       610        620        630        640        650        660 
LEDKMKAHSF LMDFIHQVGL FGRLGSFPVR GTPMATRLLL CEHAEKLSAA IVLKNHHSRL 

       670        680        690        700        710        720 
SDLVNTAILI ALNKREYEIP SNLTPADVFF REVSQVDTIC ECLLEHEEQV LRDAPMDSIE 

       730        740        750        760        770        780 
WAEVVINVNN ILKDMLQAAS HYRQNRNSLY RREESLEKEP EYVPWTATSG PGGIRTVIIR 

       790        800        810        820        830        840 
QHEIVLKVAY PQADSNLRNI VTEQLVALID CFLDGYVSQL KSVDKSSNRE RYDNLEMEYL 

       850        860        870        880        890        900 
QKRSDLLSPL LSLGQYLWAA SLAEKYCDFD ILVQMCEQTD NQSRLQRYMT QFADQNFSDF 

       910        920        930        940        950        960 
LFRWYLEKGK RGKLLSQPIS QHGQLANFLQ AHEHLSWLHE INSQELEKAH ATLLGLANME 

       970        980        990       1000       1010       1020 
TRYFAKKKTL LGLSKLAALA SDFSEDMLQE KIEEMAEQER FLLHQETLPE QLLAEKQLNL 

      1030       1040       1050       1060       1070       1080 
SAMPVLTAPQ LIGLYICEEN RRANEYDFKK ALDLLEYIDE EEDININDLK LEILCKALQR 

      1090       1100       1110       1120       1130       1140 
DNWSSSDGKD DPIEVSKDSI FVKILQKLLK DGIQLSEYLP EVKDLLQADQ LGSLKSNPYF 

      1150 
EFVLKANYEY YVQGQI 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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: Skin.
[4]"An evolutionarily conserved NPC subcomplex, which redistributes in part to kinetochores in mammalian cells."
Belgareh N., Rabut G., Bai S.W., van Overbeek M., Beaudouin J., Daigle N., Zatsepina O.V., Pasteau F., Labas V., Fromont-Racine M., Ellenberg J., Doye V.
J. Cell Biol. 154:1147-1160(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, SUBUNIT, SUBCELLULAR LOCATION.
[5]"Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export."
Vasu S., Shah S., Orjalo A., Park M., Fischer W.H., Forbes D.J.
J. Cell Biol. 155:339-354(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[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-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-27; THR-28; SER-41; SER-45 AND SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"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-45; SER-50 AND SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-27; THR-28; SER-45 AND SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Structural and functional analysis of Nup133 domains reveals modular building blocks of the nuclear pore complex."
Berke I.C., Boehmer T., Blobel G., Schwartz T.U.
J. Cell Biol. 167:591-597(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 67-514.
[18]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-326 AND ARG-448.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK001676 mRNA. Translation: BAA91829.1.
AK001754 mRNA. Translation: BAA91885.1. Different initiation.
AK022572 mRNA. Translation: BAB14106.1. Different initiation.
AK314431 mRNA. Translation: BAG37045.1.
AL121990, AL139252, AL160004 Genomic DNA. Translation: CAI22011.1.
AL139252, AL121990, AL160004 Genomic DNA. Translation: CAI22354.1.
AL160004, AL121990, AL139252 Genomic DNA. Translation: CAI19048.1.
BC020107 mRNA. Translation: AAH20107.1.
RefSeqNP_060700.2. NM_018230.2.
UniGeneHs.12457.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XKSX-ray2.35A67-514[»]
3CQCX-ray2.53B935-1156[»]
3CQGX-ray3.00B934-1156[»]
3I4RX-ray3.53B517-1156[»]
DisProtDP00318.
ProteinModelPortalQ8WUM0.
SMRQ8WUM0. Positions 75-477, 518-1156.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120864. 27 interactions.
IntActQ8WUM0. 14 interactions.
MINTMINT-3046670.
STRING9606.ENSP00000261396.

PTM databases

PhosphoSiteQ8WUM0.

Polymorphism databases

DMDM143811430.

Proteomic databases

PaxDbQ8WUM0.
PRIDEQ8WUM0.

Protocols and materials databases

DNASU55746.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261396; ENSP00000261396; ENSG00000069248.
GeneID55746.
KEGGhsa:55746.
UCSCuc001htn.3. human.

Organism-specific databases

CTD55746.
GeneCardsGC01M229580.
H-InvDBHIX0001680.
HGNCHGNC:18016. NUP133.
HPAHPA059767.
MIM607613. gene.
neXtProtNX_Q8WUM0.
PharmGKBPA31847.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG312399.
HOGENOMHOG000293246.
HOVERGENHBG052678.
InParanoidQ8WUM0.
KOK14300.
OMAMCRLMVP.
OrthoDBEOG7P8P70.
PhylomeDBQ8WUM0.
TreeFamTF106141.

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

ArrayExpressQ8WUM0.
BgeeQ8WUM0.
CleanExHS_NUP133.
GenevestigatorQ8WUM0.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR007187. Nucleoporin_Nup133/Nup155_C.
IPR014908. Nucleoporin_Nup133/Nup155_N.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamPF03177. Nucleoporin_C. 1 hit.
PF08801. Nucleoporin_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNUP133. human.
EvolutionaryTraceQ8WUM0.
GeneWikiNUP133.
GenomeRNAi55746.
NextBio60719.
PROQ8WUM0.
SOURCESearch...

Entry information

Entry nameNU133_HUMAN
AccessionPrimary (citable) accession number: Q8WUM0
Secondary accession number(s): B2RAZ8 expand/collapse secondary AC list , Q5T8N0, Q9H9W2, Q9NV71, Q9NVC4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: April 3, 2007
Last modified: April 16, 2014
This is version 121 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM