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Reviewed, UniProtKB/Swiss-Prot Q8WUM0 (NU133_HUMAN)

Last modified February 9, 2010. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Nuclear pore complex protein Nup133
Alternative name(s):
    Nucleoporin Nup133
    133 kDa nucleoporin
Gene names
Name: NUP133
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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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.5 Ref.4

Subcellular location

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

Sequence similarities

Belongs to the nucleoporin Nup133 family.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

NUP107P577401EBI-295695,EBI-295687

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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.14
Modified residue71Phosphoserine Ref.14 Ref.9 Ref.11
Modified residue101Phosphothreonine Ref.14
Modified residue271Phosphoserine Ref.14 Ref.7 Ref.12
Modified residue281Phosphothreonine Ref.14 Ref.7 Ref.12
Modified residue411Phosphoserine Ref.12
Modified residue451Phosphoserine Ref.14 Ref.11 Ref.7 Ref.12 Ref.6 Ref.8 Ref.10 Ref.15
Modified residue501Phosphoserine Ref.14 Ref.11 Ref.12 Ref.6 Ref.8 Ref.10 Ref.15
Modified residue571Phosphoserine Ref.9
Modified residue1311Phosphoserine Ref.14
Modified residue4801Phosphoserine Ref.15
Modified residue4891Phosphoserine Ref.9
Modified residue5011Phosphoserine By similarity

Natural variations

Natural variant1061T → P: dbSNP rs428231.
VAR_030829
Natural variant2941I → V: dbSNP rs11805194.
VAR_030830
Natural variant3261G → V in a breast cancer sample; somatic mutation. Ref.17
VAR_035854
Natural variant4061Q → R: dbSNP rs1065674.
VAR_030831
Natural variant4481G → R in a breast cancer sample; somatic mutation. Ref.17
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

1 ..................................................................... 1156
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q8WUM0-1 [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

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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: 14702039] [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: 16710414] [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: 15489334] [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: 11564755] [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: 11684705] [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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-50, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"Phosphoproteome analysis of the human mitotic spindle."
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; THR-28 AND SER-45, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-50, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-57 AND SER-489, MASS SPECTROMETRY.
[10]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-50, MASS SPECTROMETRY.
[11]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-45 AND SER-50, MASS SPECTROMETRY.
[12]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; THR-28; SER-41; SER-45 AND SER-50, MASS SPECTROMETRY.
[13]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]"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: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; THR-10; SER-27; THR-28; SER-45; SER-50 AND SER-131, MASS SPECTROMETRY.
[15]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-50 AND SER-480, MASS SPECTROMETRY.
Tissue: T-cell.
[16]"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: 15557116] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 67-514.
[17]"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: 16959974] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-326 AND ARG-448.
+Additional computationally mapped references.

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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.
IPIIPI00291200.
RefSeqNP_060700.2.
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.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8WUM0. 5 interactions.
STRINGQ8WUM0.

PTM databases

PhosphoSiteQ8WUM0.

Proteomic databases

PRIDEQ8WUM0.

Genome annotation databases

EnsemblENST00000261396; ENSP00000261396; ENSG00000069248; Homo sapiens. [Genome view]
GeneID55746.
KEGGhsa:55746.
UCSCuc001htn.1. human.

Organism-specific databases

CTD55746.
GeneCardsGC01M227643.
H-InvDBHIX0001680.
HGNCHGNC:18016. NUP133.
MIM607613. gene.
PharmGKBPA31847.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG10158.
HOGENOMHBG356350.
HOVERGENQ8WUM0.
InParanoidQ8WUM0.
OMASNQTAYL.
OrthoDBEOG9K9DZ1.
PhylomeDBQ8WUM0.

Enzyme and pathway databases

ReactomeREACT_152. Cell Cycle, Mitotic.
REACT_6185. HIV Infection.

Gene expression databases

ArrayExpressQ8WUM0.
BgeeQ8WUM0.
CleanExHS_NUP133.
GenevestigatorQ8WUM0.
GermOnlineENSG00000069248. Homo sapiens.

Family and domain databases

InterProIPR007187. Nucleoporin_Nup133/Nup155_C.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
Gene3DG3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
PfamPF03177. Nucleoporin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio60719.
SOURCESearch...

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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: February 9, 2010
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Relevant documents

Human chromosome 1

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents