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Q8WUM0

- NU133_HUMAN

UniProt

Q8WUM0 - NU133_HUMAN

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Protein
Nuclear pore complex protein Nup133
Gene
NUP133
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in poly(A)+ RNA transport.1 Publication

GO - Molecular functioni

  1. nucleocytoplasmic transporter activity Source: UniProtKB
  2. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cytokine-mediated signaling pathway Source: Reactome
  3. glucose transport Source: Reactome
  4. hexose transport Source: Reactome
  5. mRNA export from nucleus Source: UniProtKB
  6. mitotic cell cycle Source: Reactome
  7. mitotic nuclear envelope disassembly Source: Reactome
  8. nuclear pore organization Source: UniProtKB
  9. paraxial mesoderm development Source: Ensembl
  10. protein transport Source: UniProtKB-KW
  11. regulation of glucose transport Source: Reactome
  12. small molecule metabolic process Source: Reactome
  13. transmembrane transport Source: Reactome
  14. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
REACT_682. Mitotic Prometaphase.
REACT_7991. Vpr-mediated nuclear import of PICs.
REACT_9395. Nuclear import of Rev protein.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear pore complex protein Nup133
Alternative name(s):
133 kDa nucleoporin
Nucleoporin Nup133
Gene namesi
Name:NUP133
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:18016. NUP133.

Subcellular locationi

Nucleusnuclear pore complex. Chromosomecentromerekinetochore
Note: Located on both the cytoplasmic and nuclear sides of the nuclear pore. During mitosis, localizes to the kinetochores.2 Publications

GO - Cellular componenti

  1. condensed chromosome kinetochore Source: UniProtKB-SubCell
  2. cytosol Source: Reactome
  3. nuclear envelope Source: Reactome
  4. nuclear pore Source: UniProtKB
  5. nuclear pore outer ring Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nuclear pore complex, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31847.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11561156Nuclear pore complex protein Nup133
PRO_0000204838Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei7 – 71Phosphoserine1 Publication
Modified residuei27 – 271Phosphoserine2 Publications
Modified residuei28 – 281Phosphothreonine2 Publications
Modified residuei41 – 411Phosphoserine1 Publication
Modified residuei45 – 451Phosphoserine4 Publications
Modified residuei50 – 501Phosphoserine7 Publications
Modified residuei480 – 4801Phosphoserine1 Publication
Modified residuei787 – 7871N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8WUM0.
PaxDbiQ8WUM0.
PRIDEiQ8WUM0.

PTM databases

PhosphoSiteiQ8WUM0.

Expressioni

Gene expression databases

ArrayExpressiQ8WUM0.
BgeeiQ8WUM0.
CleanExiHS_NUP133.
GenevestigatoriQ8WUM0.

Organism-specific databases

HPAiHPA059767.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CENPFP494542EBI-295695,EBI-968343
NUP107P577406EBI-295695,EBI-295687

Protein-protein interaction databases

BioGridi120864. 29 interactions.
IntActiQ8WUM0. 15 interactions.
MINTiMINT-3046670.
STRINGi9606.ENSP00000261396.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi77 – 837
Helixi90 – 989
Beta strandi105 – 1095
Beta strandi113 – 1197
Beta strandi122 – 1276
Helixi134 – 1363
Beta strandi139 – 1435
Helixi153 – 1553
Beta strandi156 – 1605
Beta strandi172 – 1787
Beta strandi183 – 1886
Beta strandi197 – 2004
Beta strandi209 – 2157
Turni216 – 2183
Beta strandi219 – 2246
Beta strandi229 – 2346
Beta strandi240 – 2445
Beta strandi274 – 2807
Turni281 – 2844
Beta strandi285 – 29915
Beta strandi304 – 3118
Helixi312 – 32514
Helixi331 – 3355
Beta strandi339 – 34810
Beta strandi351 – 3599
Beta strandi363 – 3653
Beta strandi367 – 3759
Beta strandi386 – 3905
Helixi400 – 4023
Beta strandi406 – 4083
Beta strandi412 – 4209
Beta strandi422 – 4298
Beta strandi440 – 4434
Helixi446 – 4483
Beta strandi451 – 4577
Beta strandi460 – 4656
Turni466 – 4683
Beta strandi469 – 4757
Helixi936 – 9427
Helixi946 – 95914
Helixi964 – 98017
Helixi985 – 100622
Helixi1012 – 10154
Beta strandi1020 – 10234
Helixi1028 – 10347
Helixi1045 – 10517
Turni1052 – 10576
Helixi1067 – 107913
Helixi1096 – 11027
Helixi1125 – 11284
Helixi1142 – 115514

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XKSX-ray2.35A67-514[»]
3CQCX-ray2.53B935-1156[»]
3CQGX-ray3.00B934-1156[»]
3I4RX-ray3.53B517-1156[»]
DisProtiDP00318.
ProteinModelPortaliQ8WUM0.
SMRiQ8WUM0. Positions 75-477, 518-1156.

Miscellaneous databases

EvolutionaryTraceiQ8WUM0.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG312399.
HOGENOMiHOG000293246.
HOVERGENiHBG052678.
InParanoidiQ8WUM0.
KOiK14300.
OMAiMCRLMVP.
OrthoDBiEOG7P8P70.
PhylomeDBiQ8WUM0.
TreeFamiTF106141.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR007187. Nucleoporin_Nup133/Nup155_C.
IPR014908. Nucleoporin_Nup133/Nup155_N.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamiPF03177. Nucleoporin_C. 1 hit.
PF08801. Nucleoporin_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8WUM0-1 [UniParc]FASTAAdd to Basket

« Hide

MFPAAPSPRT PGTGSRRGPL AGLGPGSTPR TASRKGLPLG SAVSSPVLFS     50
PVGRRSSLSS RGTPTRMFPH HSITESVNYD VKTFGSSLPV KVMEALTLAE 100
VDDQLTINID EGGWACLVCK EKLIIWKIAL SPITKLSVCK ELQLPPSDFH 150
WSADLVALSY SSPSGEAHST QAVAVMVATR EGSIRYWPSL AGEDTYTEAF 200
VDSGGDKTYS FLTAVQGGSF ILSSSGSQLI RLIPESSGKI HQHILPQGQG 250
MLSGIGRKVS SLFGILSPSS DLTLSSVLWD RERSSFYSLT SSNISKWELD 300
DSSEKHAYSW DINRALKENI TDAIWGSESN YEAIKEGVNI RYLDLKQNCD 350
GLVILAAAWH SADNPCLIYY SLITIEDNGC QMSDAVTVEV TQYNPPFQSE 400
DLILCQLTVP NFSNQTAYLY NESAVYVCST GTGKFSLPQE KIVFNAQGDS 450
VLGAGACGGV PIIFSRNSGL VSITSRENVS ILAEDLEGSL ASSVAGPNSE 500
SMIFETTTKN ETIAQEDKIK LLKAAFLQYC RKDLGHAQMV VDELFSSHSD 550
LDSDSELDRA VTQISVDLMD DYPASDPRWA ESVPEEAPGF SNTSLIILHQ 600
LEDKMKAHSF LMDFIHQVGL FGRLGSFPVR GTPMATRLLL CEHAEKLSAA 650
IVLKNHHSRL SDLVNTAILI ALNKREYEIP SNLTPADVFF REVSQVDTIC 700
ECLLEHEEQV LRDAPMDSIE WAEVVINVNN ILKDMLQAAS HYRQNRNSLY 750
RREESLEKEP EYVPWTATSG PGGIRTVIIR QHEIVLKVAY PQADSNLRNI 800
VTEQLVALID CFLDGYVSQL KSVDKSSNRE RYDNLEMEYL QKRSDLLSPL 850
LSLGQYLWAA SLAEKYCDFD ILVQMCEQTD NQSRLQRYMT QFADQNFSDF 900
LFRWYLEKGK RGKLLSQPIS QHGQLANFLQ AHEHLSWLHE INSQELEKAH 950
ATLLGLANME TRYFAKKKTL LGLSKLAALA SDFSEDMLQE KIEEMAEQER 1000
FLLHQETLPE QLLAEKQLNL SAMPVLTAPQ LIGLYICEEN RRANEYDFKK 1050
ALDLLEYIDE EEDININDLK LEILCKALQR DNWSSSDGKD DPIEVSKDSI 1100
FVKILQKLLK DGIQLSEYLP EVKDLLQADQ LGSLKSNPYF EFVLKANYEY 1150
YVQGQI 1156
Length:1,156
Mass (Da):128,979
Last modified:April 3, 2007 - v2
Checksum:i78B733E353824577
GO

Sequence cautioni

The sequence BAA91885.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAB14106.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061T → P.
Corresponds to variant rs428231 [ dbSNP | Ensembl ].
VAR_030829
Natural varianti294 – 2941I → V.
Corresponds to variant rs11805194 [ dbSNP | Ensembl ].
VAR_030830
Natural varianti326 – 3261G → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_035854
Natural varianti406 – 4061Q → R.
Corresponds to variant rs1065674 [ dbSNP | Ensembl ].
VAR_030831
Natural varianti448 – 4481G → R in a breast cancer sample; somatic mutation. 1 Publication
VAR_035855

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611R → G in BAA91829. 1 Publication
Sequence conflicti146 – 1461P → S in BAA91829. 1 Publication
Sequence conflicti345 – 3451L → F in AAH20107. 1 Publication
Sequence conflicti626 – 6261S → N in BAA91829. 1 Publication
Sequence conflicti928 – 9281F → L in BAA91885. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1579.1.
RefSeqiNP_060700.2. NM_018230.2.
UniGeneiHs.12457.

Genome annotation databases

EnsembliENST00000261396; ENSP00000261396; ENSG00000069248.
GeneIDi55746.
KEGGihsa:55746.
UCSCiuc001htn.3. human.

Polymorphism databases

DMDMi143811430.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1579.1.
RefSeqi NP_060700.2. NM_018230.2.
UniGenei Hs.12457.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XKS X-ray 2.35 A 67-514 [» ]
3CQC X-ray 2.53 B 935-1156 [» ]
3CQG X-ray 3.00 B 934-1156 [» ]
3I4R X-ray 3.53 B 517-1156 [» ]
DisProti DP00318.
ProteinModelPortali Q8WUM0.
SMRi Q8WUM0. Positions 75-477, 518-1156.
ModBasei Search...

Protein-protein interaction databases

BioGridi 120864. 29 interactions.
IntActi Q8WUM0. 15 interactions.
MINTi MINT-3046670.
STRINGi 9606.ENSP00000261396.

PTM databases

PhosphoSitei Q8WUM0.

Polymorphism databases

DMDMi 143811430.

Proteomic databases

MaxQBi Q8WUM0.
PaxDbi Q8WUM0.
PRIDEi Q8WUM0.

Protocols and materials databases

DNASUi 55746.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261396 ; ENSP00000261396 ; ENSG00000069248 .
GeneIDi 55746.
KEGGi hsa:55746.
UCSCi uc001htn.3. human.

Organism-specific databases

CTDi 55746.
GeneCardsi GC01M229580.
H-InvDB HIX0001680.
HGNCi HGNC:18016. NUP133.
HPAi HPA059767.
MIMi 607613. gene.
neXtProti NX_Q8WUM0.
PharmGKBi PA31847.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG312399.
HOGENOMi HOG000293246.
HOVERGENi HBG052678.
InParanoidi Q8WUM0.
KOi K14300.
OMAi MCRLMVP.
OrthoDBi EOG7P8P70.
PhylomeDBi Q8WUM0.
TreeFami TF106141.

Enzyme and pathway databases

Reactomei REACT_115831. ISG15 antiviral mechanism.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
REACT_682. Mitotic Prometaphase.
REACT_7991. Vpr-mediated nuclear import of PICs.
REACT_9395. Nuclear import of Rev protein.

Miscellaneous databases

ChiTaRSi NUP133. human.
EvolutionaryTracei Q8WUM0.
GeneWikii NUP133.
GenomeRNAii 55746.
NextBioi 60719.
PROi Q8WUM0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8WUM0.
Bgeei Q8WUM0.
CleanExi HS_NUP133.
Genevestigatori Q8WUM0.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR007187. Nucleoporin_Nup133/Nup155_C.
IPR014908. Nucleoporin_Nup133/Nup155_N.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view ]
Pfami PF03177. Nucleoporin_C. 1 hit.
PF08801. Nucleoporin_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-326 AND ARG-448.

Entry informationi

Entry nameiNU133_HUMAN
AccessioniPrimary (citable) accession number: Q8WUM0
Secondary accession number(s): B2RAZ8
, Q5T8N0, Q9H9W2, Q9NV71, Q9NVC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: April 3, 2007
Last modified: September 3, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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