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Protein

Nuclear pore complex protein Nup133

Gene

NUP133

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciZFISH:ENSG00000069248-MONOMER.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-168271. Transport of Ribonucleoproteins into the Host Nucleus.
R-HSA-168276. NS1 Mediated Effects on Host Pathways.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
R-HSA-191859. snRNP Assembly.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6784531. tRNA processing in the nucleus.
R-HSA-68877. Mitotic Prometaphase.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

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)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18016. NUP133.

Subcellular locationi

GO - Cellular componenti

  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • membrane Source: UniProtKB
  • nuclear envelope Source: Reactome
  • nuclear membrane Source: HPA
  • nuclear pore Source: UniProtKB
  • nuclear pore outer ring Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nuclear pore complex, Nucleus

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000069248.
PharmGKBiPA31847.

Polymorphism and mutation databases

BioMutaiNUP133.
DMDMi143811430.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002048381 – 1156Nuclear pore complex protein Nup133Add BLAST1156

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei7PhosphoserineCombined sources1
Modified residuei15PhosphoserineCombined sources1
Modified residuei17Omega-N-methylarginineCombined sources1
Modified residuei27PhosphoserineCombined sources1
Modified residuei28PhosphothreonineCombined sources1
Modified residuei30Omega-N-methylarginineBy similarity1
Modified residuei41PhosphoserineCombined sources1
Modified residuei45PhosphoserineCombined sources1
Modified residuei50PhosphoserineCombined sources1
Modified residuei72PhosphoserineCombined sources1
Modified residuei131PhosphoserineCombined sources1
Modified residuei480PhosphoserineCombined sources1
Modified residuei489PhosphoserineBy similarity1
Modified residuei493PhosphoserineBy similarity1
Modified residuei501PhosphoserineBy similarity1
Modified residuei755PhosphoserineCombined sources1
Modified residuei787N6-acetyllysineBy similarity1
Modified residuei1133PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ8WUM0.
MaxQBiQ8WUM0.
PaxDbiQ8WUM0.
PeptideAtlasiQ8WUM0.
PRIDEiQ8WUM0.

PTM databases

iPTMnetiQ8WUM0.
PhosphoSitePlusiQ8WUM0.
SwissPalmiQ8WUM0.

Expressioni

Gene expression databases

BgeeiENSG00000069248.
CleanExiHS_NUP133.
GenevisibleiQ8WUM0. HS.

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CENPFP494542EBI-295695,EBI-968343
LRRK2Q5S0072EBI-295695,EBI-5323863
NUP107P5774010EBI-295695,EBI-295687
NUP85P466735EBI-295695,EBI-12345From a different organism.
NUP85Q9BW272EBI-295695,EBI-716392

Protein-protein interaction databases

BioGridi120864. 58 interactors.
IntActiQ8WUM0. 36 interactors.
MINTiMINT-3046670.
STRINGi9606.ENSP00000261396.

Structurei

Secondary structure

11156
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi77 – 83Combined sources7
Helixi90 – 98Combined sources9
Beta strandi105 – 109Combined sources5
Beta strandi113 – 119Combined sources7
Beta strandi122 – 127Combined sources6
Helixi134 – 136Combined sources3
Beta strandi139 – 143Combined sources5
Helixi153 – 155Combined sources3
Beta strandi156 – 160Combined sources5
Beta strandi172 – 178Combined sources7
Beta strandi183 – 188Combined sources6
Beta strandi197 – 200Combined sources4
Beta strandi209 – 215Combined sources7
Turni216 – 218Combined sources3
Beta strandi219 – 224Combined sources6
Beta strandi229 – 234Combined sources6
Beta strandi240 – 244Combined sources5
Beta strandi274 – 280Combined sources7
Turni281 – 284Combined sources4
Beta strandi285 – 299Combined sources15
Beta strandi304 – 311Combined sources8
Helixi312 – 325Combined sources14
Helixi331 – 335Combined sources5
Beta strandi339 – 348Combined sources10
Beta strandi351 – 359Combined sources9
Beta strandi363 – 365Combined sources3
Beta strandi367 – 375Combined sources9
Beta strandi386 – 390Combined sources5
Helixi400 – 402Combined sources3
Beta strandi406 – 408Combined sources3
Beta strandi412 – 420Combined sources9
Beta strandi422 – 429Combined sources8
Beta strandi440 – 443Combined sources4
Helixi446 – 448Combined sources3
Beta strandi451 – 457Combined sources7
Beta strandi460 – 465Combined sources6
Turni466 – 468Combined sources3
Beta strandi469 – 475Combined sources7
Helixi936 – 942Combined sources7
Helixi946 – 959Combined sources14
Helixi964 – 980Combined sources17
Helixi985 – 1006Combined sources22
Helixi1012 – 1015Combined sources4
Beta strandi1020 – 1023Combined sources4
Helixi1028 – 1034Combined sources7
Helixi1045 – 1051Combined sources7
Turni1052 – 1057Combined sources6
Helixi1067 – 1079Combined sources13
Helixi1096 – 1102Combined sources7
Helixi1125 – 1128Combined sources4
Helixi1142 – 1155Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XKSX-ray2.35A67-514[»]
3CQCX-ray2.53B935-1156[»]
3CQGX-ray3.00B934-1156[»]
3I4RX-ray3.53B517-1156[»]
5A9Qelectron microscopy23.003/C/L/U1-1156[»]
DisProtiDP00318.
ProteinModelPortaliQ8WUM0.
SMRiQ8WUM0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WUM0.

Family & Domainsi

Sequence similaritiesi

Belongs to the nucleoporin Nup133 family.Curated

Phylogenomic databases

eggNOGiKOG4121. Eukaryota.
ENOG410XNUX. LUCA.
GeneTreeiENSGT00390000011529.
HOGENOMiHOG000293246.
HOVERGENiHBG052678.
InParanoidiQ8WUM0.
KOiK14300.
OMAiRQHGIIL.
OrthoDBiEOG091G01HJ.
PhylomeDBiQ8WUM0.
TreeFamiTF106141.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q8WUM0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFPAAPSPRT PGTGSRRGPL AGLGPGSTPR TASRKGLPLG SAVSSPVLFS
60 70 80 90 100
PVGRRSSLSS RGTPTRMFPH HSITESVNYD VKTFGSSLPV KVMEALTLAE
110 120 130 140 150
VDDQLTINID EGGWACLVCK EKLIIWKIAL SPITKLSVCK ELQLPPSDFH
160 170 180 190 200
WSADLVALSY SSPSGEAHST QAVAVMVATR EGSIRYWPSL AGEDTYTEAF
210 220 230 240 250
VDSGGDKTYS FLTAVQGGSF ILSSSGSQLI RLIPESSGKI HQHILPQGQG
260 270 280 290 300
MLSGIGRKVS SLFGILSPSS DLTLSSVLWD RERSSFYSLT SSNISKWELD
310 320 330 340 350
DSSEKHAYSW DINRALKENI TDAIWGSESN YEAIKEGVNI RYLDLKQNCD
360 370 380 390 400
GLVILAAAWH SADNPCLIYY SLITIEDNGC QMSDAVTVEV TQYNPPFQSE
410 420 430 440 450
DLILCQLTVP NFSNQTAYLY NESAVYVCST GTGKFSLPQE KIVFNAQGDS
460 470 480 490 500
VLGAGACGGV PIIFSRNSGL VSITSRENVS ILAEDLEGSL ASSVAGPNSE
510 520 530 540 550
SMIFETTTKN ETIAQEDKIK LLKAAFLQYC RKDLGHAQMV VDELFSSHSD
560 570 580 590 600
LDSDSELDRA VTQISVDLMD DYPASDPRWA ESVPEEAPGF SNTSLIILHQ
610 620 630 640 650
LEDKMKAHSF LMDFIHQVGL FGRLGSFPVR GTPMATRLLL CEHAEKLSAA
660 670 680 690 700
IVLKNHHSRL SDLVNTAILI ALNKREYEIP SNLTPADVFF REVSQVDTIC
710 720 730 740 750
ECLLEHEEQV LRDAPMDSIE WAEVVINVNN ILKDMLQAAS HYRQNRNSLY
760 770 780 790 800
RREESLEKEP EYVPWTATSG PGGIRTVIIR QHEIVLKVAY PQADSNLRNI
810 820 830 840 850
VTEQLVALID CFLDGYVSQL KSVDKSSNRE RYDNLEMEYL QKRSDLLSPL
860 870 880 890 900
LSLGQYLWAA SLAEKYCDFD ILVQMCEQTD NQSRLQRYMT QFADQNFSDF
910 920 930 940 950
LFRWYLEKGK RGKLLSQPIS QHGQLANFLQ AHEHLSWLHE INSQELEKAH
960 970 980 990 1000
ATLLGLANME TRYFAKKKTL LGLSKLAALA SDFSEDMLQE KIEEMAEQER
1010 1020 1030 1040 1050
FLLHQETLPE QLLAEKQLNL SAMPVLTAPQ LIGLYICEEN RRANEYDFKK
1060 1070 1080 1090 1100
ALDLLEYIDE EEDININDLK LEILCKALQR DNWSSSDGKD DPIEVSKDSI
1110 1120 1130 1140 1150
FVKILQKLLK DGIQLSEYLP EVKDLLQADQ LGSLKSNPYF EFVLKANYEY

YVQGQI
Length:1,156
Mass (Da):128,979
Last modified:April 3, 2007 - v2
Checksum:i78B733E353824577
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti61R → G in BAA91829 (PubMed:14702039).Curated1
Sequence conflicti146P → S in BAA91829 (PubMed:14702039).Curated1
Sequence conflicti345L → F in AAH20107 (PubMed:15489334).Curated1
Sequence conflicti626S → N in BAA91829 (PubMed:14702039).Curated1
Sequence conflicti928F → L in BAA91885 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_030829106T → P.Corresponds to variant rs428231dbSNPEnsembl.1
Natural variantiVAR_030830294I → V.Corresponds to variant rs11805194dbSNPEnsembl.1
Natural variantiVAR_035854326G → V in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_030831406Q → R.Corresponds to variant rs1065674dbSNPEnsembl.1
Natural variantiVAR_035855448G → R in a breast cancer sample; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XKSX-ray2.35A67-514[»]
3CQCX-ray2.53B935-1156[»]
3CQGX-ray3.00B934-1156[»]
3I4RX-ray3.53B517-1156[»]
5A9Qelectron microscopy23.003/C/L/U1-1156[»]
DisProtiDP00318.
ProteinModelPortaliQ8WUM0.
SMRiQ8WUM0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120864. 58 interactors.
IntActiQ8WUM0. 36 interactors.
MINTiMINT-3046670.
STRINGi9606.ENSP00000261396.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiQ8WUM0.
PhosphoSitePlusiQ8WUM0.
SwissPalmiQ8WUM0.

Polymorphism and mutation databases

BioMutaiNUP133.
DMDMi143811430.

Proteomic databases

EPDiQ8WUM0.
MaxQBiQ8WUM0.
PaxDbiQ8WUM0.
PeptideAtlasiQ8WUM0.
PRIDEiQ8WUM0.

Protocols and materials databases

DNASUi55746.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261396; ENSP00000261396; ENSG00000069248.
GeneIDi55746.
KEGGihsa:55746.
UCSCiuc001htn.4. human.

Organism-specific databases

CTDi55746.
GeneCardsiNUP133.
H-InvDBHIX0001680.
HGNCiHGNC:18016. NUP133.
HPAiHPA059767.
MIMi607613. gene.
neXtProtiNX_Q8WUM0.
OpenTargetsiENSG00000069248.
PharmGKBiPA31847.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4121. Eukaryota.
ENOG410XNUX. LUCA.
GeneTreeiENSGT00390000011529.
HOGENOMiHOG000293246.
HOVERGENiHBG052678.
InParanoidiQ8WUM0.
KOiK14300.
OMAiRQHGIIL.
OrthoDBiEOG091G01HJ.
PhylomeDBiQ8WUM0.
TreeFamiTF106141.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000069248-MONOMER.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-168271. Transport of Ribonucleoproteins into the Host Nucleus.
R-HSA-168276. NS1 Mediated Effects on Host Pathways.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
R-HSA-191859. snRNP Assembly.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6784531. tRNA processing in the nucleus.
R-HSA-68877. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSiNUP133. human.
EvolutionaryTraceiQ8WUM0.
GeneWikiiNUP133.
GenomeRNAii55746.
PROiQ8WUM0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000069248.
CleanExiHS_NUP133.
GenevisibleiQ8WUM0. HS.

Family and domain databases

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

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: November 30, 2016
This is version 151 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

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 one 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.