NUP133 | ENSG00000069248 | NCBI 55746

Details for: NUP133

Gene ID: 55746

Symbol: NUP133

Ensembl ID: ENSG00000069248

Description: nucleoporin 133

Associated with

Amplification of signal from the kinetochores
(R-HSA-141424)
Amplification of signal from unattached kinetochores via a mad2 inhibitory signal
(R-HSA-141444)
Antiviral mechanism by ifn-stimulated genes
(R-HSA-1169410)
Cell cycle
(R-HSA-1640170)
Cell cycle, mitotic
(R-HSA-69278)
Cell cycle checkpoints
(R-HSA-69620)
Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Cellular response to heat stress
(R-HSA-3371556)
Cytokine signaling in immune system
(R-HSA-1280215)
Defective tpr may confer susceptibility towards thyroid papillary carcinoma (tpc)
(R-HSA-5619107)
Disease
(R-HSA-1643685)
Disorders of transmembrane transporters
(R-HSA-5619115)
Eml4 and nudc in mitotic spindle formation
(R-HSA-9648025)
Export of viral ribonucleoproteins from nucleus
(R-HSA-168274)
Gene expression (transcription)
(R-HSA-74160)
Gene silencing by rna
(R-HSA-211000)
Glucose metabolism
(R-HSA-70326)
Glycolysis
(R-HSA-70171)
Hcmv early events
(R-HSA-9609690)
Hcmv infection
(R-HSA-9609646)
Hcmv late events
(R-HSA-9610379)
Hiv infection
(R-HSA-162906)
Hiv life cycle
(R-HSA-162587)
Host interactions of hiv factors
(R-HSA-162909)
Immune system
(R-HSA-168256)
Infectious disease
(R-HSA-5663205)
Influenza infection
(R-HSA-168255)
Influenza viral rna transcription and replication
(R-HSA-168273)
Interactions of rev with host cellular proteins
(R-HSA-177243)
Interactions of vpr with host cellular proteins
(R-HSA-176033)
Interferon signaling
(R-HSA-913531)
Isg15 antiviral mechanism
(R-HSA-1169408)
Late phase of hiv life cycle
(R-HSA-162599)
Metabolism
(R-HSA-1430728)
Metabolism of carbohydrates
(R-HSA-71387)
Metabolism of non-coding rna
(R-HSA-194441)
Metabolism of proteins
(R-HSA-392499)
Metabolism of rna
(R-HSA-8953854)
Mitotic anaphase
(R-HSA-68882)
Mitotic metaphase and anaphase
(R-HSA-2555396)
Mitotic prometaphase
(R-HSA-68877)
Mitotic prophase
(R-HSA-68875)
Mitotic spindle checkpoint
(R-HSA-69618)
M phase
(R-HSA-68886)
Nep/ns2 interacts with the cellular export machinery
(R-HSA-168333)
Ns1 mediated effects on host pathways
(R-HSA-168276)
Nuclear envelope (ne) reassembly
(R-HSA-2995410)
Nuclear envelope breakdown
(R-HSA-2980766)
Nuclear import of rev protein
(R-HSA-180746)
Nuclear pore complex (npc) disassembly
(R-HSA-3301854)
Post-translational protein modification
(R-HSA-597592)
Postmitotic nuclear pore complex (npc) reformation
(R-HSA-9615933)
Processing of capped intron-containing pre-mrna
(R-HSA-72203)
Regulation of glucokinase by glucokinase regulatory protein
(R-HSA-170822)
Regulation of hsf1-mediated heat shock response
(R-HSA-3371453)
Resolution of sister chromatid cohesion
(R-HSA-2500257)
Rev-mediated nuclear export of hiv rna
(R-HSA-165054)
Rho gtpase effectors
(R-HSA-195258)
Rho gtpases activate formins
(R-HSA-5663220)
Sars-cov-2 activates/modulates innate and adaptive immune responses
(R-HSA-9705671)
Sars-cov-2 infection
(R-HSA-9694516)
Sars-cov-2-host interactions
(R-HSA-9705683)
Sars-cov infections
(R-HSA-9679506)
Separation of sister chromatids
(R-HSA-2467813)
Signaling by rho gtpases
(R-HSA-194315)
Signaling by rho gtpases, miro gtpases and rhobtb3
(R-HSA-9716542)
Signal transduction
(R-HSA-162582)
Slc transporter disorders
(R-HSA-5619102)
Snrnp assembly
(R-HSA-191859)
Sumo e3 ligases sumoylate target proteins
(R-HSA-3108232)
Sumoylation
(R-HSA-2990846)
Sumoylation of chromatin organization proteins
(R-HSA-4551638)
Sumoylation of dna damage response and repair proteins
(R-HSA-3108214)
Sumoylation of dna replication proteins
(R-HSA-4615885)
Sumoylation of rna binding proteins
(R-HSA-4570464)
Sumoylation of sumoylation proteins
(R-HSA-4085377)
Sumoylation of ubiquitinylation proteins
(R-HSA-3232142)
Transcriptional regulation by small rnas
(R-HSA-5578749)
Transport of mature mrna derived from an intron-containing transcript
(R-HSA-159236)
Transport of mature mrna derived from an intronless transcript
(R-HSA-159231)
Transport of mature mrnas derived from intronless transcripts
(R-HSA-159234)
Transport of mature transcript to cytoplasm
(R-HSA-72202)
Transport of ribonucleoproteins into the host nucleus
(R-HSA-168271)
Transport of the slbp dependant mature mrna
(R-HSA-159230)
Transport of the slbp independent mature mrna
(R-HSA-159227)
Trna processing
(R-HSA-72306)
Trna processing in the nucleus
(R-HSA-6784531)
Viral infection pathways
(R-HSA-9824446)
Viral messenger rna synthesis
(R-HSA-168325)
Vpr-mediated nuclear import of pics
(R-HSA-180910)
Mrna export from nucleus
(GO:0006406)
Nuclear pore organization
(GO:0006999)
Nucleocytoplasmic transport
(GO:0006913)
Poly(a)+ mrna export from nucleus
(GO:0016973)
Protein binding
(GO:0005515)
Protein import into nucleus
(GO:0006606)
Structural constituent of nuclear pore
(GO:0017056)
Transcription-dependent tethering of rna polymerase ii gene dna at nuclear periphery
(GO:0000972)

Other Information

Proteins

Nuclear pore complex protein Nup133

Genular Protein ID: 2883074267

Symbol: NU133_HUMAN

Name: Nuclear pore complex protein Nup133

UniProtKB Accession Codes:

Q8WUM0 B2RAZ8 Q5T8N0 Q9H9W2 Q9NV71 Q9NVC4

Database IDs:

Citations:

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16710414

Title: The DNA sequence and biological annotation of human chromosome 1.

PubMed ID: 16710414

DOI: 10.1038/nature04727

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 11564755

Title: An evolutionarily conserved NPC subcomplex, which redistributes in part to kinetochores in mammalian cells.

PubMed ID: 11564755

DOI: 10.1083/jcb.200101081

PubMed ID: 11684705

Title: Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export.

PubMed ID: 11684705

DOI: 10.1083/jcb.200108007

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 26411495

Title: Biallelic mutations in nuclear pore complex subunit NUP107 cause early-childhood-onset steroid-resistant nephrotic syndrome.

PubMed ID: 26411495

DOI: 10.1016/j.ajhg.2015.08.013

PubMed ID: 30427554

Title: Homozygous splicing mutation in NUP133 causes Galloway-Mowat syndrome.

PubMed ID: 30427554

DOI: 10.1002/ana.25370

PubMed ID: 30817857

Title:

PubMed ID: 30817857

DOI: 10.1002/ana.25427

PubMed ID: 30179222

Title: Mutations in multiple components of the nuclear pore complex cause nephrotic syndrome.

PubMed ID: 30179222

DOI: 10.1172/jci98688

PubMed ID: 15557116

Title: Structural and functional analysis of Nup133 domains reveals modular building blocks of the nuclear pore complex.

PubMed ID: 15557116

DOI: 10.1083/jcb.200408109

PubMed ID: 16959974

Title: The consensus coding sequences of human breast and colorectal cancers.

PubMed ID: 16959974

DOI: 10.1126/science.1133427

Sequence Information:

Length: 1156
Mass: 128979
Checksum: 78B733E353824577
Sequence:

MFPAAPSPRT PGTGSRRGPL AGLGPGSTPR TASRKGLPLG SAVSSPVLFS PVGRRSSLSS 
RGTPTRMFPH HSITESVNYD VKTFGSSLPV KVMEALTLAE VDDQLTINID EGGWACLVCK 
EKLIIWKIAL SPITKLSVCK ELQLPPSDFH WSADLVALSY SSPSGEAHST QAVAVMVATR 
EGSIRYWPSL AGEDTYTEAF VDSGGDKTYS FLTAVQGGSF ILSSSGSQLI RLIPESSGKI 
HQHILPQGQG MLSGIGRKVS SLFGILSPSS DLTLSSVLWD RERSSFYSLT SSNISKWELD 
DSSEKHAYSW DINRALKENI TDAIWGSESN YEAIKEGVNI RYLDLKQNCD GLVILAAAWH 
SADNPCLIYY SLITIEDNGC QMSDAVTVEV TQYNPPFQSE DLILCQLTVP NFSNQTAYLY 
NESAVYVCST GTGKFSLPQE KIVFNAQGDS VLGAGACGGV PIIFSRNSGL VSITSRENVS 
ILAEDLEGSL ASSVAGPNSE SMIFETTTKN ETIAQEDKIK LLKAAFLQYC RKDLGHAQMV 
VDELFSSHSD LDSDSELDRA VTQISVDLMD DYPASDPRWA ESVPEEAPGF SNTSLIILHQ 
LEDKMKAHSF LMDFIHQVGL FGRLGSFPVR GTPMATRLLL CEHAEKLSAA IVLKNHHSRL 
SDLVNTAILI ALNKREYEIP SNLTPADVFF REVSQVDTIC ECLLEHEEQV LRDAPMDSIE 
WAEVVINVNN ILKDMLQAAS HYRQNRNSLY RREESLEKEP EYVPWTATSG PGGIRTVIIR 
QHEIVLKVAY PQADSNLRNI VTEQLVALID CFLDGYVSQL KSVDKSSNRE RYDNLEMEYL 
QKRSDLLSPL LSLGQYLWAA SLAEKYCDFD ILVQMCEQTD NQSRLQRYMT QFADQNFSDF 
LFRWYLEKGK RGKLLSQPIS QHGQLANFLQ AHEHLSWLHE INSQELEKAH ATLLGLANME 
TRYFAKKKTL LGLSKLAALA SDFSEDMLQE KIEEMAEQER FLLHQETLPE QLLAEKQLNL 
SAMPVLTAPQ LIGLYICEEN RRANEYDFKK ALDLLEYIDE EEDININDLK LEILCKALQR 
DNWSSSDGKD DPIEVSKDSI FVKILQKLLK DGIQLSEYLP EVKDLLQADQ LGSLKSNPYF 
EFVLKANYEY YVQGQI

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: NUP133

Associated with

Other Information

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The DNA sequence and biological annotation of human chromosome 1. PubMed ID: 16710414

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

An evolutionarily conserved NPC subcomplex, which redistributes in part to kinetochores in mammalian cells. PubMed ID: 11564755

Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export. PubMed ID: 11684705

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PubMed ID: 16964243

Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. PubMed ID: 18220336

Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PubMed ID: 18691976

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features. PubMed ID: 22223895

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. PubMed ID: 22814378

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Immunoaffinity enrichment and mass spectrometry analysis of protein methylation. PubMed ID: 24129315

Biallelic mutations in nuclear pore complex subunit NUP107 cause early-childhood-onset steroid-resistant nephrotic syndrome. PubMed ID: 26411495

Homozygous splicing mutation in NUP133 causes Galloway-Mowat syndrome. PubMed ID: 30427554