NUP50 | ENSG00000093000 | NCBI 10762

Details for: NUP50

Gene ID: 10762

Symbol: NUP50

Ensembl ID: ENSG00000093000

Description: nucleoporin 50

Associated with

Antiviral mechanism by ifn-stimulated genes
(R-HSA-1169410)
Cell cycle
(R-HSA-1640170)
Cell cycle, mitotic
(R-HSA-69278)
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)
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 prophase
(R-HSA-68875)
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 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)
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)
Rev-mediated nuclear export of hiv rna
(R-HSA-165054)
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)
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 transport
(GO:0051028)
Nuclear envelope
(GO:0005635)
Nuclear membrane
(GO:0031965)
Nuclear pore
(GO:0005643)
Nucleocytoplasmic transport
(GO:0006913)
Nucleoplasm
(GO:0005654)
Protein binding
(GO:0005515)
Protein import into nucleus
(GO:0006606)

Other Information

Proteins

Nuclear pore complex protein Nup50

Genular Protein ID: 375216542

Symbol: NUP50_HUMAN

Name: Nuclear pore complex protein Nup50

UniProtKB Accession Codes:

Q9UKX7 B1AHA4 B2RB15 O75644 Q8N6V5 Q9NPM9 Q9NPR6 Q9P1K5

Database IDs:

Citations:

PubMed ID: 10449902

Title: Mapping and complex expression pattern of the human NPAP60L nucleoporin gene.

PubMed ID: 10449902

DOI: 10.1159/000015297

PubMed ID: 15461802

Title: A genome annotation-driven approach to cloning the human ORFeome.

PubMed ID: 15461802

DOI: 10.1186/gb-2004-5-10-r84

PubMed ID: 14702039

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

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 10591208

Title: The DNA sequence of human chromosome 22.

PubMed ID: 10591208

DOI: 10.1038/990031

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: 12802065

Title: Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex.

PubMed ID: 12802065

DOI: 10.1091/mbc.e02-09-0620

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: 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: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20016008

Title: Two isoforms of Npap60 (Nup50) differentially regulate nuclear protein import.

PubMed ID: 20016008

DOI: 10.1091/mbc.e09-05-0374

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: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

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: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

Sequence Information:

Length: 468
Mass: 50144
Checksum: 1F2775AE9AC8FAC4
Sequence:

MAKRNAEKEL TDRNWDQEDE AEEVGTFSMA SEEVLKNRAI KKAKRRNVGF ESDTGGAFKG 
FKGLVVPSGG GRFSGFGSGA GGKPLEGLSN GNNITSAPPF ASAKAAADPK VAFGSLAANG 
PTTLVDKVSN PKTNGDSQQP SSSGLASSKA CVGNAYHKQL AALNCSVRDW IVKHVNTNPL 
CDLTPIFKDY EKYLANIEQQ HGNSGRNSES ESNKVAAETQ SPSLFGSTKL QQESTFLFHG 
NKTEDTPDKK MEVASEKKTD PSSLGATSAS FNFGKKVDSS VLGSLSSVPL TGFSFSPGNS 
SLFGKDTTQS KPVSSPFPTK PLEGQAEGDS GECKGGDEEE NDEPPKVVVT EVKEEDAFYS 
KKCKLFYKKD NEFKEKGIGT LHLKPTANQK TQLLVRADTN LGNILLNVLI PPNMPCTRTG 
KNNVLIVCVP NPPIDEKNAT MPVTMLIRVK TSEDADELHK ILLEKKDA

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: NUP50

Associated with

Other Information

Mapping and complex expression pattern of the human NPAP60L nucleoporin gene. PubMed ID: 10449902

A genome annotation-driven approach to cloning the human ORFeome. PubMed ID: 15461802

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

The DNA sequence of human chromosome 22. PubMed ID: 10591208

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

Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex. PubMed ID: 12802065

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

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

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Two isoforms of Npap60 (Nup50) differentially regulate nuclear protein import. PubMed ID: 20016008

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

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

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

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

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733