NUP62
Nuclear pore glycoprotein p62
Also known as: DKFZp547L134, FLJ20822, FLJ43869, IBSN, MGC841, NUP62_HUMAN, p62, SNDI
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P37198
- Gene
- NUP62
- Ensembl
- ENSG00000213024
- Chromosome
- 19
- Canonical length
- 522 aa
- Protein class
- Disease related genes, Human disease related genes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins, Transporters
- Subcellular location
- Nucleoplasm,Nuclear membrane
OverviewNCBI Gene
The nuclear pore complex is a massive structure that extends across the nuclear envelope, forming a gateway that regulates the flow of macromolecules between the nucleus and the cytoplasm. Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells. The protein encoded by this gene is a member of the FG-repeat containing nucleoporins and is localized to the nuclear pore central plug. This protein associates with the importin alpha/beta complex which is involved in the import of proteins containing nuclear localization signals. Multiple transcript variants of this gene encode a single protein isoform. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
522 residues, UniProt reviewed canonical sequence.
>P37198|NUP62
1 MSGFNFGGTG APTGGFTFGT AKTATTTPAT GFSFSTSGTG GFNFGAPFQP ATSTPSTGLF
61 SLATQTPATQ TTGFTFGTAT LASGGTGFSL GIGASKLNLS NTAATPAMAN PSGFGLGSSN
121 LTNAISSTVT SSQGTAPTGF VFGPSTTSVA PATTSGGFSF TGGSTAQPSG FNIGSAGNSA
181 QPTAPATLPF TPATPAATTA GATQPAAPTP TATITSTGPS LFASIATAPT SSATTGLSLC
241 TPVTTAGAPT AGTQGFSLKA PGAASGTSTT TSTAATATAT TTSSSSTTGF ALNLKPLAPA
301 GIPSNTAAAV TAPPGPGAAA GAAASSAMTY AQLESLINKW SLELEDQERH FLQQATQVNA
361 WDRTLIENGE KITSLHREVE KVKLDQKRLD QELDFILSQQ KELEDLLSPL EELVKEQSGT
421 IYLQHADEER EKTYKLAENI DAQLKRMAQD LKDIIEHLNT SGAPADTSDP LQQICKILNA
481 HMDSLQWIDQ NSALLQRKVE EVTKVCEGRR KEQERSFRIT FDLocalizationUniProt · AlphaFold · HPA
Whether an antibody against NUP62 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.65
- Highest tissue expression
- 45 nTPM
Expression across tissuesHPA
Tissue
- testis: 45 nTPM
- thymus: 38 nTPM
- lymph node: 36 nTPM
- appendix: 35 nTPM
- tonsil: 34 nTPM
- skeletal muscle: 31 nTPM
Single-cell type
- late primary spermatocytes: 9.3 nCPM
- late spermatids: 6.9 nCPM
- early spermatids: 4.7 nCPM
- oocytes: 4.6 nCPM
- early primary spermatocytes: 3.7 nCPM
- epididymal clear cells: 2 nCPM
Immune cell
- intermediate monocyte: 35 nTPM
- classical monocyte: 34 nTPM
- myeloid DC: 34 nTPM
- plasmacytoid DC: 30 nTPM
- MAIT T-cell: 24 nTPM
- total PBMC: 23 nTPM
Brain region
- white matter: 33 nTPM
- cerebellum: 32 nTPM
- medulla oblongata: 31 nTPM
- hypothalamus: 31 nTPM
- pons: 30 nTPM
- thalamus: 30 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about NUP62.
Disease | AllUniProt
Conditions NUP62 is implicated in, by any mechanism.
- Infantile striatonigral degeneration (SNDI) MIM:271930
Disease | GeneticClinVar
1 pathogenic / likely-pathogenic of 248 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
- Infantile bilateral striatal necrosis
- Familial infantile bilateral striatal necrosis
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.32
- gnomAD pLI
- 0.95
- gnomAD missense Z
- 0.01
- DepMap mean gene effect
- -0.61
- DepMap dependency class
- common
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 7% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cell surface receptor signaling pathway
- cellular senescence
- centriole assembly
- centrosome cycle
- mitotic centrosome separation
- mitotic metaphase chromosome alignment
- mRNA transport
- negative regulation of apoptotic process
- negative regulation of cell population proliferation
- negative regulation of epidermal growth factor receptor signaling pathway
- negative regulation of programmed cell death
- negative regulation of Ras protein signal transduction
- nucleocytoplasmic transport
- positive regulation of canonical NF-kappaB signal transduction
- positive regulation of centriole replication
- positive regulation of DNA-templated transcription
- positive regulation of epidermal growth factor receptor signaling pathway
- positive regulation of mitotic cytokinetic process
- positive regulation of mitotic nuclear division
- positive regulation of protein localization to centrosome
- protein import into nucleus
- regulation of mitotic spindle organization
- regulation of Ras protein signal transduction
- regulation of signal transduction
- RNA export from nucleus
Molecular functions
- chromatin binding
- Hsp70 protein binding
- Hsp90 protein binding
- phospholipid binding
- PTB domain binding
- SH2 domain binding
- signaling receptor complex adaptor activity
- structural constituent of nuclear pore
- ubiquitin binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of NUP62 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads NUP62 as an antibody target. Whether an autoantibody or antibody against NUP62 could matter depends on whether native NUP62 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
NUP62 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label NUP62 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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