RAN
GTP-binding nuclear protein Ran
Also known as: ARA24, Gsp1, RAN_HUMAN, TC4
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P62826
- Gene
- RAN
- Ensembl
- ENSG00000132341
- Chromosome
- 12
- Canonical length
- 216 aa
- Protein class
- Plasma proteins, Predicted intracellular proteins, Transporters
- Subcellular location
- Nucleoplasm
OverviewNCBI Gene
RAN (ras-related nuclear protein) is a small GTP binding protein belonging to the RAS superfamily that is essential for the translocation of RNA and proteins through the nuclear pore complex. The RAN protein is also involved in control of DNA synthesis and cell cycle progression. Nuclear localization of RAN requires the presence of regulator of chromosome condensation 1 (RCC1). Mutations in RAN disrupt DNA synthesis. Because of its many functions, it is likely that RAN interacts with several other proteins. RAN regulates formation and organization of the microtubule network independently of its role in the nucleus-cytosol exchange of macromolecules. RAN could be a key signaling molecule regulating microtubule polymerization during mitosis. RCC1 generates a high local concentration of RAN-GTP around chromatin which, in turn, induces the local nucleation of microtubules. RAN is an androgen receptor (AR) coactivator that binds differentially with different lengths of polyglutamine within the androgen receptor. Polyglutamine repeat expansion in the AR is linked to Kennedy's disease (X-linked spinal and bulbar muscular atrophy). RAN coactivation of the AR diminishes with polyglutamine expansion within the AR, and this weak coactivation may lead to partial androgen insensitivity during the development of Kennedy's disease. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
216 residues, UniProt reviewed canonical sequence.
>P62826|RAN
1 MAAQGEPQVQ FKLVLVGDGG TGKTTFVKRH LTGEFEKKYV ATLGVEVHPL VFHTNRGPIK
61 FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN VPNWHRDLVR VCENIPIVLC
121 GNKVDIKDRK VKAKSIVFHR KKNLQYYDIS AKSNYNFEKP FLWLARKLIG DPNLEFVAMP
181 ALAPPEVVMD PALAAQYEHD LEVAQTTALP DEDDDLLocalizationUniProt · AlphaFold · HPA
Whether an antibody against RAN 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)
- 0.29
- Highest tissue expression
- 537 nTPM
Expression across tissuesHPA
Tissue
- thymus: 537 nTPM
- tonsil: 449 nTPM
- esophagus: 431 nTPM
- skeletal muscle: 395 nTPM
- lymph node: 388 nTPM
- bone marrow: 383 nTPM
Single-cell type
- esophageal basal cells: 1,498 nCPM
- extravillous trophoblasts: 1,366 nCPM
- migrating cytotrophoblasts: 1,242 nCPM
- esophageal suprabasal cells: 1,062 nCPM
- late primary spermatocytes: 1,001 nCPM
- gastric progenitor cells: 906 nCPM
Immune cell
- total PBMC: 1,007 nTPM
- T-reg: 770 nTPM
- memory B-cell: 730 nTPM
- memory CD4 T-cell: 685 nTPM
- MAIT T-cell: 616 nTPM
- naive CD4 T-cell: 614 nTPM
Brain region
- hypothalamus: 311 nTPM
- pons: 253 nTPM
- white matter: 248 nTPM
- spinal cord: 244 nTPM
- basal ganglia: 226 nTPM
- cerebral cortex: 223 nTPM
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)
- 0.26
- gnomAD pLI
- 0.98
- gnomAD missense Z
- 3.42
- DepMap mean gene effect
- -3.93
- DepMap dependency class
- pan
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 6% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- actin cytoskeleton organization
- cell division
- cellular response to mineralocorticoid stimulus
- DNA metabolic process
- GTP metabolic process
- hippocampus development
- mitotic cell cycle
- mitotic sister chromatid segregation
- mitotic spindle organization
- positive regulation of protein import into nucleus
- pre-miRNA export from nucleus
- protein export from nucleus
- protein import into nucleus
- protein localization to nucleolus
- protein-containing complex localization
- ribosomal large subunit export from nucleus
- ribosomal small subunit export from nucleus
- ribosomal subunit export from nucleus
- snRNA import into nucleus
- spermatid development
- viral process
Molecular functions
- cadherin binding
- chromatin binding
- dynein intermediate chain binding
- G protein activity
- GDP binding
- GTP binding
- GTPase activity
- importin-alpha family protein binding
- magnesium ion binding
- protein domain specific binding
- protein heterodimerization activity
- protein-containing complex binding
- RNA binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of RAN 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 RAN as an antibody target. Whether an autoantibody or antibody against RAN could matter depends on whether native RAN is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
RAN 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 RAN as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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