NARF

Protein identityUniProt · HPA

UniProt accession

Q9UHQ1

Gene

NARF

Ensembl

ENSG00000141562

Chromosome

17

Canonical length

456 aa

Protein class

Predicted intracellular proteins

Subcellular location

Nucleoplasm,Nucleoli

OverviewNCBI Gene

Several proteins have been found to be prenylated and methylated at their carboxyl-terminal ends. Prenylation was initially believed to be important only for membrane attachment. However, another role for prenylation appears to be its importance in protein-protein interactions. The only nuclear proteins known to be prenylated in mammalian cells are prelamin A- and B-type lamins. Prelamin A is farnesylated and carboxymethylated on the cysteine residue of a carboxyl-terminal CaaX motif. This post-translationally modified cysteine residue is removed from prelamin A when it is endoproteolytically processed into mature lamin A. The protein encoded by this gene binds to the prenylated prelamin A carboxyl-terminal tail domain. It may be a component of a prelamin A endoprotease complex. The encoded protein is located in the nucleus, where it partially colocalizes with the nuclear lamina. It shares limited sequence similarity with iron-only bacterial hydrogenases. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene, including one with a novel exon that is generated by RNA editing. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

456 residues, UniProt reviewed canonical sequence.

>Q9UHQ1|NARF
     1  MKCEHCTRKE CSKKTKTDDQ ENVSADAPSP AQENGEKGEF HKLADAKIFL SDCLACDSCM
    61  TAEEGVQLSQ QNAKDFFRVL NLNKKCDTSK HKVLVVSVCP QSLPYFAAKF NLSVTDASRR
   121  LCGFLKSLGV HYVFDTTIAA DFSILESQKE FVRRYRQHSE EERTLPMLTS ACPGWVRYAE
   181  RVLGRPITAH LCTAKSPQQV MGSLVKDYFA RQQNLSPEKI FHVIVAPCYD KKLEALQESL
   241  PPALHGSRGA DCVLTSGEIA QIMEQGDLSV RDAAVDTLFG DLKEDKVTRH DGASSDGHLA
   301  HIFRHAAKEL FNEDVEEVTY RALRNKDFQE VTLEKNGEVV LRFAAAYGFR NIQNMILKLK
   361  KGKFPFHFVE VLACAGGCLN GRGQAQTPDG HADKALLRQM EGIYADIPVR RPESSAHVQE
   421  LYQEWLEGIN SPKAREVLHT TYQSQERGTH SLDIKW

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against NARF 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)

0.28

Highest tissue expression

55 nTPM

Expression across tissuesHPA

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)

1.29

gnomAD pLI

0

gnomAD missense Z

-0.04

DepMap mean gene effect

-0.02

DepMap dependency class

selective

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

Molecular functions

• lamin binding

Cellular components

• lamin filament
• nuclear lamina
• nuclear lumen
• nucleolus
• nucleoplasm

Protein domainsUniProt · Pfam · InterPro

• Iron hydrogenase, small subunit
• Iron hydrogenase, large subunit, C-terminal
• Iron hydrogenase
• Cytosolic Fe-S Cluster Assembly Factor
• Iron hydrogenase small subunit
• Iron only hydrogenase large subunit, C-terminal domain

KeywordsUniProt

• Nucleus
• Phosphoprotein

InteractionsUniProt · HPA

Protein binding partners of NARF in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• LMNA