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Protein

Ran guanine nucleotide release factor

Gene

RANGRF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

May regulate the intracellular trafficking of RAN (PubMed:11290418). Promotes guanine nucleotide release from RAN and inhibits binding of new GTP by preventing the binding of the RAN guanine nucleotide exchange factor RCC1 (PubMed:29040603). Regulates the levels of GTP-bound RAN in the nucleus, and thereby plays a role in the regulation of RAN-dependent mitotic spindle dynamics (PubMed:29040603). Enhances the expression of SCN5A at the cell membrane in cardiomyocytes (PubMed:18184654, PubMed:23420830, PubMed:21621375).5 Publications

Miscellaneous

Overexpression can rescue the trafficking defect caused by some SCN5A mutations that impair trafficking to the cell membrane.1 Publication

GO - Molecular functioni

  • guanyl-nucleotide exchange factor activity Source: BHF-UCL
  • ion channel binding Source: BHF-UCL
  • protein transporter activity Source: BHF-UCL
  • Ran GTPase binding Source: UniProtKB
  • Ran guanyl-nucleotide exchange factor activity Source: BHF-UCL
  • sodium channel regulator activity Source: BHF-UCL

GO - Biological processi

  • ER to Golgi vesicle-mediated transport Source: BHF-UCL
  • positive regulation of protein localization to cell surface Source: BHF-UCL
  • positive regulation of protein localization to plasma membrane Source: BHF-UCL
  • protein exit from endoplasmic reticulum Source: BHF-UCL
  • regulation of bundle of His cell action potential Source: BHF-UCL
  • regulation of cardiac muscle cell action potential involved in regulation of contraction Source: BHF-UCL
  • regulation of heart rate Source: BHF-UCL
  • regulation of membrane depolarization Source: BHF-UCL
  • regulation of membrane depolarization during cardiac muscle cell action potential Source: BHF-UCL
  • regulation of membrane potential Source: BHF-UCL
  • regulation of microtubule nucleation by Ran protein signal transduction Source: UniProtKB
  • regulation of sodium ion transmembrane transport Source: BHF-UCL
  • regulation of sodium ion transmembrane transporter activity Source: BHF-UCL

Keywordsi

Molecular functionGuanine-nucleotide releasing factor
Biological processProtein transport, Transport

Enzyme and pathway databases

ReactomeiR-HSA-5576892 Phase 0 - rapid depolarisation

Names & Taxonomyi

Protein namesi
Recommended name:
Ran guanine nucleotide release factor
Short name:
RanGNRF
Alternative name(s):
Ran-binding protein MOG1
Gene namesi
Name:RANGRF
Synonyms:MOG1, RANGNRF
ORF Names:HSPC165, HSPC236, MDS5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000108961.13
HGNCiHGNC:17679 RANGRF
MIMi607954 gene
neXtProtiNX_Q9HD47

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi27D → K: Decreased binding to RAN. 1 Publication1
Mutagenesisi50E → K: Strongly decreased binding to RAN. Abolishes binding to RAN; when associated with K-53. 1 Publication1
Mutagenesisi53E → K: Decreased binding to RAN. Abolishes binding to RAN; when associated with K-50. 1 Publication1
Mutagenesisi70D → K: Decreased binding to RAN. 1 Publication1

Organism-specific databases

DisGeNETi29098
MalaCardsiRANGRF
OpenTargetsiENSG00000108961
PharmGKBiPA162400661

Polymorphism and mutation databases

BioMutaiRANGRF
DMDMi74718913

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003306361 – 186Ran guanine nucleotide release factorAdd BLAST186

Proteomic databases

EPDiQ9HD47
MaxQBiQ9HD47
PaxDbiQ9HD47
PeptideAtlasiQ9HD47
PRIDEiQ9HD47

PTM databases

iPTMnetiQ9HD47
PhosphoSitePlusiQ9HD47

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 are ubiquitously expressed (PubMed:11290418). Detected in heart and brain (PubMed:21621375).2 Publications

Gene expression databases

BgeeiENSG00000108961
CleanExiHS_RANGRF
GenevisibleiQ9HD47 HS

Organism-specific databases

HPAiHPA057280
HPA057888

Interactioni

Subunit structurei

Monomer. Interacts with RAN, both RAN-GTP and RAN-GDP (PubMed:11290418, PubMed:29040603). Competes with RCC1 for a common binding site on RAN and thereby inhibits RCC1-mediated nucleotide exchange (PubMed:29040603). Forms a complex with RAN-GTP and RANBP1 (By similarity). Interacts with the cytoplasmic loop 2 of SCN5A (PubMed:18184654).By similarity3 Publications

GO - Molecular functioni

  • guanyl-nucleotide exchange factor activity Source: BHF-UCL
  • ion channel binding Source: BHF-UCL
  • Ran GTPase binding Source: UniProtKB
  • Ran guanyl-nucleotide exchange factor activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi118866, 28 interactors
IntActiQ9HD47, 2 interactors
STRINGi9606.ENSP00000226105

Structurei

Secondary structure

1186
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Turni10 – 12Combined sources3
Beta strandi13 – 17Combined sources5
Helixi25 – 27Combined sources3
Beta strandi35 – 40Combined sources6
Turni41 – 44Combined sources4
Beta strandi45 – 50Combined sources6
Helixi61 – 71Combined sources11
Turni72 – 74Combined sources3
Beta strandi81 – 87Combined sources7
Helixi90 – 92Combined sources3
Beta strandi100 – 108Combined sources9
Beta strandi123 – 131Combined sources9
Turni132 – 135Combined sources4
Beta strandi136 – 144Combined sources9
Beta strandi156 – 159Combined sources4
Helixi165 – 172Combined sources8
Helixi173 – 175Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5YFGNMR-A1-186[»]
ProteinModelPortaliQ9HD47
SMRiQ9HD47
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni27 – 70Interaction with RAN1 PublicationAdd BLAST44

Sequence similaritiesi

Belongs to the MOG1 family.Curated

Phylogenomic databases

eggNOGiKOG3329 Eukaryota
ENOG4111I9Z LUCA
GeneTreeiENSGT00390000013834
HOVERGENiHBG075266
InParanoidiQ9HD47
OMAiNQPPPDN
OrthoDBiEOG091G0KIN
PhylomeDBiQ9HD47
TreeFamiTF332074

Family and domain databases

CDDicd00224 Mog1, 1 hit
Gene3Di3.40.1000.10, 1 hit
InterProiView protein in InterPro
IPR007681 Mog1
IPR016123 Mog1/PsbP_a/b/a-sand
PANTHERiPTHR15837 PTHR15837, 1 hit
PfamiView protein in Pfam
PF04603 Mog1, 1 hit
SUPFAMiSSF55724 SSF55724, 1 hit

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9HD47-1) [UniParc]FASTAAdd to basket
Also known as: MOG1a

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEPTRDCPLF GGAFSAILPM GAIDVSDLRP VPDNQEVFCH PVTDQSLIVE
60 70 80 90 100
LLELQAHVRG EAAARYHFED VGGVQGARAV HVESVQPLSL ENLALRGRCQ
110 120 130 140 150
EAWVLSGKQQ IAKENQQVAK DVTLHQALLR LPQYQTDLLL TFNQPPPDNR
160 170 180
SSLGPENLSP APWSLGDFEQ LVTSLTLHDP NIFGPQ
Length:186
Mass (Da):20,448
Last modified:March 1, 2001 - v1
Checksum:iBE2C459C90459042
GO
Isoform 2 (identifier: Q9HD47-2) [UniParc]FASTAAdd to basket
Also known as: MOG1b

The sequence of this isoform differs from the canonical sequence as follows:
     147-186: Missing.

Show »
Length:146
Mass (Da):16,118
Checksum:i2EA661B68733EF9B
GO
Isoform 3 (identifier: Q9HD47-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     119-163: AKDVTLHQAL...GPENLSPAPW → RARECVMSWK...GLAEAAPVPD
     164-186: Missing.

Show »
Length:165
Mass (Da):17,711
Checksum:iE69ECDD84D5B4011
GO
Isoform 4 (identifier: Q9HD47-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     118-118: V → P
     119-186: Missing.

Show »
Length:118
Mass (Da):12,900
Checksum:i464DE437624F7A9B
GO

Sequence cautioni

The sequence AAF29129 differs from that shown. Reason: Frameshift at positions 62 and 93.Curated
The sequence AAF87316 differs from that shown. Reason: Frameshift at position 62.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti94 – 96ALR → PE in AAF36156 (PubMed:11042152).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_08007961 – 186Missing Found in patients with cardiac arrhythmia and in patients with Brugada syndrome; loss of function in enhancing the expression of SCN5A at the cell membrane; unknown pathological significance. 2 PublicationsAdd BLAST126
Natural variantiVAR_08008083E → D Found in patients with Brugada syndrome; loss of function in enhancing the expression of SCN5A at the cell membrane; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs751751942EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_033057118V → P in isoform 4. 1 Publication1
Alternative sequenceiVSP_033058119 – 186Missing in isoform 4. 1 PublicationAdd BLAST68
Alternative sequenceiVSP_033059119 – 163AKDVT…SPAPW → RARECVMSWKGGSGDAEIQV SILTLIPLGSKGRDTSSGLA EAAPVPD in isoform 3. 1 PublicationAdd BLAST45
Alternative sequenceiVSP_033060147 – 186Missing in isoform 2. 4 PublicationsAdd BLAST40
Alternative sequenceiVSP_033061164 – 186Missing in isoform 3. 1 PublicationAdd BLAST23

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF265205 mRNA Translation: AAG01291.1
AF265206 mRNA Translation: AAG01292.1
AF168714 mRNA Translation: AAF87316.1 Frameshift.
AF151070 mRNA Translation: AAF36156.1
AF161514 mRNA Translation: AAF29129.1 Frameshift.
AK290399 mRNA Translation: BAF83088.1
CR457206 mRNA Translation: CAG33487.1
CR749387 mRNA Translation: CAH18237.1
CH471108 Genomic DNA Translation: EAW90064.1
CH471108 Genomic DNA Translation: EAW90065.1
CH471108 Genomic DNA Translation: EAW90066.1
BC006486 mRNA Translation: AAH06486.1
BC012552 mRNA Translation: AAH12552.1
BC100017 mRNA Translation: AAI00018.1
CCDSiCCDS11137.1 [Q9HD47-1]
CCDS54086.1 [Q9HD47-2]
CCDS54087.1 [Q9HD47-3]
CCDS82066.1 [Q9HD47-4]
RefSeqiNP_001171272.1, NM_001177801.1 [Q9HD47-2]
NP_001171273.1, NM_001177802.1 [Q9HD47-3]
NP_001317056.1, NM_001330127.1 [Q9HD47-4]
NP_057576.2, NM_016492.4 [Q9HD47-1]
UniGeneiHs.408233

Genome annotation databases

EnsembliENST00000226105; ENSP00000226105; ENSG00000108961 [Q9HD47-1]
ENST00000407006; ENSP00000383940; ENSG00000108961 [Q9HD47-2]
ENST00000439238; ENSP00000413190; ENSG00000108961 [Q9HD47-3]
ENST00000580434; ENSP00000462310; ENSG00000108961 [Q9HD47-4]
GeneIDi29098
KEGGihsa:29098
UCSCiuc002gkv.4 human [Q9HD47-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiMOG1_HUMAN
AccessioniPrimary (citable) accession number: Q9HD47
Secondary accession number(s): D3DTR6
, Q68DI3, Q9BR68, Q9HD48, Q9NRU9, Q9P001, Q9P0P2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: March 1, 2001
Last modified: May 23, 2018
This is version 114 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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