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Protein

GTP-binding nuclear protein Ran

Gene

RAN

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

Functioni

GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs (PubMed:10400640, PubMed:8276887, PubMed:8896452, PubMed:8636225, PubMed:8692944, PubMed:9351834, PubMed:9428644, PubMed:9822603, PubMed:26272610). Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis (PubMed:7819259, PubMed:8896452, PubMed:8636225, PubMed:8692944, PubMed:9351834, PubMed:9428644, PubMed:9822603, PubMed:29040603, PubMed:11336674, PubMed:26272610). Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport (PubMed:8896452, PubMed:9351834, PubMed:9428644). Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins (PubMed:20485264). RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation (PubMed:10408446, PubMed:29040603). Required for normal progress through mitosis (PubMed:8421051, PubMed:12194828, PubMed:29040603). The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules (PubMed:18591255). Acts as a negative regulator of the kinase activity of VRK1 and VRK2 (PubMed:18617507). Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases (PubMed:10400640).1 Publication17 Publications

Cofactori

Mg2+1 PublicationNote: Mg2+ interacts primarily with the phosphate groups of the bound guanine nucleotide.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei68GTP; via amide nitrogenCombined sources11 Publications1
Sitei69Essential for GTP hydrolysis3 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi18 – 25GTPCombined sources11 Publications8
Nucleotide bindingi36 – 42GTPCombined sources9 Publications7
Nucleotide bindingi122 – 125GTPCombined sources11 Publications4
Nucleotide bindingi150 – 152GTPCombined sources11 Publications3

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • cadherin binding Source: BHF-UCL
  • chromatin binding Source: UniProtKB
  • dynein intermediate chain binding Source: Ensembl
  • GDP binding Source: UniProtKB
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB
  • importin-alpha family protein binding Source: Ensembl
  • magnesium ion binding Source: UniProtKB
  • protein complex binding Source: Ensembl
  • protein domain specific binding Source: Ensembl
  • protein heterodimerization activity Source: CAFA
  • RNA binding Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: Ensembl
  • androgen receptor signaling pathway Source: UniProtKB
  • cell division Source: UniProtKB-KW
  • cellular protein complex localization Source: Ensembl
  • cellular response to mineralocorticoid stimulus Source: Ensembl
  • DNA metabolic process Source: UniProtKB
  • GTP metabolic process Source: UniProtKB
  • hippocampus development Source: Ensembl
  • intracellular transport of virus Source: Reactome
  • miRNA metabolic process Source: Reactome
  • mitotic cell cycle Source: UniProtKB
  • mitotic sister chromatid segregation Source: UniProtKB
  • mitotic spindle organization Source: UniProtKB
  • positive regulation of protein binding Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • pre-miRNA export from nucleus Source: BHF-UCL
  • protein export from nucleus Source: BHF-UCL
  • protein import into nucleus Source: UniProtKB
  • protein import into nucleus, translocation Source: UniProtKB
  • protein localization to nucleolus Source: UniProtKB
  • regulation of cholesterol biosynthetic process Source: Reactome
  • regulation of gene silencing by miRNA Source: Reactome
  • ribosomal large subunit export from nucleus Source: ParkinsonsUK-UCL
  • ribosomal small subunit export from nucleus Source: ParkinsonsUK-UCL
  • snRNA import into nucleus Source: UniProtKB
  • spermatid development Source: Ensembl
  • tRNA export from nucleus Source: Reactome
  • viral process Source: Reactome

Keywordsi

Biological processCell cycle, Cell division, Host-virus interaction, Mitosis, Protein transport, Transport
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-1655829. Regulation of cholesterol biosynthesis by SREBP (SREBF).
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-203927. MicroRNA (miRNA) biogenesis.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-6784531. tRNA processing in the nucleus.
SignaLinkiP62826.
SIGNORiP62826.

Protein family/group databases

TCDBi9.A.60.1.1. the small nuclear rna exporter (snrna-e).

Names & Taxonomyi

Protein namesi
Recommended name:
GTP-binding nuclear protein Ran
Alternative name(s):
Androgen receptor-associated protein 241 Publication
GTPase Ran
Ras-like protein TC43 Publications
Ras-related nuclear protein
Gene namesi
Name:RAN
Synonyms:ARA241 Publication
ORF Names:OK/SW-cl.81
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000132341.11.
HGNCiHGNC:9846. RAN.
MIMi601179. gene.
neXtProtiNX_P62826.

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

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi19G → V: Blocks DNA replication; when associated with L-69. 1 Publication1
Mutagenesisi24T → L: Has low binding affinity for GTP and GDP. Almost completely abolishes interaction with BIRC5. 1 Publication1
Mutagenesisi24T → N: Has low binding affinity for GTP and GDP. Decreases nuclear import of proteins and RNA. Stabilizes the interaction with RCC1. No effect on nuclear location during interphase. Loss of activity in triggering microtubule assembly at mitotic chromosomes. 5 Publications1
Mutagenesisi25T → A: Minor effect on the interaction with the alpha phosphate group of bound GTP. 1 Publication1
Mutagenesisi39Y → A: Abolishes steric hindrance that traps the essential Q-69 in an unreactive position, and causes slow GTP hydrolysis in wild-type. Loss of one hydrogen bond with the gamma phosphate group of bound GTP. 1 Publication1
Mutagenesisi69Q → L: Strongly decreased GTPase activity. Probably locked in the GTP-bound form. Loss of interaction with NUTF2. Decreases nuclear location and leads to cytoplasmic location during interphase. Loss of function in importin-mediated protein nuclear import. High activity in triggering microtubule assembly at mitotic chromosomes. Blocks DNA replication; when associated with V-19. 8 Publications1
Mutagenesisi69Q → N: Unable to hydrolyze GTP. Increases binding to BIRC5 and promotes exaggerated spindle formation. 1 Publication1
Mutagenesisi70E → A: Strongly decreases the relase of bound GDP. 1 Publication1
Mutagenesisi76R → E: Probable loss of interaction with NUTF2. Loss of transport to the nucleus. 1 Publication1
Mutagenesisi134K → Q: Loss of normal mitotic chromosome segregation and defective mitotic spindle orientation. 1 Publication1
Mutagenesisi134K → R: Loss of normal mitotic chromosome segregation and formation of sister chromatid bridges. 1 Publication1
Mutagenesisi211 – 216Missing : No effect on GTPase activity. Abolishes interaction with RANBP1. 1 Publication6

Organism-specific databases

DisGeNETi5901.
OpenTargetsiENSG00000132341.
PharmGKBiPA34205.

Chemistry databases

DrugBankiDB04315. Guanosine-5'-Diphosphate.

Polymorphism and mutation databases

BioMutaiRAN.
DMDMi51338598.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00002086962 – 216GTP-binding nuclear protein RanAdd BLAST215

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei24PhosphothreonineCombined sources1
Modified residuei60N6-acetyllysineCombined sources1
Modified residuei71N6-acetyllysine; alternateCombined sources1
Cross-linki71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residuei99N6-acetyllysineCombined sources1
Modified residuei134N6-acetyllysine1 Publication1
Cross-linki152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei159N6-acetyllysine; alternateCombined sources1
Modified residuei159N6-succinyllysine; alternateBy similarity1

Post-translational modificationi

Acetylation by KAT5 at Lys-134 is increased during mitosis, impairs RANGRF binding and enhances RCC1 binding.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP62826.
MaxQBiP62826.
PaxDbiP62826.
PeptideAtlasiP62826.
PRIDEiP62826.
TopDownProteomicsiP62826.

2D gel databases

OGPiP62826.
REPRODUCTION-2DPAGEiP62826.
UCD-2DPAGEiP62826.

PTM databases

iPTMnetiP62826.
PhosphoSitePlusiP62826.
SwissPalmiP62826.

Expressioni

Tissue specificityi

Expressed in a variety of tissues.1 Publication

Gene expression databases

BgeeiENSG00000132341.
ExpressionAtlasiP62826. baseline and differential.
GenevisibleiP62826. HS.

Organism-specific databases

HPAiHPA063353.

Interactioni

Subunit structurei

Monomer. Interacts with RANGAP1, which promotes RAN-mediated GTP hydrolysis (PubMed:7819259, PubMed:9428644). Interacts with KPNB1 (PubMed:8896452, PubMed:9428644, PubMed:10367892). Interaction with KPNB1 inhibits RANGAP1-mediated stimulation of GTPase activity (PubMed:9428644). Interacts with RCC1 which promotes the exchange of RAN-bound GDP by GTP (PubMed:1961752, PubMed:7819259, PubMed:12194828, PubMed:11336674). Interaction with KPNB1 inhibits RCC1-mediated exchange of RAN-bound GDP by GTP (PubMed:8896452). Interacts (GTP-bound form) with TNPO1; the interaction is direct (PubMed:9351834). Interacts with KPNB1 and with TNPO1; both inhibit RAN GTPase activity (PubMed:8896452, PubMed:9428644). Interacts (via C-terminus) with RANBP1, which alleviates the inhibition of RAN GTPase activity (PubMed:7891706, PubMed:8896452, PubMed:9428644, PubMed:11832950). Interacts with RANGRF, which promotes the release of bound guanine nucleotide (PubMed:29040603). RANGRF and RCC1 compete for an overlapping binding site on RAN (PubMed:29040603). Identified in a complex with KPNA2 and CSE1L; interaction with RANBP1 mediates dissociation of RAN from this complex (PubMed:9428644). Interaction with both RANBP1 and KPNA2 promotes dissociation of the complex between RAN and KPNB1 (PubMed:9428644). Identified in a complex composed of RAN, RANGAP1 and RANBP1 (PubMed:16428860). Identified in a complex that contains TNPO1, RAN and RANBP1 (PubMed:9428644). Identified in a nuclear export complex with XPO1 (PubMed:9323133, PubMed:15574331, PubMed:10209022). Found in a nuclear export complex with RANBP3 and XPO1 (PubMed:11571268, PubMed:11425870). Interacts with RANBP2/NUP358 (PubMed:10078529, PubMed:26272610). Interaction with RANBP1 or RANBP2 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins (PubMed:20485264). Component of a nuclear export receptor complex composed of KPNB1, RAN, SNUPN and XPO1 (PubMed:10209022, PubMed:19389996). Found in a nuclear export complex with RAN, XPO5 and pre-miRNA (By similarity). Interacts (GTP-bound form) with XPO5 (By similarity). Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5 (PubMed:14500717). Interacts with RANBP9 and RANBP10 (PubMed:14684163). Interacts in its GTP-bound form with BIRC5/survivin at S and M phases of the cell cycle (PubMed:18591255). Interacts with TERT; the interaction requires hydrogen peroxide-mediated phosphorylation of TERT and transports TERT to the nucleus (PubMed:12808100). Interacts with MAD2L2 (PubMed:19753112). Interacts with VRK1 and VRK3 (PubMed:18617507). Interacts with isoform 1 and isoform 2 of VRK2 (PubMed:18617507). Interacts with NEMP1 and KPNB1 (By similarity). Interacts (GDP-bound form) with NUTF2; regulates RAN nuclear import (PubMed:9822603, PubMed:10679025, PubMed:18266911). Interacts with CAPG; mediates CAPG nuclear import (PubMed:10679025, PubMed:18266911). Interacts with NUP153 (PubMed:18611384, PubMed:19505478). Interacts with the AR N-terminal poly-Gln region; the interaction with AR is inversely correlated with the poly-Gln length (PubMed:10400640).By similarity31 Publications
(Microbial infection) In case of HIV-1 infection, found in a complex with HIV-1 Rev, RNAs containing a Rev response element (RRE) and XPO1.1 Publication
(Microbial infection) Found in a complex with HTLV-1 Rex, RANBP3 and XPO1.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • cadherin binding Source: BHF-UCL
  • dynein intermediate chain binding Source: Ensembl
  • importin-alpha family protein binding Source: Ensembl
  • protein complex binding Source: Ensembl
  • protein domain specific binding Source: Ensembl
  • protein heterodimerization activity Source: CAFA

Protein-protein interaction databases

BioGridi111837. 153 interactors.
CORUMiP62826.
DIPiDIP-5929N.
IntActiP62826. 91 interactors.
MINTiP62826.
STRINGi9606.ENSP00000376176.

Structurei

Secondary structure

1216
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni2 – 5Combined sources4
Beta strandi10 – 17Combined sources8
Beta strandi18 – 22Combined sources5
Helixi23 – 27Combined sources5
Helixi31 – 35Combined sources5
Beta strandi38 – 40Combined sources3
Turni41 – 44Combined sources4
Beta strandi45 – 54Combined sources10
Beta strandi57 – 66Combined sources10
Helixi69 – 71Combined sources3
Helixi74 – 76Combined sources3
Helixi77 – 80Combined sources4
Beta strandi85 – 91Combined sources7
Beta strandi92 – 94Combined sources3
Helixi95 – 99Combined sources5
Helixi101 – 111Combined sources11
Beta strandi112 – 114Combined sources3
Beta strandi117 – 122Combined sources6
Beta strandi126 – 128Combined sources3
Helixi133 – 135Combined sources3
Helixi138 – 142Combined sources5
Beta strandi145 – 148Combined sources4
Turni151 – 154Combined sources4
Turni156 – 158Combined sources3
Helixi159 – 169Combined sources11
Beta strandi176 – 178Combined sources3
Turni185 – 187Combined sources3
Helixi191 – 205Combined sources15
Helixi211 – 215Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I2MX-ray1.76A/C1-216[»]
1IBRX-ray2.30A/C1-216[»]
1K5DX-ray2.70A/D/G/J1-216[»]
1K5GX-ray3.10A/D/G/J1-216[»]
1QBKX-ray3.00C1-216[»]
1RRPX-ray2.96A/C8-211[»]
2MMCNMR-A1-216[»]
2MMGNMR-A1-216[»]
2N1BNMR-A1-216[»]
3CH5X-ray2.10A1-216[»]
3EA5X-ray2.50A/C1-216[»]
3GJ0X-ray1.48A/B2-216[»]
3GJ3X-ray1.79A2-216[»]
3GJ4X-ray2.15A/C2-216[»]
3GJ5X-ray1.79A/C2-216[»]
3GJ6X-ray2.70A2-216[»]
3GJ7X-ray1.93A/C2-216[»]
3GJ8X-ray1.82A/C2-216[»]
3GJXX-ray2.50C/F1-216[»]
3NBYX-ray3.42C/F5-180[»]
3NBZX-ray2.80C/F5-180[»]
3NC0X-ray2.90C/F5-180[»]
3NC1X-ray3.35C1-180[»]
3ZJYX-ray3.60A/D/F1-180[»]
4C0QX-ray3.42C/D2-216[»]
4GMXX-ray2.10A1-216[»]
4GPTX-ray2.22A1-216[»]
4HATX-ray1.78A1-216[»]
4HAUX-ray2.00A1-216[»]
4HAVX-ray2.00A1-216[»]
4HAWX-ray1.90A1-216[»]
4HAXX-ray2.28A1-216[»]
4HAYX-ray2.30A1-216[»]
4HAZX-ray1.90A1-216[»]
4HB0X-ray2.20A1-216[»]
4HB2X-ray1.80A1-216[»]
4HB3X-ray2.80A1-216[»]
4HB4X-ray2.05A1-216[»]
4OL0X-ray2.90A1-216[»]
4WVFX-ray1.80A1-216[»]
5CIQX-ray1.65A/B1-216[»]
5CITX-ray1.75A/B1-216[»]
5CIWX-ray1.75A/B1-216[»]
5CJ2X-ray1.75A/B/C/D/E/F/G/H1-216[»]
5CLLX-ray2.45A/C1-191[»]
5CLQX-ray3.20A/C1-216[»]
5DH9X-ray2.55A1-216[»]
5DHAX-ray2.95A1-216[»]
5DHFX-ray2.29A1-216[»]
5DI9X-ray2.28A1-216[»]
5DIFX-ray2.09A1-216[»]
5DISX-ray2.85B8-179[»]
5DLQX-ray3.20C/D5-180[»]
5FYQX-ray3.00C/D31-43[»]
5JLJX-ray2.50A1-216[»]
5UWHX-ray2.26A1-216[»]
5UWIX-ray2.14A1-216[»]
5UWJX-ray2.22A1-216[»]
5UWOX-ray2.35A1-216[»]
5UWPX-ray2.05A1-216[»]
5UWQX-ray2.28A1-216[»]
5UWRX-ray2.24A1-216[»]
5UWSX-ray2.40A1-216[»]
5UWTX-ray2.34A1-216[»]
5UWUX-ray2.24A1-216[»]
5UWWX-ray2.15A1-216[»]
ProteinModelPortaliP62826.
SMRiP62826.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62826.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni211 – 216Interaction with RANBP11 Publication6

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ran family.Curated

Phylogenomic databases

eggNOGiKOG0096. Eukaryota.
ENOG410XNRS. LUCA.
GeneTreeiENSGT00840000129836.
HOVERGENiHBG107376.
InParanoidiP62826.
KOiK07936.
PhylomeDBiP62826.
TreeFamiTF106302.

Family and domain databases

InterProiView protein in InterPro
IPR027417. P-loop_NTPase.
IPR002041. Ran_GTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
PANTHERiPTHR24071. PTHR24071. 1 hit.
PfamiView protein in Pfam
PF00071. Ras. 1 hit.
PRINTSiPR00627. GTPRANTC4.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiView protein in PROSITE
PS51418. RAN. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62826-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQGEPQVQ FKLVLVGDGG TGKTTFVKRH LTGEFEKKYV ATLGVEVHPL
60 70 80 90 100
VFHTNRGPIK FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN
110 120 130 140 150
VPNWHRDLVR VCENIPIVLC GNKVDIKDRK VKAKSIVFHR KKNLQYYDIS
160 170 180 190 200
AKSNYNFEKP FLWLARKLIG DPNLEFVAMP ALAPPEVVMD PALAAQYEHD
210
LEVAQTTALP DEDDDL
Length:216
Mass (Da):24,423
Last modified:January 23, 2007 - v3
Checksum:iD5C9B7275C34BCE0
GO

Sequence cautioni

The sequence BAB93486 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2A → T in AAH72000 (PubMed:15489334).Curated1
Sequence conflicti181A → C in AAC99400 (PubMed:11042152).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31469 mRNA. Translation: AAA36546.1.
AF052578 mRNA. Translation: AAC05840.1.
AF054183 mRNA. Translation: AAC99400.1.
AF501887 mRNA. Translation: AAM15923.1.
BT007271 mRNA. Translation: AAP35935.1.
CR450347 mRNA. Translation: CAG29343.1.
AK290763 mRNA. Translation: BAF83452.1.
AK312466 mRNA. Translation: BAG35373.1.
CH471054 Genomic DNA. Translation: EAW98516.1.
BC004272 mRNA. Translation: AAH04272.3.
BC014518 mRNA. Translation: AAH14518.1.
BC014901 mRNA. Translation: AAH14901.1.
BC016654 mRNA. Translation: AAH16654.1.
BC051908 mRNA. Translation: AAH51908.2.
BC072000 mRNA. Translation: AAH72000.1.
AB062399 mRNA. Translation: BAB93486.1. Different initiation.
CCDSiCCDS9271.1.
PIRiA44393. TVHUC3.
RefSeqiNP_001287725.1. NM_001300796.1.
NP_001287726.1. NM_001300797.1.
NP_006316.1. NM_006325.4.
UniGeneiHs.10842.

Genome annotation databases

EnsembliENST00000392369; ENSP00000376176; ENSG00000132341.
ENST00000543796; ENSP00000446215; ENSG00000132341.
GeneIDi5901.
KEGGihsa:5901.
UCSCiuc001uir.4. human.

Similar proteinsi

Entry informationi

Entry nameiRAN_HUMAN
AccessioniPrimary (citable) accession number: P62826
Secondary accession number(s): A8K3Z8
, P17080, P28746, P28747, Q6IPB2, Q86V08, Q8NI90, Q9CSP3, Q9CWI7, Q9CZA2, Q9UDJ5, Q9UEU9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 177 of the entry and version 3 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, Direct protein sequencing, Reference proteome