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Protein

GTP-binding nuclear protein Ran

Gene

Ran

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle. 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. Acts as a negative regulator of the kinase activity of VRK1 and VRK2 (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 248GTPBy similarity
Nucleotide bindingi65 – 695GTPBy similarity
Nucleotide bindingi122 – 1254GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_276462. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_280637. Transcriptional regulation by small RNAs.
REACT_315548. MicroRNA (miRNA) biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP-binding nuclear protein Ran
Alternative name(s):
GTPase Ran
Ras-like protein TC4
Ras-related nuclear protein
Gene namesi
Name:Ran
Synonyms:Rasl2-8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1333112. Ran.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: MGI
  • chromatin Source: Ensembl
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: MGI
  • midbody Source: MGI
  • nucleolus Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • recycling endosome Source: MGI
  • RNA nuclear export complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi24 – 241T → N: No effect on RANBP10-binding. Loss of interaction with NEMP1. 2 Publications
Mutagenesisi42 – 421T → A: Loss of interaction with NEMP1. 1 Publication
Mutagenesisi69 – 691Q → L: Partial decrease in RANBP10-binding. No effect on interaction with NEMP1 and KPNB1. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 216215GTP-binding nuclear protein RanPRO_0000208697Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei60 – 601N6-acetyllysineBy similarity
Modified residuei71 – 711N6-acetyllysine; alternateBy similarity
Cross-linki71 – 71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei99 – 991N6-acetyllysineBy similarity
Modified residuei159 – 1591N6-acetyllysine; alternate1 Publication
Modified residuei159 – 1591N6-succinyllysine; alternate1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP62827.
PaxDbiP62827.
PRIDEiP62827.

2D gel databases

REPRODUCTION-2DPAGEP62827.

PTM databases

PhosphoSiteiP62827.

Expressioni

Tissue specificityi

Expressed in a variety of tissues, including testis.1 Publication

Gene expression databases

BgeeiP62827.
CleanExiMM_RAN.
GenevisibleiP62827. MM.

Interactioni

Subunit structurei

Monomer (By similarity). Also forms a complex with CHC1. Found in a complex with nuclear export signal-cargo peptides, RANBP3 and XPO1. Component of a nuclear export receptor complex composed of KPNB1, Ran, SNUPN and XPO1. Found in a trimeric export complex with SNUPN, Ran and XPO1. Interacts with RANBP10. Interacts in its GTP-bound form with BIRC5/survivin at S and M phases of the cell cycle. Interacts with TERT; the interaction requires hydrogen peroxide-mediated phosphorylation of TERT and transports TERT to the nucleus. Interacts with MAD2L2 (By similarity). Interacts with RANBP10. Interacts with VRK1, VRK2 and VRK3 (By similarity). Interacts with NEMP1 and KPNB1 (PubMed:25946333).By similarity1 Publication

Protein-protein interaction databases

BioGridi202580. 4 interactions.
IntActiP62827. 6 interactions.
MINTiMINT-1869723.
STRINGi10090.ENSMUSP00000031383.

Structurei

3D structure databases

ProteinModelPortaliP62827.
SMRiP62827. Positions 8-216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ran family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00750000117729.
HOVERGENiHBG107376.
InParanoidiP62827.
KOiK07936.
OMAiQYQQEME.
OrthoDBiEOG7C8GJ1.
PhylomeDBiP62827.
TreeFamiTF106302.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR002041. Ran_GTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00627. GTPRANTC4.
SMARTiSM00176. RAN. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51418. RAN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62827-1 [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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91V → G in BAB27105 (PubMed:16141072).Curated
Sequence conflicti43 – 431L → P in BAB27105 (PubMed:16141072).Curated
Sequence conflicti49 – 491P → T in AAK14838 (PubMed:1555775).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L32751 mRNA. Translation: AAA64247.1.
S83456 mRNA. Translation: AAB50841.1.
AF159256 mRNA. Translation: AAD45343.1.
AK010569 mRNA. Translation: BAB27034.1.
AK010672 mRNA. Translation: BAB27105.1.
AK012268 mRNA. No translation available.
AK012844 mRNA. No translation available.
AK075900 mRNA. Translation: BAC36040.1.
AK087974 mRNA. Translation: BAC40068.1.
AK151341 mRNA. Translation: BAE30319.1.
AK151937 mRNA. Translation: BAE30813.1.
AK153197 mRNA. Translation: BAE31797.1.
AK153411 mRNA. Translation: BAE31971.1.
AK160647 mRNA. Translation: BAE35939.1.
AK167040 mRNA. Translation: BAE39208.1.
AK168183 mRNA. Translation: BAE40143.1.
BC014829 mRNA. Translation: AAH14829.3.
BC083356 mRNA. Translation: AAH83356.1.
M79316 mRNA. Translation: AAK14838.1.
CCDSiCCDS19693.1.
PIRiI57020.
JH0654.
RefSeqiNP_033417.1. NM_009391.3.
XP_006504343.1. XM_006504280.2.
XP_006544502.1. XM_006544439.2.
UniGeneiMm.297440.
Mm.386831.

Genome annotation databases

EnsembliENSMUST00000031383; ENSMUSP00000031383; ENSMUSG00000029430.
ENSMUST00000111343; ENSMUSP00000106975; ENSMUSG00000029430.
GeneIDi102641332.
19384.
KEGGimmu:102641332.
mmu:19384.
UCSCiuc008zsr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L32751 mRNA. Translation: AAA64247.1.
S83456 mRNA. Translation: AAB50841.1.
AF159256 mRNA. Translation: AAD45343.1.
AK010569 mRNA. Translation: BAB27034.1.
AK010672 mRNA. Translation: BAB27105.1.
AK012268 mRNA. No translation available.
AK012844 mRNA. No translation available.
AK075900 mRNA. Translation: BAC36040.1.
AK087974 mRNA. Translation: BAC40068.1.
AK151341 mRNA. Translation: BAE30319.1.
AK151937 mRNA. Translation: BAE30813.1.
AK153197 mRNA. Translation: BAE31797.1.
AK153411 mRNA. Translation: BAE31971.1.
AK160647 mRNA. Translation: BAE35939.1.
AK167040 mRNA. Translation: BAE39208.1.
AK168183 mRNA. Translation: BAE40143.1.
BC014829 mRNA. Translation: AAH14829.3.
BC083356 mRNA. Translation: AAH83356.1.
M79316 mRNA. Translation: AAK14838.1.
CCDSiCCDS19693.1.
PIRiI57020.
JH0654.
RefSeqiNP_033417.1. NM_009391.3.
XP_006504343.1. XM_006504280.2.
XP_006544502.1. XM_006544439.2.
UniGeneiMm.297440.
Mm.386831.

3D structure databases

ProteinModelPortaliP62827.
SMRiP62827. Positions 8-216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202580. 4 interactions.
IntActiP62827. 6 interactions.
MINTiMINT-1869723.
STRINGi10090.ENSMUSP00000031383.

PTM databases

PhosphoSiteiP62827.

2D gel databases

REPRODUCTION-2DPAGEP62827.

Proteomic databases

MaxQBiP62827.
PaxDbiP62827.
PRIDEiP62827.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031383; ENSMUSP00000031383; ENSMUSG00000029430.
ENSMUST00000111343; ENSMUSP00000106975; ENSMUSG00000029430.
GeneIDi102641332.
19384.
KEGGimmu:102641332.
mmu:19384.
UCSCiuc008zsr.1. mouse.

Organism-specific databases

CTDi5901.
MGIiMGI:1333112. Ran.

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00750000117729.
HOVERGENiHBG107376.
InParanoidiP62827.
KOiK07936.
OMAiQYQQEME.
OrthoDBiEOG7C8GJ1.
PhylomeDBiP62827.
TreeFamiTF106302.

Enzyme and pathway databases

ReactomeiREACT_276462. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_280637. Transcriptional regulation by small RNAs.
REACT_315548. MicroRNA (miRNA) biogenesis.

Miscellaneous databases

NextBioi296489.
PROiP62827.
SOURCEiSearch...

Gene expression databases

BgeeiP62827.
CleanExiMM_RAN.
GenevisibleiP62827. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR002041. Ran_GTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00627. GTPRANTC4.
SMARTiSM00176. RAN. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51418. RAN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "Restoration of lipopolysaccharide-mediated B-cell response after expression of a cDNA encoding a GTP-binding protein."
    Kang A.D., Wong P.M., Chen H., Castagna R., Chung S.W., Sultzer B.M.
    Infect. Immun. 64:4612-4617(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H/HeJ.
    Tissue: Spleen.
  3. "Lps(d)/Ran of endotoxin-resistant C3H/HeJ mice is defective in mediating lipopolysaccharide endotoxin responses."
    Wong P.M.C., Kang A., Chen H., Yuan Q., Fan P., Sultzer B.M., Kan Y.W., Chung S.-W.
    Proc. Natl. Acad. Sci. U.S.A. 96:11543-11548(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H/HeJ.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/c, C57BL/6J and NOD.
    Tissue: Bone marrow, Embryo, Embryonic stem cell, Thymus and Tongue.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain and Mammary tumor.
  6. "The complexity of the Rab and Rho GTP-binding protein subfamilies revealed by a PCR cloning approach."
    Chavrier P., Simons K., Zerial M.
    Gene 112:261-264(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-70.
    Tissue: Kidney.
  7. Bienvenut W.V., Sandilands E., Serrels B., Brunton V.G., Frame M.C.
    Submitted (FEB-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-23; 57-71 AND 143-152, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic fibroblast.
  8. "RanBP10 is a cytoplasmic guanine nucleotide exchange factor that modulates noncentrosomal microtubules."
    Schulze H., Dose M., Korpal M., Meyer I., Italiano J.E. Jr., Shivdasani R.A.
    J. Biol. Chem. 283:14109-14119(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RANBP10, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-24 AND GLN-69.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-159, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. "The inner nuclear membrane protein Nemp1 is a new type of RanGTP-binding protein in eukaryotes."
    Shibano T., Mamada H., Hakuno F., Takahashi S., Taira M.
    PLoS ONE 10:E0127271-E0127271(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEMP1 AND KPNB1, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-24; THR-42 AND GLN-69.

Entry informationi

Entry nameiRAN_MOUSE
AccessioniPrimary (citable) accession number: P62827
Secondary accession number(s): P17080
, P28746, P28747, Q3U954, Q811M2, Q86V08, Q9CSP3, Q9CWI7, Q9CZA2, Q9UDJ5, Q9UEU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.