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P62827 (RAN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTP-binding nuclear protein Ran
Alternative name(s):
GTPase Ran
Ras-like protein TC4
Ras-related nuclear protein
Gene names
Name:Ran
Synonyms:Rasl2-8
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.8

Subcellular location

Nucleus. Cytoplasm. Melanosome By similarity. Note: Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis. Ref.8

Tissue specificity

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

Sequence similarities

Belongs to the small GTPase superfamily. Ran family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 216215GTP-binding nuclear protein Ran
PRO_0000208697

Regions

Nucleotide binding17 – 248GTP By similarity
Nucleotide binding65 – 695GTP By similarity
Nucleotide binding122 – 1254GTP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.7
Modified residue601N6-acetyllysine By similarity
Modified residue711N6-acetyllysine; alternate By similarity
Modified residue991N6-acetyllysine By similarity
Modified residue1591N6-acetyllysine; alternate Ref.9
Modified residue1591N6-succinyllysine; alternate Ref.9
Cross-link71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Experimental info

Mutagenesis241T → N: No effect on RANBP10-binding. Ref.8
Mutagenesis691Q → L: Partial decrease in RANBP10-binding. Ref.8
Sequence conflict91V → G in BAB27105. Ref.4
Sequence conflict431L → P in BAB27105. Ref.4
Sequence conflict491P → T in AAK14838. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P62827 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D5C9B7275C34BCE0

FASTA21624,423
        10         20         30         40         50         60 
MAAQGEPQVQ FKLVLVGDGG TGKTTFVKRH LTGEFEKKYV ATLGVEVHPL VFHTNRGPIK 

        70         80         90        100        110        120 
FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN VPNWHRDLVR VCENIPIVLC 

       130        140        150        160        170        180 
GNKVDIKDRK VKAKSIVFHR KKNLQYYDIS AKSNYNFEKP FLWLARKLIG DPNLEFVAMP 

       190        200        210 
ALAPPEVVMD PALAAQYEHD LEVAQTTALP DEDDDL 

« Hide

References

« Hide 'large scale' references
[1]"Tissue-specific expression of Ran isoforms in the mouse."
Coutavas E.E., Hsieh C.M., Ren M., Drivas G.T., Rush M.G., D'Eustachio P.D.
Mamm. Genome 5:623-628(1994) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI57020.
JH0654.
RefSeqNP_033417.1. NM_009391.3.
XP_006504343.1. XM_006504280.1.
XP_006544502.1. XM_006544439.1.
UniGeneMm.297440.
Mm.386831.

3D structure databases

ProteinModelPortalP62827.
SMRP62827. Positions 8-216.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202580. 3 interactions.
IntActP62827. 6 interactions.
MINTMINT-1869723.

PTM databases

PhosphoSiteP62827.

2D gel databases

REPRODUCTION-2DPAGEP62827.

Proteomic databases

PaxDbP62827.
PRIDEP62827.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031383; ENSMUSP00000031383; ENSMUSG00000029430.
ENSMUST00000111343; ENSMUSP00000106975; ENSMUSG00000029430.
GeneID102641332.
19384.
KEGGmmu:100045999.
mmu:19384.
UCSCuc008zsr.1. mouse.

Organism-specific databases

CTD5901.
MGIMGI:1333112. Ran.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00750000117729.
HOVERGENHBG107376.
InParanoidP62827.
KOK07936.
OMAVHPLSFS.
OrthoDBEOG7C8GJ1.
PhylomeDBP62827.
TreeFamTF106302.

Gene expression databases

BgeeP62827.
CleanExMM_RAN.
GenevestigatorP62827.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR002041. Ran_GTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00627. GTPRANTC4.
SMARTSM00176. RAN. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51418. RAN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio296489.
PROP62827.
SOURCESearch...

Entry information

Entry nameRAN_MOUSE
AccessionPrimary (citable) accession number: P62827
Secondary accession number(s): P17080 expand/collapse secondary AC list , P28746, P28747, Q3U954, Q811M2, Q86V08, Q9CSP3, Q9CWI7, Q9CZA2, Q9UDJ5, Q9UEU9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot