P62827 (RAN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	216 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Protein transport Transport
Cellular component	Cytoplasm Nucleus
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	actin cytoskeleton organization Inferred from mutant phenotype. Source: MGI cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular protein complex localization Inferred from mutant phenotype. Source: MGI mitosis Inferred from electronic annotation. Source: UniProtKB-KW protein import into nucleus Inferred from direct assay. Source: MGI small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.8. Source: MGI
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 216	215	GTP-binding nuclear protein Ran		PRO_0000208697
Regions
	Nucleotide binding	17 – 24	8	GTP By similarity
	Nucleotide binding	65 – 69	5	GTP By similarity
	Nucleotide binding	122 – 125	4	GTP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.7
	Modified residue	60	1	N6-acetyllysine By similarity
	Modified residue	71	1	N6-acetyllysine By similarity
	Modified residue	99	1	N6-acetyllysine By similarity
	Modified residue	147	1	Phosphotyrosine By similarity
	Modified residue	155	1	Phosphotyrosine By similarity
	Modified residue	159	1	N6-acetyllysine By similarity
	Cross-link	71		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Experimental info
	Mutagenesis	24	1	T → N: No effect on RANBP10-binding. Ref.8
	Mutagenesis	69	1	Q → L: Partial decrease in RANBP10-binding. Ref.8
	Sequence conflict	9	1	V → G in BAB27105. Ref.4
	Sequence conflict	43	1	L → P in BAB27105. Ref.4
	Sequence conflict	49	1	P → T in AAK14838. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P62827 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: D5C9B7275C34BCE0	FASTA	216	24,423
	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

References

	« Hide 'large scale' referencesShow '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: 7849398] [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: 8890215] [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: 10500213] [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: 16141072] [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: 15489334] [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: 1555775] [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, 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: 18347012] [Abstract] Cited for: INTERACTION WITH RANBP10, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-24 AND GLN-69.
+	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.
IPI	IPI00134621.
PIR	I57020. JH0654.
RefSeq	NP_033417.1. NM_009391.3. XP_001475472.1. XM_001475422.2.
UniGene	Mm.297440. Mm.386831.
3D structure databases
ProteinModelPortal	P62827.
SMR	P62827. Positions 2-207.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62827. 3 interactions.
STRING	P62827.
PTM databases
PhosphoSite	P62827.
2D gel databases
REPRODUCTION-2DPAGE	P62827.
Proteomic databases
PRIDE	P62827.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000031383; ENSMUSP00000031383; ENSMUSG00000029430. ENSMUST00000111343; ENSMUSP00000106975; ENSMUSG00000029430.
GeneID	100045999. 19384.
KEGG	mmu:100045999. mmu:19384.
UCSC	uc008shc.1. mouse.
Organism-specific databases
CTD	5901.
MGI	MGI:1333112. Ran.
Phylogenomic databases
eggNOG	roNOG08298.
HOVERGEN	HBG107376.
InParanoid	P62827.
OMA	ERVCENI.
OrthoDB	EOG4640CV.
PhylomeDB	P62827.
Gene expression databases
ArrayExpress	P62827.
Bgee	P62827.
CleanEx	MM_RAN.
Genevestigator	P62827.
GermOnline	ENSMUSG00000029430. Mus musculus.
Family and domain databases
InterPro	IPR002041. Ran_GTPase. IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. [Graphical view]
KO	K07936.
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00627. GTPRANTC4.
SMART	SM00176. RAN. 1 hit. [Graphical view]
TIGRFAMs	TIGR00231. Small_GTP. 1 hit.
PROSITE	PS51418. RAN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	459449.
SOURCE	Search...

Entry information

Entry name

RAN_MOUSE

Accession

Primary (citable) accession number: P62827
Secondary accession number(s): P17080 , 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:	January 25, 2012
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program