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P62827

- RAN_MOUSE

UniProt

P62827 - RAN_MOUSE

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Protein

GTP-binding nuclear protein Ran

Gene

Ran

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: Ensembl

GO - Biological processi

  1. actin cytoskeleton organization Source: MGI
  2. cellular protein complex localization Source: MGI
  3. cellular protein localization Source: MGI
  4. mitotic nuclear division Source: UniProtKB-KW
  5. positive regulation of protein binding Source: Ensembl
  6. protein export from nucleus Source: Ensembl
  7. protein import into nucleus Source: MGI
  8. ribosomal large subunit export from nucleus Source: Ensembl
  9. ribosomal small subunit export from nucleus Source: Ensembl
  10. small GTPase mediated signal transduction Source: InterPro
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_198968. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_221178. 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: Chromosome 5

Organism-specific databases

MGIiMGI:1333112. Ran.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication. Melanosome By similarity
Note: Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis.

GO - Cellular componenti

  1. chromatin Source: Ensembl
  2. cytoplasm Source: MGI
  3. extracellular vesicular exosome Source: Ensembl
  4. nucleus 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. 1 Publication
Mutagenesisi69 – 691Q → L: Partial decrease in RANBP10-binding. 1 Publication

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.
GenevestigatoriP62827.

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.By similarity

Protein-protein interaction databases

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

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.
OMAiVHPLSFS.
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:
EMBL
GenBank
DDBJ
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_006504280.1.
XP_006544502.1. XM_006544439.1.
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS19693.1.
PIRi I57020.
JH0654.
RefSeqi NP_033417.1. NM_009391.3.
XP_006504343.1. XM_006504280.1.
XP_006544502.1. XM_006544439.1.
UniGenei Mm.297440.
Mm.386831.

3D structure databases

ProteinModelPortali P62827.
SMRi P62827. Positions 8-216.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202580. 4 interactions.
IntActi P62827. 6 interactions.
MINTi MINT-1869723.

PTM databases

PhosphoSitei P62827.

2D gel databases

REPRODUCTION-2DPAGE P62827.

Proteomic databases

MaxQBi P62827.
PaxDbi P62827.
PRIDEi P62827.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031383 ; ENSMUSP00000031383 ; ENSMUSG00000029430 .
ENSMUST00000111343 ; ENSMUSP00000106975 ; ENSMUSG00000029430 .
GeneIDi 102641332.
19384.
KEGGi mmu:102641332.
mmu:19384.
UCSCi uc008zsr.1. mouse.

Organism-specific databases

CTDi 5901.
MGIi MGI:1333112. Ran.

Phylogenomic databases

eggNOGi COG1100.
GeneTreei ENSGT00750000117729.
HOVERGENi HBG107376.
InParanoidi P62827.
KOi K07936.
OMAi VHPLSFS.
OrthoDBi EOG7C8GJ1.
PhylomeDBi P62827.
TreeFami TF106302.

Enzyme and pathway databases

Reactomei REACT_198968. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_221178. MicroRNA (miRNA) biogenesis.

Miscellaneous databases

NextBioi 296489.
PROi P62827.
SOURCEi Search...

Gene expression databases

Bgeei P62827.
CleanExi MM_RAN.
Genevestigatori P62827.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR002041. Ran_GTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view ]
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00627. GTPRANTC4.
SMARTi SM00176. RAN. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51418. RAN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.

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: October 29, 2014
This is version 116 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