Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P62826 (RAN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTP-binding nuclear protein Ran
Alternative name(s):
Androgen receptor-associated protein 24
GTPase Ran
Ras-like protein TC4
Ras-related nuclear protein
Gene names
Name:RAN
Synonyms:ARA24
ORF Names:OK/SW-cl.81
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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 By similarity. 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. Ref.4 Ref.16 Ref.28 Ref.29

Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases. Ref.4 Ref.16 Ref.28 Ref.29

Subunit structure

Monomer. Also forms a complex with CHC1 and interacts with the AR N-terminal poly-Gln region. The interaction with AR is inversely correlated with the poly-Gln length. Part of a complex consisting of RANBP9, Ran, DYRK1B and COPS5. Found in a nuclear export complex with 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. In case of HIV-1 infection, found in a complex with HIV-1 Rev, RNAs containing a Rev response element (RRE) and XPO1. Found in a complex with HTLV-1 Rex, RANBP3 and XPO1. 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. Interacts with RANBP10 By similarity. Interacts with VRK1 and VRK3. Interacts with isoform 1and isoform 2of VRK2. Ref.4 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29 Ref.31

Subcellular location

Nucleus. Cytoplasm. Melanosome. Note: Predominantly nuclear during interphase By similarity. Becomes dispersed throughout the cytoplasm during mitosis. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.3 Ref.15 Ref.27 Ref.29 Ref.31

Tissue specificity

Expressed in a variety of tissues. Ref.1

Sequence similarities

Belongs to the small GTPase superfamily. Ran family.

Sequence caution

The sequence BAB93486.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Host-virus interaction
Mitosis
Protein transport
Transport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA metabolic process

Traceable author statement Ref.3. Source: UniProtKB

androgen receptor signaling pathway

Non-traceable author statement PubMed 15572661. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

intracellular transport of virus

Traceable author statement. Source: Reactome

mitotic nuclear division

Traceable author statement Ref.3. Source: UniProtKB

mitotic spindle organization

Traceable author statement PubMed 10408446. Source: UniProtKB

positive regulation of protein binding

Inferred from direct assay PubMed 16449645. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Non-traceable author statement PubMed 15572661. Source: UniProtKB

protein export from nucleus

Inferred from direct assay PubMed 16449645. Source: BHF-UCL

signal transduction

Traceable author statement PubMed 7603572. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

small molecule metabolic process

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.15. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear pore

Non-traceable author statement Ref.3. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

   Molecular_functionGTP binding

Inferred from direct assay Ref.15. Source: UniProtKB

GTPase activity

Traceable author statement Ref.4. Source: UniProtKB

androgen receptor binding

Non-traceable author statement PubMed 15572661. Source: UniProtKB

chromatin binding

Traceable author statement Ref.15. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.28Ref.15. Source: UniProtKB

transcription coactivator activity

Non-traceable author statement PubMed 15572661. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 216215GTP-binding nuclear protein Ran
PRO_0000208696

Regions

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

Amino acid modifications

Modified residue21N-acetylalanine Ref.12 Ref.30 Ref.34 Ref.35
Modified residue601N6-acetyllysine Ref.32
Modified residue711N6-acetyllysine; alternate Ref.32
Modified residue991N6-acetyllysine Ref.32
Modified residue1591N6-acetyllysine; alternate Ref.32
Modified residue1591N6-succinyllysine; alternate By similarity
Cross-link71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate

Natural variations

Natural variant951R → I.
Corresponds to variant rs11546488 [ dbSNP | Ensembl ].
VAR_051900

Experimental info

Mutagenesis191G → V: Blocks DNA replication; when associated with L-69. Ref.3
Mutagenesis241T → L: Has low binding affinity for GTP and GDP. Almost completely abolishes interaction with BIRC5. Ref.28
Mutagenesis691Q → L: Blocks DNA replication; when associated with V-19. Ref.3 Ref.28
Mutagenesis691Q → N: Unable to hydrolyze GTP. Increases binding to BIRC5 and promotes exaggerated spindle formation. Ref.3 Ref.28
Sequence conflict21A → T in AAH72000. Ref.11
Sequence conflict1811A → C in AAC99400. Ref.5

Secondary structure

.............................................. 216
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62826 [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]"Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line."
Drivas G.T., Shih A., Coutavas E., Rush M.G., D'Eustachio P.
Mol. Cell. Biol. 10:1793-1798(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Teratocarcinoma.
[2]"Premature initiation of mitosis in yeast lacking RCC1 or an interacting GTPase."
Matsumoto T., Beach D.H.
Cell 66:347-360(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO C-TERMINUS.
[3]"Ran/TC4: a small nuclear GTP-binding protein that regulates DNA synthesis."
Ren M., Drivas G.T., D'Eustachio P., Rush M.G.
J. Cell Biol. 120:313-323(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-19 AND GLN-69.
Tissue: Brain.
[4]"The linkage of Kennedy's neuron disease to ARA24, the first identified androgen receptor polyglutamine region-associated coactivator."
Hsiao P.-W., Lin D.-L., Nakao R., Chang C.
J. Biol. Chem. 274:20229-20234(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH AR, FUNCTION.
Tissue: Brain.
[5]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Umbilical cord blood.
[6]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Hippocampus.
[10]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"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].
Tissue: Lymph, Ovary, Skin and Uterus.
[12]Bienvenut W.V., Claeys D.
Submitted (FEB-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-23 AND 143-166, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Platelet.
[13]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 39-56 AND 153-166, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[14]"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
Shichijo S., Itoh K.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-216.
Tissue: Colon adenocarcinoma.
[15]"Mitotic regulator protein RCC1 is complexed with a nuclear ras-related polypeptide."
Bischoff F.R., Ponstingl H.
Proc. Natl. Acad. Sci. U.S.A. 88:10830-10834(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 65-76; 90-125; 128-147 AND 154-216, INTERACTION WITH CHC1, SUBCELLULAR LOCATION.
Tissue: Cervix carcinoma.
[16]"Nuclear protein import: Ran-GTP dissociates the karyopherin alphabeta heterodimer by displacing alpha from an overlapping binding site on beta."
Moroianu J., Blobel G., Radu A.
Proc. Natl. Acad. Sci. U.S.A. 93:7059-7062(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"CRM1 is an export receptor for leucine-rich nuclear export signals."
Fornerod M., Ohno M., Yoshida M., Mattaj I.W.
Cell 90:1051-1060(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH XPO1.
[18]"The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP."
Askjaer P., Jensen T.H., Nilsson J., Englmeier L., Kjems J.
J. Biol. Chem. 273:33414-33422(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH HIV-1 REV; HIV-1 REV RESPONSE ELEMENT AND XPO1.
[19]"CRM1-mediated recycling of snurportin 1 to the cytoplasm."
Paraskeva E., Izaurralde E., Bischoff F.R., Huber J., Kutay U., Hartmann E., Luehrmann R., Goerlich D.
J. Cell Biol. 145:255-264(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX, IDENTIFICATION IN A TRIMERIC EXPORT COMPLEX WITH SNUPN AND XPO1.
[20]"RanBP3 influences interactions between CRM1 and its nuclear protein export substrates."
Englmeier L., Fornerod M., Bischoff F.R., Petosa C., Mattaj I.W., Kutay U.
EMBO Rep. 2:926-932(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH RANBP3 AND XPO1.
[21]"Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export."
Lindsay M.E., Holaska J.M., Welch K., Paschal B.M., Macara I.G.
J. Cell Biol. 153:1391-1402(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH RANBP3 AND XPO1.
[22]"Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M."
Zou Y., Lim S., Lee K., Deng X., Friedman E.
J. Biol. Chem. 278:49573-49581(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH COPS5; RANBP9 AND DYRK1B.
[23]"Hydrogen peroxide triggers nuclear export of telomerase reverse transcriptase via Src kinase family-dependent phosphorylation of tyrosine 707."
Haendeler J., Hoffmann J., Brandes R.P., Zeiher A.M., Dimmeler S.
Mol. Cell. Biol. 23:4598-4610(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TERT.
[24]"A multifunctional domain in human CRM1 (exportin 1) mediates RanBP3 binding and multimerization of human T-cell leukemia virus type 1 Rex protein."
Hakata Y., Yamada M., Shida H.
Mol. Cell. Biol. 23:8751-8761(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH HTLV-1 REX; RANBP3 AND XPO1.
[25]"A novel MET-interacting protein shares high sequence similarity with RanBPM, but fails to stimulate MET-induced Ras/Erk signaling."
Wang D., Li Z., Schoen S.R., Messing E.M., Wu G.
Biochem. Biophys. Res. Commun. 313:320-326(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RANBP9 AND RANBP10.
[26]"Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex."
Petosa C., Schoehn G., Askjaer P., Bauer U., Moulin M., Steuerwald U., Soler-Lopez M., Baudin F., Mattaj I.W., Mueller C.W.
Mol. Cell 16:761-775(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH XPO1.
[27]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[28]"A survivin-ran complex regulates spindle formation in tumor cells."
Xia F., Canovas P.M., Guadagno T.M., Altieri D.C.
Mol. Cell. Biol. 28:5299-5311(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BIRC5, MUTAGENESIS OF THR-24 AND GLN-69.
[29]"Proteomics identification of nuclear Ran GTPase as an inhibitor of human VRK1 and VRK2 (vaccinia-related kinase) activities."
Sanz-Garcia M., Lopez-Sanchez I., Lazo P.A.
Mol. Cell. Proteomics 7:2199-2214(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VRK1; VRK2 AND VRK3.
[30]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"The mitotic arrest deficient protein MAD2B interacts with the small GTPase RAN throughout the cell cycle."
Medendorp K., van Groningen J.J., Vreede L., Hetterschijt L., van den Hurk W.H., de Bruijn D.R., Brugmans L., van Kessel A.G.
PLoS ONE 4:E7020-E7020(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION.
[32]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-71; LYS-99 AND LYS-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]"Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form."
Scheffzek K., Klebe C., Fritz-Wolf K., Kabsch W., Wittinghofer A.
Nature 374:378-381(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[37]"Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp."
Chook Y.M., Blobel G.
Nature 399:230-237(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH KPNB2.
[38]"Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport."
Vetter I.R., Nowak C., Nishimoto T., Kuhlmann J., Wittinghofer A.
Nature 398:39-46(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF COMPLEX WITH NUP358.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9271.1.
PIRTVHUC3. A44393.
RefSeqNP_006316.1. NM_006325.3.
XP_005253649.1. XM_005253592.2.
UniGeneHs.10842.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
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[»]
ProteinModelPortalP62826.
SMRP62826. Positions 8-216.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111837. 110 interactions.
DIPDIP-5929N.
IntActP62826. 41 interactions.
MINTMINT-94188.

Protein family/group databases

TCDB9.A.60.1.1. the small nuclear rna exporter (snrna-e).

PTM databases

PhosphoSiteP62826.

Polymorphism databases

DMDM51338598.

2D gel databases

OGPP62826.
REPRODUCTION-2DPAGEP62826.
UCD-2DPAGEP62826.

Proteomic databases

MaxQBP62826.
PaxDbP62826.
PRIDEP62826.

Protocols and materials databases

DNASU5901.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000392369; ENSP00000376176; ENSG00000132341.
ENST00000543796; ENSP00000446215; ENSG00000132341.
GeneID5901.
KEGGhsa:5901.
UCSCuc001uir.3. human.

Organism-specific databases

CTD5901.
GeneCardsGC12P131356.
HGNCHGNC:9846. RAN.
MIM601179. gene.
neXtProtNX_P62826.
PharmGKBPA34205.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOVERGENHBG107376.
InParanoidP62826.
KOK07936.
OrthoDBEOG7C8GJ1.
PhylomeDBP62826.
TreeFamTF106302.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_71. Gene Expression.
SignaLinkP62826.

Gene expression databases

ArrayExpressP62826.
BgeeP62826.
GenevestigatorP62826.

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

ChiTaRSRAN. human.
EvolutionaryTraceP62826.
GeneWikiRan_(biology).
GenomeRNAi5901.
NextBio22956.
PROP62826.
SOURCESearch...

Entry information

Entry nameRAN_HUMAN
AccessionPrimary (citable) accession number: P62826
Secondary accession number(s): A8K3Z8 expand/collapse secondary AC list , P17080, P28746, P28747, Q6IPB2, Q86V08, Q8NI90, Q9CSP3, Q9CWI7, Q9CZA2, Q9UDJ5, Q9UEU9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM