GTP-binding nuclear protein Ran - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P62826 (RAN_HUMAN)

Last modified February 9, 2010. Version 88. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    GTP-binding nuclear protein Ran
Alternative name(s):
    GTPase Ran
    Ras-related nuclear protein
    Ras-like protein TC4
    Androgen receptor-associated protein 24

Gene names

Name:	RAN
Synonyms:	ARA24
ORF Names:	OK/SW-cl.81

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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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.

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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. Ref.4 Ref.14 Ref.29 Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases. Ref.4 Ref.14 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. Ref.4 Ref.29 Ref.13 Ref.23
Subcellular location	Nucleus. Cytoplasm. Melanosome. Note: Becomes dispersed throughout the cytoplasm during mitosis. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.13 Ref.3 Ref.26
Tissue specificity	Expressed in a variety of tissues. Ref.1
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the small GTPase superfamily. Ran family.

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Ontologies

Keywords
Biological process	Cell cycle Cell division Host-virus interaction Mitosis Protein transport Transport
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA metabolic process Ref.3 Traceable author statement. Source: UniProtKB RNA export from nucleus Non-traceable author statement. Source: UniProtKB androgen receptor signaling pathway Non-traceable author statement. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW mitosis Ref.3 Traceable author statement. Source: UniProtKB mitotic spindle organization Traceable author statement. Source: UniProtKB positive regulation of transcription, DNA-dependent Non-traceable author statement. Source: UniProtKB protein export from nucleus Non-traceable author statement. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. Source: Reactome melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear pore Ref.3 Non-traceable author statement. Source: UniProtKB nucleoplasm Ref.16 Inferred from Experiment. Source: Reactome
Molecular function	GTP binding Ref.13 Inferred from direct assay. Source: UniProtKB GTPase activity Ref.4 Traceable author statement. Source: UniProtKB androgen receptor binding Non-traceable author statement. Source: UniProtKB chromatin binding Ref.13 Traceable author statement. Source: UniProtKB transcription coactivator activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
RANBP3	Q9H6Z4	1	EBI-286642,EBI-992681
RCC1	P18754	2	EBI-286642,EBI-992720
TNPO1	Q92973	1	EBI-286642,EBI-286693
VRK1	Q99986	4	EBI-286642,EBI-1769146
VRK2	Q86Y07-1	2	EBI-286642,EBI-1207633
VRK2	Q86Y07-5	2	EBI-286642,EBI-1207649
VRK3	Q8IV63	1	EBI-286642,EBI-1795523

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.10

Chain

2 – 216

215

GTP-binding nuclear protein Ran

PRO_0000208696

Regions

Nucleotide binding

17 – 24

GTP By similarity

Nucleotide binding

65 – 69

GTP By similarity

Nucleotide binding

122 – 125

GTP By similarity

Amino acid modifications

Modified residue

N-acetylalanine Ref.10 Ref.31

Modified residue

N6-acetyllysine Ref.33

Modified residue

N6-acetyllysine Ref.33

Modified residue

N6-acetyllysine Ref.33

Modified residue

147

Phosphotyrosine Ref.25 Ref.27 Ref.32

Modified residue

155

Phosphotyrosine Ref.27

Modified residue

159

N6-acetyllysine Ref.33

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.28

Natural variations

Natural variant

R → I: dbSNP rs11546488.

VAR_051900

Experimental info

Mutagenesis

G → V: Blocks DNA replication; when associated with L-69. Ref.3

Mutagenesis

T → L: Has low binding affinity for GTP and GDP. Almost completely abolishes interaction with BIRC5. Ref.29

Mutagenesis

Q → L: Blocks DNA replication; when associated with V-19. Ref.29 Ref.3

Mutagenesis

Q → N: Unable to hydrolyze GTP. Increases binding to BIRC5 and promotes exaggerated spindle formation. Ref.29 Ref.3

Sequence conflict

A → T in AAH72000. Ref.9

Sequence conflict

181

A → C in AAC99400. Ref.5

Secondary structure

216

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P62826-1 [UniParc].

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

« Hide

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References

	« Hide 'large scale' referencesShow '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: 2108320] [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: 1855255] [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: 8421051] [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: 10400640] [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. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [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]	"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]. Tissue: Lymph, Ovary, Skin and Uterus.
[10]	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, MASS SPECTROMETRY. Tissue: Platelet.
[11]	Lubec G., Afjehi-Sadat L. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 39-56 AND 153-166, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[12]	"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.
[13]	"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: 1961752] [Abstract] Cited for: PROTEIN SEQUENCE OF 65-76; 90-125; 128-147 AND 154-216, INTERACTION WITH CHC1, SUBCELLULAR LOCATION. Tissue: Cervix carcinoma.
[14]	"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: 8692944] [Abstract] Cited for: FUNCTION.
[15]	"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: 9323133] [Abstract] Cited for: IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH XPO1.
[16]	"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: 9837918] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH HIV-1 REV; HIV-1 REV RESPONSE ELEMENT AND XPO1.
[17]	"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: 10209022] [Abstract] Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX, IDENTIFICATION IN A TRIMERIC EXPORT COMPLEX WITH SNUPN AND XPO1.
[18]	"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: 11571268] [Abstract] Cited for: IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH RANBP3 AND XPO1.
[19]	"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: 11425870] [Abstract] Cited for: IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH RANBP3 AND XPO1.
[20]	"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: 14500717] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH COPS5; RANBP9 AND DYRK1B.
[21]	"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: 12808100] [Abstract] Cited for: INTERACTION WITH TERT.
[22]	"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: 14612415] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH HTLV-1 REX; RANBP3 AND XPO1.
[23]	"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: 14684163] [Abstract] Cited for: INTERACTION WITH RANBP9 AND RANBP10.
[24]	"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: 15574331] [Abstract] Cited for: IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH XPO1.
[25]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-147, MASS SPECTROMETRY.
[26]	"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: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[27]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-147 AND TYR-155, MASS SPECTROMETRY.
[28]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed: 18781797] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-71, MASS SPECTROMETRY.
[29]	"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: 18591255] [Abstract] Cited for: FUNCTION, INTERACTION WITH BIRC5, MUTAGENESIS OF THR-24 AND GLN-69.
[30]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[31]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
[32]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-147, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[33]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-71; LYS-99 AND LYS-159, MASS SPECTROMETRY.
[34]	"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: 7885480] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[35]	"Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp." Chook Y.M., Blobel G. Nature 399:230-237(1999) [PubMed: 10353245] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH KPNB2.
[36]	"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: 10078529] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF COMPLEX WITH NUP358.
+	Additional computationally mapped references.

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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.
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.

IPI

IPI00643041.

PIR

TVHUC3. A44393.

RefSeq

NP_006316.1.

UniGene

Hs.10842

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I2M	X-ray	1.76	A/C	1-216	[»]
1IBR	X-ray	2.30	A/C	1-216	[»]
1K5D	X-ray	2.70	A/D/G/J	1-216	[»]
1K5G	X-ray	3.10	A/D/G/J	1-216	[»]
1QBK	X-ray	3.00	C	1-216	[»]
1RRP	X-ray	2.96	A/C	8-211	[»]
3CH5	X-ray	2.10	A	1-216	[»]
3EA5	X-ray	2.50	A/C	1-216	[»]
3GJ0	X-ray	1.48	A/B	2-216	[»]
3GJ3	X-ray	1.79	A	2-216	[»]
3GJ4	X-ray	2.15	A/C	2-216	[»]
3GJ5	X-ray	1.79	A/C	2-216	[»]
3GJ6	X-ray	2.70	A	2-216	[»]
3GJ7	X-ray	1.93	A/C	2-216	[»]
3GJ8	X-ray	1.82	A/C	2-216	[»]
3GJX	X-ray	2.50	C/F	1-216	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5929N.

IntAct

P62826. 25 interactions.

STRING

P62826.

PTM databases

PhosphoSite

P62826.

2-D gel databases

OGP

P62826.

REPRODUCTION-2DPAGE

P62826.

Proteomic databases

PRIDE

P62826.

Genome annotation databases

Ensembl

ENST00000392369; ENSP00000376176; ENSG00000132341; Homo sapiens. [Genome view]
ENST00000448750; ENSP00000396127; ENSG00000132341; Homo sapiens. [Genome view]

GeneID

5901.

KEGG

hsa:5901.

UCSC

uc001uir.1. human.

Organism-specific databases

CTD

5901.

GeneCards

GC12P129881.

H-InvDB

HIX0011136.

HGNC

HGNC:9846. RAN.

MIM

601179. gene.

PharmGKB

PA34205.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13266.

HOVERGEN

P62826.

InParanoid

P62826.

PhylomeDB

P62826.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_a_pathway. Aurora A signaling.
nfkappabcanonicalpathway. Canonical NF-kappaB pathway.
wnt_canonical_pathway. Canonical Wnt signaling pathway.
foxopathway. FoxO family signaling.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.
ranbp2pathway. Sumoylation by RanBP2 regulates transcriptional repression.

Reactome

REACT_12472. Regulatory RNA pathways.
REACT_6167. Influenza Infection.
REACT_6185. HIV Infection.

Gene expression databases

ArrayExpress

P62826.

Bgee

P62826.

Genevestigator

P62826.

GermOnline

ENSG00000132341. Homo sapiens.

Family and domain databases

InterPro

IPR002041. Ran_GTPase.
IPR013753. Ras.
IPR005225. Small_GTP_bd.
[Graphical view]

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 Resources

NextBio

22956.

SOURCE

Search...

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Entry information

Entry name

RAN_HUMAN

Accession

Primary (citable) accession number: P62826
Secondary accession number(s): P17080

Q9UEU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents