P62826 (RAN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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 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.29 Ref.30 Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases. Ref.4 Ref.16 Ref.29 Ref.30
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 1 and isoform 2 of 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.29 Ref.30 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.30 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 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 Reference proteome
Gene Ontology (GO)
Biological_process	DNA metabolic process Traceable author statement Ref.3. Source: UniProtKB RNA export from nucleus Non-traceable author statement. Source: UniProtKB androgen receptor signaling pathway Non-traceable author statement PubMed 15572661. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW gene expression Traceable author statement. Source: Reactome mitosis 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-dependent Non-traceable author statement PubMed 15572661. Source: UniProtKB protein export from nucleus Non-traceable author statement. Source: UniProtKB small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro viral infectious cycle Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear pore Non-traceable author statement Ref.3. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	GTP 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 transcription coactivator activity Non-traceable author statement PubMed 15572661. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RCC1	P18754	6	EBI-286642,EBI-992720
TNPO1	Q92973	2	EBI-286642,EBI-286693
VRK1	Q99986	12	EBI-286642,EBI-1769146
VRK2	Q86Y07-1	2	EBI-286642,EBI-1207633
VRK2	Q86Y07-5	2	EBI-286642,EBI-1207649

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.12

Chain

2 – 216

215

GTP-binding nuclear protein Ran

PRO_0000208696

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.12

Modified residue

60

1

N6-acetyllysine Ref.32

Modified residue

71

1

N6-acetyllysine; alternate Ref.32

Modified residue

99

1

N6-acetyllysine Ref.32

Modified residue

135

1

Phosphoserine Ref.34

Modified residue

159

1

N6-acetyllysine Ref.32

Cross-link

71

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

Natural variations

Natural variant

95

1

R → I.
Corresponds to variant rs11546488 [ dbSNP | Ensembl ].

VAR_051900

Experimental info

Mutagenesis

19

1

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

Mutagenesis

24

1

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

Mutagenesis

69

1

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

Mutagenesis

69

1

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

Sequence conflict

2

1

A → T in AAH72000. Ref.11

Sequence conflict

181

1

A → C in AAC99400. Ref.5

Secondary structure

1

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216

Helix Strand Turn

Details...

Beta strand

10 – 17

8

Beta strand

18 – 22

5

Helix

23 – 27

5

Helix

31 – 35

5

Beta strand

38 – 40

3

Turn

41 – 44

4

Beta strand

45 – 54

10

Beta strand

57 – 66

10

Helix

69 – 71

3

Helix

74 – 76

3

Helix

77 – 80

4

Beta strand

85 – 91

7

Beta strand

92 – 94

3

Helix

95 – 99

5

Helix

101 – 111

11

Beta strand

112 – 114

3

Beta strand

117 – 122

6

Beta strand

126 – 128

3

Helix

133 – 135

3

Helix

138 – 142

5

Beta strand

145 – 148

4

Turn

151 – 154

4

Turn

156 – 158

3

Helix

159 – 169

11

Beta strand

176 – 178

3

Turn

185 – 187

3

Helix

191 – 205

15

Sequences

	Sequence		Length	Mass (Da)
	P62826 [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]	"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. , 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. , 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. , 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, 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, 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], MASS SPECTROMETRY. Tissue: Melanoma.
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH BIRC5, MUTAGENESIS OF THR-24 AND GLN-69.
[30]	"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.
[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, MASS SPECTROMETRY.
[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]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, MASS SPECTROMETRY.
[35]	"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).
[36]	"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.
[37]	"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.

IPI

IPI00643041.

PIR

TVHUC3. A44393.

RefSeq

NP_006316.1. NM_006325.3.

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	[»]
3NBY	X-ray	3.42	C/F	5-180	[»]
3NBZ	X-ray	2.80	C/F	5-180	[»]
3NC0	X-ray	2.90	C/F	5-180	[»]
3NC1	X-ray	3.35	C	1-180	[»]
4GMX	X-ray	2.10	A	1-216	[»]
4GPT	X-ray	2.22	A	1-216	[»]
4HAT	X-ray	1.78	A	1-216	[»]
4HAU	X-ray	2.00	A	1-216	[»]
4HAV	X-ray	2.00	A	1-216	[»]
4HAW	X-ray	1.90	A	1-216	[»]
4HAX	X-ray	2.28	A	1-216	[»]
4HAY	X-ray	2.30	A	1-216	[»]
4HAZ	X-ray	1.90	A	1-216	[»]
4HB0	X-ray	2.20	A	1-216	[»]
4HB2	X-ray	1.80	A	1-216	[»]
4HB3	X-ray	2.80	A	1-216	[»]
4HB4	X-ray	2.05	A	1-216	[»]

ProteinModelPortal

P62826.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5929N.

IntAct

P62826. 34 interactions.

MINT

MINT-94188.

PTM databases

PhosphoSite

P62826.

Polymorphism databases

DMDM

51338598.

2D gel databases

OGP

P62826.

REPRODUCTION-2DPAGE

P62826.

UCD-2DPAGE

P62826.

Proteomic databases

PaxDb

P62826.

PRIDE

P62826.

Protocols and materials databases

DNASU

5901.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000392369; ENSP00000376176; ENSG00000132341.
ENST00000543796; ENSP00000446215; ENSG00000132341.

GeneID

5901.

KEGG

hsa:5901.

UCSC

uc001uir.3. human.

Organism-specific databases

CTD

5901.

GeneCards

GC12P131356.

HGNC

HGNC:9846. RAN.

MIM

601179. gene.

neXtProt

NX_P62826.

PharmGKB

PA34205.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOVERGEN

HBG107376.

InParanoid

P62826.

KO

K07936.

OrthoDB

EOG4640CV.

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_111217. Metabolism.
REACT_116125. Disease.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P62826.

Bgee

P62826.

Genevestigator

P62826.

GermOnline

ENSG00000132341. Homo sapiens.

Family and domain databases

InterPro

IPR002041. Ran_GTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[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

ChEMBL

CHEMBL1741190.

ChiTaRS

RAN. human.

EvolutionaryTrace

P62826.

GenomeRNAi

5901.

NextBio

22956.

SOURCE

Search...

Entry information

Entry name

RAN_HUMAN

Accession

Primary (citable) accession number: P62826
Secondary accession number(s): A8K3Z8 , 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:	May 1, 2013
This is version 122 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.