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9.A.60.1.1
The U snRNA export complex including: phosphorylated adaptor for RNA export (PHAX/RNUXA), nuclear cap-binding protein-1/2 (NCBP1/NCBP2), and RAN GTPase (see also 9.A.50).

Accession Number:P62826
Protein Name:GTP-binding nuclear protein Ran
Length:216
Molecular Weight:24423.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Nucleus1
Substrate small nuclear RNA

Cross database links:

DIP: DIP-5929N
Entrez Gene ID: 5901   
Pfam: PF00071   
KEGG: hsa:5901   

Gene Ontology

GO:0005829 C:cytosol
GO:0042470 C:melanosome
GO:0005643 C:nuclear pore
GO:0005654 C:nucleoplasm
GO:0050681 F:androgen receptor binding
GO:0003682 F:chromatin binding
GO:0005525 F:GTP binding
GO:0003924 F:GTPase activity
GO:0003713 F:transcription coactivator activity
GO:0030521 P:androgen receptor signaling pathway
GO:0051301 P:cell division
GO:0006259 P:DNA metabolic process
GO:0007067 P:mitosis
GO:0007052 P:mitotic spindle organization
GO:0045893 P:positive regulation of transcription, DNA-dependent
GO:0006611 P:protein export from nucleus
GO:0006405 P:RNA export from nucleus
GO:0007264 P:small GTPase mediated signal transduction
GO:0046796 P:viral genome transport in host cell
GO:0019058 P:viral infectious cycle

References (32)

[1] “Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line.”  Drivas G.T.et.al.   2108320
[2] “Premature initiation of mitosis in yeast lacking RCC1 or an interacting GTPase.”  Matsumoto T.et.al.   1855255
[3] “Ran/TC4: a small nuclear GTP-binding protein that regulates DNA synthesis.”  Ren M.et.al.   8421051
[4] “The linkage of Kennedy's neuron disease to ARA24, the first identified androgen receptor polyglutamine region-associated coactivator.”  Hsiao P.-W.et.al.   10400640
[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.et.al.   11042152
[6] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[7] “Mitotic regulator protein RCC1 is complexed with a nuclear ras-related polypeptide.”  Bischoff F.R.et.al.   1961752
[8] “Nuclear protein import: Ran-GTP dissociates the karyopherin alphabeta heterodimer by displacing alpha from an overlapping binding site on beta.”  Moroianu J.et.al.   8692944
[9] “CRM1 is an export receptor for leucine-rich nuclear export signals.”  Fornerod M.et.al.   9323133
[10] “The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP.”  Askjaer P.et.al.   9837918
[11] “CRM1-mediated recycling of snurportin 1 to the cytoplasm.”  Paraskeva E.et.al.   10209022
[12] “RanBP3 influences interactions between CRM1 and its nuclear protein export substrates.”  Englmeier L.et.al.   11571268
[13] “Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export.”  Lindsay M.E.et.al.   11425870
[14] “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.et.al.   14500717
[15] “Hydrogen peroxide triggers nuclear export of telomerase reverse transcriptase via Src kinase family-dependent phosphorylation of tyrosine 707.”  Haendeler J.et.al.   12808100
[16] “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.et.al.   14612415
[17] “A novel MET-interacting protein shares high sequence similarity with RanBPM, but fails to stimulate MET-induced Ras/Erk signaling.”  Wang D.et.al.   14684163
[18] “Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex.”  Petosa C.et.al.   15574331
[19] “Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.”  Rush J.et.al.   15592455
[20] “Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.”  Chi A.et.al.   17081065
[21] “Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.”  Rikova K.et.al.   18083107
[22] “Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.”  Meierhofer D.et.al.   18781797
[23] “A survivin-ran complex regulates spindle formation in tumor cells.”  Xia F.et.al.   18591255
[24] “Proteomics identification of nuclear Ran GTPase as an inhibitor of human VRK1 and VRK2 (vaccinia-related kinase) activities.”  Sanz-Garcia M.et.al.   18617507
[25] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330
[26] “An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells.”  Heibeck T.H.et.al.   19534553
[27] “The mitotic arrest deficient protein MAD2B interacts with the small GTPase RAN throughout the cell cycle.”  Medendorp K.et.al.   19753112
[28] “Lysine acetylation targets protein complexes and co-regulates major cellular functions.”  Choudhary C.et.al.   19608861
[29] “Initial characterization of the human central proteome.”  Burkard T.R.et.al.   21269460
[30] “Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form.”  Scheffzek K.et.al.   7885480
[31] “Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp.”  Chook Y.M.et.al.   10353245
[32] “Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport.”  Vetter I.R.et.al.   10078529
Structure:
1I2M   1IBR   1K5D   1K5G   1QBK   1RRP   2MMC   2MMG   3CH5   3EA5   [...more]

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FASTA formatted sequence
1:	MAAQGEPQVQ FKLVLVGDGG TGKTTFVKRH LTGEFEKKYV ATLGVEVHPL VFHTNRGPIK 
61:	FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN VPNWHRDLVR VCENIPIVLC 
121:	GNKVDIKDRK VKAKSIVFHR KKNLQYYDIS AKSNYNFEKP FLWLARKLIG DPNLEFVAMP 
181:	ALAPPEVVMD PALAAQYEHD LEVAQTTALP DEDDDL