Home RANGAP1
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(Human) GRCh37 - chr22:41641615..41698963 (57.35 kb) View in Genome Browser
HaemAtlas Expression Table for RANGAP1:|
Expression Legend
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Cell Types Showing Expression: Available
Users should be aware that the scale represents a rank within an experiment rather than a normalized expression signal.
| Human | Mouse | Rat | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| ductal cells | exocrine pancreas | pancreatic islets | primary beta cells | Pancreatic Islets MPSS | beta cell line | pancreatic islets | whole pancreas | alpha cell | beta cell line | pancreatic islets | primary beta cells | whole pancreas |
| no data | no data | no data | no data | no data | no data | no data | no data | |||||
Expression Legend
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The Beta Cell Gene Atlas is a collection of almost all available public microarray data generated with pancreatic beta cells and related cell lines and types. The expression data comes from 131 array analyses derived from 28 experiments (open details in a new window). The basal (untreated cell) expression signal intensity values in each array were converted to ranks within the experiments; the highest value was used for genes represented by more than one probe. The rank values of genes in a given cell type were averaged with other calculated values from experiments performed with the same cell type. The rank transformation of the expression values enable comparison of gene expression across different organisms and tissues.
A red border around a cell indicates greater certainty in the data; specifically, the gene has >0.95 probability of being expressed in the tissue.
Tissues Showing Expression: Available
| Users should be aware that the scale represents a rank within an experiment rather than a normalized expression signal. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Signal intensity values were converted to ranks within the experiments. For genes represented by more than one probeset, we averaged the intensity signals for each probeset across all tissues and chose the probeset with the highest average value. The rank transformation of the expression values enables comparison of gene expression across different organisms and tissues. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Interactions Table for RANGAP1:The RANGAP1 interactions are shown below. Each row lists the two interactors, the sources which document this as an interaction, a classification of the interaction as empirical or predicted, and Pubmed IDs (if any) for the interaction.
The table of interactions is downloadable as a text file. Please note that the text file will not include data from HPRD due to restrictions imposed by the HPRD funding sources.
| Interactor | Interactor | Sources | Classification | Pubmed IDs |
| RANGAP1 | TOPORS | BioGRID | empirical | 17803295 |
| RANGAP1 | IPO8 | HPRD | empirical | 9214382 |
| RANGAP1 | CENPA | Reactome | predicted | |
| RANGAP1 | CENPE | Reactome | predicted | |
| RANGAP1 | CENPF | Reactome | predicted | |
| RANGAP1 | NUDC | Reactome | predicted | |
| RANGAP1 | KIF2C | Reactome | predicted | |
| RANGAP1 | ZWINT | Reactome | predicted | |
| RANGAP1 | GABARAPL2 | IntAct | empirical | 17353931 |
| RANGAP1 | CSNK2A1 | HPRD | empirical | 16428860 |
| RANGAP1 | SGOL2 | Reactome | predicted | |
| RANGAP1 | SGOL1 | Reactome | predicted | |
| RANGAP1 | MED19 | IntAct | empirical | 15175163 |
| RANGAP1 | SKA1 | Reactome | predicted | |
| RANGAP1 | MAPRE1 | Reactome | predicted | |
| RANGAP1 | CLASP2 | Reactome | predicted | |
| RANGAP1 | CLASP1 | Reactome | predicted | |
| RANGAP1 | AHCTF1 | Reactome | predicted | |
| RANGAP1 | GNAI1 | IntAct | empirical | 21988832 |
| RANGAP1 | GNAI3 | IntAct | empirical | 21988832 |
| RANGAP1 | BABAM1 | IntAct, BioGRID | empirical | 19615732 |
| RANGAP1 | HLA-B | IntAct | empirical | 17353931 |
| RANGAP1 | INCENP | Reactome | predicted | |
| RANGAP1 | KIF2A | Reactome | predicted | |
| RANGAP1 | KIFC1 | IntAct | empirical | 20360068 |
| RANGAP1 | ARRB2 | IntAct | empirical | 17620599 |
| RANGAP1 | PAFAH1B1 | Reactome | predicted | |
| RANGAP1 | TMBIM4 | IntAct | empirical | 17353931 |
| RANGAP1 | PLK1 | IntAct, BioGRID, Reactome | empirical | 20360068 |
| RANGAP1 | PMS1 | BioGRID | empirical | 17148452 |
| RANGAP1 | NDE1 | Reactome | predicted | |
| RANGAP1 | ERCC6L | Reactome | predicted | |
| RANGAP1 | CCDC99 | Reactome | predicted | |
| RANGAP1 | PPP1CC | Reactome | predicted | |
| RANGAP1 | PRKAB1 | IntAct | empirical | 17353931 |
| RANGAP1 | RCC2 | Reactome | predicted | |
| RANGAP1 | MEPCE | BioGRID | empirical | 17643375 |
| RANGAP1 | TAOK1 | Reactome | predicted | |
| RANGAP1 | RAN | HPRD, BioGRID | empirical | 9219684 7744835 10394366 8146159 20805321 |
| RANGAP1 | RANBP2 | HPRD, IntAct, BioGRID, Reactome | empirical | 11854305 9019411 12192048 20360068 |
| RANGAP1 | RANGAP1 | HPRD, BioGRID | empirical | 8146159 |
| RANGAP1 | SENP2 | BioGRID | empirical | 12419228 |
| RANGAP1 | RPS27 | Reactome | predicted | |
| RANGAP1 | CLIP1 | Reactome | predicted | |
| RANGAP1 | CCL5 | IntAct | empirical | 21988832 |
| RANGAP1 | SUMO3 | HPRD, IntAct, BioGRID | empirical | 16620772 17000644 |
| RANGAP1 | SUMO2 | HPRD | empirical | 9556629 16620772 |
| RANGAP1 | BUB1 | Reactome | predicted | |
| RANGAP1 | TRAF6 | IntAct | empirical | 17353931 |
| RANGAP1 | UBC | BioGRID | empirical | 22178446 21139048 21890473 21906983 |
| RANGAP1 | UBE2I | HPRD, MINT, IntAct, BioGRID | empirical | 11853669 15931224 17036045 17353931 19549727 21988832 12924945 18691969 14578449 21139563 |
| RANGAP1 | SUMO1 | HPRD, MINT, IntAct | empirical | 16428860 9442102 9019411 17000644 15931224 15576338 10961991 17036045 |
| RANGAP1 | XPO1 | Reactome | predicted | |
| RANGAP1 | B9D2 | Reactome | predicted | |
| RANGAP1 | NDEL1 | Reactome | predicted | |
| RANGAP1 | KIF18A | Reactome | predicted | |
| RANGAP1 | MAD1L1 | Reactome | predicted | |
| RANGAP1 | SLX4 | IntAct | empirical | 19596235 |
| RANGAP1 | KIF2B | Reactome | predicted | |
| RANGAP1 | CKAP5 | Reactome | predicted | |
| RANGAP1 | CDC20 | Reactome | predicted |
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Publications: 62
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Integrative analysis of the ubiquitin proteome isolated using Tandem Ubiquitin Binding Entities (TUBEs).
Lopitz-Otsoa F, Rodriguez-Suarez E, Aillet F, Casado-Vela J, Lang V, Matthiesen R, Elortza F, Rodriguez MS
J Proteomics. 2011
PubMed ID: 22178446
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Isoform-specific monobody inhibitors of small ubiquitin-related modifiers engineered using structure-guided library design.
Gilbreth RN, Truong K, Madu I, Koide A, Wojcik JB, Li NS, Piccirilli JA, Chen Y, Koide S
Proc Natl Acad Sci U S A. 2011
PubMed ID: 21518904
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Alternative allosteric mechanisms can regulate the substrate and E2 in SUMO conjugation.
Karaca E, Tozluoğlu M, Nussinov R, Haliloğlu T
J Mol Biol. 2011
PubMed ID: 21216249
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Structure of Importin13-Ubc9 complex: nuclear import and release of a key regulator of sumoylation.
Grünwald M, Bono F
EMBO J. 2011
PubMed ID: 21139563
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Initial characterization of the human central proteome.
Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Bürckstümmer T, Bennett KL, Superti-Furga G, Colinge J
BMC Syst Biol. 2011
PubMed ID: 21269460
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Subgroup II PAK-mediated phosphorylation regulates Ran activity during mitosis.
Bompard G, Rabeharivelo G, Frank M, Cau J, Delsert C, Morin N
J Cell Biol. 2010
PubMed ID: 20805321
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In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification.
Blomster HA, Imanishi SY, Siimes J, Kastu J, Morrice NA, Eriksson JE, Sistonen L
J Biol Chem. 2010
PubMed ID: 20388717
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Systematic analysis of human protein complexes identifies chromosome segregation proteins.
Hutchins JR, Toyoda Y, Hegemann B, Poser I, Hériché JK, Sykora MM, Augsburg M, Hudecz O, Buschhorn BA, Bulkescher J, Conrad C, Comartin D, Schleiffer A, Sarov M, Pozniakovsky A, Slabicki MM, Schloissnig S, Steinmacher I, Leuschner M, Ssykor A, Lawo S, Pelletier L, Stark H, Nasmyth K, Ellenberg J, Durbin R, Buchholz F, Mechtler K, Hyman AA, Peters JM
Science. 2010
PubMed ID: 20360068
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Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA.
Yunus AA, Lima CD
Mol Cell. 2009
PubMed ID: 19748360
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Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M
Science. 2009
PubMed ID: 19608861
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Defining the human deubiquitinating enzyme interaction landscape.
Sowa ME, Bennett EJ, Gygi SP, Harper JW
Cell. 2009
PubMed ID: 19615732
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Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S
Anal Chem. 2009
PubMed ID: 19413330
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Ginkgolic acid inhibits protein SUMOylation by blocking formation of the E1-SUMO intermediate.
Fukuda I, Ito A, Hirai G, Nishimura S, Kawasaki H, Saitoh H, Kimura K, Sodeoka M, Yoshida M
Chem Biol. 2009
PubMed ID: 19246003
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Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK
Sci Signal. 2009
PubMed ID: 19690332
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In vitro nuclear interactome of the HIV-1 Tat protein.
Gautier VW, Gu L, O'Donoghue N, Pennington S, Sheehy N, Hall WW
Retrovirology. 2009
PubMed ID: 19454010
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Mel-18 interacts with RanGAP1 and inhibits its sumoylation.
Zhang J, Sarge KD
Biochem Biophys Res Commun. 2008
PubMed ID: 18706886
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Ubc9 sumoylation regulates SUMO target discrimination.
Knipscheer P, Flotho A, Klug H, Olsen JV, van Dijk WJ, Fish A, Johnson ES, Mann M, Sixma TK, Pichler A
Mol Cell. 2008
PubMed ID: 18691969
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A quantitative atlas of mitotic phosphorylation.
Dephoure N, Zhou C, Villén J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP
Proc Natl Acad Sci U S A. 2008
PubMed ID: 18669648
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Nuclear tumor necrosis factor receptor-associated factor 6 in lymphoid cells negatively regulates c-Myb-mediated transactivation through small ubiquitin-related modifier-1 modification.
Pham LV, Zhou HJ, Lin-Lee YC, Tamayo AT, Yoshimura LC, Fu L, Darnay BG, Ford RJ
J Biol Chem. 2008
PubMed ID: 18093978
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Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction.
Tang LY, Deng N, Wang LS, Dai J, Wang ZL, Jiang XS, Li SJ, Li L, Sheng QH, Wu DQ, Li L, Zeng R
Mol Cell Proteomics. 2007
PubMed ID: 17693683
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TOPORS functions as a SUMO-1 E3 ligase for chromatin-modifying proteins.
Pungaliya P, Kulkarni D, Park HJ, Marshall H, Zheng H, Lackland H, Saleem A, Rubin EH
J Proteome Res. 2007
PubMed ID: 17803295
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Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme.
Jeronimo C, Forget D, Bouchard A, Li Q, Chua G, Poitras C, Thérien C, Bergeron D, Bourassa S, Greenblatt J, Chabot B, Poirier GG, Hughes TR, Blanchette M, Price DH, Coulombe B
Mol Cell. 2007
PubMed ID: 17643375
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The human Nup107-160 nuclear pore subcomplex contributes to proper kinetochore functions.
Zuccolo M, Alves A, Galy V, Bolhy S, Formstecher E, Racine V, Sibarita JB, Fukagawa T, Shiekhattar R, Yen T, Doye V
EMBO J. 2007
PubMed ID: 17363900
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Characterization of the interactome of the human MutL homologues MLH1, PMS1, and PMS2.
Cannavo E, Gerrits B, Marra G, Schlapbach R, Jiricny J
J Biol Chem. 2007
PubMed ID: 17148452
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Large-scale mapping of human protein-protein interactions by mass spectrometry.
Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D
Mol Syst Biol. 2007
PubMed ID: 17353931
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SUMO protease SENP1 induces isomerization of the scissile peptide bond.
Shen L, Tatham MH, Dong C, Zagórska A, Naismith JH, Hay RT
Nat Struct Mol Biol. 2006
PubMed ID: 17099698
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Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics.
Vertegaal AC, Andersen JS, Ogg SC, Hay RT, Mann M, Lamond AI
Mol Cell Proteomics. 2006
PubMed ID: 17000644
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Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M
Cell. 2006
PubMed ID: 17081983
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A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers.
Li T, Santockyte R, Shen RF, Tekle E, Wang G, Yang DC, Chock PB
Arch Biochem Biophys. 2006
PubMed ID: 16620772
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Phosphoproteome analysis of the human mitotic spindle.
Nousiainen M, Silljé HH, Sauer G, Nigg EA, Körner R
Proc Natl Acad Sci U S A. 2006
PubMed ID: 16565220
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The mechanism of nuclear export of Smad3 involves exportin 4 and Ran.
Kurisaki A, Kurisaki K, Kowanetz M, Sugino H, Yoneda Y, Heldin CH, Moustakas A
Mol Cell Biol. 2006
PubMed ID: 16449645
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Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex.
Reverter D, Lima CD
Nature. 2005
PubMed ID: 15931224
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Phosphorylation of RanGAP1 stabilizes its interaction with Ran and RanBP1.
Takeda E, Hieda M, Katahira J, Yoneda Y
Cell Struct Funct. 2005
PubMed ID: 16428860
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A universal strategy for proteomic studies of SUMO and other ubiquitin-like modifiers.
Rosas-Acosta G, Russell WK, Deyrieux A, Russell DH, Wilson VG
Mol Cell Proteomics. 2005
PubMed ID: 15576338
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A mechanism for inhibiting the SUMO pathway.
Boggio R, Colombo R, Hay RT, Draetta GF, Chiocca S
Mol Cell. 2004
PubMed ID: 15546615
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Structural and dynamic independence of isopeptide-linked RanGAP1 and SUMO-1.
Macauley MS, Errington WJ, Okon M, Schärpf M, Mackereth CD, Schulman BA, McIntosh LP
J Biol Chem. 2004
PubMed ID: 15355965
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The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Morrin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J, MGC Project Team
Genome Res. 2004
PubMed ID: 15489334
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Large-scale characterization of HeLa cell nuclear phosphoproteins.
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP
Proc Natl Acad Sci U S A. 2004
PubMed ID: 15302935
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RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly.
Swaminathan S, Kiendl F, Körner R, Lupetti R, Hengst L, Melchior F
J Cell Biol. 2004
PubMed ID: 15037602
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A genome annotation-driven approach to cloning the human ORFeome.
Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I
Genome Biol. 2004
PubMed ID: 15461802
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Histone sumoylation is associated with transcriptional repression.
Shiio Y, Eisenman RN
Proc Natl Acad Sci U S A. 2003
PubMed ID: 14578449
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Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation.
Tatham MH, Kim S, Yu B, Jaffray E, Song J, Zheng J, Rodriguez MS, Hay RT, Chen Y
Biochemistry. 2003
PubMed ID: 12924945
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Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.
Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA, Mammalian Gene Collection Program Team
Proc Natl Acad Sci U S A. 2002
PubMed ID: 12477932
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SUMO-1 protease-1 regulates gene transcription through PML.
Best JL, Ganiatsas S, Agarwal S, Changou A, Salomoni P, Shirihai O, Meluh PB, Pandolfi PP, Zon LI
Mol Cell. 2002
PubMed ID: 12419228
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Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex.
Zhang H, Saitoh H, Matunis MJ
Mol Cell Biol. 2002
PubMed ID: 12192048
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Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.
Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T
DNA Res. 2002
PubMed ID: 12168954
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SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles.
Joseph J, Tan SH, Karpova TS, McNally JG, Dasso M
J Cell Biol. 2002
PubMed ID: 11854305
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Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1.
Bernier-Villamor V, Sampson DA, Matunis MJ, Lima CD
Cell. 2002
PubMed ID: 11853669
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Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.
Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O
DNA Res. 2001
PubMed ID: 11347906
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The DNA sequence of human chromosome 22.
Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP
Nature. 1999
PubMed ID: 10591208
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The crystal structure of rna1p: a new fold for a GTPase-activating protein.
Hillig RC, Renault L, Vetter IR, Drell T, Wittinghofer A, Becker J
Mol Cell. 1999
PubMed ID: 10394366
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In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2.
Okuma T, Honda R, Ichikawa G, Tsumagari N, Yasuda H
Biochem Biophys Res Commun. 1999
PubMed ID: 9920803
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Characterization of a second member of the sentrin family of ubiquitin-like proteins.
Kamitani T, Kito K, Nguyen HP, Fukuda-Kamitani T, Yeh ET
J Biol Chem. 1998
PubMed ID: 9556629
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Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association.
Mahajan R, Gerace L, Melchior F
J Cell Biol. 1998
PubMed ID: 9442102
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The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants.
Scheffzek K, Ahmadian MR, Kabsch W, Wiesmüller L, Lautwein A, Schmitz F, Wittinghofer A
Science. 1997
PubMed ID: 9219684
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A novel class of RanGTP binding proteins.
Görlich D, Dabrowski M, Bischoff FR, Kutay U, Bork P, Hartmann E, Prehn S, Izaurralde E
J Cell Biol. 1997
PubMed ID: 9214382
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A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2.
Mahajan R, Delphin C, Guan T, Gerace L, Melchior F
Cell. 1997
PubMed ID: 9019411
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A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex.
Matunis MJ, Coutavas E, Blobel G
J Cell Biol. 1996
PubMed ID: 8978815
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Ubiquitous expression and testis-specific alternative polyadenylation of mRNA for the human Ran GTPase activator RanGAP1.
Krebber H, Ponstingl H
Gene. 1996
PubMed ID: 8973340
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RNA1 encodes a GTPase-activating protein specific for Gsp1p, the Ran/TC4 homologue of Saccharomyces cerevisiae.
Becker J, Melchior F, Gerke V, Bischoff FR, Ponstingl H, Wittinghofer A
J Biol Chem. 1995
PubMed ID: 7744835
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Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport.
Bischoff FR, Krebber H, Kempf T, Hermes I, Ponstingl H
Proc Natl Acad Sci U S A. 1995
PubMed ID: 7878053
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RanGAP1 induces GTPase activity of nuclear Ras-related Ran.
Bischoff FR, Klebe C, Kretschmer J, Wittinghofer A, Ponstingl H
Proc Natl Acad Sci U S A. 1994
PubMed ID: 8146159
No mouse phenotype links available for this gene.
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