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P46061

- RAGP1_MOUSE

UniProt

P46061 - RAGP1_MOUSE

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Protein
Ran GTPase-activating protein 1
Gene
Rangap1, Fug1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state. Required for postimplantation development.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei564 – 5641Hydrophobic interaction with UBC9 By similarity
Sitei567 – 5671Hydrophobic interaction with UBC9 By similarity

GO - Molecular functioni

  1. Ran GTPase activator activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. negative regulation of protein export from nucleus Source: Ensembl
  2. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiREACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_207679. Separation of Sister Chromatids.

Names & Taxonomyi

Protein namesi
Recommended name:
Ran GTPase-activating protein 1
Short name:
RanGAP1
Gene namesi
Name:Rangap1
Synonyms:Fug1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:103071. Rangap1.

Subcellular locationi

Cytoplasm By similarity. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Chromosomecentromerekinetochore By similarity. Cytoplasmcytoskeletonspindle By similarity
Note: Cytoplasmic during interphase. Targeted to the nuclear rim after sumoylation. During mitosis, associates with mitotic spindles. Association with kinetochores appears soon after nuclear envelope breakdown and persists until late anaphase. Mitotic location also requires sumoylation By similarity.3 Publications

GO - Cellular componenti

  1. condensed chromosome kinetochore Source: UniProtKB-SubCell
  2. cytoplasm Source: MGI
  3. nuclear membrane Source: UniProtKB-SubCell
  4. perinuclear region of cytoplasm Source: MGI
  5. spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi411 – 4111T → D: Greatly reduced phosphorylation by CDK1 or CDK2. Completely abolished phosphorylation by CDK1 or CDK2; when associated with D-444. 1 Publication
Mutagenesisi444 – 4441S → D: Little change in phosphorylation by CDK1 or CDK2. Completely abolished phosphorylation by CDK1 or CDK2; when associated with D-411. 1 Publication
Mutagenesisi512 – 5121N → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
Mutagenesisi516 – 5161T → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
Mutagenesisi517 – 5171R → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
Mutagenesisi520 – 5201I → A: No effect on UBC9 binding nor on sumoylation.
Mutagenesisi521 – 5211H → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
Mutagenesisi522 – 5221M → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
Mutagenesisi524 – 5241L → A: No sumoylation. 1 Publication
Mutagenesisi525 – 5251L → A: Disrupted binding of UCB9, and no sumoylation. 1 Publication
Mutagenesisi526 – 5261K → A: No UBC9 binding nor sumoylation. 4 Publications
Mutagenesisi526 – 5261K → R: Absence of sumoylation. Not targeted to the nuclear envelope rim nor to nuclear pore complexes. Disrupted sumoylation. No interaction with SUMO1; when associated with A-564 and with or without SUMO1 A-97. 4 Publications
Mutagenesisi528 – 5281E → A: No UBC9 binding nor sumoylation. 1 Publication
Mutagenesisi529 – 5291D → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
Mutagenesisi531 – 5311I → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
Mutagenesisi537 – 5371L → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
Mutagenesisi560 – 5601L → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
Mutagenesisi563 – 5631A → L: No effect on UBC9 binding nor on sumoylation. 1 Publication
Mutagenesisi564 – 5641F → A: No UBC9 binding nor sumoylation. Not targeted to nuclear core complexes; when associated with R-526. 2 Publications
Mutagenesisi567 – 5671K → A: No UBC9 binding nor sumoylation. 1 Publication
Mutagenesisi569 – 5691N → A: No effect on UBC9 binding nor on sumoylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 589588Ran GTPase-activating protein 1
PRO_0000056738Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Cross-linki8 – 8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Modified residuei358 – 3581Phosphoserine By similarity
Modified residuei411 – 4111Phosphothreonine; by CDK2 By similarity
Modified residuei430 – 4301Phosphoserine By similarity
Modified residuei437 – 4371Phosphoserine By similarity
Modified residuei438 – 4381Phosphothreonine By similarity
Modified residuei444 – 4441Phosphoserine2 Publications
Modified residuei526 – 5261N6-acetyllysine; alternate By similarity
Cross-linki526 – 526Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate3 Publications

Post-translational modificationi

Phosphorylated occurs before nuclear envelope breakdown and continues throughout mitosis. Phosphorylated by the M-phase kinase cyclin B/Cdk1, in vitro. Differential timimg of dephosphorylation occurs during phases of mitosis. The phosphorylated form remains associated with RANBP2/NUP358 and the SUMO E2-conjugating enzyme, UBC9, on nuclear pore complex (NPC) diassembly and during mitosis.1 Publication
Sumoylated with SUMO1. Sumoylation is necessary for targeting to the nuclear envelope (NE), and for association with mitotic spindles and kinetochores during mitosis. Also required for interaction with RANBP2 and is mediated by UBC9 By similarity.3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP46061.
PaxDbiP46061.
PRIDEiP46061.

PTM databases

PhosphoSiteiP46061.

Expressioni

Gene expression databases

ArrayExpressiP46061.
BgeeiP46061.
CleanExiMM_RANGAP1.
GenevestigatoriP46061.

Interactioni

Subunit structurei

Homodimer. Interacts with TRAF6 By similarity. Forms a tight complex in association with RANBP2/NUP358 and UBE2I/UBC9, the ubiquitin-conjugating enzyme E2. Interacts with UBE2I; the interaction conjugates SUMO1 to RANGAP1, and subsequently stabilizes interactions of sumoylated RANGAP1 with RANBP2/NUP358. The SUMO1/RANGAP1/UBC9/NUP358 complex associates with nuclear pore complexes.

Protein-protein interaction databases

BioGridi202583. 11 interactions.
DIPiDIP-17024N.
IntActiP46061. 3 interactions.
MINTiMINT-4132270.
STRINGi10090.ENSMUSP00000057771.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi436 – 4416
Helixi445 – 4506
Helixi455 – 4617
Helixi468 – 48013
Helixi486 – 50520
Helixi511 – 52111
Helixi538 – 54912
Helixi555 – 5573
Helixi558 – 5658
Helixi577 – 58812

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KPSX-ray2.50B/D420-589[»]
ProteinModelPortaliP46061.
SMRiP46061. Positions 21-370, 434-589.

Miscellaneous databases

EvolutionaryTraceiP46061.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati48 – 7124LRR 1
Add
BLAST
Repeati111 – 13424LRR 2
Add
BLAST
Repeati207 – 23024LRR 3
Add
BLAST
Repeati235 – 25824LRR 4
Add
BLAST
Repeati292 – 31524LRR 5
Add
BLAST
Repeati320 – 34324LRR 6
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi525 – 5284SUMO conjugation By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi359 – 39941Asp/Glu-rich (highly acidic)
Add
BLAST

Sequence similaritiesi

Belongs to the RNA1 family.

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiCOG5238.
GeneTreeiENSGT00440000039203.
HOVERGENiHBG017720.
InParanoidiQ6NZB5.
KOiK14319.
OMAiSFNSNAF.
OrthoDBiEOG70W3DV.
TreeFamiTF318283.

Family and domain databases

Gene3Di1.25.40.200. 1 hit.
InterProiIPR009109. Ran_GTPase_activating_1_C.
IPR027038. RanGap.
[Graphical view]
PANTHERiPTHR24113. PTHR24113. 1 hit.
PfamiPF07834. RanGAP1_C. 1 hit.
[Graphical view]
SUPFAMiSSF69099. SSF69099. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46061-1 [UniParc]FASTAAdd to Basket

« Hide

MASEDIAKLA ETLAKTQVAG GQLSFKGKGL KLNTAEDAKD VIKEIEEFDG    50
LEALRLEGNT VGVEAARVIA KALEKKSELK RCHWSDMFTG RLRSEIPPAL 100
ISLGEGLITA GAQLVELDLS DNAFGPDGVR GFEALLKSPA CFTLQELKLN 150
NCGMGIGGGK ILAAALTECH RKSSAQGKPL ALKVFVAGRN RLENDGATAL 200
AEAFGIIGTL EEVHMPQNGI NHPGVTALAQ AFAINPLLRV INLNDNTFTE 250
KGGVAMAETL KTLRQVEVIN FGDCLVRSKG AVAIADAVRG GLPKLKELNL 300
SFCEIKRDAA LVVAEAVADK AELEKLDLNG NALGEEGCEQ LQEVMDSFNM 350
AKVLASLSDD EGEDEDEEEE GEEDDEEEED EEDEEDDDEE EEEQEEEEEP 400
PQRGSGEEPA TPSRKILDPN SGEPAPVLSS PTPTDLSTFL SFPSPEKLLR 450
LGPKVSVLIV QQTDTSDPEK VVSAFLKVAS VFRDDASVKT AVLDAIDALM 500
KKAFSCSSFN SNTFLTRLLI HMGLLKSEDK IKAIPSLHGP LMVLNHVVRQ 550
DYFPKALAPL LLAFVTKPNG ALETCSFARH NLLQTLYNI 589
Length:589
Mass (Da):63,531
Last modified:July 27, 2011 - v2
Checksum:i775ADE3A53EFD558
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti181 – 1811A → R in AAA17681. 1 Publication
Sequence conflicti413 – 4131S → L in AAB60517. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U08110 mRNA. Translation: AAA17681.1.
U20857 Genomic RNA. Translation: AAB60517.1.
AK146670 mRNA. Translation: BAE27347.1.
AK159009 mRNA. Translation: BAE34767.1.
AK159525 mRNA. Translation: BAE35154.1.
BC066213 mRNA. Translation: AAH66213.1.
BC071200 mRNA. Translation: AAH71200.1.
CCDSiCCDS27670.1.
PIRiA36983.
T52070.
RefSeqiNP_001139646.1. NM_001146174.1.
NP_035371.4. NM_011241.4.
UniGeneiMm.270975.
Mm.475271.

Genome annotation databases

EnsembliENSMUST00000052374; ENSMUSP00000057771; ENSMUSG00000022391.
ENSMUST00000170134; ENSMUSP00000126849; ENSMUSG00000022391.
ENSMUST00000171115; ENSMUSP00000130046; ENSMUSG00000022391.
GeneIDi19387.
KEGGimmu:19387.
UCSCiuc007wxb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U08110 mRNA. Translation: AAA17681.1 .
U20857 Genomic RNA. Translation: AAB60517.1 .
AK146670 mRNA. Translation: BAE27347.1 .
AK159009 mRNA. Translation: BAE34767.1 .
AK159525 mRNA. Translation: BAE35154.1 .
BC066213 mRNA. Translation: AAH66213.1 .
BC071200 mRNA. Translation: AAH71200.1 .
CCDSi CCDS27670.1.
PIRi A36983.
T52070.
RefSeqi NP_001139646.1. NM_001146174.1.
NP_035371.4. NM_011241.4.
UniGenei Mm.270975.
Mm.475271.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KPS X-ray 2.50 B/D 420-589 [» ]
ProteinModelPortali P46061.
SMRi P46061. Positions 21-370, 434-589.
ModBasei Search...

Protein-protein interaction databases

BioGridi 202583. 11 interactions.
DIPi DIP-17024N.
IntActi P46061. 3 interactions.
MINTi MINT-4132270.
STRINGi 10090.ENSMUSP00000057771.

PTM databases

PhosphoSitei P46061.

Proteomic databases

MaxQBi P46061.
PaxDbi P46061.
PRIDEi P46061.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000052374 ; ENSMUSP00000057771 ; ENSMUSG00000022391 .
ENSMUST00000170134 ; ENSMUSP00000126849 ; ENSMUSG00000022391 .
ENSMUST00000171115 ; ENSMUSP00000130046 ; ENSMUSG00000022391 .
GeneIDi 19387.
KEGGi mmu:19387.
UCSCi uc007wxb.2. mouse.

Organism-specific databases

CTDi 5905.
MGIi MGI:103071. Rangap1.

Phylogenomic databases

eggNOGi COG5238.
GeneTreei ENSGT00440000039203.
HOVERGENi HBG017720.
InParanoidi Q6NZB5.
KOi K14319.
OMAi SFNSNAF.
OrthoDBi EOG70W3DV.
TreeFami TF318283.

Enzyme and pathway databases

Reactomei REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_207679. Separation of Sister Chromatids.

Miscellaneous databases

ChiTaRSi RANGAP1. mouse.
EvolutionaryTracei P46061.
NextBioi 296501.
PROi P46061.
SOURCEi Search...

Gene expression databases

ArrayExpressi P46061.
Bgeei P46061.
CleanExi MM_RANGAP1.
Genevestigatori P46061.

Family and domain databases

Gene3Di 1.25.40.200. 1 hit.
InterProi IPR009109. Ran_GTPase_activating_1_C.
IPR027038. RanGap.
[Graphical view ]
PANTHERi PTHR24113. PTHR24113. 1 hit.
Pfami PF07834. RanGAP1_C. 1 hit.
[Graphical view ]
SUPFAMi SSF69099. SSF69099. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A murine homolog of the yeast RNA1 gene is required for postimplantation development."
    Degregori J., Russ A., von Melchner H., Rayburn H., Priyaranjan P., Jenkins N.A., Copeland N.G., Ruley H.E.
    Genes Dev. 8:265-276(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Separate domains of the Ran GTPase interact with different factors to regulate nuclear protein import and RNA processing."
    Ren M., Villamarin A., Shih A., Coutavas E., Moore M.S., Locurcio M., Clarke V., Oppenheim J.D., D'Eustachio P., Rush M.G.
    Mol. Cell. Biol. 15:2117-2124(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/c.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver and Visual cortex.
  4. "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].
    Strain: 129 and C57BL/6J.
    Tissue: Mammary tumor.
  5. "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. 140:259-270(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-526, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-526.
  6. "SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex."
    Matunis M.J., Wu J., Blobel G.
    J. Cell Biol. 140:499-509(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-526, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-526 AND PHE-564.
  7. "RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly."
    Swaminathan S., Kiendl F., Koerner R., Lupetti R., Hengst L., Melchior F.
    J. Cell Biol. 164:965-971(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-411 AND SER-444, MUTAGENESIS OF THR-411 AND SER-444.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  9. "SUMO modification through rapamycin-mediated heterodimerization reveals a dual role for Ubc9 in targeting RanGAP1 to nuclear pore complexes."
    Zhu S., Zhang H., Matunis M.J.
    Exp. Cell Res. 312:1042-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-526, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-526.
  10. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  11. "Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1."
    Bernier-Villamor V., Sampson D.A., Matunis M.J., Lima C.D.
    Cell 108:345-356(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 420-589 IN COMPLEX WITH SUMO1 AND HUMAN UBE2I, MUTAGENESIS OF ASN-512; THR-516; ARG-517; HIS-521; MET-522; LEU-524; LEU-525; LYS-526; GLU-528; ASP-529; ILE-531; LEU-537; LEU-560; ALA-563; PHE-564; LYS-567 AND ASN-569.

Entry informationi

Entry nameiRAGP1_MOUSE
AccessioniPrimary (citable) accession number: P46061
Secondary accession number(s): Q60801, Q6NZB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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