Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Ran GTPase-activating protein 1  

UniProtKB / Swiss-Prot ID :  RAGP1_HUMAN

Gene Name (Synonyms) : 
RANGAP1, KIAA1835, SD  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Chromosome, centromere, kinetochore (By similarity). Cytoplasm, cytoskeleton, spindle pole (By similarity). Note=Cytoplasmic during interphase. Targeted to the nuclear rim after  

Protein Function :  GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state. 

Protein Sequence MASEDIAKLAETLAKTQVAGGQLSFKGKSLKLNTAEDAKDVIKEIEDFDSLEALRLEGNTVGVEAARVIA...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
133E -> Q (in dbSNP:rs2229752). VAR_029240
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MASEDI
---
22.94UniProtKB
Link-
8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)EDIAKLAET
48.87Phosphositeplus
Link-
8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) (interchain with G-Cter in SUMO-EDIAKLAET
48.87UniProtKB
Link-
24PhosphoserineGGQLSFKGK
19.61HPRD
Link-
26Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)QLSFKGKSL
63.15Phosphositeplus
Link-
28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)SFKGKSLKL
53.88Phosphositeplus
Link-
169S-nitrosocysteineALTECHRKS
2.95dbSNO
Link-
251Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TFTEKGAVA
49.46Phosphositeplus
Link-
296Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LPKLKELNL
67.30Phosphositeplus
Link-
306Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)FCEIKRDAA
23.18HPRD
Link-
358PhosphoserineLASLSDDED
40.29PhosphoELM
Link-
358PhosphoserineLASLSDDED
40.29Phosphositeplus
Link-
358Phosphoserine (CSNK2A1)LASLSDDED
40.29HPRD
Link-
409PhosphothreonineEKSATPSRK
28.96Phosphositeplus
Link-
409Phosphothreonine (CDK1)EKSATPSRK
28.96PhosphoELM
Link-
409Phosphothreonine; by CDK2.EKSATPSRK
28.96UniProtKB
Link-
419PhosphothreonineLDPNTGEPA
48.59HPRD
Link-
427PhosphoserineAPVLSSPPP
40.82HPRD
Link-
427PhosphoserineAPVLSSPPP
40.82PhosphoELM
Link-
427PhosphoserineAPVLSSPPP
40.82Phosphositeplus
Link-
428PhosphoserinePVLSSPPPA
36.95HPRD
Link-
428PhosphoserinePVLSSPPPA
36.95PhosphoELM
Link-
428PhosphoserinePVLSSPPPA
36.95Phosphositeplus
Link-
428PhosphoserinePVLSSPPPA
36.95SysPTM
Link-
428Phosphoserine.PVLSSPPPA
36.95UniProtKB
Link-
435PhosphoserinePADVSTFLA
17.62Phosphositeplus
Link
435Phosphoserine.PADVSTFLA
17.62UniProtKB
Link
436PhosphothreonineADVSTFLAF
23.63HPRD
Link
436PhosphothreonineADVSTFLAF
23.63PhosphoELM
Link
436PhosphothreonineADVSTFLAF
23.63Phosphositeplus
Link
436Phosphothreonine.ADVSTFLAF
23.63UniProtKB
Link
442PhosphoserineLAFPSPEKL
38.96HPRD
Link
442PhosphoserineLAFPSPEKL
38.96PhosphoELM
Link
442PhosphoserineLAFPSPEKL
38.96Phosphositeplus
Link
442PhosphoserineLAFPSPEKL
38.96SysPTM
Link
442Phosphoserine.LAFPSPEKL
38.96UniProtKB
Link
452Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RLGPKSSVL
54.27Phosphositeplus
Link
453PhosphoserineLGPKSSVLI
28.90HPRD
Link
478PhosphoserineLKVSSVFKD
34.26HPRD
Link
478PhosphoserineLKVSSVFKD
34.26Phosphositeplus
Link
481Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)SSVFKDEAT
53.13HPRD
Link
485PhosphothreonineKDEATVRMA
13.44HPRD
Link
485PhosphothreonineKDEATVRMA
13.44Phosphositeplus
Link
524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)MGLLKSEDK
57.76HPRD
Link
524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)MGLLKSEDK
57.76Phosphositeplus
Link
524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) (interchain with G-Cter in SUMO-MGLLKSEDK
57.76UniProtKB
Link
524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MGLLKSEDK
57.76Phosphositeplus
Link
524N6-acetyllysineMGLLKSEDK
57.76HPRD
Link
524N6-acetyllysineMGLLKSEDK
57.76Phosphositeplus
Link
524N6-acetyllysine.MGLLKSEDK
57.76UniProtKB
Link
585PhosphotyrosineLQTLYKV
17.06Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
UBC9_HUMANdirect interactionMINT-3380689MINT17036045
UBC9_HUMANdirect interaction
direct interaction
DIP:57079EDIP16732283
16732283
SUMO1_HUMANcovalent bindingDIP:57080EDIP16732283
SUMO1_HUMANphysical interaction
physical interaction
physical interaction
EBI-1211893
EBI-1211614
EBI-1
intact17000644
17000644
17000644
RAN_HUMANin vitroHPRD:03839HPRD9219684
7744835
10394366
RBP2_HUMANin vitro
in vivo
HPRD:03839HPRD11854305
9019411
12192048
RAGP1_HUMANin vitroHPRD:03839HPRD8146159
SUMO1_HUMANin vitro
in vivo
HPRD:03839HPRD16428860
9442102
9019411
17000644
RAN_HUMANENSP00000348577STRING
RAN_HUMANENSP00000348577STRING
SUMO1_HUMANENSP00000348577STRING
RBP2_HUMANENSP00000348577STRING
SUMO4_HUMANENSP00000348577STRING
RANG_HUMANENSP00000348577STRING
SUMO3_HUMANENSP00000348577STRING
UBC9_HUMANENSP00000348577STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-524, AND MASS SPECTROMETRY.
"In vivo identification of sumoylation sites by a signature tag andcysteine-targeted affinity purification.";
Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A.,Eriksson J.E., Sistonen L.;
J. Biol. Chem. 285:19324-19329(2010).
Cited for: SUMOYLATION AT LYS-8 AND LYS-524, AND ACETYLATION AT ALA-2.
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428 AND SER-442, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428 AND SER-442, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428 AND SER-442, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428 AND SER-442, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428 AND SER-442, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428; SER-435; THR-436AND SER-442, AND MASS SPECTROMETRY.
"RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remainsassociated with RanBP2 upon NPC disassembly.";
Swaminathan S., Kiendl F., Koerner R., Lupetti R., Hengst L.,Melchior F.;
J. Cell Biol. 164:965-971(2004).
Cited for: PHOSPHORYLATION AT THR-409; SER-428 AND SER-442, MASS SPECTROMETRY,SUBCELLULAR LOCATION, AND INTERACTION WITH SUMO1; RANBP2 AND UBE2I.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures