dbPTM

RAGP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAGP1_HUMAN
UniProt AC	P46060
Protein Name	Ran GTPase-activating protein 1
Gene Name	RANGAP1
Organism	Homo sapiens (Human).
Sequence Length	587
Subcellular Localization	Cytoplasm . Nucleus, nucleoplasm . Nucleus envelope . Chromosome, centromere, kinetochore . Cytoplasm, cytoskeleton, spindle . Cytoplasmic during interphase. Detected at the nuclear envelope during interphase (PubMed:11854305, PubMed:15037602). Targe
Protein Description	GTPase activator for RAN. [PubMed: 8146159]
Protein Sequence	MASEDIAKLAETLAKTQVAGGQLSFKGKSLKLNTAEDAKDVIKEIEDFDSLEALRLEGNTVGVEAARVIAKALEKKSELKRCHWSDMFTGRLRTEIPPALISLGEGLITAGAQLVELDLSDNAFGPDGVQGFEALLKSSACFTLQELKLNNCGMGIGGGKILAAALTECHRKSSAQGKPLALKVFVAGRNRLENDGATALAEAFRVIGTLEEVHMPQNGINHPGITALAQAFAVNPLLRVINLNDNTFTEKGAVAMAETLKTLRQVEVINFGDCLVRSKGAVAIADAIRGGLPKLKELNLSFCEIKRDAALAVAEAMADKAELEKLDLNGNTLGEEGCEQLQEVLEGFNMAKVLASLSDDEDEEEEEEGEEEEEEAEEEEEEDEEEEEEEEEEEEEEPQQRGQGEKSATPSRKILDPNTGEPAPVLSSPPPADVSTFLAFPSPEKLLRLGPKSSVLIAQQTDTSDPEKVVSAFLKVSSVFKDEATVRMAVQDAVDALMQKAFNSSSFNSNTFLTRLLVHMGLLKSEDKVKAIANLYGPLMALNHMVQQDYFPKALAPLLLAFVTKPNSALESCSFARHSLLQTLYKV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASEDIAKL ------CCHHHHHHH	22.94	20388717
3	Phosphorylation	-----MASEDIAKLA -----CCHHHHHHHH	34.21	24719451
8	Sumoylation	MASEDIAKLAETLAK CCHHHHHHHHHHHHH	48.87	-
8	2-Hydroxyisobutyrylation	MASEDIAKLAETLAK CCHHHHHHHHHHHHH	48.87	-
8	Acetylation	MASEDIAKLAETLAK CCHHHHHHHHHHHHH	48.87	27452117
8	Sumoylation	MASEDIAKLAETLAK CCHHHHHHHHHHHHH	48.87	28112733
8	Ubiquitination	MASEDIAKLAETLAK CCHHHHHHHHHHHHH	48.87	-
12	Phosphorylation	DIAKLAETLAKTQVA HHHHHHHHHHHHCCC	26.80	20068231
15	Sumoylation	KLAETLAKTQVAGGQ HHHHHHHHHCCCCCC	42.47	28112733
15	Ubiquitination	KLAETLAKTQVAGGQ HHHHHHHHHCCCCCC	42.47	-
16	Phosphorylation	LAETLAKTQVAGGQL HHHHHHHHCCCCCCC	23.75	20068231
24	Phosphorylation	QVAGGQLSFKGKSLK CCCCCCCEECCEECC	19.61	23401153
26	Sumoylation	AGGQLSFKGKSLKLN CCCCCEECCEECCCC	63.15	-
26	Acetylation	AGGQLSFKGKSLKLN CCCCCEECCEECCCC	63.15	25953088
26	Sumoylation	AGGQLSFKGKSLKLN CCCCCEECCEECCCC	63.15	-
26	Ubiquitination	AGGQLSFKGKSLKLN CCCCCEECCEECCCC	63.15	-
28	Sumoylation	GQLSFKGKSLKLNTA CCCEECCEECCCCCH	53.88	-
28	Sumoylation	GQLSFKGKSLKLNTA CCCEECCEECCCCCH	53.88	-
28	Ubiquitination	GQLSFKGKSLKLNTA CCCEECCEECCCCCH	53.88	-
29	Phosphorylation	QLSFKGKSLKLNTAE CCEECCEECCCCCHH	39.13	28450419
31	2-Hydroxyisobutyrylation	SFKGKSLKLNTAEDA EECCEECCCCCHHHH	46.94	-
31	Acetylation	SFKGKSLKLNTAEDA EECCEECCCCCHHHH	46.94	25953088
31	Ubiquitination	SFKGKSLKLNTAEDA EECCEECCCCCHHHH	46.94	-
39	2-Hydroxyisobutyrylation	LNTAEDAKDVIKEIE CCCHHHHHHHHHHHC	65.92	-
39	Ubiquitination	LNTAEDAKDVIKEIE CCCHHHHHHHHHHHC	65.92	-
43	Ubiquitination	EDAKDVIKEIEDFDS HHHHHHHHHHCCCCC	53.11	-
50	Phosphorylation	KEIEDFDSLEALRLE HHHCCCCCCHHHHCC	28.27	30266825
71	Acetylation	EAARVIAKALEKKSE HHHHHHHHHHHHHHH	42.24	25953088
71	Ubiquitination	EAARVIAKALEKKSE HHHHHHHHHHHHHHH	42.24	-
81	Methylation	EKKSELKRCHWSDMF HHHHHHCCCCHHHHH	30.11	115490283
85	Phosphorylation	ELKRCHWSDMFTGRL HHCCCCHHHHHCCCC	8.78	21406692
89	Phosphorylation	CHWSDMFTGRLRTEI CCHHHHHCCCCCCCC	18.11	21406692
148	Acetylation	CFTLQELKLNNCGMG CEECCHHCCCCCCCC	48.71	26051181
148	Ubiquitination	CFTLQELKLNNCGMG CEECCHHCCCCCCCC	48.71	-
160	Acetylation	GMGIGGGKILAAALT CCCCCHHHHHHHHHH	37.51	26051181
169	S-nitrosocysteine	LAAALTECHRKSSAQ HHHHHHHHHHHHCCC	2.95	-
169	S-nitrosylation	LAAALTECHRKSSAQ HHHHHHHHHHHHCCC	2.95	19483679
172	Ubiquitination	ALTECHRKSSAQGKP HHHHHHHHHCCCCCC	25.71	-
174	Phosphorylation	TECHRKSSAQGKPLA HHHHHHHCCCCCCCE	27.87	24260401
178	Acetylation	RKSSAQGKPLALKVF HHHCCCCCCCEEEEE	25.44	26051181
178	Ubiquitination	RKSSAQGKPLALKVF HHHCCCCCCCEEEEE	25.44	-
183	Ubiquitination	QGKPLALKVFVAGRN CCCCCEEEEEEECCC	28.20	-
247	Phosphorylation	VINLNDNTFTEKGAV EEECCCCCCCHHHHH	34.49	23911959
251	2-Hydroxyisobutyrylation	NDNTFTEKGAVAMAE CCCCCCHHHHHHHHH	49.46	-
251	Acetylation	NDNTFTEKGAVAMAE CCCCCCHHHHHHHHH	49.46	27452117
251	Ubiquitination	NDNTFTEKGAVAMAE CCCCCCHHHHHHHHH	49.46	21906983
256	Sulfoxidation	TEKGAVAMAETLKTL CHHHHHHHHHHHHHH	2.52	30846556
261	2-Hydroxyisobutyrylation	VAMAETLKTLRQVEV HHHHHHHHHHCCEEE	53.59	-
261	Ubiquitination	VAMAETLKTLRQVEV HHHHHHHHHHCCEEE	53.59	-
274	Glutathionylation	EVINFGDCLVRSKGA EEEECCCCCHHCCCH	3.76	22555962
278	Phosphorylation	FGDCLVRSKGAVAIA CCCCCHHCCCHHHHH	28.14	23911959
279	2-Hydroxyisobutyrylation	GDCLVRSKGAVAIAD CCCCHHCCCHHHHHH	40.08	-
279	Malonylation	GDCLVRSKGAVAIAD CCCCHHCCCHHHHHH	40.08	26320211
279	Sumoylation	GDCLVRSKGAVAIAD CCCCHHCCCHHHHHH	40.08	28112733
279	Ubiquitination	GDCLVRSKGAVAIAD CCCCHHCCCHHHHHH	40.08	-
289	Methylation	VAIADAIRGGLPKLK HHHHHHHHCCCCHHH	34.54	115490275
296	Acetylation	RGGLPKLKELNLSFC HCCCCHHHHCCCCHH	67.30	26051181
296	Ubiquitination	RGGLPKLKELNLSFC HCCCCHHHHCCCCHH	67.30	21906983
301	Phosphorylation	KLKELNLSFCEIKRD HHHHCCCCHHHHHHH	27.12	21815630
306	Sumoylation	NLSFCEIKRDAALAV CCCHHHHHHHHHHHH	23.18	-
306	Acetylation	NLSFCEIKRDAALAV CCCHHHHHHHHHHHH	23.18	26051181
306	Sumoylation	NLSFCEIKRDAALAV CCCHHHHHHHHHHHH	23.18	17000644
306	Ubiquitination	NLSFCEIKRDAALAV CCCHHHHHHHHHHHH	23.18	-
317	Sulfoxidation	ALAVAEAMADKAELE HHHHHHHHHCHHHHH	3.59	21406390
320	Acetylation	VAEAMADKAELEKLD HHHHHHCHHHHHHCC	33.93	26051181
320	Ubiquitination	VAEAMADKAELEKLD HHHHHHCHHHHHHCC	33.93	-
356	Phosphorylation	NMAKVLASLSDDEDE CHHHHHHHCCCCCCH	25.01	20860994
358	Phosphorylation	AKVLASLSDDEDEEE HHHHHHCCCCCCHHH	40.29	30576142
406	Methylation	QQRGQGEKSATPSRK HHCCCCCCCCCCCCC	52.82	116252309
407	Phosphorylation	QRGQGEKSATPSRKI HCCCCCCCCCCCCCC	32.83	27966365
409	Phosphorylation	GQGEKSATPSRKILD CCCCCCCCCCCCCCC	28.96	27966365
411	Phosphorylation	GEKSATPSRKILDPN CCCCCCCCCCCCCCC	41.68	27966365
413	Acetylation	KSATPSRKILDPNTG CCCCCCCCCCCCCCC	52.54	23954790
419	Phosphorylation	RKILDPNTGEPAPVL CCCCCCCCCCCCCCC	48.59	30278072
427	Phosphorylation	GEPAPVLSSPPPADV CCCCCCCCCCCCCCH	40.82	25159151
428	Phosphorylation	EPAPVLSSPPPADVS CCCCCCCCCCCCCHH	36.95	25159151
435	Phosphorylation	SPPPADVSTFLAFPS CCCCCCHHHHCCCCC	17.62	29255136
436	Phosphorylation	PPPADVSTFLAFPSP CCCCCHHHHCCCCCH	23.63	29255136
442	Phosphorylation	STFLAFPSPEKLLRL HHHCCCCCHHHHHHH	38.96	29255136
452	Sumoylation	KLLRLGPKSSVLIAQ HHHHHCCCCEEEEEE	54.27	-
452	Sumoylation	KLLRLGPKSSVLIAQ HHHHHCCCCEEEEEE	54.27	28112733
452	Ubiquitination	KLLRLGPKSSVLIAQ HHHHHCCCCEEEEEE	54.27	21906983
453	Phosphorylation	LLRLGPKSSVLIAQQ HHHHCCCCEEEEEEC	28.90	29978859
454	Phosphorylation	LRLGPKSSVLIAQQT HHHCCCCEEEEEECC	27.37	29978859
461	Phosphorylation	SVLIAQQTDTSDPEK EEEEEECCCCCCHHH	29.21	29083192
463	Phosphorylation	LIAQQTDTSDPEKVV EEEECCCCCCHHHHH	38.12	29083192
464	Phosphorylation	IAQQTDTSDPEKVVS EEECCCCCCHHHHHH	54.71	29083192
468	Ubiquitination	TDTSDPEKVVSAFLK CCCCCHHHHHHHHHH	54.01	-
477	Phosphorylation	VSAFLKVSSVFKDEA HHHHHHHHHHCCCHH	21.14	20068231
478	Phosphorylation	SAFLKVSSVFKDEAT HHHHHHHHHCCCHHH	34.26	20068231
481	Sumoylation	LKVSSVFKDEATVRM HHHHHHCCCHHHHHH	53.13	-
481	2-Hydroxyisobutyrylation	LKVSSVFKDEATVRM HHHHHHCCCHHHHHH	53.13	-
481	Acetylation	LKVSSVFKDEATVRM HHHHHHCCCHHHHHH	53.13	25953088
481	Malonylation	LKVSSVFKDEATVRM HHHHHHCCCHHHHHH	53.13	26320211
481	Ubiquitination	LKVSSVFKDEATVRM HHHHHHCCCHHHHHH	53.13	-
485	Phosphorylation	SVFKDEATVRMAVQD HHCCCHHHHHHHHHH	13.44	22817900
504	Phosphorylation	LMQKAFNSSSFNSNT HHHHHHCCCCCCCHH	22.39	28555341
505	Phosphorylation	MQKAFNSSSFNSNTF HHHHHCCCCCCCHHH	39.80	21712546
506	Phosphorylation	QKAFNSSSFNSNTFL HHHHCCCCCCCHHHH	28.41	27067055
524	Sumoylation	LVHMGLLKSEDKVKA HHHHCCCCCHHHHHH	57.76	-
524	Acetylation	LVHMGLLKSEDKVKA HHHHCCCCCHHHHHH	57.76	19608861
524	Sumoylation	LVHMGLLKSEDKVKA HHHHCCCCCHHHHHH	57.76	19608861
524	Ubiquitination	LVHMGLLKSEDKVKA HHHHCCCCCHHHHHH	57.76	21890473
528	Acetylation	GLLKSEDKVKAIANL CCCCCHHHHHHHHHH	41.40	26051181
528	Sumoylation	GLLKSEDKVKAIANL CCCCCHHHHHHHHHH	41.40	-
530	Sumoylation	LKSEDKVKAIANLYG CCCHHHHHHHHHHHH	39.55	-
536	Phosphorylation	VKAIANLYGPLMALN HHHHHHHHHHHHHHH	19.26	24043423
550	Phosphorylation	NHMVQQDYFPKALAP HHHHHCCCCCHHHHH	19.90	24043423
583	Phosphorylation	ARHSLLQTLYKV--- HHHHHHHHHHCC---	31.83	28152594
585	Phosphorylation	HSLLQTLYKV----- HHHHHHHHCC-----	17.06	28152594
586	2-Hydroxyisobutyrylation	SLLQTLYKV------ HHHHHHHCC------	44.58	-
586	Sumoylation	SLLQTLYKV------ HHHHHHHCC------	44.58	28112733

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
358	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
358	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
409	T	Phosphorylation	Kinase	CDK1	P06493	PSP
409	T	Phosphorylation	Kinase	CDK2	P24941	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RAGP1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of RAGP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAN_HUMAN	RAN	physical	10394366
RAGP1_HUMAN	RANGAP1	physical	8146159
RBP2_HUMAN	RANBP2	physical	21518904
RBP2_HUMAN	RANBP2	physical	22194619
UBC9_HUMAN	UBE2I	physical	22194619
PCGF2_HUMAN	PCGF2	physical	18706886
U5S1_HUMAN	EFTUD2	physical	22939629
UBC9_HUMAN	UBE2I	physical	17036045
UBC9_HUMAN	UBE2I	physical	21988832
KBP_HUMAN	KIAA1279	physical	22863883
UBC9_HUMAN	UBE2I	physical	23395904
SMAP_HUMAN	C11orf58	physical	26344197
C43BP_HUMAN	COL4A3BP	physical	26344197
CPSF4_HUMAN	CPSF4	physical	26344197
EF1G_HUMAN	EEF1G	physical	26344197
GNL1_HUMAN	GNL1	physical	26344197
TF3C3_HUMAN	GTF3C3	physical	26344197
IPO5_HUMAN	IPO5	physical	26344197
KDM2A_HUMAN	KDM2A	physical	26344197
NUCL_HUMAN	NCL	physical	26344197
PCF11_HUMAN	PCF11	physical	26344197
RPC3_HUMAN	POLR3C	physical	26344197
RALY_HUMAN	RALY	physical	26344197
RBP2_HUMAN	RANBP2	physical	26344197
RGPD2_HUMAN	RGPD2	physical	26344197
RGPD5_HUMAN	RGPD5	physical	26344197
TCP4_HUMAN	SUB1	physical	26344197
SPT5H_HUMAN	SUPT5H	physical	26344197
UBR4_HUMAN	UBR4	physical	26344197
UBC9_HUMAN	UBE2I	physical	29127148

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RAGP1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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.	20388717 [Abstract]
"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.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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.	19690332 [Abstract]
"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.	19413330 [Abstract]
"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.	18669648 [Abstract]
"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.	17693683 [Abstract]
"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.	17081983 [Abstract]
"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.	16565220 [Abstract]
"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.	15302935 [Abstract]
*"RanGAP1SUMO1 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.	15037602 [Abstract]