GDS1_HUMAN - dbPTM
GDS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GDS1_HUMAN
UniProt AC P52306
Protein Name Rap1 GTPase-GDP dissociation stimulator 1
Gene Name RAP1GDS1
Organism Homo sapiens (Human).
Sequence Length 607
Subcellular Localization
Protein Description Stimulates GDP/GTP exchange reaction of a group of small GTP-binding proteins (G proteins) including Rap1a/Rap1b, RhoA, RhoB and KRas, by stimulating the dissociation of GDP from and the subsequent binding of GTP to each small G protein..
Protein Sequence MDNLSDTLKKLKITAVDKTEDSLEGCLDCLLQALAQNNTETSEKIQASGILQLFASLLTPQSSCKAKVANIIAEVAKNEFMRIPCVDAGLISPLVQLLNSKDQEVLLQTGRALGNICYDSHEGRSAVDQAGGAQIVIDHLRSLCSITDPANEKLLTVFCGMLMNYSNENDSLQAQLINMGVIPTLVKLLGIHCQNAALTEMCLVAFGNLAELESSKEQFASTNIAEELVKLFKKQIEHDKREMIFEVLAPLAENDAIKLQLVEAGLVECLLEIVQQKVDSDKEDDITELKTGSDLMVLLLLGDESMQKLFEGGKGSVFQRVLSWIPSNNHQLQLAGALAIANFARNDANCIHMVDNGIVEKLMDLLDRHVEDGNVTVQHAALSALRNLAIPVINKAKMLSAGVTEAVLKFLKSEMPPVQFKLLGTLRMLIDAQAEAAEQLGKNVKLVERLVEWCEAKDHAGVMGESNRLLSALIRHSKSKDVIKTIVQSGGIKHLVTMATSEHVIMQNEALVALALIAALELGTAEKDLESAKLVQILHRLLADERSAPEIKYNSMVLICALMGSECLHKEVQDLAFLDVVSKLRSHENKSVAQQASLTEQRLTVES
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
5Phosphorylation---MDNLSDTLKKLK
---CCCHHHHHHHCC		34.5025850435
6 (in isoform 3)Phosphorylation-60.2627251275
6 (in isoform 4)Phosphorylation-60.2627251275
6 (in isoform 5)Phosphorylation-60.2627251275
6 (in isoform 6)Phosphorylation-60.2627251275
6Phosphorylation--MDNLSDTLKKLKI
--CCCHHHHHHHCCE		60.2627251275
7Phosphorylation-MDNLSDTLKKLKIT
-CCCHHHHHHHCCEE		36.7825850435
9UbiquitinationDNLSDTLKKLKITAV
CCHHHHHHHCCEEEE		59.14-
10UbiquitinationNLSDTLKKLKITAVD
CHHHHHHHCCEEEEC		59.11-
12AcetylationSDTLKKLKITAVDKT
HHHHHHCCEEEECCC		47.0622424773
12UbiquitinationSDTLKKLKITAVDKT
HHHHHHCCEEEECCC		47.06-
18UbiquitinationLKITAVDKTEDSLEG
CCEEEECCCCCHHHH		47.41-
48PhosphorylationTSEKIQASGILQLFA
HHHHHHHHHHHHHHH		15.2526074081
56PhosphorylationGILQLFASLLTPQSS
HHHHHHHHHCCCCHH		19.3126074081
59PhosphorylationQLFASLLTPQSSCKA
HHHHHHCCCCHHHHH		25.2826074081
62PhosphorylationASLLTPQSSCKAKVA
HHHCCCCHHHHHHHH		38.6226074081
63PhosphorylationSLLTPQSSCKAKVAN
HHCCCCHHHHHHHHH		17.8726074081
67UbiquitinationPQSSCKAKVANIIAE
CCHHHHHHHHHHHHH		27.63-
77UbiquitinationNIIAEVAKNEFMRIP
HHHHHHHHCCCCCCC		63.29-
101UbiquitinationLVQLLNSKDQEVLLQ
HHHHHCCCCHHHHHH		63.46-
119PhosphorylationALGNICYDSHEGRSA
HHCCEECCCCCCCCH		38.8227642862
181AcetylationAQLINMGVIPTLVKL
HHHHHHCHHHHHHHH		3.0919608861
182AcetylationQLINMGVIPTLVKLL
HHHHHCHHHHHHHHH		1.4619608861
230UbiquitinationNIAEELVKLFKKQIE
CHHHHHHHHHHHHHH		61.91-
230AcetylationNIAEELVKLFKKQIE
CHHHHHHHHHHHHHH		61.9119608861
231AcetylationIAEELVKLFKKQIEH
HHHHHHHHHHHHHHH		6.2419608861
280PhosphorylationIVQQKVDSDKEDDIT
HHHHHCCCCCCCCCH		54.2729449344
314MalonylationQKLFEGGKGSVFQRV
HHHHHCCCCHHHHHH		59.8926320211
314UbiquitinationQKLFEGGKGSVFQRV
HHHHHCCCCHHHHHH		59.89-
316PhosphorylationLFEGGKGSVFQRVLS
HHHCCCCHHHHHHHH		24.2028857561
368MethylationKLMDLLDRHVEDGNV
HHHHHHHHHCCCCCC		35.40115490291
372UbiquitinationLLDRHVEDGNVTVQH
HHHHHCCCCCCHHHH		53.5319608861
372AcetylationLLDRHVEDGNVTVQH
HHHHHCCCCCCHHHH		53.5319608861
372 (in isoform 2)Ubiquitination-53.5321890473
373AcetylationLDRHVEDGNVTVQHA
HHHHCCCCCCHHHHH		19.5919608861
373UbiquitinationLDRHVEDGNVTVQHA
HHHHCCCCCCHHHHH		19.5919608861
373UbiquitinationLDRHVEDGNVTVQHA
HHHHCCCCCCHHHHH		19.5921890473
396 (in isoform 2)Ubiquitination-9.6721890473
412UbiquitinationEAVLKFLKSEMPPVQ
HHHHHHHHCCCCCCH		47.72-
415SulfoxidationLKFLKSEMPPVQFKL
HHHHHCCCCCCHHHH		6.1630846556
421 (in isoform 1)Ubiquitination-26.2221890473
421UbiquitinationEMPPVQFKLLGTLRM
CCCCCHHHHHHHHHH		26.2221890473
421AcetylationEMPPVQFKLLGTLRM
CCCCCHHHHHHHHHH		26.2225953088
422AcetylationMPPVQFKLLGTLRML
CCCCHHHHHHHHHHH		5.8719608861
422UbiquitinationMPPVQFKLLGTLRML
CCCCHHHHHHHHHHH		5.8719608861
422UbiquitinationMPPVQFKLLGTLRML
CCCCHHHHHHHHHHH		5.8721890473
422UbiquitinationMPPVQFKLLGTLRML
CCCCHHHHHHHHHHH		5.8721890473
445 (in isoform 1)Ubiquitination-57.0921890473
445UbiquitinationEQLGKNVKLVERLVE
HHHCCHHHHHHHHHH		57.0921906983
457AcetylationLVEWCEAKDHAGVMG
HHHHHHCCCCCCCCC		27.9625953088
457UbiquitinationLVEWCEAKDHAGVMG
HHHHHHCCCCCCCCC		27.96-
484AcetylationSKSKDVIKTIVQSGG
CCCHHHHHHHHHCCC		31.8625953088
484UbiquitinationSKSKDVIKTIVQSGG
CCCHHHHHHHHHCCC		31.86-
533UbiquitinationEKDLESAKLVQILHR
CHHHHHHHHHHHHHH		59.47-
541 (in isoform 2)Ubiquitination-3.0021890473
582PhosphorylationLAFLDVVSKLRSHEN
HHHHHHHHHHHHCCC		26.3122985185
583UbiquitinationAFLDVVSKLRSHENK
HHHHHHHHHHHCCCH		35.99-
590 (in isoform 1)Ubiquitination-43.2421890473
590UbiquitinationKLRSHENKSVAQQAS
HHHHCCCHHHHHHHC		43.2421906983
597PhosphorylationKSVAQQASLTEQRLT
HHHHHHHCHHHHCHH		31.3329978859
598PhosphorylationSVAQQASLTEQRLTV
HHHHHHCHHHHCHHC		7.3827251275
599PhosphorylationVAQQASLTEQRLTVE
HHHHHCHHHHCHHCC		27.8125072903
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

Oops, there are no upstream regulatory protein records of GDS1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GDS1_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 GDS1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHOA_HUMANRHOAphysical
11948427
RAP1A_HUMANRAP1Aphysical
11948427
RASH_HUMANHRASphysical
11948427
RASK_HUMANKRASphysical
11948427
MBIP1_HUMANMBIPphysical
16189514
ZN451_HUMANZNF451physical
16189514
KIFA3_HUMANKIFAP3physical
8900189
DCPS_HUMANDCPSphysical
22863883
G3P_HUMANGAPDHphysical
22863883
PSF3_HUMANGINS3physical
22863883
HS71L_HUMANHSPA1Lphysical
22863883
ULA1_HUMANNAE1physical
22863883
OLA1_HUMANOLA1physical
22863883
PA1B2_HUMANPAFAH1B2physical
22863883
IPP2_HUMANPPP1R2physical
22863883
PTMA_HUMANPTMAphysical
22863883
MBIP1_HUMANMBIPphysical
25416956
PKHB1_HUMANPLEKHB1physical
25416956
RAP1A_HUMANRAP1Aphysical
20709748
RASK_HUMANKRASphysical
20709748
RHOA_HUMANRHOAphysical
20709748
RAC1_HUMANRAC1physical
20709748
DIRA1_HUMANDIRAS1physical
28514442
UBF1_HUMANUBTFphysical
28514442
RAP1A_HUMANRAP1Aphysical
28514442
PKHB1_HUMANPLEKHB1physical
28514442
RAC3_HUMANRAC3physical
28514442
PRD10_HUMANPRDM10physical
28514442
RAP1B_HUMANRAP1Bphysical
28514442
RBM42_HUMANRBM42physical
28514442
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 GDS1_HUMAN

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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-230 AND LYS-421, AND MASSSPECTROMETRY.

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