GNDS_HUMAN - dbPTM
GNDS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GNDS_HUMAN
UniProt AC Q12967
Protein Name Ral guanine nucleotide dissociation stimulator
Gene Name RALGDS
Organism Homo sapiens (Human).
Sequence Length 914
Subcellular Localization Cytoplasm . Nucleus . Localizes mainly in the peripheral region of the cytoplasmic membrane in oocytes and in preimplantation embryos until the 8-cell stage. Between the late 1-cell and the early 2-cell stages, nuclear localization becomes stronger.
Protein Description Stimulates the dissociation of GDP from the Ras-related RalA and RalB GTPases which allows GTP binding and activation of the GTPases. Interacts and acts as an effector molecule for R-Ras, H-Ras, K-Ras, and Rap..
Protein Sequence MVQRMWAEAAGPAGGAEPLFPGSRRSRSVWDAVRLEVGVPDSCPVVLHSFTQLDPDLPRPESSTQEIGEELINGVIYSISLRKVQLHHGGNKGQRWLGYENESALNLYETCKVRTVKAGTLEKLVEHLVPAFQGSDLSYVTIFLCTYRAFTTTQQVLDLLFKRYGRCDALTASSRYGCILPYSDEDGGPQDQLKNAISSILGTWLDQYSEDFCQPPDFPCLKQLVAYVQLNMPGSDLERRAHLLLAQLEHSEPIEAEPEALSPVPALKPTPELELALTPARAPSPVPAPAPEPEPAPTPAPGSELEVAPAPAPELQQAPEPAVGLESAPAPALELEPAPEQDPAPSQTLELEPAPAPVPSLQPSWPSPVVAENGLSEEKPHLLVFPPDLVAEQFTLMDAELFKKVVPYHCLGSIWSQRDKKGKEHLAPTIRATVTQFNSVANCVITTCLGNRSTKAPDRARVVEHWIEVARECRILKNFSSLYAILSALQSNSIHRLKKTWEDVSRDSFRIFQKLSEIFSDENNYSLSRELLIKEGTSKFATLEMNPKRAQKRPKETGIIQGTVPYLGTFLTDLVMLDTAMKDYLYGRLINFEKRRKEFEVIAQIKLLQSACNNYSIAPDEQFGAWFRAVERLSETESYNLSCELEPPSESASNTLRTKKNTAIVKRWSDRQAPSTELSTSGSSHSKSCDQLRCGPYLSSGDIADALSVHSAGSSSSDVEEINISFVPESPDGQEKKFWESASQSSPETSGISSASSSTSSSSASTTPVAATRTHKRSVSGLCNSSSALPLYNQQVGDCCIIRVSLDVDNGNMYKSILVTSQDKAPAVIRKAMDKHNLEEEEPEDYELLQILSDDRKLKIPENANVFYAMNSTANYDFVLKKRTFTKGVKVKHGASSTLPRMKQKGLKIAKGIF
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
7 (in isoform 3)Phosphorylation-6.2924043423
8 (in isoform 3)Phosphorylation-24.4424043423
9 (in isoform 3)Phosphorylation-15.2424043423
22 (in isoform 3)Phosphorylation-26.8424043423
23 (in isoform 3)Phosphorylation-25.4324043423
25 (in isoform 3)Phosphorylation-37.8124043423
28 (in isoform 5)Phosphorylation-28.8922617229
62PhosphorylationPDLPRPESSTQEIGE
CCCCCCCCCHHHHHH		41.1730206219
63PhosphorylationDLPRPESSTQEIGEE
CCCCCCCCHHHHHHH		32.2330206219
64PhosphorylationLPRPESSTQEIGEEL
CCCCCCCHHHHHHHH		39.2330206219
77PhosphorylationELINGVIYSISLRKV
HHHHHHHEEEEEEEE		9.5030206219
78PhosphorylationLINGVIYSISLRKVQ
HHHHHHEEEEEEEEE		8.4529496963
80PhosphorylationNGVIYSISLRKVQLH
HHHHEEEEEEEEEEE		19.0430206219
480PhosphorylationCRILKNFSSLYAILS
CHHHCCHHHHHHHHH		28.9124043423
481PhosphorylationRILKNFSSLYAILSA
HHHCCHHHHHHHHHH		22.6624043423
483PhosphorylationLKNFSSLYAILSALQ
HCCHHHHHHHHHHHH		8.1124043423
487PhosphorylationSSLYAILSALQSNSI
HHHHHHHHHHHHCCH		22.3324043423
491PhosphorylationAILSALQSNSIHRLK
HHHHHHHHCCHHHHH		33.1324043423
493PhosphorylationLSALQSNSIHRLKKT
HHHHHHCCHHHHHHH		25.6424043423
542O-linked_GlycosylationEGTSKFATLEMNPKR
CCCCCCEEEECCHHH		26.7830379171
542PhosphorylationEGTSKFATLEMNPKR
CCCCCCEEEECCHHH		26.7823312004
584PhosphorylationLDTAMKDYLYGRLIN
HHHHHHHHHHHHHCC		9.05-
586PhosphorylationTAMKDYLYGRLINFE
HHHHHHHHHHHCCHH		8.2517924679
659AcetylationASNTLRTKKNTAIVK
CCCCCCCCCCCHHHC		37.287933633
669PhosphorylationTAIVKRWSDRQAPST
CHHHCCCCCCCCCCC		27.2725159151
741PhosphorylationQEKKFWESASQSSPE
CCHHHHHHHCCCCCC		24.66-
745PhosphorylationFWESASQSSPETSGI
HHHHHCCCCCCCCCC		45.42-
753PhosphorylationSPETSGISSASSSTS
CCCCCCCCCCCCCCC		24.31-
767PhosphorylationSSSSASTTPVAATRT
CCCCCCCCCCCCCCC		17.17-
778PhosphorylationATRTHKRSVSGLCNS
CCCCCCCCHHHCCCC		25.9927251275
780PhosphorylationRTHKRSVSGLCNSSS
CCCCCCHHHCCCCCC		27.5624719451
785PhosphorylationSVSGLCNSSSALPLY
CHHHCCCCCCCCCCC		25.3623898821
793 (in isoform 2)Phosphorylation-33.2322210691
800 (in isoform 2)Phosphorylation-3.2722210691
802 (in isoform 2)Phosphorylation-1.9122210691
815AcetylationVDNGNMYKSILVTSQ
CCCCCEEEEEEEECC		21.917706951
816PhosphorylationDNGNMYKSILVTSQD
CCCCEEEEEEEECCC		12.03-
820PhosphorylationMYKSILVTSQDKAPA
EEEEEEEECCCCHHH		19.75-
821PhosphorylationYKSILVTSQDKAPAV
EEEEEEECCCCHHHH		28.9821815630
890AcetylationRTFTKGVKVKHGASS
CEECCCCEEECCCCC		54.997974691
892AcetylationFTKGVKVKHGASSTL
ECCCCEEECCCCCCH		30.517974701
896PhosphorylationVKVKHGASSTLPRMK
CEEECCCCCCHHHHH		28.5726699800
897PhosphorylationKVKHGASSTLPRMKQ
EEECCCCCCHHHHHH		33.1726699800
898PhosphorylationVKHGASSTLPRMKQK
EECCCCCCHHHHHHH		37.9826699800
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 GNDS_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GNDS_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 GNDS_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RASM_HUMANMRASphysical
10498616
ARRB2_HUMANARRB2physical
12105416
ARRB1_HUMANARRB1physical
12105416
RASH_HUMANHRASphysical
7972015
RAP2B_HUMANRAP2Bphysical
10085114
RAP2A_HUMANRAP2Aphysical
10085114
RAP1A_HUMANRAP1Aphysical
10085114
RASH_HUMANHRASphysical
9038168
RRAS_HUMANRRASphysical
7809086
RASH_HUMANHRASphysical
7809086
RASK_HUMANKRASphysical
7809086
RPGF2_HUMANRAPGEF2physical
7809086
RASH_HUMANHRASphysical
9150145
CASP8_HUMANCASP8physical
21525013
FADD_HUMANFADDphysical
21525013
RAP1B_HUMANRAP1Bphysical
21988832
RRAS2_HUMANRRAS2physical
21988832
RAP1A_HUMANRAP1Aphysical
11786539
RAP2A_HUMANRAP2Aphysical
11786539
RAP2B_HUMANRAP2Bphysical
11786539
RASH_HUMANHRASphysical
11786539
CNKR1_HUMANCNKSR1physical
14749388
RASH_HUMANHRASphysical
25241761
RAP2A_HUMANRAP2Aphysical
28405688
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 GNDS_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-586, AND MASSSPECTROMETRY.

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