SYDE1_HUMAN - dbPTM
SYDE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYDE1_HUMAN
UniProt AC Q6ZW31
Protein Name Rho GTPase-activating protein SYDE1
Gene Name SYDE1
Organism Homo sapiens (Human).
Sequence Length 735
Subcellular Localization
Protein Description GTPase activator for the Rho-type GTPases. As a GCM1 downstream effector, it is involved in placental development and positively regulates trophoblast cells migration. It regulates cytoskeletal remodeling by controlling the activity of Rho GTPases including RHOA, CDC42 and RAC1. [PubMed: 27917469]
Protein Sequence MAEPLLRKTFSRLRGREKLPRKKSDAKERGHPAQRPEPSPPEPEPQAPEGSQAGAEGPSSPEASRSPARGAYLQSLEPSSRRWVLGGAKPAEDTSLGPGVPGTGEPAGEIWYNPIPEEDPRPPAPEPPGPQPGSAESEGLAPQGAAPASPPTKASRTKSPGPARRLSIKMKKLPELRRRLSLRGPRAGRERERAAPAGSVISRYHLDSSVGGPGPAAGPGGTRSPRAGYLSDGDSPERPAGPPSPTSFRPYEVGPAARAPPAALWGRLSLHLYGLGGLRPAPGATPRDLCCLLQVDGEARARTGPLRGGPDFLRLDHTFHLELEAARLLRALVLAWDPGVRRHRPCAQGTVLLPTVFRGCQAQQLAVRLEPQGLLYAKLTLSEQQEAPATAEPRVFGLPLPLLVERERPPGQVPLIIQKCVGQIERRGLRVVGLYRLCGSAAVKKELRDAFERDSAAVCLSEDLYPDINVITGILKDYLRELPTPLITQPLYKVVLEAMARDPPNRVPPTTEGTRGLLSCLPDVERATLTLLLDHLRLVSSFHAYNRMTPQNLAVCFGPVLLPARQAPTRPRARSSGPGLASAVDFKHHIEVLHYLLQSWPDPRLPRQSPDVAPYLRPKRQPPLHLPLADPEVVTRPRGRGGPESPPSNRYAGDWSVCGRDFLPCGRDFLSGPDYDHVTGSDSEDEDEEVGEPRVTGDFEDDFDAPFNPHLNLKDFDALILDLERELSKQINVCL
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
39PhosphorylationPAQRPEPSPPEPEPQ
CCCCCCCCCCCCCCC		51.9623663014
51PhosphorylationEPQAPEGSQAGAEGP
CCCCCCCCCCCCCCC		18.3923663014
59PhosphorylationQAGAEGPSSPEASRS
CCCCCCCCCCHHHCC		70.1823663014
60PhosphorylationAGAEGPSSPEASRSP
CCCCCCCCCHHHCCC		29.8723663014
64PhosphorylationGPSSPEASRSPARGA
CCCCCHHHCCCCCCC		31.4623663014
66PhosphorylationSSPEASRSPARGAYL
CCCHHHCCCCCCCCH		22.0323663014
72PhosphorylationRSPARGAYLQSLEPS
CCCCCCCCHHCCCCC		14.2223403867
75PhosphorylationARGAYLQSLEPSSRR
CCCCCHHCCCCCCCC		31.9123403867
79PhosphorylationYLQSLEPSSRRWVLG
CHHCCCCCCCCEECC		27.4023403867
80PhosphorylationLQSLEPSSRRWVLGG
HHCCCCCCCCEECCC		36.2629083192
89AcetylationRWVLGGAKPAEDTSL
CEECCCCCCCCCCCC		48.30164029
89UbiquitinationRWVLGGAKPAEDTSL
CEECCCCCCCCCCCC		48.30-
152PhosphorylationAAPASPPTKASRTKS
CCCCCCCCCCCCCCC		42.5023879269
157PhosphorylationPPTKASRTKSPGPAR
CCCCCCCCCCCCHHH		33.1226699800
159PhosphorylationTKASRTKSPGPARRL
CCCCCCCCCCHHHHH		34.1829514088
167PhosphorylationPGPARRLSIKMKKLP
CCHHHHHHHHHHHHH		20.5329514088
181PhosphorylationPELRRRLSLRGPRAG
HHHHHHHHHCCCCCH		17.7623532336
199PhosphorylationERAAPAGSVISRYHL
HHCCCCCCEEEEEEC		20.5522210691
208PhosphorylationISRYHLDSSVGGPGP
EEEEECCCCCCCCCC		33.0329083192
209PhosphorylationSRYHLDSSVGGPGPA
EEEECCCCCCCCCCC		25.1729083192
222PhosphorylationPAAGPGGTRSPRAGY
CCCCCCCCCCCCCCC		33.6130576142
224PhosphorylationAGPGGTRSPRAGYLS
CCCCCCCCCCCCCCC		20.6922617229
229PhosphorylationTRSPRAGYLSDGDSP
CCCCCCCCCCCCCCC		11.3122617229
231PhosphorylationSPRAGYLSDGDSPER
CCCCCCCCCCCCCCC		30.9421955146
235PhosphorylationGYLSDGDSPERPAGP
CCCCCCCCCCCCCCC		33.9026055452
244PhosphorylationERPAGPPSPTSFRPY
CCCCCCCCCCCCCCC		43.9026055452
246PhosphorylationPAGPPSPTSFRPYEV
CCCCCCCCCCCCCCC		44.8530175587
247PhosphorylationAGPPSPTSFRPYEVG
CCCCCCCCCCCCCCC		23.7330175587
251PhosphorylationSPTSFRPYEVGPAAR
CCCCCCCCCCCCCCC		20.9923663014
307MethylationRARTGPLRGGPDFLR
HHHCCCCCCCCCCCC		51.67115918057
478PhosphorylationITGILKDYLRELPTP
HHHHHHHHHHHCCCC		13.18-
484PhosphorylationDYLRELPTPLITQPL
HHHHHCCCCCCCHHH		43.27-
493UbiquitinationLITQPLYKVVLEAMA
CCCHHHHHHHHHHHH		33.28-
575PhosphorylationPTRPRARSSGPGLAS
CCCCCHHHCCCCHHH		38.3725850435
576PhosphorylationTRPRARSSGPGLASA
CCCCHHHCCCCHHHH		43.3821712546
582PhosphorylationSSGPGLASAVDFKHH
HCCCCHHHHHHHHHH		33.5921712546
599PhosphorylationVLHYLLQSWPDPRLP
HHHHHHHHCCCCCCC		40.3128509920
609PhosphorylationDPRLPRQSPDVAPYL
CCCCCCCCCCCHHHC		25.0922985185
640MethylationVVTRPRGRGGPESPP
HCCCCCCCCCCCCCC		48.4516288051
645PhosphorylationRGRGGPESPPSNRYA
CCCCCCCCCCCCCCC		45.2929255136
648PhosphorylationGGPESPPSNRYAGDW
CCCCCCCCCCCCCCC		37.0125850435
651PhosphorylationESPPSNRYAGDWSVC
CCCCCCCCCCCCCCC		21.1327642862
671PhosphorylationPCGRDFLSGPDYDHV
CCCCCHHCCCCCCCC		48.5523663014
675PhosphorylationDFLSGPDYDHVTGSD
CHHCCCCCCCCCCCC		15.8723927012
679PhosphorylationGPDYDHVTGSDSEDE
CCCCCCCCCCCCCCC		27.7823927012
681PhosphorylationDYDHVTGSDSEDEDE
CCCCCCCCCCCCCCC		28.7023927012
683PhosphorylationDHVTGSDSEDEDEEV
CCCCCCCCCCCCCCC		48.9523927012
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 SYDE1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYDE1_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 SYDE1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPB4_HUMANPOLR2Dphysical
28514442
KLDC2_HUMANKLHDC2physical
28514442
TYW3_HUMANTYW3physical
28514442
RPB1_HUMANPOLR2Aphysical
28514442
RPB11_HUMANPOLR2Jphysical
28514442
RPAP2_HUMANRPAP2physical
28514442
RPB9_HUMANPOLR2Iphysical
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 SYDE1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-231; SER-235; SER-244;THR-246; SER-247; SER-681 AND SER-683, AND MASS SPECTROMETRY.

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