AGO4_HUMAN - dbPTM
AGO4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AGO4_HUMAN
UniProt AC Q9HCK5
Protein Name Protein argonaute-4 {ECO:0000255|HAMAP-Rule:MF_03033}
Gene Name AGO4
Organism Homo sapiens (Human).
Sequence Length 861
Subcellular Localization Cytoplasm, P-body .
Protein Description Required for RNA-mediated gene silencing (RNAi). Binds to short RNAs such as microRNAs (miRNAs) and represses the translation of mRNAs which are complementary to them. Lacks endonuclease activity and does not appear to cleave target mRNAs. Also required for RNA-directed transcription and replication of the human hapatitis delta virus (HDV)..
Protein Sequence MEALGPGPPASLFQPPRRPGLGTVGKPIRLLANHFQVQIPKIDVYHYDVDIKPEKRPRRVNREVVDTMVRHFKMQIFGDRQPGYDGKRNMYTAHPLPIGRDRVDMEVTLPGEGKDQTFKVSVQWVSVVSLQLLLEALAGHLNEVPDDSVQALDVITRHLPSMRYTPVGRSFFSPPEGYYHPLGGGREVWFGFHQSVRPAMWNMMLNIDVSATAFYRAQPIIEFMCEVLDIQNINEQTKPLTDSQRVKFTKEIRGLKVEVTHCGQMKRKYRVCNVTRRPASHQTFPLQLENGQAMECTVAQYFKQKYSLQLKYPHLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKLTDNQTSTMIKATARSAPDRQEEISRLVKSNSMVGGPDPYLKEFGIVVHNEMTELTGRVLPAPMLQYGGRNKTVATPNQGVWDMRGKQFYAGIEIKVWAVACFAPQKQCREDLLKSFTDQLRKISKDAGMPIQGQPCFCKYAQGADSVEPMFKHLKMTYVGLQLIVVILPGKTPVYAEVKRVGDTLLGMATQCVQVKNVVKTSPQTLSNLCLKINAKLGGINNVLVPHQRPSVFQQPVIFLGADVTHPPAGDGKKPSIAAVVGSMDGHPSRYCATVRVQTSRQEISQELLYSQEVIQDLTNMVRELLIQFYKSTRFKPTRIIYYRGGVSEGQMKQVAWPELIAIRKACISLEEDYRPGITYIVVQKRHHTRLFCADKTERVGKSGNVPAGTTVDSTITHPSEFDFYLCSHAGIQGTSRPSHYQVLWDDNCFTADELQLLTYQLCHTYVRCTRSVSIPAPAYYARLVAFRARYHLVDKDHDSAEGSHVSGQSNGRDPQALAKAVQIHHDTQHTMYFA
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
11PhosphorylationLGPGPPASLFQPPRR
CCCCCCHHHCCCCCC		35.1846160415
47PhosphorylationPKIDVYHYDVDIKPE
CCCEEEEECCCCCCC		10.447326705
108PhosphorylationDRVDMEVTLPGEGKD
CCEEEEEECCCCCCC		17.5868719535
155UbiquitinationSVQALDVITRHLPSM
HHHHHHHHHHCCCCC		2.5322817900
206UbiquitinationAMWNMMLNIDVSATA
HHHHHHHCEEECCHH		15.5422817900
284UbiquitinationRPASHQTFPLQLENG
CCCCCCCCEEEECCC		4.5922817900
289UbiquitinationQTFPLQLENGQAMEC
CCCEEEECCCCEEEE		46.4822817900
324UbiquitinationCLQVGQEQKHTYLPL
CEECCCCCCCCEECH		34.6427667366
325UbiquitinationLQVGQEQKHTYLPLE
EECCCCCCCCEECHH		36.84-
327PhosphorylationVGQEQKHTYLPLEVC
CCCCCCCCEECHHHH		33.51-
328PhosphorylationGQEQKHTYLPLEVCN
CCCCCCCEECHHHHH		13.1783375
335UbiquitinationYLPLEVCNIVAGQRC
EECHHHHHHHCCCHH		36.6222817900
345UbiquitinationAGQRCIKKLTDNQTS
CCCHHHHHCCCCCHH		36.3929967540
347PhosphorylationQRCIKKLTDNQTSTM
CHHHHHCCCCCHHHH		41.61-
352PhosphorylationKLTDNQTSTMIKATA
HCCCCCHHHHHHHHH		13.25-
356UbiquitinationNQTSTMIKATARSAP
CCHHHHHHHHHHCCC		28.9421906983
374UbiquitinationEEISRLVKSNSMVGG
HHHHHHHHHCCCCCC		48.8129967540
375UbiquitinationEISRLVKSNSMVGGP
HHHHHHHHCCCCCCC		27.0227667366
412PhosphorylationLPAPMLQYGGRNKTV
ECCCCEEECCCCCCC		20.00-
418UbiquitinationQYGGRNKTVATPNQG
EECCCCCCCCCCCCC		20.9422817900
458UbiquitinationQKQCREDLLKSFTDQ
HHHHHHHHHHHHHHH		5.7827667366
460UbiquitinationQCREDLLKSFTDQLR
HHHHHHHHHHHHHHH		51.3129967540
471UbiquitinationDQLRKISKDAGMPIQ
HHHHHHHHHCCCCCC		55.88-
485UbiquitinationQGQPCFCKYAQGADS
CCCCCCCCCCCCCCC		24.3022817900
518PhosphorylationVVILPGKTPVYAEVK
EEECCCCCCCEEEHH		24.7322192777
521PhosphorylationLPGKTPVYAEVKRVG
CCCCCCCEEEHHHHH		9.76-
525UbiquitinationTPVYAEVKRVGDTLL
CCCEEEHHHHHHHHH		32.6321906983
546UbiquitinationVQVKNVVKTSPQTLS
EEEEEEECCCHHHHH		38.72-
558UbiquitinationTLSNLCLKINAKLGG
HHHHHHHHHHHHCCC		32.6829967540
562SumoylationLCLKINAKLGGINNV
HHHHHHHHCCCCCCE		43.08-
657UbiquitinationELLIQFYKSTRFKPT
HHHHHHHHHCCCCCE		46.79-
754PhosphorylationEFDFYLCSHAGIQGT
CCCEEEECCCCCCCC		17.49-
798PhosphorylationTYVRCTRSVSIPAPA
HHCHHCCCCCCCCHH		11.3216094384
800PhosphorylationVRCTRSVSIPAPAYY
CHHCCCCCCCCHHHH		24.89-
806PhosphorylationVSIPAPAYYARLVAF
CCCCCHHHHHHHHHH		9.1526074081
807PhosphorylationSIPAPAYYARLVAFR
CCCCHHHHHHHHHHH		6.3226074081
826PhosphorylationLVDKDHDSAEGSHVS
EECCCCCCCCCCCCC		25.4624247654
833PhosphorylationSAEGSHVSGQSNGRD
CCCCCCCCCCCCCCC		26.20-
836PhosphorylationGSHVSGQSNGRDPQA
CCCCCCCCCCCCHHH		44.7950563979
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 AGO4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AGO4_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 AGO4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANM5_HUMANPRMT5physical
19167051
TNR6B_HUMANTNRC6Bphysical
19167051
TNR6A_HUMANTNRC6Aphysical
19167051
IF4B_HUMANEIF4Bphysical
19167051
AGO3_HUMANAGO3physical
19167051
JAK1_HUMANJAK1physical
19167051
IPO8_HUMANIPO8physical
19167051
AGO2_HUMANAGO2physical
19167051
HS90B_HUMANHSP90AB1physical
19167051
HS90A_HUMANHSP90AA1physical
19167051
HSP7C_HUMANHSPA8physical
19167051
PABP4_HUMANPABPC4physical
19167051
GRP78_HUMANHSPA5physical
19167051
CMC2_HUMANSLC25A13physical
19167051
IF2B1_HUMANIGF2BP1physical
19167051
TCPE_HUMANCCT5physical
19167051
TBB4B_HUMANTUBB4Bphysical
19167051
TBB5_HUMANTUBBphysical
19167051
YBOX1_HUMANYBX1physical
19167051
DNJA2_HUMANDNAJA2physical
19167051
RO52_HUMANTRIM21physical
19167051
AGK_HUMANAGKphysical
19167051
ODB2_HUMANDBTphysical
19167051
EF1G_HUMANEEF1Gphysical
19167051
DNJA1_HUMANDNAJA1physical
19167051
ACTB_HUMANACTBphysical
19167051
EFTU_HUMANTUFMphysical
19167051
MEP50_HUMANWDR77physical
19167051
SUCB1_HUMANSUCLA2physical
19167051
DJB11_HUMANDNAJB11physical
19167051
GALK1_HUMANGALK1physical
19167051
HNRPC_HUMANHNRNPCphysical
19167051
EMD_HUMANEMDphysical
19167051
MPCP_HUMANSLC25A3physical
19167051
PGAM5_HUMANPGAM5physical
19167051
GHC1_HUMANSLC25A22physical
19167051
ATPG_HUMANATP5C1physical
19167051
ADT2_HUMANSLC25A5physical
19167051
TXTP_HUMANSLC25A1physical
19167051
DIC_HUMANSLC25A10physical
19167051
TEBP_HUMANPTGES3physical
19167051
PRDX1_HUMANPRDX1physical
19167051
ARF4_HUMANARF4physical
19167051
RS9_HUMANRPS9physical
19167051
RS5_HUMANRPS5physical
19167051
RS18_HUMANRPS18physical
19167051
RS26_HUMANRPS26physical
19167051
RL24_HUMANRPL24physical
19167051
RL11_HUMANRPL11physical
19167051
RL27A_HUMANRPL27Aphysical
19167051
RL27_HUMANRPL27physical
19167051
RL35_HUMANRPL35physical
19167051
RL23_HUMANRPL23physical
19167051
RL38_HUMANRPL38physical
19167051
PTPS_HUMANPTSphysical
19167051
SSBP_HUMANSSBP1physical
19167051
MYCBP_HUMANMYCBPphysical
19167051
ATP5I_HUMANATP5Iphysical
19167051
TNR6A_HUMANTNRC6Aphysical
19383768
TNR6B_HUMANTNRC6Bphysical
19383768
TNR6C_HUMANTNRC6Cphysical
19383768
A4_HUMANAPPphysical
21832049
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 AGO4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-798, AND MASSSPECTROMETRY.

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