AGO3_HUMAN - dbPTM
AGO3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AGO3_HUMAN
UniProt AC Q9H9G7
Protein Name Protein argonaute-3 {ECO:0000255|HAMAP-Rule:MF_03032}
Gene Name AGO3
Organism Homo sapiens (Human).
Sequence Length 860
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. Proposed to be involved in stabilization of small RNA derivates (riRNA) derived from processed RNA polymerase III-transcribed Alu repeats containing a DR2 retinoic acid response element (RARE) in stem cells and in the subsequent riRNA-dependent degradation of a subset of RNA polymerase II-transcribed coding mRNAs by recruiting a mRNA decapping complex involving EDC4. Possesses RNA slicer activity but only on select RNAs bearing 5'- and 3'-flanking sequences to the region of guide-target complementarity. [PubMed: 29040713]
Protein Sequence MEIGSAGPAGAQPLLMVPRRPGYGTMGKPIKLLANCFQVEIPKIDVYLYEVDIKPDKCPRRVNREVVDSMVQHFKVTIFGDRRPVYDGKRSLYTANPLPVATTGVDLDVTLPGEGGKDRPFKVSIKFVSRVSWHLLHEVLTGRTLPEPLELDKPISTNPVHAVDVVLRHLPSMKYTPVGRSFFSAPEGYDHPLGGGREVWFGFHQSVRPAMWKMMLNIDVSATAFYKAQPVIQFMCEVLDIHNIDEQPRPLTDSHRVKFTKEIKGLKVEVTHCGTMRRKYRVCNVTRRPASHQTFPLQLENGQTVERTVAQYFREKYTLQLKYPHLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKLTDNQTSTMIKATARSAPDRQEEISRLVRSANYETDPFVQEFQFKVRDEMAHVTGRVLPAPMLQYGGRNRTVATPSHGVWDMRGKQFHTGVEIKMWAIACFATQRQCREEILKGFTDQLRKISKDAGMPIQGQPCFCKYAQGADSVEPMFRHLKNTYSGLQLIIVILPGKTPVYAEVKRVGDTLLGMATQCVQVKNVIKTSPQTLSNLCLKINVKLGGINNILVPHQRPSVFQQPVIFLGADVTHPPAGDGKKPSIAAVVGSMDAHPSRYCATVRVQRPRQEIIQDLASMVRELLIQFYKSTRFKPTRIIFYRDGVSEGQFRQVLYYELLAIREACISLEKDYQPGITYIVVQKRHHTRLFCADRTERVGRSGNIPAGTTVDTDITHPYEFDFYLCSHAGIQGTSRPSHYHVLWDDNCFTADELQLLTYQLCHTYVRCTRSVSIPAPAYYAHLVAFRARYHLVDKEHDSAEGSHVSGQSNGRDPQALAKAVQIHQDTLRTMYFA
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
1Acetylation-------MEIGSAGP
-------CCCCCCCC		8.3722814378
5Phosphorylation---MEIGSAGPAGAQ
---CCCCCCCCCCCC		35.4062169233
28UbiquitinationPGYGTMGKPIKLLAN
CCCCCCCHHHHHHHH		32.52-
89UbiquitinationRRPVYDGKRSLYTAN
CCEEECCCCCEEECC		35.60-
174UbiquitinationLRHLPSMKYTPVGRS
HHCCCCCCCCCCCCC		50.76-
189PhosphorylationFFSAPEGYDHPLGGG
CCCCCCCCCCCCCCC		14.9328796482
271PhosphorylationKGLKVEVTHCGTMRR
CCCEEEEEECCCCCC		9.6528348404
275PhosphorylationVEVTHCGTMRRKYRV
EEEEECCCCCCEEEE		16.95113334153
317PhosphorylationAQYFREKYTLQLKYP
HHHHHHHEEEEEECC		14.1317384208
323PhosphorylationKYTLQLKYPHLPCLQ
HEEEEEECCCCCCEE		12.4117384208
336UbiquitinationLQVGQEQKHTYLPLE
EECCCCCCCCEECHH		36.84-
338PhosphorylationVGQEQKHTYLPLEVC
CCCCCCCCEECHHHH		33.51-
339PhosphorylationGQEQKHTYLPLEVCN
CCCCCCCEECHHHHH		13.1783375
356UbiquitinationAGQRCIKKLTDNQTS
CCCHHHHHCCCCCHH		36.39-
358PhosphorylationQRCIKKLTDNQTSTM
CHHHHHCCCCCHHHH		41.61-
363PhosphorylationKLTDNQTSTMIKATA
HCCCCCHHHHHHHHH		13.25-
367UbiquitinationNQTSTMIKATARSAP
CCHHHHHHHHHHCCC		28.9421906983
421PhosphorylationLPAPMLQYGGRNRTV
ECCCCEEECCCCCEE		20.00-
445PhosphorylationMRGKQFHTGVEIKMW
CCCCCCCCCCHHHHH		44.1837817101
480UbiquitinationDQLRKISKDAGMPIQ
HHHHHHHHHCCCCCC		55.88-
494UbiquitinationQGQPCFCKYAQGADS
CCCCCCCEECCCCCC		24.30-
512PhosphorylationMFRHLKNTYSGLQLI
HHHHHHHHCCCCEEE		19.9218452278
513PhosphorylationFRHLKNTYSGLQLII
HHHHHHHCCCCEEEE		15.3318452278
514PhosphorylationRHLKNTYSGLQLIIV
HHHHHHCCCCEEEEE		30.8718452278
527PhosphorylationIVILPGKTPVYAEVK
EEECCCCCCCEEEHH		24.7322192769
530PhosphorylationLPGKTPVYAEVKRVG
CCCCCCCEEEHHHHH		9.76-
534UbiquitinationTPVYAEVKRVGDTLL
CCCEEEHHHHHHHHH		32.6321906983
624PhosphorylationGSMDAHPSRYCATVR
CCCCCCHHHEEEEEE		26.4750563943
629PhosphorylationHPSRYCATVRVQRPR
CHHHEEEEEEECCCH		12.8050563949
656UbiquitinationELLIQFYKSTRFKPT
HHHHHHHHHCCCCCE		46.79-
682PhosphorylationGQFRQVLYYELLAIR
HHHHHHHHHHHHHHH		8.95153769
683PhosphorylationQFRQVLYYELLAIRE
HHHHHHHHHHHHHHH		8.92150039
705PhosphorylationDYQPGITYIVVQKRH
CCCCCEEEEEEECCC		6.987607403
750PhosphorylationHPYEFDFYLCSHAGI
CCCCCCEEEECCCCC		14.51-
753PhosphorylationEFDFYLCSHAGIQGT
CCCEEEECCCCCCCC		17.49-
760PhosphorylationSHAGIQGTSRPSHYH
CCCCCCCCCCCCCEE		12.7527660467
761PhosphorylationHAGIQGTSRPSHYHV
CCCCCCCCCCCCEEE		49.3627660461
797PhosphorylationTYVRCTRSVSIPAPA
HHHHHCCCCCCCCCH		11.3216094384
799PhosphorylationVRCTRSVSIPAPAYY
HHHCCCCCCCCCHHH		24.8935066013
805PhosphorylationVSIPAPAYYAHLVAF
CCCCCCHHHHHHHHH		10.5026074081
806PhosphorylationSIPAPAYYAHLVAFR
CCCCCHHHHHHHHHH		6.9426074081
816PhosphorylationLVAFRARYHLVDKEH
HHHHHHHEEECCCCC		9.8723186163
825PhosphorylationLVDKEHDSAEGSHVS
ECCCCCCCCCCCCCC		30.0825159151
829PhosphorylationEHDSAEGSHVSGQSN
CCCCCCCCCCCCCCC		16.5426657352
832PhosphorylationSAEGSHVSGQSNGRD
CCCCCCCCCCCCCCC		26.2025159151
835PhosphorylationGSHVSGQSNGRDPQA
CCCCCCCCCCCCHHH		44.7921406692
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 AGO3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AGO3_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 AGO3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FLNA_HUMANFLNAphysical
19167051
ANM5_HUMANPRMT5physical
19167051
SF3B6_HUMANSF3B6physical
19167051
SPTB2_HUMANSPTBN1physical
19167051
SPTN1_HUMANSPTAN1physical
19167051
OTUD4_HUMANOTUD4physical
19167051
MYH9_HUMANMYH9physical
19167051
TNR6B_HUMANTNRC6Bphysical
19167051
IF4B_HUMANEIF4Bphysical
19167051
IPO8_HUMANIPO8physical
19167051
AGO2_HUMANAGO2physical
19167051
HS90B_HUMANHSP90AB1physical
19167051
GRP75_HUMANHSPA9physical
19167051
SUN2_HUMANSUN2physical
19167051
PSPC1_HUMANPSPC1physical
19167051
TCPG_HUMANCCT3physical
19167051
EIF3L_HUMANEIF3Lphysical
19167051
ATD3B_HUMANATAD3Bphysical
19167051
TAB1_HUMANTAB1physical
19167051
PRP31_HUMANPRPF31physical
19167051
TBA1A_HUMANTUBA1Aphysical
19167051
STK38_HUMANSTK38physical
19167051
TBB4A_HUMANTUBB4Aphysical
19167051
TBB4B_HUMANTUBB4Bphysical
19167051
TBB2A_HUMANTUBB2Aphysical
19167051
TBB5_HUMANTUBBphysical
19167051
RO52_HUMANTRIM21physical
19167051
EF1A1_HUMANEEF1A1physical
19167051
ODB2_HUMANDBTphysical
19167051
RUVB2_HUMANRUVBL2physical
19167051
MEP50_HUMANWDR77physical
19167051
DNJA1_HUMANDNAJA1physical
19167051
OST48_HUMANDDOSTphysical
19167051
QPCTL_HUMANQPCTLphysical
19167051
ICLN_HUMANCLNS1Aphysical
19167051
PHB2_HUMANPHB2physical
19167051
SPIN1_HUMANSPIN1physical
19167051
TNR6A_HUMANTNRC6Aphysical
19470757
TNR6B_HUMANTNRC6Bphysical
19470757
TNR6C_HUMANTNRC6Cphysical
19470757
TNR6A_HUMANTNRC6Aphysical
19383768
TNR6B_HUMANTNRC6Bphysical
19383768
TNR6C_HUMANTNRC6Cphysical
19383768
S22A2_HUMANSLC22A2physical
21988832
AGO1_HUMANAGO1physical
24778252
AGO2_HUMANAGO2physical
24778252
AGO4_HUMANAGO4physical
24778252
DICER_HUMANDICER1physical
24778252
KAP0_HUMANPRKAR1Aphysical
24778252
TRBP2_HUMANTARBP2physical
24778252
TNR6A_HUMANTNRC6Aphysical
24778252
TNR6B_HUMANTNRC6Bphysical
24778252
TNR6C_HUMANTNRC6Cphysical
24778252
ZN346_HUMANZNF346physical
24778252
HS90A_HUMANHSP90AA1physical
26186194
AP3M1_HUMANAP3M1physical
26186194
AP3D1_HUMANAP3D1physical
26186194
FKBP5_HUMANFKBP5physical
26186194
AP3B1_HUMANAP3B1physical
26186194
AP3S1_HUMANAP3S1physical
26186194
ANKY2_HUMANANKMY2physical
26186194
LONF3_HUMANLONRF3physical
26186194
MOG1_HUMANRANGRFphysical
26186194
BAG5_HUMANBAG5physical
26496610
CIR1_HUMANCIR1physical
26496610
TNR6B_HUMANTNRC6Bphysical
26496610
DICER_HUMANDICER1physical
26496610
TNR6A_HUMANTNRC6Aphysical
26496610
LONF3_HUMANLONRF3physical
28514442
AP3B1_HUMANAP3B1physical
28514442
FKBP5_HUMANFKBP5physical
28514442
HS90A_HUMANHSP90AA1physical
28514442
AP3D1_HUMANAP3D1physical
28514442
ANKY2_HUMANANKMY2physical
28514442
AP3M1_HUMANAP3M1physical
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 AGO3_HUMAN

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Related Literatures of Post-Translational Modification

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