DICER_HUMAN - dbPTM
DICER_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DICER_HUMAN
UniProt AC Q9UPY3
Protein Name Endoribonuclease Dicer
Gene Name DICER1
Organism Homo sapiens (Human).
Sequence Length 1922
Subcellular Localization Cytoplasm .
Protein Description Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3' overhang of two nucleotides, producing respectively short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA-induced silencing complex (RISC) to complementary RNAs to degrade them or prevent their translation. Gene silencing mediated by siRNAs, also called RNA interference, controls the elimination of transcripts from mobile and repetitive DNA elements of the genome but also the degradation of exogenous RNA of viral origin for instance. The miRNA pathway on the other side is a mean to specifically regulate the expression of target genes..
Protein Sequence MKSPALQPLSMAGLQLMTPASSPMGPFFGLPWQQEAIHDNIYTPRKYQVELLEAALDHNTIVCLNTGSGKTFIAVLLTKELSYQIRGDFSRNGKRTVFLVNSANQVAQQVSAVRTHSDLKVGEYSNLEVNASWTKERWNQEFTKHQVLIMTCYVALNVLKNGYLSLSDINLLVFDECHLAILDHPYREIMKLCENCPSCPRILGLTASILNGKCDPEELEEKIQKLEKILKSNAETATDLVVLDRYTSQPCEIVVDCGPFTDRSGLYERLLMELEEALNFINDCNISVHSKERDSTLISKQILSDCRAVLVVLGPWCADKVAGMMVRELQKYIKHEQEELHRKFLLFTDTFLRKIHALCEEHFSPASLDLKFVTPKVIKLLEILRKYKPYERQQFESVEWYNNRNQDNYVSWSDSEDDDEDEEIEEKEKPETNFPSPFTNILCGIIFVERRYTAVVLNRLIKEAGKQDPELAYISSNFITGHGIGKNQPRNKQMEAEFRKQEEVLRKFRAHETNLLIATSIVEEGVDIPKCNLVVRFDLPTEYRSYVQSKGRARAPISNYIMLADTDKIKSFEEDLKTYKAIEKILRNKCSKSVDTGETDIDPVMDDDDVFPPYVLRPDDGGPRVTINTAIGHINRYCARLPSDPFTHLAPKCRTRELPDGTFYSTLYLPINSPLRASIVGPPMSCVRLAERVVALICCEKLHKIGELDDHLMPVGKETVKYEEELDLHDEEETSVPGRPGSTKRRQCYPKAIPECLRDSYPRPDQPCYLYVIGMVLTTPLPDELNFRRRKLYPPEDTTRCFGILTAKPIPQIPHFPVYTRSGEVTISIELKKSGFMLSLQMLELITRLHQYIFSHILRLEKPALEFKPTDADSAYCVLPLNVVNDSSTLDIDFKFMEDIEKSEARIGIPSTKYTKETPFVFKLEDYQDAVIIPRYRNFDQPHRFYVADVYTDLTPLSKFPSPEYETFAEYYKTKYNLDLTNLNQPLLDVDHTSSRLNLLTPRHLNQKGKALPLSSAEKRKAKWESLQNKQILVPELCAIHPIPASLWRKAVCLPSILYRLHCLLTAEELRAQTASDAGVGVRSLPADFRYPNLDFGWKKSIDSKSFISISNSSSAENDNYCKHSTIVPENAAHQGANRTSSLENHDQMSVNCRTLLSESPGKLHVEVSADLTAINGLSYNQNLANGSYDLANRDFCQGNQLNYYKQEIPVQPTTSYSIQNLYSYENQPQPSDECTLLSNKYLDGNANKSTSDGSPVMAVMPGTTDTIQVLKGRMDSEQSPSIGYSSRTLGPNPGLILQALTLSNASDGFNLERLEMLGDSFLKHAITTYLFCTYPDAHEGRLSYMRSKKVSNCNLYRLGKKKGLPSRMVVSIFDPPVNWLPPGYVVNQDKSNTDKWEKDEMTKDCMLANGKLDEDYEEEDEEEESLMWRAPKEEADYEDDFLEYDQEHIRFIDNMLMGSGAFVKKISLSPFSTTDSAYEWKMPKKSSLGSMPFSSDFEDFDYSSWDAMCYLDPSKAVEEDDFVVGFWNPSEENCGVDTGKQSISYDLHTEQCIADKSIADCVEALLGCYLTSCGERAAQLFLCSLGLKVLPVIKRTDREKALCPTRENFNSQQKNLSVSCAAASVASSRSSVLKDSEYGCLKIPPRCMFDHPDADKTLNHLISGFENFEKKINYRFKNKAYLLQAFTHASYHYNTITDCYQRLEFLGDAILDYLITKHLYEDPRQHSPGVLTDLRSALVNNTIFASLAVKYDYHKYFKAVSPELFHVIDDFVQFQLEKNEMQGMDSELRRSEEDEEKEEDIEVPKAMGDIFESLAGAIYMDSGMSLETVWQVYYPMMRPLIEKFSANVPRSPVRELLEMEPETAKFSPAERTYDGKVRVTVEVVGKGKFKGVGRSYRIAKSAAARRALRSLKANQPQVPNS
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
43PhosphorylationAIHDNIYTPRKYQVE
HHCCCCCCCCHHHHH
16.9024719451
57UbiquitinationELLEAALDHNTIVCL
HHHHHHHCCCEEEEE
28.4124816145
82PhosphorylationVLLTKELSYQIRGDF
EEECCCCCEEECCCC
18.9826852163
83PhosphorylationLLTKELSYQIRGDFS
EECCCCCEEECCCCC
22.1526852163
102PhosphorylationRTVFLVNSANQVAQQ
EEEEEECCHHHHHHH
22.5518785766
238PhosphorylationKSNAETATDLVVLDR
HCCCCCCCCEEEEEC
36.97-
248UbiquitinationVVLDRYTSQPCEIVV
EEEECCCCCCCEEEE
24.16-
363UbiquitinationHALCEEHFSPASLDL
HHHHHHCCCCCCCCC
12.08-
364UbiquitinationALCEEHFSPASLDLK
HHHHHCCCCCCCCCC
22.82-
397PhosphorylationYERQQFESVEWYNNR
CCHHCCCCEEECCCC
26.9928985074
409PhosphorylationNNRNQDNYVSWSDSE
CCCCCCCCCCCCCCC
12.2623090842
411PhosphorylationRNQDNYVSWSDSEDD
CCCCCCCCCCCCCCC
15.5330576142
413PhosphorylationQDNYVSWSDSEDDDE
CCCCCCCCCCCCCCC
24.6128348404
415PhosphorylationNYVSWSDSEDDDEDE
CCCCCCCCCCCCCHH
37.0928348404
415UbiquitinationNYVSWSDSEDDDEDE
CCCCCCCCCCCCCHH
37.0924816145
452PhosphorylationIIFVERRYTAVVLNR
EEEECHHHHHHHHHH
12.79-
466UbiquitinationRLIKEAGKQDPELAY
HHHHHHCCCCHHHEE
59.5829967540
475PhosphorylationDPELAYISSNFITGH
CHHHEEEECCCCCCC
13.4225332170
480PhosphorylationYISSNFITGHGIGKN
EEECCCCCCCCCCCC
20.9825332170
550UbiquitinationYRSYVQSKGRARAPI
HHHHHHCCCCCCCCC
35.0124816145
570UbiquitinationLADTDKIKSFEEDLK
EECHHHHCCHHHHHH
55.6329967540
571PhosphorylationADTDKIKSFEEDLKT
ECHHHHCCHHHHHHH
41.1723898821
577UbiquitinationKSFEEDLKTYKAIEK
CCHHHHHHHHHHHHH
63.2329967540
584AcetylationKTYKAIEKILRNKCS
HHHHHHHHHHHCCCC
40.7125953088
643PhosphorylationRYCARLPSDPFTHLA
HHHHCCCCCCCCCCC
63.6130108239
647PhosphorylationRLPSDPFTHLAPKCR
CCCCCCCCCCCCCCC
22.7429978859
652UbiquitinationPFTHLAPKCRTRELP
CCCCCCCCCCCCCCC
30.64-
654PhosphorylationTHLAPKCRTRELPDG
CCCCCCCCCCCCCCC
42.8315592455
664PhosphorylationELPDGTFYSTLYLPI
CCCCCCEEEEEEEEC
10.6922817900
668PhosphorylationGTFYSTLYLPINSPL
CCEEEEEEEECCCCC
15.55-
819PhosphorylationQIPHFPVYTRSGEVT
CCCCCCCEECCCEEE
9.1819835603
820PhosphorylationIPHFPVYTRSGEVTI
CCCCCCEECCCEEEE
20.7019835603
822PhosphorylationHFPVYTRSGEVTISI
CCCCEECCCEEEEEE
31.3528122231
828PhosphorylationRSGEVTISIELKKSG
CCCEEEEEEEEECCC
10.7219835603
847PhosphorylationLQMLELITRLHQYIF
HHHHHHHHHHHHHHH
39.5423532336
869UbiquitinationKPALEFKPTDADSAY
CCCCCCCCCCCCCCE
40.6124816145
911PhosphorylationEARIGIPSTKYTKET
HCCCCCCCCCCCCCC
35.2926074081
912PhosphorylationARIGIPSTKYTKETP
CCCCCCCCCCCCCCC
23.7926074081
914PhosphorylationIGIPSTKYTKETPFV
CCCCCCCCCCCCCEE
24.1126074081
915PhosphorylationGIPSTKYTKETPFVF
CCCCCCCCCCCCEEE
24.7826074081
946PhosphorylationFDQPHRFYVADVYTD
CCCCCCEEEEEEECC
8.4923403867
951PhosphorylationRFYVADVYTDLTPLS
CEEEEEEECCCCCHH
8.6223403867
952PhosphorylationFYVADVYTDLTPLSK
EEEEEEECCCCCHHH
25.1223403867
955PhosphorylationADVYTDLTPLSKFPS
EEEECCCCCHHHCCC
25.6223403867
958PhosphorylationYTDLTPLSKFPSPEY
ECCCCCHHHCCCCCH
33.1923403867
962PhosphorylationTPLSKFPSPEYETFA
CCHHHCCCCCHHHHH
33.23-
967PhosphorylationFPSPEYETFAEYYKT
CCCCCHHHHHHHHHH
27.52-
972UbiquitinationYETFAEYYKTKYNLD
HHHHHHHHHHHCCCC
12.0421890473
974PhosphorylationTFAEYYKTKYNLDLT
HHHHHHHHHCCCCCC
23.7326074081
976PhosphorylationAEYYKTKYNLDLTNL
HHHHHHHCCCCCCCC
26.6226074081
981PhosphorylationTKYNLDLTNLNQPLL
HHCCCCCCCCCCCCC
37.0126074081
993PhosphorylationPLLDVDHTSSRLNLL
CCCCCCCCHHHHHHC
24.7626074081
994PhosphorylationLLDVDHTSSRLNLLT
CCCCCCCHHHHHHCC
15.2726074081
995PhosphorylationLDVDHTSSRLNLLTP
CCCCCCHHHHHHCCH
41.7826074081
1001PhosphorylationSSRLNLLTPRHLNQK
HHHHHHCCHHHHCCC
22.8023312004
1006PhosphorylationLLTPRHLNQKGKALP
HCCHHHHCCCCCCCC
35.0818669648
1015PhosphorylationKGKALPLSSAEKRKA
CCCCCCCCHHHHHHH
26.0930266825
1016PhosphorylationGKALPLSSAEKRKAK
CCCCCCCHHHHHHHH
48.4030266825
1023UbiquitinationSAEKRKAKWESLQNK
HHHHHHHHHHHHHCC
55.3029967540
1046PhosphorylationAIHPIPASLWRKAVC
HHCCCCHHHHHHHCH
24.1024719451
1091PhosphorylationSLPADFRYPNLDFGW
CCCCCCCCCCCCCCC
9.10-
1111PhosphorylationSKSFISISNSSSAEN
CCCCEEECCCCCCCC
24.7029978859
1113PhosphorylationSFISISNSSSAENDN
CCEEECCCCCCCCCC
20.9129978859
1114PhosphorylationFISISNSSSAENDNY
CEEECCCCCCCCCCC
37.5129978859
1115PhosphorylationISISNSSSAENDNYC
EEECCCCCCCCCCCC
39.1529978859
1121PhosphorylationSSAENDNYCKHSTIV
CCCCCCCCCCCCCCC
13.0229978859
1140PhosphorylationAHQGANRTSSLENHD
HCCCCCCCHHCCCHH
23.6028450419
1141PhosphorylationHQGANRTSSLENHDQ
CCCCCCCHHCCCHHH
29.6828450419
1142PhosphorylationQGANRTSSLENHDQM
CCCCCCHHCCCHHHC
38.8028450419
1149SulfoxidationSLENHDQMSVNCRTL
HCCCHHHCCCCHHHH
6.3421406390
1155PhosphorylationQMSVNCRTLLSESPG
HCCCCHHHHHCCCCC
33.9629396449
1158PhosphorylationVNCRTLLSESPGKLH
CCHHHHHCCCCCCEE
38.8629396449
1160PhosphorylationCRTLLSESPGKLHVE
HHHHHCCCCCCEEEE
35.2619664994
1204PhosphorylationCQGNQLNYYKQEIPV
CCCCCCCEEECCCCC
22.1929978859
1205PhosphorylationQGNQLNYYKQEIPVQ
CCCCCCEEECCCCCC
12.7229978859
1227UbiquitinationQNLYSYENQPQPSDE
EECCCCCCCCCCCCC
51.0724816145
1245PhosphorylationLSNKYLDGNANKSTS
EECCCCCCCCCCCCC
32.3318669648
1250PhosphorylationLDGNANKSTSDGSPV
CCCCCCCCCCCCCCE
32.7125159151
1251PhosphorylationDGNANKSTSDGSPVM
CCCCCCCCCCCCCEE
32.2325159151
1252PhosphorylationGNANKSTSDGSPVMA
CCCCCCCCCCCCEEE
47.2525159151
1255PhosphorylationNKSTSDGSPVMAVMP
CCCCCCCCCEEEECC
21.2225159151
1264PhosphorylationVMAVMPGTTDTIQVL
EEEECCCCCCCHHHH
18.6723663014
1265PhosphorylationMAVMPGTTDTIQVLK
EEECCCCCCCHHHHC
36.7423663014
1267PhosphorylationVMPGTTDTIQVLKGR
ECCCCCCCHHHHCCC
15.9523663014
1280PhosphorylationGRMDSEQSPSIGYSS
CCCCCCCCCCCCCCC
19.3021815630
1282PhosphorylationMDSEQSPSIGYSSRT
CCCCCCCCCCCCCCC
33.6124719451
1317SulfoxidationFNLERLEMLGDSFLK
CCHHHHHHHHHHHHH
6.3221406390
1321PhosphorylationRLEMLGDSFLKHAIT
HHHHHHHHHHHHHHH
30.5824719451
1329PhosphorylationFLKHAITTYLFCTYP
HHHHHHHHHHCCCCC
16.47-
1330PhosphorylationLKHAITTYLFCTYPD
HHHHHHHHHCCCCCC
6.80-
1330UbiquitinationLKHAITTYLFCTYPD
HHHHHHHHHCCCCCC
6.8021890473
1350UbiquitinationLSYMRSKKVSNCNLY
HHHHHCCCCCCCCHH
52.7429967540
1362UbiquitinationNLYRLGKKKGLPSRM
CHHHCCCCCCCCCCE
50.7224816145
1373UbiquitinationPSRMVVSIFDPPVNW
CCCEEEEECCCCCCC
2.8324816145
1391AcetylationGYVVNQDKSNTDKWE
CCCCCCCCCCCCCCC
35.527367815
1403PhosphorylationKWEKDEMTKDCMLAN
CCCHHHHHHHHHHHC
22.9923403867
1417PhosphorylationNGKLDEDYEEEDEEE
CCCCCCCCCCCCHHH
24.1627642862
1433UbiquitinationSLMWRAPKEEADYED
HHHCCCCHHHCCCCC
68.1729967540
1438PhosphorylationAPKEEADYEDDFLEY
CCHHHCCCCCCCHHH
28.4528796482
1445PhosphorylationYEDDFLEYDQEHIRF
CCCCCHHHCHHHHHH
25.6928796482
1460PhosphorylationIDNMLMGSGAFVKKI
HHHHHHCCCCEEEEE
17.0025003641
1465UbiquitinationMGSGAFVKKISLSPF
HCCCCEEEEEECCCC
37.6321890473
1465UbiquitinationMGSGAFVKKISLSPF
HCCCCEEEEEECCCC
37.6321890473
1466UbiquitinationGSGAFVKKISLSPFS
CCCCEEEEEECCCCC
32.0229967540
1468PhosphorylationGAFVKKISLSPFSTT
CCEEEEEECCCCCCC
31.5121945579
1470PhosphorylationFVKKISLSPFSTTDS
EEEEEECCCCCCCCC
19.6721945579
1473PhosphorylationKISLSPFSTTDSAYE
EEECCCCCCCCCCCC
33.5121945579
1474PhosphorylationISLSPFSTTDSAYEW
EECCCCCCCCCCCCC
34.6921945579
1475PhosphorylationSLSPFSTTDSAYEWK
ECCCCCCCCCCCCCC
27.1021945579
1477PhosphorylationSPFSTTDSAYEWKMP
CCCCCCCCCCCCCCC
30.5621945579
1479PhosphorylationFSTTDSAYEWKMPKK
CCCCCCCCCCCCCCC
26.6921945579
1487PhosphorylationEWKMPKKSSLGSMPF
CCCCCCCCCCCCCCC
36.6028102081
1488PhosphorylationWKMPKKSSLGSMPFS
CCCCCCCCCCCCCCC
45.7028102081
1491PhosphorylationPKKSSLGSMPFSSDF
CCCCCCCCCCCCCCC
28.6828102081
1595UbiquitinationLKVLPVIKRTDREKA
CCHHHEECCCCHHHC
49.8629967540
1612PhosphorylationPTRENFNSQQKNLSV
CCCCCCCHHCCCHHH
29.8324719451
1615UbiquitinationENFNSQQKNLSVSCA
CCCCHHCCCHHHHHH
52.8229967540
1618PhosphorylationNSQQKNLSVSCAAAS
CHHCCCHHHHHHHHH
22.7528555341
1625PhosphorylationSVSCAAASVASSRSS
HHHHHHHHHHHCCHH
17.3124719451
1628PhosphorylationCAAASVASSRSSVLK
HHHHHHHHCCHHHCC
24.9124719451
1639PhosphorylationSVLKDSEYGCLKIPP
HHCCCCCCCCCCCCC
19.6627642862
1728PhosphorylationYEDPRQHSPGVLTDL
HCCCCCCCCCHHHHH
18.27-
1731UbiquitinationPRQHSPGVLTDLRSA
CCCCCCCHHHHHHHH
6.2124816145
1792PhosphorylationMDSELRRSEEDEEKE
CCHHHHCCHHHHHHH
38.6128985074
1852PhosphorylationFSANVPRSPVRELLE
HCCCCCCCHHHHHHH
22.9825159151
1860SulfoxidationPVRELLEMEPETAKF
HHHHHHHCCCCCCCC
11.9721406390
1864PhosphorylationLLEMEPETAKFSPAE
HHHCCCCCCCCCCCC
45.9523186163
1866UbiquitinationEMEPETAKFSPAERT
HCCCCCCCCCCCCCC
54.5224816145
1868PhosphorylationEPETAKFSPAERTYD
CCCCCCCCCCCCCCC
23.6121205968
1901AcetylationGRSYRIAKSAAARRA
CHHHHHHHHHHHHHH
37.9525953088
1922PhosphorylationNQPQVPNS-------
CCCCCCCC-------
35.2128985074

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 DICER_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DICER_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 DICER_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AGO1_HUMANAGO1physical
12906857
AGO3_HUMANAGO3physical
12906857
AGO4_HUMANAGO4physical
12906857
PIWL4_HUMANPIWIL4physical
12906857
PIWL3_HUMANPIWIL3physical
12906857
PIWL2_HUMANPIWIL2physical
12906857
AGO2_HUMANAGO2physical
12526743
AGO2_MOUSEAgo2physical
12526743
AGO2_HUMANAGO2physical
14749716
PIWL1_HUMANPIWIL1physical
14749716
GEMI4_HUMANGEMIN4physical
23143396
CACO2_HUMANCALCOCO2physical
23143396
TRBP2_HUMANTARBP2physical
15973356
HDA11_HUMANHDAC11physical
23752268
SMN_HUMANSMN1physical
23752268
DDX20_HUMANDDX20physical
23752268
GEMI4_HUMANGEMIN4physical
23752268
DICER_HUMANDICER1physical
23752268
AAKB2_HUMANPRKAB2physical
21988832
LOX5_HUMANALOX5physical
19022417
AGO1_HUMANAGO1physical
24778252
AGO2_HUMANAGO2physical
24778252
AGO3_HUMANAGO3physical
24778252
MTFR2_HUMANMTFR2physical
24778252
NOG2_HUMANGNL2physical
24778252
NOG1_HUMANGTPBP4physical
24778252
MTFR1_HUMANMTFR1physical
24778252
MYSM1_HUMANMYSM1physical
24778252
NOC3L_HUMANNOC3Lphysical
24778252
POP1_HUMANPOP1physical
24778252
PRKRA_HUMANPRKRAphysical
24778252
STAU2_HUMANSTAU2physical
24778252
TRBP2_HUMANTARBP2physical
24778252

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
601200Pleuropulmonary blastoma (PPB)
138800Goiter multinodular 1, with or without Sertoli-Leydig cell tumors (MNG1)
180295Rhabdomyosarcoma, embryonal, 2 (RMSE2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DICER_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-1016, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-664, AND MASSSPECTROMETRY.

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