DCL1_ARATH - dbPTM
DCL1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCL1_ARATH
UniProt AC Q9SP32
Protein Name Endoribonuclease Dicer homolog 1
Gene Name DCL1
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 1909
Subcellular Localization Nucleus . Localizes to nuclear dicing body (also named D body), a nuclear body distributed throughout the nucleoplasm and involved in miRNA processing.
Protein Description Ribonuclease (RNase) III involved in RNA-mediated post-transcriptional gene silencing (PTGS). Functions in the microRNAs (miRNAs) biogenesis pathway by cleaving primary miRNAs (pri-miRNAs) and precursor miRNAs (pre-miRNAs). Functions with DRB1/HYL1 and SERRATE proteins for accurate pri-miRNAs to miRNAs processing. Indirectly involved in the production of trans-acting small interfering RNAs (ta-siRNAs) derived from the TAS1, TAS2 or TAS3 endogenous transcripts by participating in the production of their initiating miRNAs. Involved in the processing of natural siRNAs (nat-siRNAs, derived from cis-natural antisense transcripts) by cleaving 24 nucleotide nat-siRNAs into 21 nucleotide nat-siRNAs. Can produce RDR6-dependent endogenous ta-siRNAs derived from TAS1 and TAS2. Required for the production of 30-40 nucleotide bacterial-induced long siRNAs (lsiRNA). Acts redundantly with DICER-LIKE 3 (DCL3) to promote flowering via repression of FLOWERING LOCUS C (FLC). Represses antiviral RNA silencing through negative regulation of the expression of DCL4 and DCL3..
Protein Sequence MVMEDEPREATIKPSYWLDACEDISCDLIDDLVSEFDPSSVAVNESTDENGVINDFFGGIDHILDSIKNGGGLPNNGVSDTNSQINEVTVTPQVIAKETVKENGLQKNGGKRDEFSKEEGDKDRKRARVCSYQSERSNLSGRGHVNNSREGDRFMNRKRTRNWDEAGNNKKKRECNNYRRDGRDREVRGYWERDKVGSNELVYRSGTWEADHERDVKKVSGGNRECDVKAEENKSKPEERKEKVVEEQARRYQLDVLEQAKAKNTIAFLETGAGKTLIAILLIKSVHKDLMSQNRKMLSVFLVPKVPLVYQQAEVIRNQTCFQVGHYCGEMGQDFWDSRRWQREFESKQVLVMTAQILLNILRHSIIRMETIDLLILDECHHAVKKHPYSLVMSEFYHTTPKDKRPAIFGMTASPVNLKGVSSQVDCAIKIRNLETKLDSTVCTIKDRKELEKHVPMPSEIVVEYDKAATMWSLHETIKQMIAAVEEAAQASSRKSKWQFMGARDAGAKDELRQVYGVSERTESDGAANLIHKLRAINYTLAELGQWCAYKVGQSFLSALQSDERVNFQVDVKFQESYLSEVVSLLQCELLEGAAAEKVAAEVGKPENGNAHDEMEEGELPDDPVVSGGEHVDEVIGAAVADGKVTPKVQSLIKLLLKYQHTADFRAIVFVERVVAALVLPKVFAELPSLSFIRCASMIGHNNSQEMKSSQMQDTISKFRDGHVTLLVATSVAEEGLDIRQCNVVMRFDLAKTVLAYIQSRGRARKPGSDYILMVERGNVSHAAFLRNARNSEETLRKEAIERTDLSHLKDTSRLISIDAVPGTVYKVEATGAMVSLNSAVGLVHFYCSQLPGDRYAILRPEFSMEKHEKPGGHTEYSCRLQLPCNAPFEILEGPVCSSMRLAQQAVCLAACKKLHEMGAFTDMLLPDKGSGQDAEKADQDDEGEPVPGTARHREFYPEGVADVLKGEWVSSGKEVCESSKLFHLYMYNVRCVDFGSSKDPFLSEVSEFAILFGNELDAEVLSMSMDLYVARAMITKASLAFKGSLDITENQLSSLKKFHVRLMSIVLDVDVEPSTTPWDPAKAYLFVPVTDNTSMEPIKGINWELVEKITKTTAWDNPLQRARPDVYLGTNERTLGGDRREYGFGKLRHNIVFGQKSHPTYGIRGAVASFDVVRASGLLPVRDAFEKEVEEDLSKGKLMMADGCMVAEDLIGKIVTAAHSGKRFYVDSICYDMSAETSFPRKEGYLGPLEYNTYADYYKQKYGVDLNCKQQPLIKGRGVSYCKNLLSPRFEQSGESETVLDKTYYVFLPPELCVVHPLSGSLIRGAQRLPSIMRRVESMLLAVQLKNLISYPIPTSKILEALTAASCQETFCYERAELLGDAYLKWVVSRFLFLKYPQKHEGQLTRMRQQMVSNMVLYQFALVKGLQSYIQADRFAPSRWSAPGVPPVFDEDTKDGGSSFFDEEQKPVSEENSDVFEDGEMEDGELEGDLSSYRVLSSKTLADVVEALIGVYYVEGGKIAANHLMKWIGIHVEDDPDEVDGTLKNVNVPESVLKSIDFVGLERALKYEFKEKGLLVEAITHASRPSSGVSCYQRLEFVGDAVLDHLITRHLFFTYTSLPPGRLTDLRAAAVNNENFARVAVKHKLHLYLRHGSSALEKQIREFVKEVQTESSKPGFNSFGLGDCKAPKVLGDIVESIAGAIFLDSGKDTTAAWKVFQPLLQPMVTPETLPMHPVRELQERCQQQAEGLEYKASRSGNTATVEVFIDGVQVGVAQNPQKKMAQKLAARNALAALKEKEIAESKEKHINNGNAGEDQGENENGNKKNGHQPFTRQTLNDICLRKNWPMPSYRCVKEGGPAHAKRFTFGVRVNTSDRGWTDECIGEPMPSVKKAKDSAAVLLLELLNKTFS
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
646PhosphorylationAVADGKVTPKVQSLI
HHCCCCCCHHHHHHH
22.3724243849
651PhosphorylationKVTPKVQSLIKLLLK
CCCHHHHHHHHHHHH
34.7424243849
1397PhosphorylationSRFLFLKYPQKHEGQ
HHHHHHHCCCHHHCH
17.0319880383
1501PhosphorylationYRVLSSKTLADVVEA
HHHCCCHHHHHHHHH
29.1828295753
1513PhosphorylationVEALIGVYYVEGGKI
HHHHHCCEEEECCEE
9.1528295753
1514PhosphorylationEALIGVYYVEGGKIA
HHHHCCEEEECCEEE
6.9328295753
1552PhosphorylationKNVNVPESVLKSIDF
ECCCCCHHHHHHCCC
27.0424894044
1849PhosphorylationRKNWPMPSYRCVKEG
HCCCCCCCCCCCCCC
20.9619880383

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 DCL1_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCL1_ARATH !!

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 DCL1_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DRB1_ARATHHYL1physical
17442570
DCL1_ARATHDCL1physical
17442570
DRB1_ARATHHYL1physical
16428603
DRB1_ARATHHYL1physical
20106953
DDL_ARATHDDLphysical
23313986
VIP2_ARATHVIP2physical
23424246
DCL1_ARATHDCL1physical
23886622
DRB1_ARATHHYL1physical
23886622
SRRT_ARATHSEphysical
23886622
HEN1_ARATHHEN1physical
25680966
PRL1_ARATHPRL1physical
25474114

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DCL1_ARATH

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Related Literatures of Post-Translational Modification

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