SRRT_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SRRT_ARATH
• UniProt AC: Q9ZVD0
• Protein Name: Serrate RNA effector molecule
• Gene Name: SE
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 720
• Subcellular Localization: Nucleus . Nucleus speckle . Localizes to nuclear dicing body (also named D body), a nuclear body distributed throughout the nucleoplasm involved in miRNA processing.
• Protein Description: Acts as a mediator between the cap-binding complex (CBC) and both the pre-mRNA splicing and primary microRNAs (miRNAs) processing machinery. Required for proper processing of primary miRNAs to miRNAs, thereby playing a role in RNA-mediated gene silencing (RNAi) by miRNAs. Does not participate in sense post-transcriptional gene silencing. Acts as a regulator of meristem activity and adaxial leaf fate via the miRNA gene-silencing pathway by regulating the expression of PHB and by limiting the competence of shoot tissue to respond to KNOX expression. Its function is however not limited to miRNA-mediated repression of leaf polarity genes, but rather acts as a general regulator of primary microRNAs processing. Also critical for the accumulation of the trans-acting small interfering RNA (ta-siRNA). Required for pre-mRNA splicing..
• Protein Sequence: MADVNLPPSDSVDNRLPEKSTSSSPPPPPPSSSLPQQEQEQDQQQLPLRRERDSRERRDERDIERPPPNRRERDRSPLPPPRRDYKRRPSLSPPPPYRDRRHSPPQRRSPPQKRYRRDDNGYDGRRGSPRGGYGPPDRRFGYDHGGGYDREMGGRPGYGDERPHGRFMGRYQDWEGGRGGYGDASNSGNPQRDGLMSYKQFIQELEDDILPSEAERRYQEYKSEYITTQKRAFFNTHKEEDWLKNKYHPTNLLSVIERRNDLAQKVAKDFLLDLQSGTLDLGPAVTALNKSGRTSEPNSEDEAAGVGKRKRHGMGGAKENELLSAAPKAPSFTSDPKRILTDVEQTQALVRKLDSEKKIEENVLQGSETEKSGREKLHSGSTGPVVIIRGLTSVKGLEGVELLDTLVTYLWRVHGLDYYGKVETNEAKGLRHVRAEGKVSDAKGDENESKFDSHWQERLKGQDPLEVMAAKEKIDAAATEALDPHVRKIRDEKYGWKYGCGAKGCTKLFHAAEFVYKHLKLKHTELVTELTTKVREELYFQNYMNDPNAPGGQPATQQSGPRDRPIRRKPSMENRLRDDRGGRRERDGRANGNDRNDRSEDQQRGDNDGGNPGEVGYDAFGGQGGVHVPPFLSDINPPPMLMPVPGAGPLGPFVPAPPEVAMQMFRDPSGPNPPFEGSGRGGPAPFLLSPAFRQDPRRLRSYQDLDAPEEEVTVIDYRSL

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
20	Phosphorylation	DNRLPEKSTSSSPPP CCCCCCCCCCCCCCC	31.68	23776212
21	Phosphorylation	NRLPEKSTSSSPPPP CCCCCCCCCCCCCCC	43.63	23776212
22	Phosphorylation	RLPEKSTSSSPPPPP CCCCCCCCCCCCCCC	35.59	23776212
23	Phosphorylation	LPEKSTSSSPPPPPP CCCCCCCCCCCCCCC	47.13	24601666
24	Phosphorylation	PEKSTSSSPPPPPPS CCCCCCCCCCCCCCC	40.99	24601666
31	Phosphorylation	SPPPPPPSSSLPQQE CCCCCCCCCCCCHHH	38.03	23776212
32	Phosphorylation	PPPPPPSSSLPQQEQ CCCCCCCCCCCHHHH	41.49	23776212
33	Phosphorylation	PPPPPSSSLPQQEQE CCCCCCCCCCHHHHH	48.70	23776212
76	Phosphorylation	NRRERDRSPLPPPRR CCCCCCCCCCCCCCC	34.77	30291188
90	Phosphorylation	RDYKRRPSLSPPPPY CCCCCCCCCCCCCCC	39.40	30291188
92	Phosphorylation	YKRRPSLSPPPPYRD CCCCCCCCCCCCCCC	39.43	30291188
97	Phosphorylation	SLSPPPPYRDRRHSP CCCCCCCCCCCCCCC	30.80	23776212
103	Phosphorylation	PYRDRRHSPPQRRSP CCCCCCCCCCCCCCC	36.14	29654922
291	Phosphorylation	AVTALNKSGRTSEPN HHHHHCCCCCCCCCC	32.22	23776212
294	Phosphorylation	ALNKSGRTSEPNSED HHCCCCCCCCCCCHH	40.75	19880383
295	Phosphorylation	LNKSGRTSEPNSEDE HCCCCCCCCCCCHHH	50.09	19880383
299	Phosphorylation	GRTSEPNSEDEAAGV CCCCCCCCHHHHCCC	58.08	30291188
571	Phosphorylation	RPIRRKPSMENRLRD CCCCCCCHHHHHCCC	41.59	27531888
689	Phosphorylation	GPAPFLLSPAFRQDP CCCCCCCCHHHHCCH	19.14	23172892
701	Phosphorylation	QDPRRLRSYQDLDAP CCHHHHHCCCCCCCC	31.57	23111157

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SRRT_ARATH !!

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SRRT_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRRT_ARATH	SE	physical	17442570
DCL1_ARATH	DCL1	physical	17442570
DRB1_ARATH	HYL1	physical	17442570
DRB1_ARATH	HYL1	physical	16889646
VIP2_ARATH	VIP2	physical	23424246
DCL1_ARATH	DCL1	physical	23921632
GBLPA_ARATH	ATARCA	physical	23941160
GPLPC_ARATH	RACK1C_AT	physical	23941160
GPLPB_ARATH	RACK1B_AT	physical	23941160
NCBP2_ARATH	CBP20	physical	24137006
NCBP1_ARATH	ABH1	physical	24137006
DRB1_ARATH	HYL1	physical	23141542
PRL1_ARATH	PRL1	physical	25474114

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-90; SER-92;THR-294 AND SER-299, AND MASS SPECTROMETRY.
PubMed: 19376835

"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana.";
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.;
J. Proteomics 72:439-451(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689, SUBCELLULARLOCATION, AND MASS SPECTROMETRY.
PubMed: 19245862

"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis.";
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.;
J. Proteome Res. 7:2458-2470(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND SER-92, AND MASSSPECTROMETRY.
PubMed: 18433157