※ dbPPT Protein Information

TagContent
UniProt Accession
Theoretical PI
8.41 
Molecular Weight
81097.88 
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Serrate RNA effector molecule 
Gene Name
SE; At2g27100; T20P8.15 
Created Date
2009-09-22 
Organism
Arabidopsis thaliana(Mouse-ear cress) 
NCBI Taxa ID
3702 
Phosphorylation Sites
Position
Peptide
Source
References
21
NRLPEKSTSSSPPPP
dbPPT, P3DB, PhosPhAt
[1, 10, 14, 15, 2, 4, 9]
22
RLPEKSTSSSPPPPP
dbPPT, P3DB, PhosPhAt
[1, 11, 14, 15, 2, 4, 9]
90
RDYKRRPSLSPPPPY
dbPPT, P3DB, PhosPhAt
[1, 10, 11, 14, 2, 4, 5, 6, 7, 9]
701
QDPRRLRSYQDLDAP
dbPPT, P3DB, PhosPhAt
[10]
92
YKRRPSLSPPPPYRD
dbPPT, P3DB, PhosPhAt
[1, 10, 11, 14, 2, 4, 5, 6, 7, 9]
31
SPPPPPPSSSLPQQE
dbPPT, P3DB, PhosPhAt
[10, 11, 14, 15, 4]
23
LPEKSTSSSPPPPPP
dbPPT, P3DB, PhosPhAt
[1, 10, 11, 14, 15, 2, 3, 4, 8, 9]
299
GRTSEPNSEDEAAGV
dbPPT, P3DB, PhosPhAt
[1, 10, 11, 14, 4, 5, 6, 7, 8, 9]
76
NRRERDRSPLPPPRR
dbPPT, P3DB, PhosPhAt
[1, 10, 11, 13, 14, 4, 5, 6, 9]
295
LNKSGRTSEPNSEDE
dbPPT, P3DB, PhosPhAt
[1, 10, 11, 14, 4, 5, 8, 9]
689
GPAPFLLSPAFRQDP
dbPPT, P3DB, PhosPhAt
[1, 12, 14, 8]
291
AVTALNKSGRTSEPN
dbPPT, P3DB, PhosPhAt
[1, 10, 14, 4, 5, 7]
20
DNRLPEKSTSSSPPP
dbPPT, P3DB, PhosPhAt
[1, 10, 11, 14, 15, 2, 4, 9]
33
PPPPPSSSLPQQEQE
dbPPT, P3DB, PhosPhAt
[11, 14, 15, 4]
97
SLSPPPPYRDRRHSP
dbPPT, P3DB, PhosPhAt
[1, 11, 14, 5, 9]
294
ALNKSGRTSEPNSED
dbPPT, P3DB, PhosPhAt
[1, 10, 14, 4, 5, 6, 8, 9]
32
PPPPPPSSSLPQQEQ
dbPPT, P3DB, PhosPhAt
[14, 4]
24
PEKSTSSSPPPPPPS
dbPPT, P3DB, PhosPhAt
[1, 11, 14, 15, 2, 3, 4, 8, 9]
Functional 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. 
Sequence Annotation
chain 1 720 Serrate RNA effector molecule
zinc finger region 498 523 C2H2-type
compositionally biased region 25 111 Pro-rich
compositionally biased region 121 182 Gly-rich
compositionally biased region 562 598 Arg-rich
compositionally biased region 629 690 Pro-rich
modified residue 76 Phosphoserine
modified residue 90 Phosphoserine
modified residue 92 Phosphoserine
modified residue 689 Phosphoserine
helix 198 201
helix 202 204
turn 205 207
helix 211 237
helix 241 247
helix 249 275
strand 283 286
helix 331 333
helix 336 357
strand 386 388
strand 395 397
helix 400 414
helix 418 420
helix 446 460
helix 464 469
helix 471 482
helix 483 485
strand 486 490
strand 492 500
strand 502 504
strand 508 511
helix 512 522
helix 524 543
Keyword
3D-structure,Complete proteome,Metal-binding,mRNA processing,mRNA splicing,Nucleus,Phosphoprotein,Reference proteome,RNA-mediated gene silencing,Zinc,Zinc-finger 
Sequence Source
UniProt 
Protein Sequence
MADVNLPPSD SVDNRLPEKS TSSSPPPPPP SSSLPQQEQE QDQQQLPLRR ERDSRERRDE 60
RDIERPPPNR RERDRSPLPP PRRDYKRRPS LSPPPPYRDR RHSPPQRRSP PQKRYRRDDN 120
GYDGRRGSPR GGYGPPDRRF GYDHGGGYDR EMGGRPGYGD ERPHGRFMGR YQDWEGGRGG 180
YGDASNSGNP QRDGLMSYKQ FIQELEDDIL PSEAERRYQE YKSEYITTQK RAFFNTHKEE 240
DWLKNKYHPT NLLSVIERRN DLAQKVAKDF LLDLQSGTLD LGPAVTALNK SGRTSEPNSE 300
DEAAGVGKRK RHGMGGAKEN ELLSAAPKAP SFTSDPKRIL TDVEQTQALV RKLDSEKKIE 360
ENVLQGSETE KSGREKLHSG STGPVVIIRG LTSVKGLEGV ELLDTLVTYL WRVHGLDYYG 420
KVETNEAKGL RHVRAEGKVS DAKGDENESK FDSHWQERLK GQDPLEVMAA KEKIDAAATE 480
ALDPHVRKIR DEKYGWKYGC GAKGCTKLFH AAEFVYKHLK LKHTELVTEL TTKVREELYF 540
QNYMNDPNAP GGQPATQQSG PRDRPIRRKP SMENRLRDDR GGRRERDGRA NGNDRNDRSE 600
DQQRGDNDGG NPGEVGYDAF GGQGGVHVPP FLSDINPPPM LMPVPGAGPL GPFVPAPPEV 660
AMQMFRDPSG PNPPFEGSGR GGPAPFLLSP AFRQDPRRLR SYQDLDAPEE EVTVIDYRSL 720
 
Gene Ontology
GO:0009507; C: chloroplast; IDA: TAIR
GO:0005829; C: cytosol; IDA: TAIR
GO:0010445; C: nuclear dicing body; IDA: UniProtKB
GO:0016607; C: nuclear speck; IDA: TAIR
GO:0005730; C: nucleolus; IDA: TAIR
GO:0005634; C: nucleus; IDA: TAIR
GO:0003677; F: DNA binding; ISS: TAIR
GO:0046872; F: metal ion binding; IEA: UniProtKB-KW
GO:0005515; F: protein binding; IPI: UniProtKB
GO:0003700; F: sequence-specific DNA binding transcription factor activity; ISS: TAIR
GO:0016568; P: chromatin modification; TAS: TAIR
GO:0006397; P: mRNA processing; IEA: UniProtKB-KW
GO:0031053; P: primary miRNA processing; IMP: UniProtKB
GO:0010267; P: production of ta-siRNAs involved in RNA interference; IMP: TAIR
GO:2000011; P: regulation of adaxial/abaxial pattern formation; IMP: TAIR
GO:0048509; P: regulation of meristem development; IMP: TAIR
GO:0006355; P: regulation of transcription, DNA-templated; TAS: TAIR
GO:0008380; P: RNA splicing; IMP: UniProtKB
GO:0048367; P: shoot system development; IMP: TAIR 
Interpro
InterPro; IPR007042; Arsenite-R_2
InterPro; IPR021933; DUF3546
InterPro; IPR007087; Znf_C2H2
InterPro; IPR015880; Znf_C2H2-like
Pfam
Pfam; PF04959; ARS2
Pfam; PF12066; DUF3546 
SMART
SMART; SM00355; ZnF_C2H2 
PROSITE
PS00028; ZINC_FINGER_C2H2_1 
PRINTS