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JobID 15120800031 (slimprob) Finished.
IP:129.94.133.155
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slimprob&uniprotid=E1A_ADE02&motifs=LxCxE,PxDLS
Run Started: 2015-12-08 22:35:32; PID=38726
Run finished: 2015-12-08 22:36:36
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###~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~###
# OUTFMT:
...
Outputs available:
main
= main results file (
[extras=-1]{cmd:extras}
)
motifs
= Input motifs for searching (
[extras=-1]{cmd:extras}
)
seqin
= Input file (
[extras=-1]{cmd:extras}
)
occ
= occurrence file (
[extras=0]{cmd:extras}
)
upc
= UPC file (
[extras=0]{cmd:extras}
)
slimdb
= Fasta file used for UPC generation etc. (
[extras=0]{cmd:extras}
)
masked
= masked.fas (
[extras=1]{cmd:extras}
)
mapping
= mapping.fas file (
[extras=2]{cmd:extras}
)
motifaln
= motif alignments (
[extras=2]{cmd:extras}
)
maskaln
= masked motif alignments (
[extras=2]{cmd:extras}
)
dismatrix
= *.dis.tdt file (
[extras=3]{cmd:extras}
)
&rest=OUTFMT
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Dataset |
RunID |
Masking |
RunTime |
SeqNum |
UPNum |
AANum |
Motif |
Pattern |
IC |
N_Occ |
E_Occ |
p_Occ |
pUnd_Occ |
N_Seq |
E_Seq |
p_Seq |
pUnd_Seq |
N_UPC |
E_UPC |
p_UPC |
pUnd_UPC |
slimprob |
15120800031 |
FreqNoMask |
00:00:00 |
1 |
1 |
289 |
LxCxE |
L.C.E |
3.0 |
1 |
0.11 |
0.10 |
0.99 |
1 |
0.10 |
0.10 |
1.00 |
1 |
0.10 |
0.10 |
1.00 |
slimprob |
15120800031 |
FreqNoMask |
00:00:00 |
1 |
1 |
289 |
PxDLS |
P.DLS |
4.0 |
1 |
0.017 |
0.017 |
1.00 |
1 |
0.017 |
0.017 |
1.00 |
1 |
0.017 |
0.017 |
1.00 |
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Dataset |
RunID |
Masking |
Motif |
Seq |
Start_Pos |
End_Pos |
Prot_Len |
Pattern |
Match |
Variant |
MisMatch |
Desc |
UPC |
slimprob |
15120800031 |
FreqNoMask |
LxCxE |
E1A_ADE02__P03254 |
122 |
126 |
289 |
L.C.E |
LTCHE |
L.C.E |
0 |
RecName: Full=Early E1A protein {ECO:0000305}; AltName: Full=Early E1A 32 kDa protein; |
1 |
slimprob |
15120800031 |
FreqNoMask |
PxDLS |
E1A_ADE02__P03254 |
279 |
283 |
289 |
P.DLS |
PLDLS |
P.DLS |
0 |
RecName: Full=Early E1A protein {ECO:0000305}; AltName: Full=Early E1A 32 kDa protein; |
1 |
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#slimprob# 1 Seq; 1 UPC; 1.000 MST; Single sequence
UP N MST Seqs
1 1 1.000 E1A_ADE02__P03254
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LxCxE
PxDLS
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ID E1A_ADE02 Reviewed; 289 AA.
AC P03254; P24934; Q67788;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 11-NOV-2015, entry version 96.
DE RecName: Full=Early E1A protein {ECO:0000305};
DE AltName: Full=Early E1A 32 kDa protein;
OS Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2).
OC Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=10515;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS EARLY E1A 32 KDA PROTEIN
RP AND EARLY E1A 26 KDA PROTEIN).
RX PubMed=551290; DOI=10.1038/281694a0;
RA Perricaudet M., Akusjaervi G., Virtanen A., Pettersson U.;
RT "Structure of two spliced mRNAs from the transforming region of human
RT subgroup C adenoviruses.";
RL Nature 281:694-696(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS EARLY E1A 32 KDA PROTEIN;
RP EARLY E1A 26 KDA PROTEIN AND EARLY E1A 6 KDA PROTEIN).
RX PubMed=7142161;
RA Gingeras T.R., Sciaky D., Gelinas R.E., Bing-Dong J., Yen C.E.,
RA Kelly M.M., Bullock P.A., Parsons B.L., O'Neill K.E., Roberts R.J.;
RT "Nucleotide sequences from the adenovirus-2 genome.";
RL J. Biol. Chem. 257:13475-13491(1982).
RN [3]
RP INTERACTION WITH HOST ATF7, AND MUTAGENESIS OF CYS-157; THR-178 AND
RP SER-185.
RX PubMed=8417352;
RA Chatton B., Bocco J.L., Gaire M., Hauss C., Reimund B., Goetz J.,
RA Kedinger C.;
RT "Transcriptional activation by the adenovirus larger E1a product is
RT mediated by members of the cellular transcription factor ATF family
RT which can directly associate with E1a.";
RL Mol. Cell. Biol. 13:561-570(1993).
CC -!- FUNCTION: Plays a role in viral genome replication by driving
CC entry of quiescent cells into the cell cycle. Stimulation of
CC progression from G1 to S phase allows the virus to efficiently use
CC the cellular DNA replicating machinery to achieve viral genome
CC replication. E1A protein has both transforming and trans-
CC activating activities. Induces the disassembly of the E2F1
CC transcription factor from RB1 by direct competition for the same
CC binding site on RB1, with subsequent transcriptional activation of
CC E2F1-regulated S-phase genes and of the E2 region of the
CC adenoviral genome. Release of E2F1 leads to the ARF-mediated
CC inhibition of MDM2 and causes TP53/p53 to accumulate because it is
CC not targeted for degradation by MDM2-mediated ubiquitination
CC anymore. This increase in TP53, in turn, would arrest the cell
CC proliferation and direct its death but this effect is counteracted
CC by the viral protein E1B-55K. Inactivation of the ability of RB1
CC to arrest the cell cycle is critical for cellular transformation,
CC uncontrolled cellular growth and proliferation induced by viral
CC infection. Interaction with RBX1 and CUL1 inhibits ubiquitination
CC of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex,
CC and may be linked to unregulated host cell proliferation. The
CC tumorigenesis-restraining activity of E1A may be related to the
CC disruption of the host CtBP-CtIP complex through the CtBP binding
CC motif. Interacts with host TBP protein; this interaction probably
CC disrupts the TBP-TATA complex. {ECO:0000250|UniProtKB:P03255}.
CC -!- SUBUNIT: Interacts with host UBE2I; this interaction interferes
CC with polySUMOylation. Interacts with host RB1; this interaction
CC induces the aberrant dissociation of RB1-E2F1 complex thereby
CC disrupting the activity of RB1 and activating E2F1-regulated
CC genes. Interacts with host ATF7; the interaction enhances ATF7-
CC mediated viral transactivation activity which requires the zinc
CC binding domains of both proteins. Isoform early E1A 32 kDa protein
CC and isoform early E1A 26 kDa protein interact (via N-terminus)
CC with CUL1 and E3 ubiquitin ligase RBX1; these interactions inhibit
CC RBX1-CUL1-dependent elongation reaction of ubiquitin chains and
CC attenuate ubiquitination of SCF(FBXW7) target proteins. Interacts
CC (via PXLXP motif) with host ZMYND11/BS69 (via MYND-type zinc
CC finger); this interaction inhibits E1A mediated transactivation.
CC Interacts with host EP300; this interaction stimulates the
CC acetylation of RB1 by recruiting EP300 and RB1 into a multimeric-
CC protein complex. Interacts with host CTBP1 and CTBP2; this
CC interaction seems to potentiate viral replication. Interacts with
CC host DCAF7. Interacts with host DYRK1A. Interacts with host KPNA4;
CC this interaction allows E1A import into the host nucleus.
CC Interacts with host EP400; this interaction stabilizes MYC.
CC {ECO:0000250|UniProtKB:P03255}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Isoforms are derived from the E1 region of the genome.;
CC Name=early E1A 32 kDa protein; Synonyms=289R, L-E1A;
CC IsoId=P03254-1; Sequence=Displayed;
CC Name=early E1A 26 kDa protein; Synonyms=243R, S-E1A;
CC IsoId=P03254-2; Sequence=VSP_000197;
CC Name=early E1A 6 kDa protein;
CC IsoId=P03254-3; Sequence=VSP_028916, VSP_028917;
CC -!- SIMILARITY: Belongs to the adenoviridae E1A protein family.
CC {ECO:0000305}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; J01917; AAA92197.1; -; Genomic_DNA.
DR EMBL; J01917; AAA92198.1; -; Genomic_DNA.
DR EMBL; J01917; AAA92199.1; -; Genomic_DNA.
DR PIR; A03824; Q2AD2.
DR RefSeq; AP_000161.1; AC_000007.1.
DR DIP; DIP-570N; -.
DR IntAct; P03254; 1.
DR MINT; MINT-198575; -.
DR Proteomes; UP000008167; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0039695; P:DNA-templated viral transcription; IDA:UniProtKB.
DR GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR GO; GO:0039649; P:modulation by virus of host ubiquitin-protein ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR014410; Aden_E1A.
DR Pfam; PF02703; Adeno_E1A; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Complete proteome; Early protein;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host transcription shutoff by virus;
KW G1/S host cell cycle checkpoint dysregulation by virus;
KW Host gene expression shutoff by virus; Host nucleus;
KW Host-virus interaction;
KW Inhibition of eukaryotic host transcription initiation by virus;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host STAT1 by virus; Metal-binding;
KW Modulation of host cell cycle by virus;
KW Modulation of host E3 ubiquitin ligases by virus;
KW Modulation of host ubiquitin pathway by virus; Oncogene;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Viral immunoevasion; Zinc; Zinc-finger.
FT CHAIN 1 289 Early E1A protein.
FT /FTId=PRO_0000221692.
FT ZN_FING 154 174 {ECO:0000250|UniProtKB:P03255}.
FT REGION 41 49 Interaction with RB1 in competition with
FT E2F1. {ECO:0000250}.
FT REGION 76 140 Interaction with UBE2I. {ECO:0000250}.
FT MOTIF 113 117 PXLXP motif, interaction with host
FT ZMYND11. {ECO:0000250}.
FT MOTIF 122 126 LXCXE motif, interaction with host RB1.
FT {ECO:0000255}.
FT MOTIF 258 289 Bipartite nuclear localization signal.
FT {ECO:0000250|UniProtKB:P03255,
FT ECO:0000255}.
FT MOTIF 279 283 PXDLS motif, CTBP-binding.
FT {ECO:0000250|UniProtKB:P03255}.
FT MOD_RES 89 89 Phosphoserine; by host. {ECO:0000250}.
FT MOD_RES 219 219 Phosphoserine; by host. {ECO:0000250}.
FT MOD_RES 231 231 Phosphoserine; by host. {ECO:0000250}.
FT VAR_SEQ 29 55 ADNLPPPSHFEPPTLHELYDLDVTAPE -> CLNLSLSPSQ
FT NRSLQDLPGVLNWCLLS (in isoform early E1A 6
FT kDa protein). {ECO:0000305}.
FT /FTId=VSP_028916.
FT VAR_SEQ 56 289 Missing (in isoform early E1A 6 kDa
FT protein). {ECO:0000305}.
FT /FTId=VSP_028917.
FT VAR_SEQ 140 185 Missing (in isoform early E1A 26 kDa
FT protein). {ECO:0000305}.
FT /FTId=VSP_000197.
FT MUTAGEN 157 157 C->S: Abolishes ATF7-mediated
FT transcriptional activation.
FT {ECO:0000269|PubMed:8417352}.
FT MUTAGEN 178 178 T->P: No effect on ATF7-mediated
FT transcriptional activation.
FT {ECO:0000269|PubMed:8417352}.
FT MUTAGEN 185 185 S->R: Abolishes ATF7-mediated
FT transcriptional activation.
FT {ECO:0000269|PubMed:8417352}.
FT CONFLICT 68 68 D -> E (in Ref. 2; AAA92197/AAA92199).
FT {ECO:0000305}.
FT CONFLICT 81 81 L -> F (in Ref. 2; AAA92197/AAA92199).
FT {ECO:0000305}.
SQ SEQUENCE 289 AA; 31851 MW; 4264747DAD74FFC5 CRC64;
MRHIICHGGV ITEEMAASLL DQLIEEVLAD NLPPPSHFEP PTLHELYDLD VTAPEDPNEE
AVSQIFPDSV MLAVQEGIDL LTFPPAPGSP EPPHLSRQPE QPEQRALGPV SMPNLVPEVI
DLTCHEAGFP PSDDEDEEGE EFVLDYVEHP GHGCRSCHYH RRNTGDPDIM CSLCYMRTCG
MFVYSPVSEP EPEPEPEPEP ARPTRRPKLV PAILRRPTSP VSRECNSSTD SCDSGPSNTP
PEIHPVVPLC PIKPVAVRVG GRRQAVECIE DLLNESGQPL DLSCKRPRP
//
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#~~# |
#~+~~+~# |
#~~# |
#LOG |
00:00:00 |
Activity Log for SLiMSuite V1.5.2: Tue Dec 8 22:35:32 2015 |
#DIR |
00:00:00 |
Run from directory: /srv/slimsuite/logs/prod |
#ARG |
00:00:00 |
Commandline arguments: run ip=129.94.133.155 slimprob&uniprotid=E1A_ADE02&motifs=LxCxE,PxDLS&jobid=15120800031 |
#VIO |
00:00:00 |
Verbosity: -1; Interactivity: -1. |
#PROG |
00:00:00 |
SLiMProb V2.2.5: Short Linear Motif Probability tool |
#CMD |
00:00:00 |
Full SLiMProb CmdList: proglog=F iucut=0.2 usegopher=T protscores=T megablam=F orthdb=qfo_ref.2015-04.Eukaryota.fas sourcedate=2015-04-15 walltime=0 runid=15120800031 rest=format uniprotid=E1A_ADE02 motifs=LxCxE,PxDLS jobid=15120800031 resfile=slimprob.csv savespace=0 targz=F megaslim=seqin basefile=slimprob |
#DB |
00:00:00 |
/srv/slimsuite/data/orthdb/qfo_ref.2015-04/qfo_ref.2015-04.Eukaryota.fas already formatted. (Force = False). |
#DB |
00:00:00 |
/srv/slimsuite/data/orthdb/qfo_ref.2015-04/qfo_ref.2015-04.Eukaryota.fas already formatted. (Force = False). |
#MOT |
00:00:00 |
2 motifs read from LxCxE,PxDLS (2 lines): 2 retained. |
#ALPH |
00:00:00 |
Alphabet: A C D E F G H I K L M N P Q R S T V W Y |
#URL |
00:01:04 |
Extracting 1 AccNum from http://www.uniprot.org/uniprot/: 1 read, 1 extracted; 0 failed; 0 duplicates. |
#DAT |
00:01:04 |
Extracting entries from slimprob.dat: 1 read, 1 extracted. |
#SEQ |
00:01:04 |
1 sequences loaded from /srv/slimsuite/scratch/prod/slimprob/15120800031/slimprob.dat (Format: uniprot). |
#FAS |
00:01:04 |
1 Sequences output to /srv/slimsuite/scratch/prod/slimprob/15120800031/slimprob.fas. |
#UPC |
00:01:04 |
No UPC file found. |
#UP |
00:01:04 |
slimprob: 1 Seq; 1 UPC; 1.000 MST; Single sequence |
#FTMASK |
00:01:04 |
FTMask: None |
#SEARCH |
00:01:04 |
1 sequences searched for 2 motifs: 2 occ. |
#SAVE |
00:01:04 |
SLiMProb Intermediate saved as /srv/slimsuite/scratch/prod/slimprob/15120800031/slimprob.Commandline.FreqNoMask.pickle (Python pickle). |
#GZIP |
00:01:04 |
/srv/slimsuite/scratch/prod/slimprob/15120800031/slimprob.Commandline.FreqNoMask.pickle zipped. |
#OCC |
00:01:04 |
Processing 2 occurrences complete. |
#PROB |
00:01:04 |
Calculating SLiM Probabilities complete. |
#COMB |
00:01:04 |
Combined Occurrence Attributes complete. |
#OUT |
00:01:04 |
Summary data for slimprob saved to /srv/slimsuite/scratch/prod/slimprob/15120800031/slimprob.csv |
#RES |
00:01:04 |
SLiMProb results output to /srv/slimsuite/scratch/prod/slimprob/15120800031/slimprob.(occ.)csv and /srv/slimsuite/scratch/prod/slimprob/15120800031/slimprob.* |
#LOG |
00:01:04 |
SLiMProb V2.2.5 End: Tue Dec 8 22:36:36 2015 |
#JOBID |
00:01:04 |
15120800031 |
#REST |
00:01:04 |
URL for future retrieval: http://rest.slimsuite.unsw.edu.au/retrieve&jobid=15120800031&rest=format&password=None |
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