ELM   Currently 128 Elms in ELM database.

o Summary of features reported by ELM. (Mouseover the matches for details.)

MOD_CDKLIG_SH3_1LIG_TRAF2_1LIG_CYCLIN_1MOD_GSK3_1LIG_APCC_Dbox_1MOD_CK1_1LIG_MAPK_1MOD_PLKLIG_14-3-3_3LIG_SH2_STAT5 LIG_EH1LIG_FHA_1Submit to SmartSubmit to PfamMOD_ProDKin_1MOD_PKA_1MOD_PKA_2MOD_CK2_1LIG_SH3_3MOD_PIKK_1Submit to GlobPlotLIG_PDZ_3LIG_WW_4LIG_BRCT_BRCA1_1HelpHelpHelpHelpHelpHelpHelpHelpHelpHelpHelpMOD_CDK: [118,124] QRQTPKKLIG_SH3_1: [229,235] KSRPGSPLIG_TRAF2_1: [11,14] PGEELIG_TRAF2_1: [87,90] ALEELIG_CYCLIN_1: [31,35] KPLTPLIG_CYCLIN_1: [76,79] RALLLIG_CYCLIN_1: [97,101] KGLEVLIG_CYCLIN_1: [143,146] RFLY
[148,152] KYLSPLIG_CYCLIN_1: [195,199] KKLGPMOD_GSK3_1: [43,50] NKPSVRRSMOD_GSK3_1: [227,234] RAKSRPGSMOD_GSK3_1: [262,269] PASSQDCSLIG_APCC_Dbox_1: [16,21] RRSPLDLIG_APCC_Dbox_1: [75,80] GRALLSLIG_APCC_Dbox_1: [176,181] RRAKLKMOD_CK1_1: [80,86] SQTSPLCMOD_CK1_1: [215,221] SEATAGGMOD_CK1_1: [253,259] SPASPLT
[256,262] SPLTDQPLIG_MAPK_1: [94,103] KTFKGLEVSVMOD_PLK: [99,105] LEVSVLQMOD_PLK: [215,221] SEATAGGLIG_14-3-3_3: [127,132] KSRTAFLIG_14-3-3_3: [227,232] RAKSRPLIG_SH2_STAT5: [149,152] YLSPLIG_EH1: [35,43] PFSIEDILNLIG_FHA_1: [80,86] SQTSPLCSmart: low_complexity_region: 
[56,67] AAHLLAAADKHASmart: HOX: 
[125,187] RRKSRTAFTNHQIYELEKRF
LYQKYLSPADRDQIAQQLGL
TNAQVITWFQNRRAKLKRDL
EEMSmart: low_complexity_region: 
[220,226] GGGGGCGSmart: low_complexity_region: 
[238,249] PPGAPKAPGAGASmart: low_complexity_region: 
[270,281] EDEEDEEIDVDDMOD_ProDKin_1: [15,21] RRRSPLDMOD_ProDKin_1: [31,37] KPLTPFSMOD_ProDKin_1: [80,86] SQTSPLCMOD_ProDKin_1: [118,124] QRQTPKKMOD_ProDKin_1: [148,154] KYLSPADMOD_ProDKin_1: [231,237] RPGSPVLMOD_ProDKin_1: [250,256] LQLSPAS
[253,259] SPASPLTMOD_PKA_1: [15,21] RRRSPLDMOD_PKA_1: [125,131] RRKSRTAMOD_PKA_2: [15,21] RRRSPLDMOD_PKA_2: [47,53] VRRSYSLMOD_PKA_2: [118,124] QRQTPKK
[125,131] RRKSRTAMOD_CK2_1: [266,272] QDCSEDELIG_SH3_3: [29,35] SNKPLTPLIG_SH3_3: [229,235] KSRPGSP
[232,238] PGSPVLP
[233,239] GSPVLPP
[236,242] VLPPGAP
[239,245] PGAPKAPLIG_SH3_3: [251,257] QLSPASPMOD_PIKK_1: [77,83] ALLSQTSMOD_PIKK_1: [262,268] PASSQDCDisOrder: [1,36] MTSKEDGKAAPGEERRRSPL
DHLPPPANSNKPLTPFDisOrder: [216,281] EATAGGGGGCGRAKSRPGSP
VLPPGAPKAPGAGALQLSPA
SPLTDQPASSQDCSEDEEDE
EIDVDDGlobDom: [37,215] SIEDILNKPSVRRSYSLCGA
AHLLAAADKHAQGGLPLAGR
ALLSQTSPLCALEELASKTF
KGLEVSVLQAAEGRDGMTIF
GQRQTPKKRRKSRTAFTNHQ
IYELEKRFLYQKYLSPADRD
QIAQQLGLTNAQVITWFQNR
RAKLKRDLEEMKADVESAKK
LGPSGQMDIVALAELEQNSLIG_PDZ_3: [20,23] LDHLLIG_PDZ_3: [38,41] IEDI
[39,42] EDILLIG_PDZ_3: [88,91] LEELLIG_PDZ_3: [155,158] RDQILIG_PDZ_3: [203,206] MDIVLIG_PDZ_3: [274,277] DEEILIG_WW_4: [15,20] RRRSPLLIG_WW_4: [31,36] KPLTPFLIG_WW_4: [80,85] SQTSPLLIG_WW_4: [118,123] QRQTPKLIG_WW_4: [148,153] KYLSPALIG_WW_4: [231,236] RPGSPVLIG_WW_4: [250,255] LQLSPA
[253,258] SPASPLLIG_BRCT_BRCA1_1: [92,96] ASKTF F9SD_RaMmI6.png

o Filtering summary

User supplied cellular location(s): nucleus, cytosol
User supplied taxon: Homo sapiens

(An ELM is listed as filtered when all its matching instances have been filtered out.)

ElmsInstances
retained2160
Species filtered18
Smart filtered18
Cellular location
filtered
624
all found
(before filtering)
2892
   
Query sequence:
>unknown MTSKEDGKAAPGEERRRSPLDHLPPPANSNKPLTPFSIEDILNKPSVRRSYSLCGAAHLL
AAADKHAQGGLPLAGRALLSQTSPLCALEELASKTFKGLEVSVLQAAEGRDGMTIFGQRQ
TPKKRRKSRTAFTNHQIYELEKRFLYQKYLSPADRDQIAQQLGLTNAQVITWFQNRRAKL
KRDLEEMKADVESAKKLGPSGQMDIVALAELEQNSEATAGGGGGCGRAKSRPGSPVLPPG
APKAPGAGALQLSPASPLTDQPASSQDCSEDEEDEEIDVDD


o Globular domains/ TM domains and signal peptide detected by the SMART server

Domain Start End
HOX 125 187

o Results of ELM motif search after globular domain filtering and context filtering.

The matches shown in the following table are ELMs filtered out by a SMART/PFAM domain. But it is known that these ELMs occur in a specific domain. We call them rescued.

Elm Name Instances
(Matched Sequence)
Positions Elm Description Cell Compartment Pattern
LIG_CYCLIN_1
RFLY
KYLSP
143-146
148-152
Substrate recognition site that interacts with cyclin and thereby increases phosphorylation by cyclin/cdk complexes. Predicted protein should have the MOD_CDK site. Also used by cyclin inhibitors. nucleus,
cytosol
[RK].L.{0,1}[FYLIVMP]


o Results of ELM motif search after globular domain filtering and context filtering.

All matches falling inside SMART/PFAM domains are excluded from this list.

Elm Name Instances
(Matched Sequence)
Positions PHI-Blast Instance Mapping Elm Description Cell Compartment Pattern
LIG_14-3-3_3
RAKSRP
227-232
- Consensus derived from natural interactors which do not exactly match the mode1 and mode2 ligands nucleus,
cytosol,
internal side of plasma membrane
[RHK][STALV].[ST].[PESRDIF]
LIG_APCC_Dbox_1
RRSPLD
GRALLS
16-21
75-80
- An RXXL motif that binds to the Cdh1 and Cdc20 components of APC/C thereby targeting the protein for destruction in a cell cycle dependent manner nucleus,
cytosol
.R..L.
LIG_BRCT_BRCA1_1
ASKTF
92-96
- Phosphopeptide motif which directly interacts with the BRCT (carboxy-terminal) domain of the Breast Cancer Gene BRCA1 with low affinity nucleus,
BRCA1-BARD1 complex
.S..F
LIG_CYCLIN_1
KPLTP
RALL
KGLEV
RFLY
KYLSP
KKLGP
31-35
76-79
97-101
143-146
148-152
195-199
- Substrate recognition site that interacts with cyclin and thereby increases phosphorylation by cyclin/cdk complexes. Predicted protein should have the MOD_CDK site. Also used by cyclin inhibitors. nucleus,
cytosol
[RK].L.{0,1}[FYLIVMP]
LIG_EH1
PFSIEDILN
35-43
- The engrailed homology domain 1 motif is found in homeodomain containing active repressors and other transcription families, and allows for the recruitment of Groucho/TLE corepressors. nucleus .[FYH].[IVM][^WFYP][^WFYP][ILM][ILMV].
LIG_FHA_1
SQTSPLC
80-86
- Phosphothreonine motif binding a subset of FHA domains that show a preference for a large aliphatic amino acid at the pT+3 position. nucleus ..(T)..[ILV].
LIG_MAPK_1
KTFKGLEVSV
94-103
- MAPK interacting molecules (e.g. MAPKKs, substrates, phosphatases) carry docking motif that help to regulate specific interaction in the MAPK cascade. The classic motif approximates (R/K)xxxx#x# where # is a hydrophobic residue. nucleus,
cytosol
[KR]{0,2}[KR].{0,2}[KR].{2,4}[ILVM].[ILVF]
LIG_WW_4
RRRSPL
KPLTPF
SQTSPL
QRQTPK
RPGSPV
LQLSPA
SPASPL
15-20
31-36
80-85
118-123
231-236
250-255
253-258
- Class IV WW domains interaction motif; phosphorylation-dependent interaction. nucleus,
cytosol
...[ST]P.
MOD_CDK
QRQTPKK
118-124
- Substrate motif for phosphorylation by CDK cycloplasmic cyclin-dependent protein kinase holoenzyme complex,
nucleus,
cytosol
...([ST])P.[KR]
MOD_CK1_1
SQTSPLC
SEATAGG
SPASPLT
SPLTDQP
80-86
215-221
253-259
256-262
- CK1 phosphorylation site nucleus,
cytosol
S..([ST])...
MOD_CK2_1
QDCSEDE
266-272
- CK2 phosphorylation site nucleus,
cytosol,
protein kinase CK2 complex
...([ST])..E
MOD_GSK3_1
NKPSVRRS
RAKSRPGS
PASSQDCS
43-50
227-234
262-269
- GSK3 phosphorylation recognition site nucleus,
cytosol
...([ST])...[ST]
MOD_PIKK_1
ALLSQTS
PASSQDC
77-83
262-268
- (ST)Q motif which is phosphorylated by PIKK family members nucleus ...([ST])Q..
MOD_PLK
LEVSVLQ
SEATAGG
99-105
215-221
- Site phosphorylated by the Polo-like-kinase nucleus,
cytosol
.[DE].[ST][ILFWMVA]..
MOD_ProDKin_1
RRRSPLD
KPLTPFS
SQTSPLC
QRQTPKK
RPGSPVL
LQLSPAS
SPASPLT
15-21
31-37
80-86
118-124
231-237
250-256
253-259
- Proline-Directed Kinase (e.g. MAPK) phosphorylation site in higher eukaryotes. nucleus,
cytosol
...([ST])P..
LIG_PDZ_3
LDHL
IEDI
EDIL
LEEL
MDIV
DEEI
20-23
38-41
39-42
88-91
203-206
274-277
- Class III PDZ domains binding motif cytosol,
plasma membrane,
membrane
.[DE].[IVL]
LIG_SH3_1
KSRPGSP
229-235
- This is the motif recognized by class I SH3 domains cytosol,
plasma membrane,
focal adhesion
[RKY]..P..P
LIG_SH3_3
SNKPLTP
KSRPGSP
PGSPVLP
GSPVLPP
VLPPGAP
PGAPKAP
QLSPASP
29-35
229-235
232-238
233-239
236-242
239-245
251-257
- This is the motif recognized by those SH3 domains with a non-canonical class I recognition specificity cytosol,
plasma membrane,
focal adhesion
...[PV]..P
LIG_TRAF2_1
PGEE
ALEE
11-14
87-90
- Major TRAF2-binding consensus motif. Members of the tumor necrosis factor receptor (TNFR) superfamily initiate intracellular signaling by recruiting the C-domain of the TNFR-associated factors (TRAFs) through their cytoplasmic tails. cytosol [PSAT].[QE]E
MOD_PKA_1
RRRSPLD
15-21
- PKA is a protein kinase involved in cell signalling cytosol,
cAMP-dependent protein kinase complex
[RK][RK].[ST]...
MOD_PKA_2
RRRSPLD
VRRSYSL
QRQTPKK
15-21
47-53
118-124
- PKA phosphorylation site cytosol .R.([ST])...


o List of excluded ELMs falling inside SMART/PFAM domains.

Matches in this list are only likely to be of interest if they are in surface-exposed loops.
Consult the SMART or PFAM entries for useful links to solved 3D structures.

Elm Name Positions PHI-Blast Instance Mapping Elm Description Cell Compartment Pattern
LIG_14-3-3_3
127-132
- Consensus derived from natural interactors which do not exactly match the mode1 and mode2 ligands nucleus,
cytosol,
internal side of plasma membrane
[RHK][STALV].[ST].[PESRDIF]
LIG_APCC_Dbox_1
176-181
- An RXXL motif that binds to the Cdh1 and Cdc20 components of APC/C thereby targeting the protein for destruction in a cell cycle dependent manner nucleus,
cytosol
.R..L.
LIG_WW_4
148-153
- Class IV WW domains interaction motif; phosphorylation-dependent interaction. nucleus,
cytosol
...[ST]P.
MOD_ProDKin_1
148-154
- Proline-Directed Kinase (e.g. MAPK) phosphorylation site in higher eukaryotes. nucleus,
cytosol
...([ST])P..
LIG_PDZ_3
155-158
- Class III PDZ domains binding motif cytosol,
plasma membrane,
membrane
.[DE].[IVL]
LIG_SH2_STAT5
149-152
- STAT5 Src Homology 2 (SH2) domain binding motif. cytosol Y[VLTFIC]..
MOD_PKA_1
125-131
- PKA is a protein kinase involved in cell signalling cytosol,
cAMP-dependent protein kinase complex
[RK][RK].[ST]...
MOD_PKA_2
125-131
- PKA phosphorylation site cytosol .R.([ST])...