ELM   Currently 128 Elms in ELM database.

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

MOD_SUMOTRG_ENDOCYTIC_2LIG_CYCLIN_1MOD_GSK3_1LIG_AP2alpha_2LIG_APCC_Dbox_1MOD_CK1_1LIG_MAPK_1MOD_PLKLIG_SH2_STAT5LIG_SH2_STAT3LIG_EH1LIG_FHA_2LIG_FHA_1Submit to SmartSubmit to PfamMOD_ProDKin_1MOD_PKA_2MOD_CK2_1LIG_SH3_3MOD_PIKK_1Submit to GlobPlotLIG_PDZ_3LIG_WW_4HelpHelp HelpHelpHelpHelpHelpHelpHelpHelpHelpMOD_SUMO: [283,286] IKSETRG_ENDOCYTIC_2: [273,276] YPDVTRG_ENDOCYTIC_2: [325,328] YPVVLIG_CYCLIN_1: [31,34] RPLPLIG_CYCLIN_1: [56,60] RQLRVMOD_GSK3_1: [161,168] PGHTIVPS
[168,175] STASPPVSMOD_GSK3_1: [239,246] DSQSGVDSMOD_GSK3_1: [303,310] VKSSLSASMOD_GSK3_1: [317,324] SNVSGTQTMOD_GSK3_1: [345,352] VPPTGQGS
[349,356] GQGSYPTSLIG_AP2alpha_2: [8,10] DPFLIG_APCC_Dbox_1: [114,119] IRDRLLLIG_APCC_Dbox_1: [247,252] LRKHLRMOD_CK1_1: [131,137] SVSSINRMOD_CK1_1: [168,174] STASPPV
[175,181] SSASNDPMOD_CK1_1: [231,237] SEGSVPNMOD_CK1_1: [305,311] SSLSAST
[308,314] SASTNPEMOD_CK1_1: [317,323] SNVSGTQMOD_CK1_1: [352,358] SYPTSTLMOD_CK1_1: [365,371] SEFSGNPLIG_MAPK_1: [200,208] KRKRDEVEV
[201,208] RKRDEVEV
[202,208] KRDEVEVMOD_PLK: [231,237] SEGSVPNMOD_PLK: [289,295] NEYSLPALIG_SH2_STAT5: [209,212] YTDPLIG_SH2_STAT5: [377,380] YTAYLIG_SH2_STAT3: [102,105] YKRQLIG_EH1: [184,192] SYSINGILGLIG_FHA_2: [224,230] VWTLRDVLIG_FHA_2: [309,315] ASTNPELLIG_FHA_2: [327,333] VVTGRDMLIG_FHA_1: [73,79] YETGSIKLIG_FHA_1: [90,96] VATPKVVLIG_FHA_1: [295,301] ALTPGLDLIG_FHA_1: [322,328] TQTYPVVLIG_FHA_1: [353,359] YPTSTLASmart: PAX: 
[16,140] GHGGVNQLGGVFVNGRPLPD
VVRQRIVELAHQGVRPCDIS
RQLRVSHGCVSKILGRYYET
GSIKPGVIGGSKPKVATPKV
VDKIAEYKRQNPTMFAWEIR
DRLLAEGICDNDTVPSVSSI
NRIIRSmart: low_complexity_region: 
[166,178] VPSTASPPVSSASSmart: low_complexity_region: 
[389,413] PALLSSPYYYSAAPRSAPAA
RAAAYMOD_ProDKin_1: [89,95] KVATPKVMOD_ProDKin_1: [147,153] FHPTPDGMOD_ProDKin_1: [168,174] STASPPVMOD_ProDKin_1: [294,300] PALTPGLMOD_ProDKin_1: [391,397] LLSSPYYMOD_PKA_2: [58,64] LRVSHGCMOD_PKA_2: [269,275] ERPSYPDMOD_PKA_2: [384,390] WRFSNPAMOD_CK2_1: [193,199] IPRSNGEMOD_CK2_1: [308,314] SASTNPELIG_SH3_3: [87,93] KPKVATPLIG_SH3_3: [140,146] RTKVQQP
[143,149] VQQPFHPLIG_SH3_3: [155,161] GTGVTAPLIG_SH3_3: [268,274] FERPSYPLIG_SH3_3: [336,342] TTLPGYP
[340,346] GYPPHVPMOD_PIKK_1: [237,243] NGDSQSGMOD_PIKK_1: [254,260] DTFTQQQMOD_PIKK_1: [319,325] VSGTQTYDisOrder: [1,30] MDMHCKADPFSAMHPGHGGV
NQLGGVFVNGDisOrder: [76,89] GSIKPGVIGGSKPKDisOrder: [145,197] QPFHPTPDGAGTGVTAPGHT
IVPSTASPPVSSASNDPVGS
YSINGILGIPRSNDisOrder: [212,219] PAHIRGGGDisOrder: [231,245] SEGSVPNGDSQSGVDDisOrder: [291,376] YSLPALTPGLDEVKSSLSAS
TNPELGSNVSGTQTYPVVTG
RDMASTTLPGYPPHVPPTGQ
GSYPTSTLAGMVPGSEFSGN
PYSHPQLIG_PDZ_3: [34,37] PDVVLIG_PDZ_3: [96,99] VDKILIG_PDZ_3: [115,118] RDRL
[120,123] AEGILIG_PDZ_3: [126,129] NDTVLIG_PDZ_3: [179,182] NDPVLIG_PDZ_3: [203,206] RDEVLIG_PDZ_3: [244,247] VDSLLIG_PDZ_3: [261,264] LEAL
[264,267] LDRVLIG_PDZ_3: [280,283] SEHILIG_PDZ_3: [300,303] LDEVLIG_WW_4: [89,94] KVATPKLIG_WW_4: [147,152] FHPTPDLIG_WW_4: [168,173] STASPPLIG_WW_4: [294,299] PALTPGLIG_WW_4: [391,396] LLSSPY yDkBbdD_RbxBkb.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
retained1961
Species filtered13
Smart filtered217
Cellular location
filtered
620
all found
(before filtering)
2798
   
Query sequence:
>unknown MDMHCKADPFSAMHPGHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRV
SHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKVVDKIAEYKRQNPTMFAWEIRDRLLA
EGICDNDTVPSVSSINRIIRTKVQQPFHPTPDGAGTGVTAPGHTIVPSTASPPVSSASND
PVGSYSINGILGIPRSNGEKRKRDEVEVYTDPAHIRGGGGLHLVWTLRDVSEGSVPNGDS
QSGVDSLRKHLRADTFTQQQLEALDRVFERPSYPDVFQASEHIKSEQGNEYSLPALTPGL
DEVKSSLSASTNPELGSNVSGTQTYPVVTGRDMASTTLPGYPPHVPPTGQGSYPTSTLAG
MVPGSEFSGNPYSHPQYTAYNEAWRFSNPALLSSPYYYSAAPRSAPAARAAAYDRH


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

Domain Start End
PAX 16 140


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_APCC_Dbox_1
LRKHLR
247-252
- 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_EH1
SYSINGILG
184-192
Output
Summary
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
ALTPGLD
TQTYPVV
YPTSTLA
295-301
322-328
353-359
- 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_FHA_2
VWTLRDV
ASTNPEL
VVTGRDM
224-230
309-315
327-333
- Phosphothreonine motif binding a subset of FHA domains that have a preference for an acidic amino acid at the pT+3 position. nucleus,
Replication fork
..(T)..[DE].
LIG_MAPK_1
KRKRDEVEV
RKRDEVEV
KRDEVEV
200-208
201-208
202-208
- 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
FHPTPD
STASPP
PALTPG
LLSSPY
147-152
168-173
294-299
391-396
- Class IV WW domains interaction motif; phosphorylation-dependent interaction. nucleus,
cytosol
...[ST]P.
MOD_CK1_1
STASPPV
SSASNDP
SEGSVPN
SSLSAST
SASTNPE
SNVSGTQ
SYPTSTL
SEFSGNP
168-174
175-181
231-237
305-311
308-314
317-323
352-358
365-371
- CK1 phosphorylation site nucleus,
cytosol
S..([ST])...
MOD_CK2_1
IPRSNGE
SASTNPE
193-199
308-314
- CK2 phosphorylation site nucleus,
cytosol,
protein kinase CK2 complex
...([ST])..E
MOD_GSK3_1
PGHTIVPS
STASPPVS
DSQSGVDS
VKSSLSAS
SNVSGTQT
VPPTGQGS
GQGSYPTS
161-168
168-175
239-246
303-310
317-324
345-352
349-356
- GSK3 phosphorylation recognition site nucleus,
cytosol
...([ST])...[ST]
MOD_PIKK_1
NGDSQSG
DTFTQQQ
VSGTQTY
237-243
254-260
319-325
- (ST)Q motif which is phosphorylated by PIKK family members nucleus ...([ST])Q..
MOD_PLK
SEGSVPN
NEYSLPA
231-237
289-295
- Site phosphorylated by the Polo-like-kinase nucleus,
cytosol
.[DE].[ST][ILFWMVA]..
MOD_ProDKin_1
FHPTPDG
STASPPV
PALTPGL
LLSSPYY
147-153
168-174
294-300
391-397
- Proline-Directed Kinase (e.g. MAPK) phosphorylation site in higher eukaryotes. nucleus,
cytosol
...([ST])P..
MOD_SUMO
IKSE
283-286
- Motif recognised for modification by SUMO-1 nucleus,
PML body
[VILMAFP]K.E
LIG_AP2alpha_2
DPF
8-10
- DPF/W motif binds alpha and beta subunits of AP2 adaptor complex. cytosol,
clathrin-coated endocytic vesicle
DP[FW]
LIG_PDZ_3
NDPV
RDEV
VDSL
LEAL
LDRV
SEHI
LDEV
179-182
203-206
244-247
261-264
264-267
280-283
300-303
- Class III PDZ domains binding motif cytosol,
plasma membrane,
membrane
.[DE].[IVL]
LIG_SH2_STAT5
YTDP
YTAY
209-212
377-380
- STAT5 Src Homology 2 (SH2) domain binding motif. cytosol Y[VLTFIC]..
LIG_SH3_3
VQQPFHP
GTGVTAP
FERPSYP
TTLPGYP
GYPPHVP
143-149
155-161
268-274
336-342
340-346
- This is the motif recognized by those SH3 domains with a non-canonical class I recognition specificity cytosol,
plasma membrane,
focal adhesion
...[PV]..P
MOD_PKA_2
ERPSYPD
WRFSNPA
269-275
384-390
- PKA phosphorylation site cytosol .R.([ST])...
TRG_ENDOCYTIC_2
YPDV
YPVV
273-276
325-328
- Tyrosine-based sorting signal responsible for the interaction with mu subunit of AP (Adaptor Protein) complex cytosol,
plasma membrane,
clathrin-coated endocytic vesicle
Y..[LMVIF]


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_APCC_Dbox_1
114-119
- 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_CYCLIN_1
31-34
56-60
- 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_FHA_1
73-79
90-96
- 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_WW_4
89-94
- Class IV WW domains interaction motif; phosphorylation-dependent interaction. nucleus,
cytosol
...[ST]P.
MOD_CK1_1
131-137
- CK1 phosphorylation site nucleus,
cytosol
S..([ST])...
MOD_ProDKin_1
89-95
- Proline-Directed Kinase (e.g. MAPK) phosphorylation site in higher eukaryotes. nucleus,
cytosol
...([ST])P..
LIG_PDZ_3
34-37
96-99
115-118
120-123
126-129
- Class III PDZ domains binding motif cytosol,
plasma membrane,
membrane
.[DE].[IVL]
LIG_SH2_STAT3
102-105
- YXXQ motif found in the cytoplasmic region of cytokine receptors that bind STAT3 SH2 domain. cytosol Y..Q
LIG_SH3_3
87-93
140-146
- This is the motif recognized by those SH3 domains with a non-canonical class I recognition specificity cytosol,
plasma membrane,
focal adhesion
...[PV]..P
MOD_PKA_2
58-64
- PKA phosphorylation site cytosol .R.([ST])...