The Eukaryote Linear Motif resource for Functional Sites in Proteins

o Summary for sequence 'Q9UNQ0'.

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(Mouseover the matches for more details )

CLV_C14_Caspase3-7CLV_PCSK_PC1ET2_1TRG_NES_CRM1_1DOC_CYCLIN_RxL_1TRG_Pf-PMV_PEXEL_1CLV_PCSK_KEX2_1MOD_PKA_1MOD_CK2_1LIG_Clathr_ClatBox_1CLV_PCSK_PC7_1LIG_TRAF2_1MOD_GlcNHglycanDOC_USP7_MATH_1LIG_SH3_3LIG_Rb_pABgroove_1DOC_PP1_RVXF_1LIG_Actin_RPEL_3MOD_NEK2_2TRG_ENDOCYTIC_2Secondary StructureLIG_TYR_ITIMLIG_LIR_Apic_2LIG_PTB_Phospho_1LIG_MLH1_MIPbox_1MOD_CK1_1LIG_Actin_WH2_2MOD_NEK2_1LIG_SH2_STAT5DOC_WW_Pin1_4LIG_SH2_STAT3LIG_FHA_2LIG_SUMO_SIM_par_1DOC_MAPK_RevD_3LIG_SH2_SRCLIG_14-3-3_CanoR_1LIG_PTB_Apo_2Submit to SmartSubmit to PfamCLV_PCSK_SKI1_1MOD_PK_1LIG_LIR_Gen_1MOD_GSK3_1LIG_APCC_ABBAyCdc20_2MOD_Plk_4MOD_ProDKin_1DOC_MAPK_MEF2A_6MOD_CMANNOSLIG_NRBOXCLV_NRD_NRD_1LIG_SUMO_SIM_anti_2MOD_PKA_2LIG_APCC_ABBA_1LIG_Pex14_2LIG_Pex14_1MOD_Plk_1LIG_SH3_4LIG_SH2_GRB2DOC_MAPK_gen_1MOD_PIKK_1LIG_FHA_1Submit to GlobPlotTRG_NLS_MonoExtN_4TRG_LysEnd_APsAcLL_1LIG_BIR_II_1MOD_N-GLC_2MOD_N-GLC_1MOD_SUMO_rev_2PhosphoELMLIG_GBD_Chelix_1LIG_eIF4E_1LIG_UBA3_1LIG_LIR_Nem_3MOD_OFUCOSYLIG_WD40_WDR5_VDV_1LIG_WD40_WDR5_VDV_2LIG_RRM_PRI_1TRG_ER_diLys_1LIG_BRCT_BRCA1_1DOC_USP7_UBL2_3ConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredSmart: AAA: 
<b>[72,270]</b><br /><b>KPGLNAILGPTGGGKSSLLD
VLAARKDPSGLSGDVLINGA
PRPANFKCNSGYVVQDDVVM
GTLTVRENLQFSAALRLATT
MTNHEKNERINRVIQELGLD
KVADSKVGTQFIRGVSGGER
KRTSIGMELITDPSILFLDE
PTTGLDSSTANAVLLLLKRM
SKQGRTIIFSIHQPRYSIFK
LFDSLTLLASGRLMFHGPA</b><br /><b></b><br />Smart: transmembrane_domain: 
<b>[394,416]</b><br /><b>ASIAQIIVTVVLGLVIGAIY
FGL</b><br /><b></b><br />Smart: transmembrane_domain: 
<b>[428,450]</b><br /><b>GVLFFLTTNQCFSSVSAVEL
FVV</b><br /><b></b><br />Smart: transmembrane_domain: 
<b>[478,499]</b><br /><b>LLPMRMLPSIIFTCIVYFML
GL</b><br /><b></b><br />Smart: transmembrane_domain: 
<b>[506,528]</b><br /><b>FFVMMFTLMMVAYSASSMAL
AIA</b><br /><b></b><br />Smart: transmembrane_domain: 
<b>[533,555]</b><br /><b>VVSVATLLMTICFVFMMIFS
GLL</b><br /><b></b><br />Smart: transmembrane_domain: 
<b>[629,651]</b><br /><b>NHVALACMIVIFLTIAYLKL
LFL</b><br /><b></b><br />ConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredDisOrder: <b>[1,24]</b><br /><b>MSSSNVEVFIPVSQGNTNGF
PATA</b><br /><b></b><br />DisOrder: <b>[72,88]</b><br /><b>KPGLNAILGPTGGGKSS</b><br /><b></b><br />DisOrder: <b>[99,119]</b><br /><b>PSGLSGDVLINGAPRPANFK
C</b><br /><b></b><br />DisOrder: <b>[209,217]</b><br /><b>LDEPTTGLD</b><br /><b></b><br />DisOrder: <b>[589,606]</b><br /><b>QNFCPGLNATGNNPCNYA</b><br /><b></b><br />GlobDom: <b>[120,208]</b><br /><b>NSGYVVQDDVVMGTLTVREN
LQFSAALRLATTMTNHEKNE
RINRVIQELGLDKVADSKVG
TQFIRGVSGGERKRTSIGME
LITDPSILF</b><br /><b></b><br />GlobDom: <b>[218,588]</b><br /><b>SSTANAVLLLLKRMSKQGRT
IIFSIHQPRYSIFKLFDSLT
LLASGRLMFHGPAQEALGYF
ESAGYHCEAYNNPADFFLDI
INGDSTAVALNREEDFKATE
IIEPSKQDKPLIEKLAEIYV
NSSFYKETKAELHQLSGGEK
KKKITVFKEISYTTSFCHQL
RWVSKRSFKNLLGNPQASIA
QIIVTVVLGLVIGAIYFGLK
NDSTGIQNRAGVLFFLTTNQ
CFSSVSAVELFVVEKKLFIH
EYISGYYRVSSYFLGKLLSD
LLPMRMLPSIIFTCIVYFML
GLKPKADAFFVMMFTLMMVA
YSASSMALAIAAGQSVVSVA
TLLMTICFVFMMIFSGLLVN
LTTIASWLSWLQYFSIPRYG
FTALQHNEFLG</b><br /><b></b><br />ConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscored QiKSQCMVGC.png


Homologous sequences were used to calculate a multiple sequence alignment visualizing the conservation of individual short linear motifs.
Click here to enable the multiple sequence alignment viewer Jalview (requires Java browser plugin) (unsigned version)
Alternatively, you can download the alignment, conservation features, and phosphosite features to load into Jalview Desktop.


o Filtering summary

No user supplied cellular location.
User supplied taxon: root

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

ElmsInstances
FILTERED BY: Species00
Cellular location (counts only those ELMs not already excluded by species.)00
Structural score (below medium threshold score)00
Smart (in a domain and no structural filter info available)17154
TOTAL FILTERED:17154
RETAINED BY:Smart (outside domain and no structural filter info available)57122
Structural score (at or above medium threshold score)00
TOTAL RETAINED:57122
TOTALall found
(before filtering)
74276
   
Query sequence:
>Q9UNQ0
MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVE
KEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCN
SGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGT
QFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIF
SIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIING
DSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKK
ITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDS
TGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLP
MRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLL
MTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGN
NPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS


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

Domain Start End
AAA 72 270
transmembrane_domain 394 416
transmembrane_domain 428 450
transmembrane_domain 478 499
transmembrane_domain 506 528
transmembrane_domain 533 555
transmembrane_domain 629 651


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

Matches falling inside globular protein domains are excluded from this list unless having an acceptable structural score (if the structural filter (BETA version) is applicable). If the structural filter (BETA version)is applicable it is possible to view these structures with Jmol

Elm Name Instances
(Matched Sequence)
Positions View in Jmol Elm Description Cell Compartment Pattern PHI-Blast Instance Mapping Structural Filter Info Probability
CLV_NRD_NRD_1
CRK
55-57 [A]
-
N-Arg dibasic convertase (NRD/Nardilysin) cleavage site (X-|-R-K or R-|-R-X). extracellular,
Golgi apparatus,
cell surface
(.RK)|(RR[^KR]) - - 7.465e-03
CLV_PCSK_KEX2_1
KRS
382-384 [A]
-
Yeast kexin 2 cleavage site (K-R-|-X or R-R-|-X). extracellular,
Golgi apparatus
[KR]R. - - 7.973e-03
CLV_PCSK_PC1ET2_1
KRS
382-384 [A]
-
NEC1/NEC2 cleavage site (K-R-|-X). extracellular,
Golgi apparatus,
Golgi membrane
KR. - - 3.903e-03
CLV_PCSK_PC7_1
RWVSKRS
378-384 [A]
-
Proprotein convertase 7 (PC7, PCSK7) cleavage site (R-X-X-X-[RK]-R-|-X). extracellular,
Golgi apparatus,
Golgi membrane
R...[KR]R. - - 5.087e-04
CLV_PCSK_SKI1_1
KAFTE
KEILS
KKITV
RSFKN
KNLLG
KKLFI
29-33 [A]
61-65 [A]
359-363 [A]
383-387 [A]
386-390 [A]
452-456 [A]
-
-
-
-
-
-
Subtilisin/kexin isozyme-1 (SKI1) cleavage site ([RK]-X-[hydrophobic]-[LTKF]-|-X). endoplasmic reticulum lumen,
endoplasmic reticulum,
Golgi apparatus,
extracellular
[RK].[AILMFV][LTKF]. - - 6.821e-03
DOC_MAPK_gen_1
KKKKITV
357-363 [A]
-
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] - - 4.324e-03
DOC_USP7_MATH_1
ATASN
22-26 [A]
-
The USP7 MATH domain binding motif variant based on the MDM2 and p53 interactions. nucleus [PA][^P][^FYWIL]S[^P] - - 1.239e-02
DOC_USP7_UBL2_3
KPVEK
KRSFK
57-61 [A]
382-386 [A]
-
-
The USP7 CTD domain binding motif variant based on the ICP0 and DNMT1 interactions nucleus K...K - - 3.742e-03
DOC_WW_Pin1_4
IDLSPW
619-624 [A]
-
The Class IV WW domain interaction motif is recognised primarily by the Pin1 phosphorylation-dependent prolyl isomerase. cytosol,
nucleus
...([ST])P. - - 1.543e-02
LIG_14-3-3_CanoR_1
RVSSYF
465-470 [A]
-
Canonical Arg-containing phospho-motif mediating a strong interaction with 14-3-3 proteins. nucleus,
internal side of plasma membrane,
cytosol
R[^DE]{0,2}[^DEPG]([ST])(([FWYLMV].)|([^PRIKGN]P)|([^PRIKGN].{2,4}[VILMFWYP])) - - 4.477e-03
LIG_Actin_WH2_2
AVLSFHNICYRVKLKSG
35-51 [A]
-
The WH2 motif is of variable length (16-19 amino acids) binding to the hydrophobic cleft formed by actin's subdomains 1 and 3. At the N-terminus it forms an alpha-helix followed by a flexible loop stabilised upon actin binding. cytosol [^R]..((.[ILMVF])|([ILMVF].))[^P][^P][ILVM].{4,7}L(([KR].)|(NK))[VATIGS] - - 6.603e-04
LIG_APCC_ABBA_1
ITVFKE
361-366 [A]
-
Amphipathic motif that is involved in APC/C inhibition by binding of CDH1/CDC20. In metazoan cyclin A, the motif also acts as a degron, enabling the cyclin's degradation in prometaphase. spindle pole,
nucleus,
cytosol
[ILVMF].[ILMVP][FHY].[DE] - - 3.843e-04
LIG_APCC_ABBAyCdc20_2
KITVFKE
360-366 [A]
-
Amphipathic motif that binds to yeast Cdc20 and acts as an APC/C degron enabling cyclin Clb5 degradation during mitosis. not annotated [KR]..[ILVM][FHY].[DE] - - 1.669e-04
LIG_BIR_II_1
MSSSN
1-5 [A]
-
These IBMs are found in pro-apoptotic proteins and function in the abrogation of caspase inhibition by Inhibitor of Apoptosis Proteins (IAPs) in apoptotic cells. The motif binds specifically to type II BIR domains. cytosol,
mitochondrion
^M{0,1}[AS]... - - 3.252e-04
LIG_BRCT_BRCA1_1
VSSYF
466-470 [A]
-
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 - - 1.912e-03
LIG_eIF4E_1
YFLGKLL
469-475 [A]
-
Motif binding to the dorsal surface of eIF4E. cytosol Y....L[VILMF] - - 1.891e-04
LIG_FHA_1
KATEIIE
314-320 [A]
-
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]. - - 8.662e-03
LIG_FHA_2
KETKAEL
TCTGEEY
343-349 [A]
607-613 [A]
-
-
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]. - - 8.286e-03
LIG_LIR_Apic_2
EAYNNP
285-290 [A]
-
Apicomplexa specific variant of the canonical LIR motif that binds to Atg8 protein family members to mediate processes involved in autophagy. cytosol,
cytoplasmic side of late endosome membrane
[EDST].{0,2}[WFY]..P - - 3.371e-03
LIG_LIR_Gen_1
EVFIPV
SFHNI
DFFLDI
TVFKEI
SFKNL
SGYYRV
7-12 [A]
38-42 [A]
292-297 [A]
362-367 [A]
384-388 [A]
461-466 [A]
-
-
-
-
-
-
Canonical LIR motif that binds to Atg8 protein family members to mediate processes involved in autophagy. cytosol,
cytoplasmic side of late endosome membrane
[EDST].{0,2}[WFY]..[ILV] - - 5.200e-03
LIG_LIR_Nem_3
EVFIPV
SFHNI
DFFLDI
TVFKEI
SFKNL
SGYYRV
SWLQY
7-12 [A]
38-42 [A]
292-297 [A]
362-367 [A]
384-388 [A]
461-466 [A]
566-570 [A]
-
-
-
-
-
-
-
Nematode-specific variant of the canonical LIR motif that binds to Atg8 protein family members to mediate processes involved in autophagy. cytosol,
cytoplasmic side of late endosome membrane
[EDST].{0,2}[WFY]..[ILVFY] - - 6.362e-03
LIG_MLH1_MIPbox_1
VSSYF
466-470 [A]
-
Proteins involved in DNA repair and replication employ conserved MIP-box motifs to bind the C-terminal domain of mismatch repair protein MLH1. MutLalpha complex,
nucleus
.S.[FY][F] - - 6.212e-05
LIG_NRBOX
FLGKLLS
470-476 [A]
-
The nuclear receptor box motif (LXXLL) confers binding to nuclear receptors. nucleus [^P]L[^P][^P]LL[^P] - - 2.628e-04
LIG_Pex14_1
WLQYF
567-571 [A]
-
Wxxx[FY] motifs present in N-terminal half of Pex5 bind to Pex13 and Pex14 at peroxisomal and glycosomal membranes to facilitate entrance of PTS1 cargo proteins into the organellar lumen. peroxisome,
cytosol,
glycosome
W...[FY] - - 2.226e-04
LIG_PTB_Apo_2
SFHNICYR
IYVNSSFY
38-45 [A]
335-342 [A]
-
-
These phosphorylation-independent motifs bind to Dab-like PTB domains. Binding is not driven by contacts at the 0 or FY position, but instead is dependent upon the large number of hydrophobic and hydrogen bond contacts between motif and domain. integrin,
internal side of plasma membrane,
cytosol,
receptor complex,
cytoplasmic membrane-bounded vesicle
(.[^P].NP.[FY].)|(.[ILVMFY].N..[FY].) - - 3.108e-04
LIG_PTB_Phospho_1
SFHNICY
38-44 [A]
-
This phosphorylation-dependent motif binds to Shc-like and IRS-like PTB domains. The pTyr is positioned within a highly basic-charged anchoring pocket. A hydrophobic residue -5 (compared to pY) increases the affinity of the interaction. integrin,
internal side of plasma membrane,
cytosol,
receptor complex,
cytoplasmic membrane-bounded vesicle
(.[^P].NP.(Y))|(.[ILVMFY].N..(Y)) - - 1.352e-04
LIG_SH2_GRB2
YVNS
336-339 [A]
-
GRB2-like Src Homology 2 (SH2) domains binding motif. Early endosome,
cytosol
(Y)([EDST]|[MLIVAFYQ])N. - - 3.019e-04
LIG_SH2_SRC
YVNS
336-339 [A]
-
Src-family Src Homology 2 (SH2) domains binding motif. cytosol (Y)[QDEVAIL][DENPYHI][IPVGAHS] - - 8.729e-04
LIG_SH2_STAT5
YFES
YVNS
YTTS
YISG
YFLG
YFSI
YLVK
276-279 [A]
336-339 [A]
369-372 [A]
459-462 [A]
469-472 [A]
570-573 [A]
613-616 [A]
-
-
-
-
-
-
-
STAT5 Src Homology 2 (SH2) domain binding motif. cytosol (Y)[VLTFIC].. - - 3.296e-03
LIG_SH3_3
NVEVFIP
5-11 [A]
-
This is the motif recognized by those SH3 domains with a non-canonical class I recognition specificity plasma membrane,
focal adhesion,
cytosol
...[PV]..P - - 1.317e-02
LIG_SH3_4
KPVEKEIL
57-64 [A]
-
This is the motif recognized by those SH3 domains with a non-canonical class II recognition specificity focal adhesion,
cytosol
KP..[QK]... - - 6.781e-04
LIG_TRAF2_1
TGEE
609-612 [A]
-
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 - - 4.300e-03
LIG_TYR_ITIM
LQYFSI
568-573 [A]
-
ITIM (immunoreceptor tyrosine-based inhibitory motif). Phosphorylation of the ITIM motif, found in the cytoplasmic tail of some inhibitory receptors (KIRs) that bind MHC Class I, leads to the recruitment and activation of a protein tyrosine phosphatase. cytosol [ILV].(Y)..[ILV] - - 2.992e-04
LIG_WD40_WDR5_VDV_1
DFFLDI
292-297 [A]
-
This WDR5-binding motif binds to a cleft between blades 5 and 6 of the WD40 repeat domain of WDR5, opposite of the Win motif-binding site, to mediate assembly of histone modification complexes. nucleus,
histone methyltransferase complex
[ED].{0,3}[VIL]D[VI] - - 2.939e-04
LIG_WD40_WDR5_VDV_2
SSSNVEV
SSNVEV
SNVEV
TNGFPATA
TASNDLKA
SNDLKA
DLKA
YRVKL
DFFLDI
EKLAEI
YKETKAEL
ETKAEL
TKAEL
EKKKKITV
2-8 [A]
3-8 [A]
4-8 [A]
17-24 [A]
23-30 [A]
25-30 [A]
27-30 [A]
44-48 [A]
292-297 [A]
330-335 [A]
342-349 [A]
344-349 [A]
345-349 [A]
356-363 [A]
-
-
-
-
-
-
-
-
-
-
-
-
-
-
Fungi-specific variant of the WDR5-binding motif that binds to a cleft between blades 5 and 6 of the WD40 repeat domain of WDR5, opposite of the Win motif-binding site, to mediate assembly of histone modification complexes. nucleus,
histone methyltransferase complex
[EDSTY].{0,4}[VIPLA][TSDEKR][ILVA] - - 4.678e-02
MOD_CK1_1
SYTTSFC
SKRSFKN
SWLSWLQ
368-374 [A]
381-387 [A]
563-569 [A]
-
-
-
CK1 phosphorylation site cytosol,
nucleus
S..([ST])... - - 1.704e-02
MOD_CK2_1
MSSSNVE
YKETKAE
HQLSGGE
ATCTGEE
1-7 [A]
342-348 [A]
350-356 [A]
606-612 [A]
-
-
-
-
CK2 phosphorylation site nucleus,
cytosol,
protein kinase CK2 complex
...([ST])..E - - 1.457e-02
MOD_CMANNOS
WLSW
WGLW
564-567 [A]
624-627 [A]
-
-
Motif for attachment of a mannosyl residue to a tryptophan extracellular (W)..W - - 4.692e-05
MOD_GlcNHglycan
KSGF
ESAG
LSGG
ISGY
49-52 [A]
278-281 [A]
352-355 [A]
460-463 [A]
-
-
-
-
Glycosaminoglycan attachment site extracellular,
Golgi apparatus
[ED]{0,3}.(S)[GA]. - - 1.792e-02
MOD_GSK3_1
IPVSQGNT
KEISYTTS
VNLTTIAS
10-17 [A]
365-372 [A]
556-563 [A]
-
-
-
GSK3 phosphorylation recognition site cytosol,
nucleus
...([ST])...[ST] - - 2.679e-02
MOD_N-GLC_1
VNSSFY
KNDSTG
VNLTTI
LNATGN
337-342 [A]
417-422 [A]
556-561 [A]
595-600 [A]
-
-
-
-
Generic motif for N-glycosylation. It was shown that Trp, Asp, and Glu are uncommon before the Ser/Thr position. Efficient glycosylation usually occurs when ~60 residues or more separate the glycosylation acceptor site from the C-terminus. extracellular,
Golgi apparatus,
endoplasmic reticulum
.(N)[^P][ST].. - - 5.018e-03
MOD_N-GLC_2
NIC
NFC
41-43 [A]
590-592 [A]
-
-
Atipical motif for N-glycosylation site. Examples are Human CD69, which is uniquely glycosylated at typical (Asn-X-Ser/Thr) and atypical (Asn-X-Cys) motifs, beta protein C extracellular,
Golgi apparatus,
endoplasmic reticulum
(N)[^P]C - - 2.973e-04
MOD_NEK2_1
MSSSNV
LNATGN
1-6 [A]
595-600 [A]
-
-
NEK2 phosphorylation motif with preferred Phe, Leu or Met in the -3 position to compensate for less favorable residues in the +1 and +2 position. centrosome,
Ndc80 complex,
condensed nuclear chromosome outer kinetochore,
cytosol,
nucleus
[FLM][^P][^P]([ST])[^DEP][^DE] - - 9.798e-03
MOD_NEK2_2
AVLSFH
35-40 [A]
-
NEK2 phosphorylation motif with specific set of residues in the +1 and +2 position to compensate for less favorable residues in the -3 position. centrosome,
Ndc80 complex,
condensed nuclear chromosome outer kinetochore,
cytosol,
nucleus
[WYPCAG][^P][^P]([ST])[IFCVML][KRHYF] - - 1.295e-03
MOD_OFUCOSY
CNYATC
603-608 [A]
-
Site for attachment of a fucose residue to a serine. extracellular C.{3,5}([ST])C - - 4.617e-05
MOD_PIKK_1
IPVSQGN
10-16 [A]
-
(ST)Q motif which is phosphorylated by PIKK family members. nucleus,
cytosol
...([ST])Q.. - - 9.230e-03
MOD_PKA_1
KKITVFK
359-365 [A]
-
Main preference for PKA-type AGC kinase phosphorylation. cAMP-dependent protein kinase complex,
cytosol,
nucleus
[RK][RK].([ST])[^P].. - - 2.315e-03
MOD_PKA_2
YRVSSYF
464-470 [A]
-
Secondary preference for PKA-type AGC kinase phosphorylation. cytosol,
nucleus,
cAMP-dependent protein kinase complex
.R.([ST])[^P].. - - 9.458e-03
MOD_Plk_1
GDSTAVA
VNSSFYK
KEISYTT
VNLTTIA
300-306 [A]
337-343 [A]
365-371 [A]
556-562 [A]
-
-
-
-
Ser/Thr residue phosphorylated by the Plk1 kinase centralspindlin complex,
nucleus,
spindle,
gamma-tubulin complex,
midbody,
cytosol,
kinetochore,
spindle midzone,
nuclear condensin complex,
cleavage furrow,
nucleoplasm,
microtubule organizing center
.[DNE][^PG][ST](([FYILMVW]..)|([^PEDGKN][FWYLIVM]).) - - 7.674e-03
MOD_Plk_4
VNSSFYK
RVSSYFL
TIASWLS
SWLSWLQ
337-343 [A]
465-471 [A]
560-566 [A]
563-569 [A]
-
-
-
-
Ser/Thr residue phosphorylated by Plk4 nucleus,
cytosol,
SCF ubiquitin ligase complex,
cleavage furrow,
centriole,
gamma-tubulin ring complex,
centriolar satellite,
pericentriolar material
..[^IRFW]([ST])[ILMVFWY][ILMVFWY]. - - 6.019e-03
MOD_ProDKin_1
IDLSPWG
619-625 [A]
-
Proline-Directed Kinase (e.g. MAPK) phosphorylation site in higher eukaryotes. cytosol,
nucleus
...([ST])P.. - - 1.543e-02
MOD_SUMO_rev_2
SNDLKAF
EEDFKAT
EDFKAT
SSFYKETKA
SFYKETKA
25-31 [A]
310-316 [A]
311-316 [A]
339-347 [A]
340-347 [A]
-
-
-
-
-
Inverted version of SUMOylation motif recognized for modification by SUMO-1 PML body,
nucleus
[SDE].{0,5}[DE].(K).{0,1}[AIFLMPSTV] - - 1.280e-02
TRG_ENDOCYTIC_2
YYRV
YFSI
463-466 [A]
570-573 [A]
-
-
Tyrosine-based sorting signal responsible for the interaction with mu subunit of AP (Adaptor Protein) complex plasma membrane,
clathrin-coated endocytic vesicle,
cytosol
Y..[LMVIF] - - 2.587e-03
TRG_ER_diLys_1
KKYS
652-655 [A]
-
ER retention and retrieving signal found at the C-terminus of type I ER membrane proteins (cytoplasmic in this topology). Di-Lysine signal is responsible for COPI-mediated retrieval from post-ER compartments. endoplasmic reticulum membrane, integral protein,
ER-Golgi transport vesicle membrane,
endoplasmic reticulum membrane,
Golgi-ER transport vesicle membrane,
rough endoplasmic reticulum,
endoplasmic reticulum,
endoplasmic reticulum cisterna,
COPI coated vesicle membrane,
cytosol
K.{0,1}K.{2,3}$ - - 2.677e-05
TRG_LysEnd_APsAcLL_1
QDKPLI
324-329 [A]
-
Sorting and internalisation signal found in the cytoplasmic juxta-membrane region of type I transmembrane proteins. Targets them from the Trans Golgi Network to the lysosomal-endosomal-melanosomal compartments. Interacts with adaptor protein (AP) complexes cytosol,
Endocytic vesicle
[DERQ]...L[LVI] - - 2.758e-03
TRG_NLS_MonoExtN_4
KKKKIT
357-362 [A]
-
Monopartite variant of the classical basically charged NLS. N-extended version. nucleus,
Nuclear pore,
NLS-dependent protein nuclear import complex
(([PKR].{0,1}[^DE])|([PKR]))((K[RK])|(RK))(([^DE][KR])|([KR][^DE]))[^DE] - - 1.276e-03
TRG_Pf-PMV_PEXEL_1
KPLIE
326-330 [A]
-
Plasmodium Export Element, PEXEL, is a trafficking signal for protein cleavage by PMV protease and export from Plasmodium parasites to infected host cells. endoplasmic reticulum,
host cell cytoplasm,
extracellular,
host cell outer membrane,
pathogen-containing vacuole membrane
(R.[LI].[EDQ])|(R.L..[EDQ])|(K.L.E) - - 2.161e-03


o  List of excluded ELMs falling inside SMART/PFAM domains and/or scoring poorly with the structural filter (if applicable).

Matches in this list are only likely to be of interest if they are in accessible surface-exposed loops. Motif matches buried in stably folded cores of globular domains are not plausible candidates.
If the structural filter (BETA version) is applicable it is possible to view these structures with Jmol. For more info consult the PDB structure entry used for structure filtering or the SMART or PFAM entries for useful links to solved 3D structures.

Elm Name Positions View in Jmol Elm Description Cell Compartment Pattern PHI-Blast Instance Mapping Structural Filter Info Probability
CLV_C14_Caspase3-7
214-218 [A]
-
Caspase-3 and Caspase-7 cleavage site. cytosol,
nucleus
[DSTE][^P][^DEWHFYC]D[GSAN] - - 3.094e-03
CLV_NRD_NRD_1
95-97 [A]
190-192 [A]
-
-
N-Arg dibasic convertase (NRD/Nardilysin) cleavage site (X-|-R-K or R-|-R-X). extracellular,
Golgi apparatus,
cell surface
(.RK)|(RR[^KR]) - - 7.465e-03
CLV_PCSK_KEX2_1
192-194 [A]
229-231 [A]
-
-
Yeast kexin 2 cleavage site (K-R-|-X or R-R-|-X). extracellular,
Golgi apparatus
[KR]R. - - 7.973e-03
CLV_PCSK_PC1ET2_1
192-194 [A]
229-231 [A]
-
-
NEC1/NEC2 cleavage site (K-R-|-X). extracellular,
Golgi apparatus,
Golgi membrane
KR. - - 3.903e-03
CLV_PCSK_SKI1_1
147-151 [A]
263-267 [A]
647-651 [A]
-
-
-
Subtilisin/kexin isozyme-1 (SKI1) cleavage site ([RK]-X-[hydrophobic]-[LTKF]-|-X). endoplasmic reticulum lumen,
endoplasmic reticulum,
Golgi apparatus,
extracellular
[RK].[AILMFV][LTKF]. - - 6.821e-03
DOC_CYCLIN_RxL_1
449-458 [A]
479-486 [A]
644-655 [A]
-
-
-
This motif is mainly based on cyclin A binding peptides and may not apply to all cyclins. nucleus,
membrane,
cytosol,
centriole,
Cajal body
(.|([KRH].{0,3}))[^EDWNSG][^D][RK][^D]L.{0,1}[FLMP].{0,3}[EDST] - - 4.211e-03
DOC_MAPK_gen_1
160-170 [A]
191-200 [A]
192-200 [A]
229-240 [A]
230-240 [A]
-
-
-
-
-
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] - - 4.324e-03
DOC_MAPK_MEF2A_6
482-489 [A]
-
A kinase docking motif that mediates interaction towards the ERK1/2 and p38 subfamilies of MAP kinases. nucleus,
cytosol,
Transcription factor complex
[RK].{2,4}[LIVMP].[LIV].[LIVMF] - - 2.584e-03
DOC_MAPK_RevD_3
639-653 [A]
-
Reverse (C to N direction) of the classical MAPK docking motif ELM:DOC_MAPK_gen_1 with an often extended linker region of the bipartite motif. cytosol,
nucleus
[LIVMPFA].[LIV].{1,2}[LIVMP].{4,6}[LIV]..[RK][RK] - - 1.805e-04
DOC_PP1_RVXF_1
234-241 [A]
261-267 [A]
645-651 [A]
-
-
-
Protein phosphatase 1 catalytic subunit (PP1c) interacting motif binds targeting proteins that dock to the substrate for dephosphorylation. The motif defined is [RK]{0,1}[VI][^P][FW]. nucleus,
protein phosphatase type 1 complex,
cytosol
..[RK].{0,1}[VIL][^P][FW]. - - 8.301e-04
DOC_USP7_MATH_1
392-396 [A]
529-533 [A]
-
-
The USP7 MATH domain binding motif variant based on the MDM2 and p53 interactions. nucleus [PA][^P][^FYWIL]S[^P] - - 1.239e-02
DOC_USP7_UBL2_3
229-233 [A]
-
The USP7 CTD domain binding motif variant based on the ICP0 and DNMT1 interactions nucleus K...K - - 3.742e-03
LIG_14-3-3_CanoR_1
147-153 [A]
191-200 [A]
-
-
Canonical Arg-containing phospho-motif mediating a strong interaction with 14-3-3 proteins. nucleus,
internal side of plasma membrane,
cytosol
R[^DE]{0,2}[^DEPG]([ST])(([FWYLMV].)|([^PRIKGN]P)|([^PRIKGN].{2,4}[VILMFWYP])) - - 4.477e-03
LIG_Actin_RPEL_3
89-108 [A]
-
RPEL motif, present in proteins in several repeats, mediates binding to the hydrophobic cleft created by subdomains 1 and 3 of G-actin. cytosol [IL]..[^P][^P][^P][^P]R.....[IL]..[^P][^P][ILV][ILM] - - 6.116e-06
LIG_Actin_WH2_2
133-149 [A]
-
The WH2 motif is of variable length (16-19 amino acids) binding to the hydrophobic cleft formed by actin's subdomains 1 and 3. At the N-terminus it forms an alpha-helix followed by a flexible loop stabilised upon actin binding. cytosol [^R]..((.[ILMVF])|([ILMVF].))[^P][^P][ILVM].{4,7}L(([KR].)|(NK))[VATIGS] - - 6.603e-04
LIG_BRCT_BRCA1_1
204-208 [A]
485-489 [A]
-
-
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 - - 1.912e-03
LIG_Clathr_ClatBox_1
447-451 [A]
-
Clathrin box motif found on cargo adaptor proteins, it interacts with the beta propeller structure located at the N-terminus of Clathrin heavy chain. cytosol,
Golgi apparatus,
cytoskeleton,
clathrin-coated endocytic vesicle,
Golgi trans-face
L[IVLMF].[IVLMF][DE] - - 3.406e-04
LIG_eIF4E_1
247-253 [A]
-
Motif binding to the dorsal surface of eIF4E. cytosol Y....L[VILMF] - - 1.891e-04
LIG_FHA_1
131-137 [A]
178-184 [A]
211-217 [A]
400-406 [A]
488-494 [A]
-
-
-
-
-
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]. - - 8.662e-03
LIG_FHA_2
133-139 [A]
151-157 [A]
212-218 [A]
-
-
-
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]. - - 8.286e-03
LIG_GBD_Chelix_1
633-641 [A]
-
Amphipatic alpha helix that binds the GTPase-binding domain (GBD) in WASP and N-WASP. extracellular exosome,
vesicle membrane,
cytosol,
actin cytoskeleton,
cell-cell junction
[ILV][VA][^P][^P][LI][^P][^P][^P][LM] - - 9.792e-05
LIG_LIR_Gen_1
486-492 [A]
642-648 [A]
-
-
Canonical LIR motif that binds to Atg8 protein family members to mediate processes involved in autophagy. cytosol,
cytoplasmic side of late endosome membrane
[EDST].{0,2}[WFY]..[ILV] - - 5.200e-03
LIG_LIR_Nem_3
248-253 [A]
486-492 [A]
642-648 [A]
-
-
-
Nematode-specific variant of the canonical LIR motif that binds to Atg8 protein family members to mediate processes involved in autophagy. cytosol,
cytoplasmic side of late endosome membrane
[EDST].{0,2}[WFY]..[ILVFY] - - 6.362e-03
LIG_Pex14_2
507-511 [A]
547-551 [A]
-
-
Fxxx[WF] motifs are present in Pex19 and S. cerevisiae Pex5 cytosolic receptors that bind to peroxisomal membrane docking member, Pex14 cytosol,
peroxisome,
glycosome
F...[WF] - - 4.628e-04
LIG_Rb_pABgroove_1
247-255 [A]
-
The LxxLFD motif binds in a deep groove between pocket A and pocket B of the Retinoblastoma protein nucleus,
Transcription factor complex,
Rb-E2F complex
..[LIMV]..[LM][FY]D. - - 2.475e-05
LIG_RRM_PRI_1
495-502 [A]
-
The PTB RRM2 Interacting (PRI) motif is found in some splicing regulators, possibly only in the chordate lineage. As part of splicing complex regulation, it interacts with the 2nd RNA binding domain (RRM) of PTB, the polypyrimidine tract binding protein. nucleus,
heterogeneous nuclear ribonucleoprotein complex
.[ILVM]LG..P. - - 8.391e-05
LIG_SH2_STAT3
123-126 [A]
-
YXXQ motif found in the cytoplasmic region of cytokine receptors that bind STAT3 SH2 domain. cytosol (Y)..Q - - 7.975e-04
LIG_SH2_STAT5
123-126 [A]
413-416 [A]
494-497 [A]
645-648 [A]
-
-
-
-
STAT5 Src Homology 2 (SH2) domain binding motif. cytosol (Y)[VLTFIC].. - - 3.296e-03
LIG_SUMO_SIM_anti_2
87-94 [A]
88-94 [A]
254-261 [A]
255-261 [A]
-
-
-
-
Motif for the antiparallel beta augmentation mode of non-covalent binding to SUMO protein. PML body,
nucleus,
nuclear body
[DEST]{1,10}.{0,1}[VIL][DESTVILMA][VIL][VILM].[DEST]{0,5} - - 2.349e-03
LIG_SUMO_SIM_par_1
132-138 [A]
532-538 [A]
-
-
Motif for the parallel beta augmentation mode of non-covalent binding to SUMO protein. PML body,
nucleus,
nuclear body
[DEST]{0,5}.[VILPTM][VIL][DESTVILMA][VIL].{0,1}[DEST]{1,10} - - 4.545e-03
LIG_TRAF2_1
269-272 [A]
-
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 - - 4.300e-03
LIG_TYR_ITIM
492-497 [A]
643-648 [A]
-
-
ITIM (immunoreceptor tyrosine-based inhibitory motif). Phosphorylation of the ITIM motif, found in the cytoplasmic tail of some inhibitory receptors (KIRs) that bind MHC Class I, leads to the recruitment and activation of a protein tyrosine phosphatase. cytosol [ILV].(Y)..[ILV] - - 2.992e-04
LIG_UBA3_1
63-72 [A]
89-97 [A]
225-233 [A]
227-233 [A]
496-502 [A]
639-647 [A]
648-653 [A]
-
-
-
-
-
-
-
UBA3 adenylation domain binding motif variant based on the UBE2M and UBE2F interactions. nucleus [ILM][ILMF].{1,2}[ILM].{0,4}K - - 1.196e-03
LIG_WD40_WDR5_VDV_2
87-92 [A]
88-92 [A]
133-136 [A]
143-148 [A]
199-206 [A]
202-206 [A]
203-206 [A]
254-258 [A]
255-258 [A]
440-447 [A]
441-447 [A]
443-447 [A]
532-539 [A]
535-539 [A]
642-648 [A]
645-648 [A]
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
Fungi-specific variant of the WDR5-binding motif that binds to a cleft between blades 5 and 6 of the WD40 repeat domain of WDR5, opposite of the Win motif-binding site, to mediate assembly of histone modification complexes. nucleus,
histone methyltransferase complex
[EDSTY].{0,4}[VIPLA][TSDEKR][ILVA] - - 4.678e-02
MOD_CK1_1
100-106 [A]
440-446 [A]
519-525 [A]
532-538 [A]
535-541 [A]
-
-
-
-
-
CK1 phosphorylation site cytosol,
nucleus
S..([ST])... - - 1.704e-02
MOD_CK2_1
132-138 [A]
150-156 [A]
184-190 [A]
440-446 [A]
-
-
-
-
CK2 phosphorylation site nucleus,
cytosol,
protein kinase CK2 complex
...([ST])..E - - 1.457e-02
MOD_GlcNHglycan
98-102 [A]
99-102 [A]
102-105 [A]
120-123 [A]
142-145 [A]
186-189 [A]
260-263 [A]
442-445 [A]
518-521 [A]
551-554 [A]
-
-
-
-
-
-
-
-
-
-
Glycosaminoglycan attachment site extracellular,
Golgi apparatus
[ED]{0,3}.(S)[GA]. - - 1.792e-02
MOD_GSK3_1
173-180 [A]
211-218 [A]
234-241 [A]
254-261 [A]
483-490 [A]
535-542 [A]
-
-
-
-
-
-
GSK3 phosphorylation recognition site cytosol,
nucleus
...([ST])...[ST] - - 2.679e-02
MOD_N-GLC_2
436-438 [A]
-
Atipical motif for N-glycosylation site. Examples are Human CD69, which is uniquely glycosylated at typical (Asn-X-Ser/Thr) and atypical (Asn-X-Cys) motifs, beta protein C extracellular,
Golgi apparatus,
endoplasmic reticulum
(N)[^P]C - - 2.973e-04
MOD_NEK2_1
140-145 [A]
148-153 [A]
216-221 [A]
252-257 [A]
258-263 [A]
431-436 [A]
432-437 [A]
509-514 [A]
539-544 [A]
549-554 [A]
-
-
-
-
-
-
-
-
-
-
NEK2 phosphorylation motif with preferred Phe, Leu or Met in the -3 position to compensate for less favorable residues in the +1 and +2 position. centrosome,
Ndc80 complex,
condensed nuclear chromosome outer kinetochore,
cytosol,
nucleus
[FLM][^P][^P]([ST])[^DEP][^DE] - - 9.798e-03
MOD_NEK2_2
132-137 [A]
245-250 [A]
-
-
NEK2 phosphorylation motif with specific set of residues in the +1 and +2 position to compensate for less favorable residues in the -3 position. centrosome,
Ndc80 complex,
condensed nuclear chromosome outer kinetochore,
cytosol,
nucleus
[WYPCAG][^P][^P]([ST])[IFCVML][KRHYF] - - 1.295e-03
MOD_PIKK_1
177-183 [A]
-
(ST)Q motif which is phosphorylated by PIKK family members. nucleus,
cytosol
...([ST])Q.. - - 9.230e-03
MOD_PK_1
192-198 [A]
-
Phosphorylase kinase phosphorylation site cytosol [RK]..(S)[VI].. - - 9.418e-04
MOD_PKA_1
191-197 [A]
192-198 [A]
229-235 [A]
-
-
-
Main preference for PKA-type AGC kinase phosphorylation. cAMP-dependent protein kinase complex,
cytosol,
nucleus
[RK][RK].([ST])[^P].. - - 2.315e-03
MOD_PKA_2
192-198 [A]
229-235 [A]
245-251 [A]
-
-
-
Secondary preference for PKA-type AGC kinase phosphorylation. cytosol,
nucleus,
cAMP-dependent protein kinase complex
.R.([ST])[^P].. - - 9.458e-03
MOD_Plk_4
85-91 [A]
202-208 [A]
245-251 [A]
254-260 [A]
399-405 [A]
483-489 [A]
529-535 [A]
535-541 [A]
-
-
-
-
-
-
-
-
Ser/Thr residue phosphorylated by Plk4 nucleus,
cytosol,
SCF ubiquitin ligase complex,
cleavage furrow,
centriole,
gamma-tubulin ring complex,
centriolar satellite,
pericentriolar material
..[^IRFW]([ST])[ILMVFWY][ILMVFWY]. - - 6.019e-03
MOD_SUMO_rev_2
171-178 [A]
187-194 [A]
446-455 [A]
-
-
-
Inverted version of SUMOylation motif recognized for modification by SUMO-1 PML body,
nucleus
[SDE].{0,5}[DE].(K).{0,1}[AIFLMPSTV] - - 1.280e-02
TRG_ENDOCYTIC_2
247-250 [A]
413-416 [A]
494-497 [A]
645-648 [A]
-
-
-
-
Tyrosine-based sorting signal responsible for the interaction with mu subunit of AP (Adaptor Protein) complex plasma membrane,
clathrin-coated endocytic vesicle,
cytosol
Y..[LMVIF] - - 2.587e-03
TRG_LysEnd_APsAcLL_1
254-259 [A]
-
Sorting and internalisation signal found in the cytoplasmic juxta-membrane region of type I transmembrane proteins. Targets them from the Trans Golgi Network to the lysosomal-endosomal-melanosomal compartments. Interacts with adaptor protein (AP) complexes cytosol,
Endocytic vesicle
[DERQ]...L[LVI] - - 2.758e-03
TRG_NES_CRM1_1
159-171 [A]
446-458 [A]
-
-
Some proteins re-exported from the nucleus contain a Leucine-rich nuclear export signal (NES) binding to the CRM1 exportin protein. nucleus,
cytosol
([DEQ].{0,1}[LIM].{2,3}[LIVMF][^P]{2,3}[LMVF].[LMIV].{0,3}[DE])|([DE].{0,1}[LIM].{2,3}[LIVMF][^P]{2,3}[LMVF].[LMIV].{0,3}[DEQ]) - - 7.626e-04
TRG_Pf-PMV_PEXEL_1
163-167 [A]
-
Plasmodium Export Element, PEXEL, is a trafficking signal for protein cleavage by PMV protease and export from Plasmodium parasites to infected host cells. endoplasmic reticulum,
host cell cytoplasm,
extracellular,
host cell outer membrane,
pathogen-containing vacuole membrane
(R.[LI].[EDQ])|(R.L..[EDQ])|(K.L.E) - - 2.161e-03