Summary for sequence 'TAU_HUMAN'.

(Mouseover the matches for more details )

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)
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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.)

		Elms	Instances
FILTERED BY:	Species	0	0
	Cellular location (counts only those ELMs not already excluded by species.)	0	0
	Structural score (below medium threshold score)	0	0
	Smart (in a domain and no structural filter info available)	0	0
TOTAL FILTERED:		0	0
RETAINED BY:	Smart (outside domain and no structural filter info available)	42	98
	Structural score (at or above medium threshold score)	0	0
TOTAL RETAINED:		42	98
TOTAL	all found (before filtering)	42	98

Query sequence:
>TAU_HUMAN
MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPG
SETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAG
HVTQEPESGKVVQEGFLREPGPPGLSHQLMSGMPGAPLLPEGPREATRQPSGTGPEDTEG
GRHAPELLKHQLLGDLHQEGPPLKGAGGKERPGSKEEVDEDRDVDESSPQDSPPSKASPA
QDGRPPQTAAREATSIPGFPAEGAIPLPVDFLSKVSTEIPASEPDGPSVGRAKGQDAPLE
FTFHVEITPNVQKEQAHSEEHLGRAAFPGAPGEGPEARGPSLGEDTKEADLPEPSEKQPA
AAPRGKPVSRVPQLKARMVSKSKDGTGSDDKKAKTSTRSSAKTLKNRPCLSPKHPTPGSS
DPLIQPSSPAVCPEPPSSPKYVSSVTSRTGSSGAKEMKLKGADGKTKIATPRGAAPPGQK
GQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREP
KKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLD
LSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEK
LDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDT
SPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL

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

The Smart domains low_complexity_region Tubulin-binding were found. They were not used for filtering because they do not correspond to structural elements.

The ELMs in the following table are known instances annotated from the literature.

Click on the link at positions to see experimental evidence.

Elm Name

Instances
(Matched Sequence)

Positions

Logic

Elm Description

Cell Compartment

Pattern

LIG_SH3_1

RTPPKSP

547-553

true positive

This is the motif recognized by class I SH3 domains

plasma membrane,
focal adhesion,
cytosol

[RKY]..P..P

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_C14_Caspase3-7

ETSDA

SEPDG

DMVDS

62-66 [A]

282-286 [A]

735-739 [A]

Caspase-3 and Caspase-7 cleavage site.

cytosol,
nucleus

[DSTE][^P][^DEWHFYC]D[GSAN]

3.094e-03

CLV_NRD_NRD_1

DRK

22-24 [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_SKI1_1

REATR

REATS

RAAFP

KKAKT

KTLKN

KEMKL

KIATP

KNVKS

164-168 [A]

251-255 [A]

324-328 [A]

391-395 [A]

402-406 [A]

455-459 [A]

467-471 [A]

571-575 [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

DEG_SCF_FBW7_1

PTPGSS

PKTPPSS

VVRTPPKS

VRTPPKS

415-420 [A]

496-502 [A]

545-552 [A]

546-552 [A]

The TPxxS phospho-dependent degron binds the FBW7 F box proteins of the SCF (Skp1_Cullin-Fbox) complex.

cytosol,
nucleus

[LIVMP].{0,2}(T)P..([ST])

7.138e-04

DEG_SCF_FBW7_2

IGDTPSLE

108-115 [A]

The TPxxE phospho-dependent degron binds the FBW7 F box proteins of the SCF (Skp1_Cullin-Fbox) complex.

nucleus,
cytosol

[LIVMP].{0,2}(T)P..E

3.882e-04

DEG_SPOP_SBC_1

AKTST

393-397 [A]

The S/T rich motif known as the SPOP-binding consensus (SBC) of the MATH-BTB protein, SPOP, is present in substrates that undergo SPOP/Cul3-dependant ubiquitination.

nuclear speck,
nucleus,
Cul3-RING ubiquitin ligase complex

[AVP].[ST][ST][ST]

9.380e-04

DOC_CKS1_1

LQTPTE

IATPRG

PKTPPS

PGTPGS

LPTPPT

VRTPPK

48-53 [A]

468-473 [A]

496-501 [A]

520-525 [A]

532-537 [A]

546-551 [A]

Phospho-dependent motif that mediates docking of CDK substrates and regulators to cyclin-CDK-bound Cks1.

cytosol,
nucleus

[MPVLIFWYQ].(T)P..

1.991e-03

DOC_CYCLIN_1

KKLDL

597-601 [A]

Substrate recognition site that interacts with cyclin and thereby increases phosphorylation by cyclin/cdk complexes. Predicted proteins should have a CDK phosphorylation site. Also used by cyclin/cdk inhibitors.

cytosol,
nucleus

[RK].L.{0,1}[FYLIVMP]

5.324e-03

DOC_PP1_RVXF_1

SEKLDFK

THKLTFR

658-664 [A]

690-696 [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_2

PTEDGSE

51-57 [A]

The USP7 MATH domain binding motif variant based on the EBV EBNA1 interaction.

nucleus

P.E[^P].S[^P]

7.169e-04

DOC_USP7_UBL2_3

KCGSK

KDNIK

KVTSK

KLDFK

607-611 [A]

611-615 [A]

634-638 [A]

660-664 [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

RSSAKTL

RSGYSSP

RLQTAP

398-404 [A]

511-517 [A]

559-564 [A]

Canonical Arg-containing phospho-motif mediating a strong interaction with 14-3-3 proteins.

cytosol,
internal side of plasma membrane,
nucleus

R[^DE]{0,2}[^DEPG]([ST])(([FWYLMV].)|([^PRIKGN]P)|([^PRIKGN].{2,4}[VILMFWYP]))

4.477e-03

LIG_Actin_WH2_2

KHQLLGDLHQEGPPLKGA

189-206 [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_BIR_II_1

MAEPR

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_BIR_III_1

MAEPR

1-5 [A]

cytosol,
mitochondrion

^M{0,1}A.P.

1.277e-05

LIG_BIR_III_3

MAEPR

1-5 [A]

These IBMs are found in arthropodal 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 III BIR domains of arthropodal IAPs.

cytosol,
mitochondrion

^M{0,1}A.[AP].

2.282e-05

LIG_CtBP_PxDLS_1

PVDLS

629-633 [A]

The PxDLS motif interacts with the NAD-dependent repressor CtBP proteins.

nucleus,
cytosol,
transcriptional repressor complex

(P[LVIPME][DENS][LM][VASTRG])|(G[LVIPME][DENS][LM][VASTRG]((K)|(.[KR])))

1.173e-04

LIG_EVH1_1

LPTPP

532-536 [A]

Proline-rich motif binding to signal transduction class I EVH1 domains.

cytosol,
internal side of plasma membrane

([FYWL]P.PP)|([FYWL]PP[ALIVTFY]P)

1.237e-04

LIG_FHA_1

AGTYGLG

DVTAPLV

GDTPSLE

EFTFHVE

EITPNVQ

SRTPSLP

LQTAPVP

GSTENLK

IETHKLT

SSTGSID

15-21 [A]

74-80 [A]

109-115 [A]

300-306 [A]

306-312 [A]

527-533 [A]

560-566 [A]

578-584 [A]

688-694 [A]

729-735 [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

LQTPTED

TPTAEDV

EGTTAEE

GTTAEEA

SGTGPED

DGTGSDD

KLTFREN

LATLADE

48-54 [A]

69-75 [A]

99-105 [A]

100-106 [A]

171-177 [A]

384-390 [A]

692-698 [A]

742-748 [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

SGYSSP

EIVYKSP

512-517 [A]

708-714 [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_MYND_1

PCLSP

408-412 [A]

PxLxP motif is recognized by a subset of MYND domain containing proteins.

nucleus

P.L.P

6.499e-04

LIG_SH2_STAT5

YTMH

YVSS

29-32 [A]

441-444 [A]

STAT5 Src Homology 2 (SH2) domain binding motif.

cytosol

(Y)[VLTFIC]..

3.296e-03

LIG_SH3_1

YSSPGSP

RTPPKSP

514-520 [A]

547-553

This is the motif recognized by class I SH3 domains

plasma membrane,
focal adhesion,
cytosol

[RKY]..P..P

Output
Summary

1.237e-03

LIG_SH3_2

PTPPTR

533-538 [A]

This is the motif recognized by class II SH3 domains

cytosol,
plasma membrane,
focal adhesion

P..P.[KR]

1.111e-03

LIG_SUMO_SIM_par_1

KPVDLS

628-633 [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_SxIP_EBH_1

KGQANATRIPAKTPP

GQANATRIPAK

480-494 [A]

481-491 [A]

SxIP motifs bind to EBH domains.

cytosol,
microtubule

([KR][^ED]{0,5}[ST].IP[^ED]{5,5})|([^ED]{5,5}[ST].IP[^ED]{0,5}[KR])

2.096e-04

LIG_TRAF2_1

PRQE

TAEE

SKEE

4-7 [A]

102-105 [A]

214-217 [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_TRAF6

DAPLEFTFH

GAPGEGPEA

296-304 [A]

329-337 [A]

TRAF6 binding site. 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 cytoplasmatic tails.

cytosol

..P.E..[FYWHDE].

1.715e-03

LIG_TYR_ITIM

IVYKPV

625-630 [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

MOD_CDK_SPK_2

PCLSPK

PPSSPK

KIATPR

GDTSPR

408-413 [A]

435-440 [A]

467-472 [A]

718-723 [A]

Short version of the CDK phosphorylation site which shows specificity towards a lysine/arginine residue at the [ST] +2 position.

microtubule,
cytosol,
origin recognition complex,
cycloplasmic cyclin-dependent protein kinase holoenzyme complex,
spindle,
nucleus

...([ST])P[RK]

1.929e-03

MOD_CDK_SPxK_1

VVRTPPK

545-551 [A]

Canonical version of the CDK phosphorylation site which shows specificity towards a lysine/arginine residue at the [ST]+3 position.

nucleus,
cycloplasmic cyclin-dependent protein kinase holoenzyme complex,
cytosol

...([ST])P.[KR]

1.929e-03

MOD_CDK_SPxxK_3

PQDSPPSK

SPGTPGSR

SLPTPPTR

229-236 [A]

519-526 [A]

531-538 [A]

Longer version of the CDK phosphorylation site which shows specificity towards a lysine/arginine residue at position +4 after the phospho-Ser/Thr

cycloplasmic cyclin-dependent protein kinase holoenzyme complex,
origin recognition complex,
spindle,
microtubule,
cytosol,
nucleus

...([ST])P..[RK]

1.929e-03

MOD_N-GLC_1

ANATRI

DNITHV

SNVSST

483-488 [A]

675-680 [A]

726-731 [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_NEK2_1

LEFTFH

LDLSNV

299-304 [A]

599-604 [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

GGYTMH

27-32 [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

GHVTQEP

120-126 [A]

(ST)Q motif which is phosphorylated by PIKK family members.

nucleus

...([ST])Q..

9.230e-03

MOD_PKA_2

TRSSAKT

397-403 [A]

Secondary preference for PKA-type AGC kinase phosphorylation.

cytosol,
nucleus,
cAMP-dependent protein kinase complex

.R.([ST])[^P]..

9.458e-03

MOD_PKB_1

RSRTPSLPT

526-534 [A]

PKB Phosphorylation site

cytosol,
nucleus

R.R..([ST])[^P]..

6.034e-04

MOD_PLK

EDVTAPL

LEFTFHV

DEVSASL

73-79 [A]

299-305 [A]

747-753 [A]

Site phosphorylated by the Polo-like kinase.

nucleus,
cytosol

.[DE].([ST])[ILFWMVA]..

6.015e-03

MOD_SUMO_for_1

VKSE

656-659 [A]

Motif recognised for modification by SUMO-1

nucleus,
PML body

[VILMAFP](K).E

1.914e-03

TRG_ENDOCYTIC_2

YKPV

627-630 [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

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.

No Elms excluded by Smart filter.