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Search for the desired protein with Uniprot accession, protein name/keyword, ProteomeXchange ID or PDB id

Ex.: O00571, ddx3x (keyword), ATP-dependent RNA helicase DDX3X, PXD000680 or 3JRV

E2AK2_HUMAN : Interferon-induced, double-stranded RNA-activated protein kinase

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PDB

AlphaFold

Phospho-sites

Showing 13 results

Swiss-Prot Position	Modification	Source	Evidence	Singly phosphorylated
6	SER	PRIDE		yes
33	SER	PRIDE		yes
83	SER	UP, PRIDE	Combined	yes
92	SER	PRIDE		yes
255	THR	UP	Experimental
258	THR	UP	Experimental
293	TYR	UP	Experimental
446	THR	UP	Experimental
451	THR	UP	Experimental
454	TYR	PRIDE		yes
456	SER	UP, PRIDE	Combined	yes
513	THR	PRIDE		yes
542	SER	UP, PRIDE	Combined	yes

Swiss-Prot Position

Modification

Source

Evidence

Singly phosphorylated

SER

PRIDE

yes

SER

PRIDE

yes

SER

UP, PRIDE

Combined

yes

SER

PRIDE

yes

255

THR

Experimental

258

THR

Experimental

293

TYR

Experimental

446

THR

Experimental

451

THR

Experimental

454

TYR

PRIDE

yes

456

SER

UP, PRIDE

Combined

yes

513

THR

PRIDE

yes

542

SER

UP, PRIDE

Combined

yes

3D structure is not available

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Phosphorylated amino acids are colored red on the inner ring.

The first amino acid of the protein sequence is colored darker on each ring.

Phospho peptides

Showing 10 results

Sequence

Modified position (Swiss-Prot)

Peptide start

Peptide end

Modified position (Peptide)

Number of projects

MAGDLSAGFFMEELNTYR

YQELPNSGPPHDRR

YQELPNSGPPHDR

KAVSPLLLTTTNSSEGLSMGNYIGLINR

107

AVSPLLLTTTNSSEGLSMGNYIGLINR

107

AVSPLLLTTTNSSEGLSMGNYIGLINR

107

YMSPEQISSQDYGK

454

467

YMSPEQISSQDYGK

456

454

467

EKTLLQK

513

511

517

TLTVWKKSPEK

542

535

545

Structures

Showing 3 results

PDB id

Chain

Method

Resolution

Stoichiometry

Interfacing Molecule/Chain

Complex Formation Significance Score (CSS)

P-sites

View Structure

3UIU

X-ray

2.9

Monomer

0.0

255, 258, 293, 451, 454, 456, 513

Swiss-Prot position	PDB position	Residue	Secondary Structure	Conserved Scale	Accessible surface area	Buried surface area
255	255	THR	C	0.25	99.02521514892578	0.0
258	258	THR	C	0.49	14.360877990722656	0.0
293	293	TYR	E	0.9	32.9112548828125	21.315410614013672
451	451	THR	C	1.0	115.88829803466797	0.0
454	454	TYR	C	0.98	21.472808837890625	0.0
456	456	SER	C	0.87	34.26747131347656	0.0
513	513	THR	H	0.21	59.25385284423828	0.0

2A19

X-ray

2.5

0.3398959

258, 293, 451, 454, 456, 513

Swiss-Prot position	PDB position	Residue	Secondary Structure	Conserved Scale	Accessible surface area	Buried surface area
258	258	THR	C	0.49	25.9688777923584	0.0
293	293	TYR	E	0.9	23.108060836791992	0.0
451	451	THR	C	1.0	101.60995483398438	28.49002456665039
454	454	TYR	C	0.98	21.73587989807129	0.0
456	456	SER	C	0.87	0.0	0.0
513	513	THR	H	0.21	70.18539428710938	0.0

2A1A

X-ray

2.8

Monomer

0.0

258, 293, 451, 454, 456, 513

Swiss-Prot position	PDB position	Residue	Secondary Structure	Conserved Scale	Accessible surface area	Buried surface area
258	258	THR	C	0.49	14.712423324584961	0.0
293	293	TYR	E	0.9	18.355430603027344	0.0
451	451	THR	C	1.0	100.08309173583984	21.606414794921875
454	454	TYR	C	0.98	16.441862106323242	0.0
456	456	SER	C	0.87	0.0	0.0
513	513	THR	H	0.21	57.660484313964844	0.0

Mutations

Showing 3 results

Swiss-Prot Position	Amino acid (Wild type)	Amino acid (Variant)	Variant Type	Disease
428	V	E	Polymorphism
439	L	V	Unclassified	A lung adenocarcinoma sample
506	I	V	Polymorphism

Swiss-Prot Position

Amino acid (Wild type)

Amino acid (Variant)

Variant Type

Disease

428

Polymorphism

439

Unclassified

A lung adenocarcinoma sample

506

Polymorphism