Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7QIM

In situ structure of nebulin bound to actin filament in skeletal sarcomere

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0001725	cellular_component	stress fiber
A	0005200	molecular_function	structural constituent of cytoskeleton
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005856	cellular_component	cytoskeleton
A	0005865	cellular_component	striated muscle thin filament
A	0005884	cellular_component	actin filament
A	0010628	biological_process	positive regulation of gene expression
A	0015629	cellular_component	actin cytoskeleton
A	0016787	molecular_function	hydrolase activity
A	0030017	cellular_component	sarcomere
A	0030027	cellular_component	lamellipodium
A	0030175	cellular_component	filopodium
A	0030240	biological_process	skeletal muscle thin filament assembly
A	0032991	cellular_component	protein-containing complex
A	0044297	cellular_component	cell body
A	0048741	biological_process	skeletal muscle fiber development
A	0090131	biological_process	mesenchyme migration
B	0000166	molecular_function	nucleotide binding
B	0001725	cellular_component	stress fiber
B	0005200	molecular_function	structural constituent of cytoskeleton
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005856	cellular_component	cytoskeleton
B	0005865	cellular_component	striated muscle thin filament
B	0005884	cellular_component	actin filament
B	0010628	biological_process	positive regulation of gene expression
B	0015629	cellular_component	actin cytoskeleton
B	0016787	molecular_function	hydrolase activity
B	0030017	cellular_component	sarcomere
B	0030027	cellular_component	lamellipodium
B	0030175	cellular_component	filopodium
B	0030240	biological_process	skeletal muscle thin filament assembly
B	0032991	cellular_component	protein-containing complex
B	0044297	cellular_component	cell body
B	0048741	biological_process	skeletal muscle fiber development
B	0090131	biological_process	mesenchyme migration
C	0000166	molecular_function	nucleotide binding
C	0001725	cellular_component	stress fiber
C	0005200	molecular_function	structural constituent of cytoskeleton
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005856	cellular_component	cytoskeleton
C	0005865	cellular_component	striated muscle thin filament
C	0005884	cellular_component	actin filament
C	0010628	biological_process	positive regulation of gene expression
C	0015629	cellular_component	actin cytoskeleton
C	0016787	molecular_function	hydrolase activity
C	0030017	cellular_component	sarcomere
C	0030027	cellular_component	lamellipodium
C	0030175	cellular_component	filopodium
C	0030240	biological_process	skeletal muscle thin filament assembly
C	0032991	cellular_component	protein-containing complex
C	0044297	cellular_component	cell body
C	0048741	biological_process	skeletal muscle fiber development
C	0090131	biological_process	mesenchyme migration
D	0000166	molecular_function	nucleotide binding
D	0001725	cellular_component	stress fiber
D	0005200	molecular_function	structural constituent of cytoskeleton
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005856	cellular_component	cytoskeleton
D	0005865	cellular_component	striated muscle thin filament
D	0005884	cellular_component	actin filament
D	0010628	biological_process	positive regulation of gene expression
D	0015629	cellular_component	actin cytoskeleton
D	0016787	molecular_function	hydrolase activity
D	0030017	cellular_component	sarcomere
D	0030027	cellular_component	lamellipodium
D	0030175	cellular_component	filopodium
D	0030240	biological_process	skeletal muscle thin filament assembly
D	0032991	cellular_component	protein-containing complex
D	0044297	cellular_component	cell body
D	0048741	biological_process	skeletal muscle fiber development
D	0090131	biological_process	mesenchyme migration
E	0000166	molecular_function	nucleotide binding
E	0001725	cellular_component	stress fiber
E	0005200	molecular_function	structural constituent of cytoskeleton
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005856	cellular_component	cytoskeleton
E	0005865	cellular_component	striated muscle thin filament
E	0005884	cellular_component	actin filament
E	0010628	biological_process	positive regulation of gene expression
E	0015629	cellular_component	actin cytoskeleton
E	0016787	molecular_function	hydrolase activity
E	0030017	cellular_component	sarcomere
E	0030027	cellular_component	lamellipodium
E	0030175	cellular_component	filopodium
E	0030240	biological_process	skeletal muscle thin filament assembly
E	0032991	cellular_component	protein-containing complex
E	0044297	cellular_component	cell body
E	0048741	biological_process	skeletal muscle fiber development
E	0090131	biological_process	mesenchyme migration

Functional Information from PROSITE/UniProt

site_id	PS00406
Number of Residues	11
Details	ACTINS_1 Actins signature 1. YVGDEAQs.KRG

Chain	Residue	Details
C	TYR53-GLY63

site_id	PS00432
Number of Residues	9
Details	ACTINS_2 Actins signature 2. WITKqEYDE

Chain	Residue	Details
C	TRP356-GLU364

site_id	PS01132
Number of Residues	13
Details	ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR

Chain	Residue	Details
C	LEU104-ARG116

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	125
Details	Region: {"description":"Interaction with alpha-actinin","evidences":[{"source":"UniProtKB","id":"P68135","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	10
Details	Modified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"PubMed","id":"23911929","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	5
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	5
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"UniProtKB","id":"P68138","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	5
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)