Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8ZBM

RAT skeletal muscle ATM complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003774	molecular_function	cytoskeletal motor activity
A	0005524	molecular_function	ATP binding
A	0016459	cellular_component	myosin complex
A	0051015	molecular_function	actin filament binding
D	0003774	molecular_function	cytoskeletal motor activity
D	0005524	molecular_function	ATP binding
D	0016459	cellular_component	myosin complex
D	0051015	molecular_function	actin filament binding
E	0000166	molecular_function	nucleotide binding
E	0001725	cellular_component	stress fiber
E	0005200	molecular_function	structural constituent of cytoskeleton
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	0009612	biological_process	response to mechanical stimulus
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	0035865	biological_process	cellular response to potassium ion
E	0043503	biological_process	skeletal muscle fiber adaptation
E	0044297	cellular_component	cell body
E	0048545	biological_process	response to steroid hormone
E	0048741	biological_process	skeletal muscle fiber development
E	0090131	biological_process	mesenchyme migration
H	0000166	molecular_function	nucleotide binding
H	0001725	cellular_component	stress fiber
H	0005200	molecular_function	structural constituent of cytoskeleton
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0005856	cellular_component	cytoskeleton
H	0005865	cellular_component	striated muscle thin filament
H	0005884	cellular_component	actin filament
H	0009612	biological_process	response to mechanical stimulus
H	0010628	biological_process	positive regulation of gene expression
H	0015629	cellular_component	actin cytoskeleton
H	0016787	molecular_function	hydrolase activity
H	0030017	cellular_component	sarcomere
H	0030027	cellular_component	lamellipodium
H	0030175	cellular_component	filopodium
H	0030240	biological_process	skeletal muscle thin filament assembly
H	0035865	biological_process	cellular response to potassium ion
H	0043503	biological_process	skeletal muscle fiber adaptation
H	0044297	cellular_component	cell body
H	0048545	biological_process	response to steroid hormone
H	0048741	biological_process	skeletal muscle fiber development
H	0090131	biological_process	mesenchyme migration
J	0003774	molecular_function	cytoskeletal motor activity
J	0005524	molecular_function	ATP binding
J	0016459	cellular_component	myosin complex
J	0051015	molecular_function	actin filament binding
K	0003774	molecular_function	cytoskeletal motor activity
K	0005524	molecular_function	ATP binding
K	0016459	cellular_component	myosin complex
K	0051015	molecular_function	actin filament binding
L	0003774	molecular_function	cytoskeletal motor activity
L	0005524	molecular_function	ATP binding
L	0016459	cellular_component	myosin complex
L	0051015	molecular_function	actin filament binding
N	0003774	molecular_function	cytoskeletal motor activity
N	0005524	molecular_function	ATP binding
N	0016459	cellular_component	myosin complex
N	0051015	molecular_function	actin filament binding
O	0000166	molecular_function	nucleotide binding
O	0001725	cellular_component	stress fiber
O	0005200	molecular_function	structural constituent of cytoskeleton
O	0005524	molecular_function	ATP binding
O	0005737	cellular_component	cytoplasm
O	0005856	cellular_component	cytoskeleton
O	0005865	cellular_component	striated muscle thin filament
O	0005884	cellular_component	actin filament
O	0009612	biological_process	response to mechanical stimulus
O	0010628	biological_process	positive regulation of gene expression
O	0015629	cellular_component	actin cytoskeleton
O	0016787	molecular_function	hydrolase activity
O	0030017	cellular_component	sarcomere
O	0030027	cellular_component	lamellipodium
O	0030175	cellular_component	filopodium
O	0030240	biological_process	skeletal muscle thin filament assembly
O	0035865	biological_process	cellular response to potassium ion
O	0043503	biological_process	skeletal muscle fiber adaptation
O	0044297	cellular_component	cell body
O	0048545	biological_process	response to steroid hormone
O	0048741	biological_process	skeletal muscle fiber development
O	0090131	biological_process	mesenchyme migration
P	0000166	molecular_function	nucleotide binding
P	0001725	cellular_component	stress fiber
P	0005200	molecular_function	structural constituent of cytoskeleton
P	0005524	molecular_function	ATP binding
P	0005737	cellular_component	cytoplasm
P	0005856	cellular_component	cytoskeleton
P	0005865	cellular_component	striated muscle thin filament
P	0005884	cellular_component	actin filament
P	0009612	biological_process	response to mechanical stimulus
P	0010628	biological_process	positive regulation of gene expression
P	0015629	cellular_component	actin cytoskeleton
P	0016787	molecular_function	hydrolase activity
P	0030017	cellular_component	sarcomere
P	0030027	cellular_component	lamellipodium
P	0030175	cellular_component	filopodium
P	0030240	biological_process	skeletal muscle thin filament assembly
P	0035865	biological_process	cellular response to potassium ion
P	0043503	biological_process	skeletal muscle fiber adaptation
P	0044297	cellular_component	cell body
P	0048545	biological_process	response to steroid hormone
P	0048741	biological_process	skeletal muscle fiber development
P	0090131	biological_process	mesenchyme migration
Q	0000166	molecular_function	nucleotide binding
Q	0001725	cellular_component	stress fiber
Q	0005200	molecular_function	structural constituent of cytoskeleton
Q	0005524	molecular_function	ATP binding
Q	0005737	cellular_component	cytoplasm
Q	0005856	cellular_component	cytoskeleton
Q	0005865	cellular_component	striated muscle thin filament
Q	0005884	cellular_component	actin filament
Q	0009612	biological_process	response to mechanical stimulus
Q	0010628	biological_process	positive regulation of gene expression
Q	0015629	cellular_component	actin cytoskeleton
Q	0016787	molecular_function	hydrolase activity
Q	0030017	cellular_component	sarcomere
Q	0030027	cellular_component	lamellipodium
Q	0030175	cellular_component	filopodium
Q	0030240	biological_process	skeletal muscle thin filament assembly
Q	0035865	biological_process	cellular response to potassium ion
Q	0043503	biological_process	skeletal muscle fiber adaptation
Q	0044297	cellular_component	cell body
Q	0048545	biological_process	response to steroid hormone
Q	0048741	biological_process	skeletal muscle fiber development
Q	0090131	biological_process	mesenchyme migration
R	0000166	molecular_function	nucleotide binding
R	0001725	cellular_component	stress fiber
R	0005200	molecular_function	structural constituent of cytoskeleton
R	0005524	molecular_function	ATP binding
R	0005737	cellular_component	cytoplasm
R	0005856	cellular_component	cytoskeleton
R	0005865	cellular_component	striated muscle thin filament
R	0005884	cellular_component	actin filament
R	0009612	biological_process	response to mechanical stimulus
R	0010628	biological_process	positive regulation of gene expression
R	0015629	cellular_component	actin cytoskeleton
R	0016787	molecular_function	hydrolase activity
R	0030017	cellular_component	sarcomere
R	0030027	cellular_component	lamellipodium
R	0030175	cellular_component	filopodium
R	0030240	biological_process	skeletal muscle thin filament assembly
R	0035865	biological_process	cellular response to potassium ion
R	0043503	biological_process	skeletal muscle fiber adaptation
R	0044297	cellular_component	cell body
R	0048545	biological_process	response to steroid hormone
R	0048741	biological_process	skeletal muscle fiber development
R	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
E	TYR55-GLY65

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

Chain	Residue	Details
E	TRP358-GLU366

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

Chain	Residue	Details
E	LEU106-ARG118

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	150
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	12
Details	Modified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
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	6
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	76
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	108
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	12
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07951","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	12
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06753","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07951","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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