Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P09739

Entry ID Method Resolution Chain Position Source
AF-P09739-F1 Predicted AlphaFoldDB

No variants for P09739

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P09739

No associated diseases with P09739

No regional properties for P09739

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P09739

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
troponin complex A complex of accessory proteins (typically troponin T, troponin I and troponin C) found associated with actin in muscle thin filaments; involved in calcium regulation of muscle contraction.

5 GO annotations of molecular function

Name Definition
calcium-dependent protein binding Binding to a protein or protein complex in the presence of calcium.
tropomyosin binding Binding to tropomyosin, a protein associated with actin filaments both in cytoplasm and, in association with troponin, in the thin filament of striated muscle.
troponin C binding Binding to troponin C, the calcium-binding subunit of the troponin complex.
troponin I binding Binding to troponin I, the inhibitory subunit of the troponin complex.
troponin T binding Binding to troponin T, the tropomyosin-binding subunit of the troponin complex.

7 GO annotations of biological process

Name Definition
muscle contraction A process in which force is generated within muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis.
positive regulation of calcium-dependent ATPase activity Any process that activates or increases the frequency, rate or extent of calcium-dependent ATPase activity.
regulation of ATP-dependent activity Any process that modulates the rate of an ATP-dependent activity.
regulation of muscle contraction Any process that modulates the frequency, rate or extent of muscle contraction.
regulation of striated muscle contraction Any process that modulates the frequency, rate or extent of striated muscle contraction.
sarcomere organization The myofibril assembly process that results in the organization of muscle actomyosin into sarcomeres. The sarcomere is the repeating unit of a myofibril in a muscle cell, composed of an array of overlapping thick and thin filaments between two adjacent Z discs.
skeletal muscle contraction A process in which force is generated within skeletal muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. In the skeletal muscle, the muscle contraction takes advantage of an ordered sarcomeric structure and in most cases it is under voluntary control.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P13789 TNNT2 Troponin T, cardiac muscle Bos taurus (Bovine) PR
P02642 TNNT2 Troponin T, cardiac muscle isoforms Gallus gallus (Chicken) PR
P45378 TNNT3 Troponin T, fast skeletal muscle Homo sapiens (Human) PR
P50752 Tnnt2 Troponin T, cardiac muscle Mus musculus (Mouse) PR
Q9QZ47 Tnnt3 Troponin T, fast skeletal muscle Mus musculus (Mouse) PR
P50753 Tnnt2 Troponin T, cardiac muscle Rattus norvegicus (Rat) PR
Q27371 mup-2 Troponin T Caenorhabditis elegans PR
10 20 30 40 50 60
MSDEETEQVE EQYEEEEEAQ EEEVQEEAPE PEEVQEEEKP RPKLTAPKIP EGEKVDFDDI
70 80 90 100 110 120
QKKRQNKDLM ELQALIDSHF EARKKEEEEL IALKERIEKR RAERAEQQRI RAEKERERQN
130 140 150 160 170 180
RLAEEKARRE EEDAKRRAED DLKKKKALSS MGANYSSYLA KADQKRGKKQ TAREMKKKIL
190 200 210 220 230 240
AERRKPLNID HLSDDKLRDK AKELWDTLYQ LETDKFEFGE KLKRQKYDIT TLRSRIDQAQ
250
KHSKKAGATA KGKVGGRWK