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 Q5E9V3

Entry ID Method Resolution Chain Position Source
AF-Q5E9V3-F1 Predicted AlphaFoldDB

19 variants for Q5E9V3

Variant ID(s) Position Change Description Diseaes Association Provenance
rs456221414 8 V>G No EVA
rs475010972 27 V>G No EVA
rs458500346 29 V>I No EVA
rs438073441 48 S>A No EVA
rs452166714 75 Y>H No EVA
rs378463335 97 L>F No EVA
rs434155650 106 F>S No EVA
rs1114453477 153 E>D No EVA
rs450209818 169 K>R No EVA
rs464344314 170 F>L No EVA
rs478345031 170 F>S No EVA
rs447514164 171 F>V No EVA
rs454143496 202 V>G No EVA
rs434115960 207 P>Q No EVA
rs437834266 239 W>L No EVA
rs469129597 242 E>G No EVA
rs445565861 249 T>S No EVA
rs476812267 255 D>Y No EVA
rs460200203 258 I>L No EVA

No associated diseases with Q5E9V3

No regional properties for Q5E9V3

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q5E9V3

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, myofibril, sarcomere, Z line
  • Colocalizes with ACTN1 and PPP3CA at the Z-line of heart and skeletal muscle
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
actin cytoskeleton The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.
Z disc Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.

3 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
FATZ binding Binding to a member of the FATZ family of proteins, filamin-, actinin-, and telethonin-binding proteins of the Z-disc of striated muscle. FATZ proteins are located in the Z-disc of the sarcomere and are involved in a complex network of interactions with other Z-band components.
telethonin binding Binding to telethonin, a protein found in the Z disc of striated muscle and which is a substrate of the titin kinase.

5 GO annotations of biological process

Name Definition
negative regulation of calcineurin-NFAT signaling cascade Any process that stops, prevents, or reduces the frequency, rate or extent of the calcineurin-NFAT signaling cascade.
negative regulation of transcription by RNA polymerase II Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II.
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 fiber adaptation Any process in which the skeletal muscle fibers change their phenotypic profiles in response to altered functional demands and a variety of signals. Muscle fibers are formed by the maturation of myotubes. They can be classed as slow, intermediate/fast or fast.
skeletal muscle tissue development The developmental sequence of events leading to the formation of adult skeletal muscle tissue. The main events are: the fusion of myoblasts to form myotubes that increase in size by further fusion to them of myoblasts, the formation of myofibrils within their cytoplasm and the establishment of functional neuromuscular junctions with motor neurons. At this stage they can be regarded as mature muscle fibers.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9NPC6 MYOZ2 Myozenin-2 Homo sapiens (Human) PR
Q9JJW5 Myoz2 Myozenin-2 Mus musculus (Mouse) PR
10 20 30 40 50 60
MLSHNTMVKQ RKQQASAIMK EIHGNDVDVM HLGKKVSIPR DIMLEELSHL SNRGARLFKM
70 80 90 100 110 120
RQRRSDKYTF ENFQYETKAQ INHNIAMQNE KLDGINLESG SQQAPFTPPN TPDPRSPPNP
130 140 150 160 170 180
ENIAPGYSGP LKEIPPERFN TTAVPKYYQS PWEQAISNDP ELLEALYPKF FKPEGKAELP
190 200 210 220 230 240
DYRSFNRVAT PFGGFEKASK MVKFKVPDFD LLLLTDPRFM AFANPLSGRR SFNRTPKGWI
250 260
SENIPIVITT EPTEDNTIPE SEDL