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

168-188 (Activation loop from InterPro)

Target domain

25-309 (Protein kinase domain)

Relief mechanism

Assay

Autoinhibited structure

Activated structure

1 structures for P47812

Entry ID Method Resolution Chain Position Source
AF-P47812-F1 Predicted AlphaFoldDB

No variants for P47812

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P47812

No associated diseases with P47812

3 regional properties for P47812

Type Name Position InterPro Accession
domain Protein kinase domain 25 - 309 IPR000719
conserved_site Mitogen-activated protein (MAP) kinase, conserved site 60 - 163 IPR003527
binding_site Protein kinase, ATP binding site 31 - 55 IPR017441

Functions

Description
EC Number 2.7.11.24 Protein-serine/threonine kinases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
MAP kinase activity Catalysis of the reaction: protein + ATP = protein phosphate + ADP. This reaction is the phosphorylation of proteins. Mitogen-activated protein kinase; a family of protein kinases that perform a crucial step in relaying signals from the plasma membrane to the nucleus. They are activated by a wide range of proliferation- or differentiation-inducing signals; activation is strong with agonists such as polypeptide growth factors and tumor-promoting phorbol esters, but weak (in most cell backgrounds) by stress stimuli.
protein serine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate.

7 GO annotations of biological process

Name Definition
intracellular signal transduction The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell.
p38MAPK cascade An intracellular protein kinase cascade containing at least a p38 MAPK, a MAPKK and a MAP3K. The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinases in the downstream tier to transmit a signal within a cell.
positive regulation of myoblast differentiation Any process that activates or increases the frequency, rate or extent of myoblast differentiation. A myoblast is a mononucleate cell type that, by fusion with other myoblasts, gives rise to the myotubes that eventually develop into skeletal muscle fibers.
positive regulation of myoblast fusion Any process that activates or increases the frequency, rate or extent of myoblast fusion.
positive regulation of myotube differentiation Any process that activates, maintains or increases the frequency, rate or extent of myotube differentiation. Myotube differentiation is the process in which a relatively unspecialized cell acquires specialized features of a myotube cell. Myotubes are multinucleated cells that are formed when proliferating myoblasts exit the cell cycle, differentiate and fuse.
protein phosphorylation The process of introducing a phosphate group on to a protein.
regulation of transcription by RNA polymerase II Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSSNQSYVFY RQELNKTLWE VPDRYQNLTP VGSGAYGSVC SSFDTRTALR IAVKKLSRPF
70 80 90 100 110 120
QSIIHAKRTY RELRLLKHMK HENVIGLLDV FSPAKSFEEF NDVYLVTHLM GADLNNIVKC
130 140 150 160 170 180
QKLTDDHVQF LIYQILRGLK YIHSAGIIHR DLKPSNLAVN EDCELKILDF GLARHTDEEM
190 200 210 220 230 240
TGYVATRWYR APEIMLNWMH YNQTVDIWSV GCIMAELLTG RTLFPGTDHI DQLKLILRLV
250 260 270 280 290 300
GTPEPELLQK ISSEAARNYI QSLPYMPKMN FEDVFLGANP QAVDLLEKML VLDTDKRITA
310 320 330 340 350 360
AEALAHSYFA QYHDPDDEPI AEPYDQSFES RELDIEEWKR LTYEEVTCFV PPPLDSEEME
S