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1MYO

SOLUTION STRUCTURE OF MYOTROPHIN, NMR, 44 STRUCTURES

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006584biological_processcatecholamine metabolic process
A0008290cellular_componentF-actin capping protein complex
A0008361biological_processregulation of cell size
A0010557biological_processpositive regulation of macromolecule biosynthetic process
A0010613biological_processpositive regulation of cardiac muscle hypertrophy
A0021707biological_processcerebellar granule cell differentiation
A0030182biological_processneuron differentiation
A0030307biological_processpositive regulation of cell growth
A0030424cellular_componentaxon
A0043403biological_processskeletal muscle tissue regeneration
A0043565molecular_functionsequence-specific DNA binding
A0048471cellular_componentperinuclear region of cytoplasm
A0051092biological_processpositive regulation of NF-kappaB transcription factor activity
A0051146biological_processstriated muscle cell differentiation
A0051247biological_processpositive regulation of protein metabolic process
A0071260biological_processcellular response to mechanical stimulus
A2000812biological_processregulation of barbed-end actin filament capping
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylcysteine => ECO:0000269|PubMed:1633812
ChainResidueDetails
AASP3

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P58546
ChainResidueDetails
AGLU5
AASN12
AGLY25

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P58546
ChainResidueDetails
ALEU32

224931

PDB entries from 2024-09-11

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