SCUBA

CALD1 — Caldesmon 1

CALD1 belongs to a gene co-expression module in 5 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

CALD1's module in each cell type

Cell typeModuleShares the module with
EndothelialVascular Tone Regulation
Endothelial cell development
ADAMTS6, ATP1A1, ATP1B3, ATP5PF, CAVIN3, CCDC3, CD81, HMOX2 +13 moreView in SCUBA
Glial cellsActin Remodeling Migration
migration & adhesion
CAST, CD46, GLIPR2, GSTK1, KTN1, SPATA13, TCEAL4View in SCUBA
Lymphatic endothelialLymphatic Specification
endothelial development
ARHGAP29, BOD1L1, CLCN3, DECR1, GCC2, MINDY2, MPHOSPH8, MTUS1 +9 moreView in SCUBA
PericytesPericyte ECM Production
ECM production
AEBP1, COL14A1, GUCY1B1, LURAP1L, PMP22, SDC2, TPPP3, VCLView in SCUBA
Smooth muscle cellsSMC contractile apparatus
Contractility
ACTA2, ACTB, CAV1, DSTN, MYL6, MYL9, PPP1R14A, SH3BGRL +2 moreView in SCUBA

About the gene

SynonymsCDM, H-CAD, h-CD, L-CAD
Chromosome7: 134744252-134970729
Predicted locationIntracellular
Essential geneNo
Protein classPlasma proteins, Predicted intracellular proteins
Molecular functionActin-binding, Calmodulin-binding, Muscle protein

Function

Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also plays an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity).

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.