CHICK:CALM

Species (Taxon ID)	Gallus gallus (Chicken). (9031)
Gene Name(s)	CALM (synonyms: CAM)
Protein Name(s)	Calmodulin CaM
External Links
UniProt	P62149
EMBL	L00101 L00096 L00097 L00098 L00099 L00100 M36167 AJ720728
PIR	A92394
UniGene	Gga.11685
PDB	1AHR 1UP5 2BCX 2BKI 2KZ2 2M3S 2O5G 2O60 2VB6 3GOF 3GP2 4BYA
PDBsum	1AHR 1UP5 2BCX 2BKI 2KZ2 2M3S 2O5G 2O60 2VB6 3GOF 3GP2 4BYA
ProteinModelPortal	P62149
SMR	P62149
DIP	DIP-29154N
STRING	9031.ENSGALP00000037503
BindingDB	P62149
PaxDb	P62149
PRIDE	P62149
eggNOG	COG5126
HOVERGEN	HBG012180
InParanoid	P62149
OrthoDB	EOG7F7WBV
TreeFam	TF300912
Reactome	REACT_272591 REACT_275573 REACT_283814 REACT_285977 REACT_288861 REACT_289326 REACT_293967 REACT_299857 REACT_301600 REACT_308989 REACT_315717 REACT_318735 REACT_324415 REACT_326286 REACT_326506 REACT_327184 REACT_329972 REACT_335363 REACT_338002 REACT_343334 REACT_347414 REACT_353617 REACT_354094 REACT_359218 REACT_360300 REACT_360664
EvolutionaryTrace	P62149
NextBio	20873068
Proteomes	UP000000539
ExpressionAtlas	P62149
GO	GO:0034704 GO:0005813 GO:0070062 GO:0005634 GO:0030017 GO:0005876 GO:0000922 GO:0005509 GO:0017022 GO:0072542 GO:0005513 GO:0030801 GO:0051343 GO:0032516 GO:0035307 GO:0060316 GO:0055117 GO:0032465 GO:0002027 GO:0010880 GO:0021762
Gene3D	1.10.238.10
InterPro	IPR011992 IPR018247 IPR002048
Pfam	PF13499
SMART	SM00054
PROSITE	PS00018 PS50222

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
enables	GO:0051401	CH domain binding	PMID:18477568^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q99LM3	F	Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:14635127^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:19106096^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:19106096^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0097718	disordered domain specific binding	PMID:19106096^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P48539	F	Seeded From UniProt	complete
enables	GO:0097718	disordered domain specific binding	PMID:14635127^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P12957	F	Seeded From UniProt	complete
enables	GO:0008022	protein C-terminus binding	PMID:14635127^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P12957	F	Seeded From UniProt	complete
enables	GO:0017022	myosin binding	PMID:15037754^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q29122	F	Seeded From UniProt	complete
involved_in	GO:0019722	calcium-mediated signaling	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000549861 RGD:2257 TAIR:locus:2083700 TAIR:locus:2130035	P	Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002048 InterPro:IPR039030	F	Seeded From UniProt	complete
involved_in	GO:0019722	calcium-mediated signaling	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR039030	P	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Ishida, H et al. (2008) Solution structure of the calponin homology (CH) domain from the smoothelin-like 1 protein: a unique apocalmodulin-binding mode and the possible role of the C-terminal type-2 CH-domain in smooth muscle relaxation. J. Biol. Chem. 283 20569-78 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Permyakov, SE et al. (2003) Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin. Proteins 53 855-62 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Kleerekoper, QK & Putkey, JA (2009) PEP-19, an intrinsically disordered regulator of calmodulin signaling. J. Biol. Chem. 284 7455-64 PubMed GONUTS page
↑ Bahloul, A et al. (2004) The unique insert in myosin VI is a structural calcium-calmodulin binding site. Proc. Natl. Acad. Sci. U.S.A. 101 4787-92 PubMed GONUTS page
↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:18477568-1] Ishida, H et al. (2008) Solution structure of the calponin homology (CH) domain from the smoothelin-like 1 protein: a unique apocalmodulin-binding mode and the possible role of the C-terminal type-2 CH-domain in smooth muscle relaxation. J. Biol. Chem. 283 20569-78 PubMed GONUTS page

[PMID:14635127-2] 2.0 ^2.1 ^2.2 Permyakov, SE et al. (2003) Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin. Proteins 53 855-62 PubMed GONUTS page

[PMID:19106096-3] 3.0 ^3.1 ^3.2 Kleerekoper, QK & Putkey, JA (2009) PEP-19, an intrinsically disordered regulator of calmodulin signaling. J. Biol. Chem. 284 7455-64 PubMed GONUTS page

[PMID:15037754-4] Bahloul, A et al. (2004) The unique insert in myosin VI is a structural calcium-calmodulin binding site. Proc. Natl. Acad. Sci. U.S.A. 101 4787-92 PubMed GONUTS page

[PMID:21873635-5] Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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CHICK:CALM

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