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CHICK:CALM

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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 Extension 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

Notes

References

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

  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
  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
  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
  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
  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