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Reviewed, UniProtKB/Swiss-Prot P62157 (CALM_BOVIN)

Last modified June 16, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Calmodulin
      Short name=CaM
Gene names
Name: CALM
Synonyms: CAM
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length149 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Calmodulin mediates the control of a large number of enzymes and other proteins by Ca2+. Among the enzymes to be stimulated by the calmodulin-Ca2+ complex are a number of protein kinases and phosphatases. Together with CEP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis By similarity. Interacts with MYO1C.

Subunit structure

Interacts with CEP97, CEP110, TTN/titin and SRY By similarity.

Subcellular location

Spindle. Note: Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules By similarity.

Post-translational modification

Ubiquitination results in a strongly decreased activity.

Phosphorylation results in a decreased activity By similarity.

Miscellaneous

This protein has four functional calcium-binding sites.

Sequence similarities

Belongs to the calmodulin family.

Contains 4 EF-hand domains.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

O221791EBI-397403,EBI-1238013From a different organism.
P274501EBI-397403,EBI-1238108From a different organism.
Q2V3591EBI-397403,EBI-1235819From a different organism.
Q3E6U71EBI-397403,EBI-1239156From a different organism.
Q3EAG31EBI-397403,EBI-1238312From a different organism.
Q3EBV71EBI-397403,EBI-1235683From a different organism.
Q4PSE31EBI-397403,EBI-1238507From a different organism.
Q7X9N21EBI-397403,EBI-622264From a different organism.
Q84K401EBI-397403,EBI-1239149From a different organism.
Q84W011EBI-397403,EBI-1238923From a different organism.
Q8LPR41EBI-397403,EBI-1238087From a different organism.
Q8VZF41EBI-397403,EBI-1239168From a different organism.
Q93Z301EBI-397403,EBI-1237782From a different organism.
Q944J21EBI-397403,EBI-1238944From a different organism.
Q9FIW61EBI-397403,EBI-1237967From a different organism.
Q9FL191EBI-397403,EBI-622440From a different organism.
Q9FLL01EBI-397403,EBI-1238516From a different organism.
Q9LNX61EBI-397403,EBI-1238840From a different organism.
Q9LW661EBI-397403,EBI-1238066From a different organism.
Q9LX561EBI-397403,EBI-1235891From a different organism.
Q9SJX81EBI-397403,EBI-1238001From a different organism.
ABF4Q9M7Q21EBI-397403,EBI-1237867From a different organism.
ACA8Q9LF792EBI-397403,EBI-980643From a different organism.
AGL15Q388471EBI-397403,EBI-622076From a different organism.
AGL61Q4PSU41EBI-397403,EBI-1237976From a different organism.
AGL8Q388761EBI-397403,EBI-621912From a different organism.
AGL80Q9FJK31EBI-397403,EBI-622424From a different organism.
ALDH3F1Q70E961EBI-397403,EBI-1237774From a different organism.
ASK10Q390191EBI-397403,EBI-1238904From a different organism.
ASK6Q390101EBI-397403,EBI-1238323From a different organism.
At1g27190O045671EBI-397403,EBI-1238687From a different organism.
At1g34300Q9XID31EBI-397403,EBI-1238855From a different organism.
At1g54610Q9ZVM91EBI-397403,EBI-1235713From a different organism.
At1g58110Q84WC81EBI-397403,EBI-1237819From a different organism.
At1g60040Q9ZUI91EBI-397403,EBI-622185From a different organism.
At1g77145O806511EBI-397403,EBI-1238133From a different organism.
At3g02880Q9M8T01EBI-397403,EBI-1238677From a different organism.
At3g04430Q9M8441EBI-397403,EBI-1238479From a different organism.
At3g17600Q2VW981EBI-397403,EBI-1235997From a different organism.
At3g19100Q9LJL91EBI-397403,EBI-1238393From a different organism.
AT4g02410O812921EBI-397403,EBI-1237950From a different organism.
AT4g02640O227631EBI-397403,EBI-969959From a different organism.
AT4g34380Q9SZ031EBI-397403,EBI-1238343From a different organism.
At4g37240/C7A10_120Q8LE561EBI-397403,EBI-1237996From a different organism.
At5g49760/K2I5_13Q8GZ991EBI-397403,EBI-1238218From a different organism.
AtMg00870P925251EBI-397403,EBI-1238547From a different organism.
BIK1O488141EBI-397403,EBI-1238176From a different organism.
CDKB2-2Q8LG641EBI-397403,EBI-1235761From a different organism.
CIPK24Q9LDI31EBI-397403,EBI-537551From a different organism.
CIPK6O655541EBI-397403,EBI-537615From a different organism.
CKI1Q390501EBI-397403,EBI-1237881From a different organism.
CPK3Q424791EBI-397403,EBI-1235782From a different organism.
CPK30Q9SSF81EBI-397403,EBI-1235738From a different organism.
CRK40Q9SYS31EBI-397403,EBI-1238119From a different organism.
CRK9O654691EBI-397403,EBI-1238158From a different organism.
CYP705A20Q9LJY71EBI-397403,EBI-1237907From a different organism.
dl4570wO235521EBI-397403,EBI-1235805From a different organism.
EGFRP005331EBI-397403,EBI-297353From a different organism.
EgfrQ9QX701EBI-397403,EBI-1256812From a different organism.
ERBB2P046261EBI-397403,EBI-641062From a different organism.
F11C1_150Q9SND61EBI-397403,EBI-1235872From a different organism.
F14F8_210Q9LFU31EBI-397403,EBI-1237805From a different organism.
F18O21_230Q9LYL61EBI-397403,EBI-1238139From a different organism.
F7H19.240O827541EBI-397403,EBI-1238561From a different organism.
FBW2Q9ZPE41EBI-397403,EBI-604740From a different organism.
FBX14Q8RWQ81EBI-397403,EBI-1235922From a different organism.
GBF1P427741EBI-397403,EBI-1239126From a different organism.
GRB7Q144511EBI-397403,EBI-970191From a different organism.
HSP81-2P557371EBI-397403,EBI-1235834From a different organism.
LRR-RLKQ3ECN41EBI-397403,EBI-1238268From a different organism.
LRR-RLKQ8VYG71EBI-397403,EBI-1238236From a different organism.
LRR-RLKQ9LSI91EBI-397403,EBI-1238253From a different organism.
LRR-RLKQ9M9C51EBI-397403,EBI-1238661From a different organism.
MHKP432941EBI-397403,EBI-1238022From a different organism.
MPK1Q390211EBI-397403,EBI-1238932From a different organism.
MPK18Q9C5C01EBI-397403,EBI-1238534From a different organism.
NEK7Q9LHI71EBI-397403,EBI-1238055From a different organism.
PCKAQ9T0741EBI-397403,EBI-1238593From a different organism.
PEPKR2Q8W4901EBI-397403,EBI-1238381From a different organism.
psbAP837551EBI-397403,EBI-1236013From a different organism.
RKF3P930501EBI-397403,EBI-1238281From a different organism.
RPK1Q9ZRF91EBI-397403,EBI-1238953From a different organism.
SCL23Q9FHZ11EBI-397403,EBI-1238460From a different organism.
SHP1Q5XXJ31EBI-397403,EBI-1237985From a different organism.
TT16Q8RYD91EBI-397403,EBI-621993From a different organism.
WAKL21Q8GYF51EBI-397403,EBI-1238355From a different organism.
WRKY50Q8VWQ51EBI-397403,EBI-1239177From a different organism.
WRKY53Q9SUP61EBI-397403,EBI-1235980From a different organism.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4 Ref.5 Ref.6
Chain2 – 149148Calmodulin
PRO_0000198222

Regions

Domain8 – 4336EF-hand 1
Domain44 – 7936EF-hand 2
Domain81 – 11636EF-hand 3
Domain117 – 14933EF-hand 4
Calcium binding21 – 32121
Calcium binding57 – 68122
Calcium binding94 – 105123
Calcium binding130 – 141124

Amino acid modifications

Modified residue21N-acetylalanine Ref.5
Modified residue451Phosphothreonine; by CaMK4 By similarity
Modified residue1001Phosphotyrosine By similarity
Modified residue1161N6,N6,N6-trimethyllysine Ref.5 Ref.8
Cross-link22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6

Secondary structure

1 ....................... 149
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P62157-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6B4BC3FCDE10727B

FASTA14916,838
        10         20         30         40         50         60 
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG 

        70         80         90        100        110        120 
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE 

       130        140 
EVDEMIREAD IDGDGQVNYE EFVQMMTAK

« Hide

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References

« Hide 'large scale' references
[1]"Characterization of gene expression profiles in early bovine pregnancy using a custom cDNA microarray."
Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.
Mol. Reprod. Dev. 65:9-18(2003) [PubMed: 12658628] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus and Hereford.
Tissue: Fetal pons, Ileum and Uterus.
[3]"The amino acid sequence of the troponin C-like protein (modulator protein) from bovine uterus."
Grand R.J.A., Perry S.V.
FEBS Lett. 92:137-142(1978)
Cited for: PROTEIN SEQUENCE OF 2-149.
Tissue: Uterus.
[4]"Determination of the complete amino acid sequence of calmodulin (phenylalanine-rich acidic protein II) from bovine brain."
Kasai H., Kato Y., Isobe T., Kawasaki H., Okuyama T.
Biomed. Res. 1:248-264(1980)
Cited for: PROTEIN SEQUENCE OF 2-149.
Tissue: Brain.
[5]"The complete amino acid sequence of the Ca2+-dependent modulator protein (calmodulin) of bovine brain."
Watterson D.M., Sharief F., Vanaman T.C.
J. Biol. Chem. 255:962-975(1980) [PubMed: 7356670] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, METHYLATION AT LYS-116.
Tissue: Brain.
[6]"Modulation of calmodulin function by ubiquitin-calmodulin ligase and identification of the responsible ubiquitylation site in vertebrate calmodulin."
Laub M., Steppuhn J.A., Blueggel M., Immler D., Meyer H.E., Jennissen H.P.
Eur. J. Biochem. 255:422-431(1998) [PubMed: 9716384] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-28, UBIQUITINATION AT LYS-22.
[7]"Heat-resistant inhibitors of protein kinase C from bovine brain."
Pribilla I., Krueger H., Buchner K., Otto H., Schiebler W., Tripier D., Hucho F.
Eur. J. Biochem. 177:657-664(1988) [PubMed: 3058479] [Abstract]
Cited for: PROTEIN SEQUENCE OF 39-61.
[8]Weise C.
Unpublished observations (OCT-2002)
Cited for: METHYLATION AT LYS-116.
[9]"Domain Structure of a mammalian myosin I-beta."
Reizes O., Barylko B., Li C., Suedhof T.C., Albenisi J.P.
Proc. Natl. Acad. Sci. U.S.A. 91:6349-6353(1994) [PubMed: 8022785] [Abstract]
Cited for: INTERACTION WITH MYO1C.
[10]"Two trifluoperazine-binding sites on calmodulin predicted from comparative molecular modeling with troponin-C."
Strynadka N.C.J., James M.N.G.
Proteins 3:1-17(1988) [PubMed: 3375233] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF TRIMETHYLATED CALMODULIN.
[11]"Solution structure of the paramagnetic complex of the N-terminal domain of calmodulin with two Ce3+ ions by 1H NMR."
Bentrop D., Bertini I., Cremonini M.A., Forsen S., Luchinat C., Malmendal A.
Biochemistry 36:11605-11618(1997) [PubMed: 9305950] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-75.
[12]"The structure of apo-calmodulin. A 1H NMR examination of the carboxy-terminal domain."
Finn B.E., Drakenberg T., Forsen S.
FEBS Lett. 336:368-374(1993) [PubMed: 8262263] [Abstract]
Cited for: STRUCTURE BY NMR OF 77-149.
[13]"Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex."
Meador W.E., Means A.R., Quiocho F.A.
Science 257:1251-1255(1992) [PubMed: 1519061] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[14]"Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures."
Meador W.E., Means A.R., Quiocho F.A.
Science 262:1718-1721(1993) [PubMed: 8259515] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-148.
[15]"The linker of des-Glu84-calmodulin is bent."
Raghunathan S., Chandross R.J., Cheng B.P., Persechini A., Sobottka S.E., Kretsinger R.H.
Proc. Natl. Acad. Sci. U.S.A. 90:6869-6873(1993) [PubMed: 8341712] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 6-148 GLU-85 DEL.
[16]"Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex."
Cook W.J., Walter L.J., Walter M.R.
Biochemistry 33:15259-15265(1994) [PubMed: 7803388] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
[17]"Trifluoperazine-induced conformational change in Ca(2+)-calmodulin."
Vandonselaar M., Hickie R.A., Quail J.W., Delbaere L.T.
Nat. Struct. Biol. 1:795-801(1994) [PubMed: 7634090] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4-149.
[18]"Motions of calmodulin characterized using both Bragg and diffuse X-ray scattering."
Wall M.E., Clarage J.B., Phillips G.N.
Structure 5:1599-1612(1997) [PubMed: 9438860] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-147.
[19]"Structure of Escherichia coli fragment TR2C from calmodulin to 1.7 A resolution."
Olsson L.L., Sjolin L.
Acta Crystallogr. D 57:664-669(2001) [PubMed: 11320306] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 79-149.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AB099053 mRNA. Translation: BAC56543.1.
BC105380 mRNA. Translation: AAI05381.1.
BC120080 mRNA. Translation: AAI20081.1.
BC123890 mRNA. Translation: AAI23891.1.
IPIIPI00695508.
PIRMCBO. A90719.
RefSeqNP_001039714.1.
UniGeneBt.12896
Bt.53264
Bt.61778
Bt.63542

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1A29X-ray2.74A2-148[»]
1AK8NMR-A1-76[»]
1CDMX-ray2.00A5-148[»]
1CM1X-ray2.00A2-149[»]
1CM4X-ray2.00A2-149[»]
1CMFNMR-A77-148[»]
1CMGNMR-A77-148[»]
1DEGX-ray2.90A6-148[»]
1FW4X-ray1.70A79-149[»]
1LINX-ray2.00A2-149[»]
1PRWX-ray1.70A2-148[»]
1QIVX-ray2.64A1-149[»]
1QIWX-ray2.30A/B1-149[»]
1XA5X-ray2.12A2-148[»]
2CLNmodel-A1-149[»]
2FOTX-ray2.45A2-149[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP62157. 89 interactions.

Proteomic databases

PRIDEP62157.

Genome annotation databases

EnsemblENSBTAG00000014583. Bos taurus. [Contig view]
GeneID520277.
KEGGbta:520277.

Phylogenomic databases

HOVERGENP62157.
OMAP62157. DEQIAEF.

Family and domain databases

InterProIPR011992. EF-Hand_type.
IPR018248. EF_hand.
IPR018247. EF_HAND_1.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
IPR001125. Recoverin.
[Graphical view]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 1 hit.
PfamPF00036. efhand. 4 hits.
[Graphical view]
PRINTSPR00450. RECOVERIN.
ProDomPD000012. EF-hand. 2 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00054. EFh. 4 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameCALM_BOVIN
AccessionPrimary (citable) accession number: P62157
Secondary accession number(s): P02593 expand/collapse secondary AC list , P70667, P99014, Q08D84, Q2KJE6, Q61379, Q61380
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents