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Protein
Submitted name:

Calmodulin

Gene

Calm2

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

CalciumUniRule annotation

Enzyme and pathway databases

ReactomeiREACT_271496. CREB phosphorylation through the activation of CaMKK.
REACT_272967. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_275454. Ca2+ pathway.
REACT_276289. CREB phosphorylation through the activation of CaMKII.
REACT_280475. VEGFR2 mediated vascular permeability.
REACT_281385. Smooth Muscle Contraction.
REACT_288006. Platelet degranulation.
REACT_288103. Activation of CaMK IV.
REACT_296726. VEGFR2 mediated cell proliferation.
REACT_303296. Glycogen breakdown (glycogenolysis).
REACT_305912. eNOS activation.
REACT_308497. CaM pathway.
REACT_310165. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_313751. Cam-PDE 1 activation.
REACT_333484. CaMK IV-mediated phosphorylation of CREB.
REACT_335974. Calmodulin induced events.
REACT_337505. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_337837. Synthesis of IP3 and IP4 in the cytosol.
REACT_340722. FCERI mediated Ca+2 mobilization.
REACT_341785. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_347698. Activation of Ca-permeable Kainate Receptor.
REACT_347820. Translocation of GLUT4 to the plasma membrane.
REACT_348359. DARPP-32 events.
REACT_362366. CLEC7A (Dectin-1) induces NFAT activation.
REACT_362390. RHO GTPases activate PAKs.
REACT_362399. RHO GTPases activate IQGAPs.

Names & Taxonomyi

Protein namesi
Submitted name:
CalmodulinImported
Gene namesi
Name:Calm2Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi2258. Calm2.

PTM / Processingi

Proteomic databases

PRIDEiD4ABV5.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000040477.

Structurei

3D structure databases

ProteinModelPortaliD4ABV5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

GeneTreeiENSGT00760000118901.
OMAiVMMAKKR.
OrthoDBiEOG7F7WBV.
PhylomeDBiD4ABV5.
TreeFamiTF300912.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D4ABV5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ
60 70 80 90 100
DMINEVDADG NGTIDFPEFL TMMARKMKDT DNEEEIREAF HVFDKDGNGY
110 120 130 140
ISAAELRHVT TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAK
Length:149
Mass (Da):16,815
Last modified:April 20, 2010 - v1
Checksum:i9D7734F73FFA798C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06084445 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENSRNOT00000046240; ENSRNOP00000040477; ENSRNOG00000030871.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06084445 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortaliD4ABV5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000040477.

Proteomic databases

PRIDEiD4ABV5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000046240; ENSRNOP00000040477; ENSRNOG00000030871.

Organism-specific databases

RGDi2258. Calm2.

Phylogenomic databases

GeneTreeiENSGT00760000118901.
OMAiVMMAKKR.
OrthoDBiEOG7F7WBV.
PhylomeDBiD4ABV5.
TreeFamiTF300912.

Enzyme and pathway databases

ReactomeiREACT_271496. CREB phosphorylation through the activation of CaMKK.
REACT_272967. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_275454. Ca2+ pathway.
REACT_276289. CREB phosphorylation through the activation of CaMKII.
REACT_280475. VEGFR2 mediated vascular permeability.
REACT_281385. Smooth Muscle Contraction.
REACT_288006. Platelet degranulation.
REACT_288103. Activation of CaMK IV.
REACT_296726. VEGFR2 mediated cell proliferation.
REACT_303296. Glycogen breakdown (glycogenolysis).
REACT_305912. eNOS activation.
REACT_308497. CaM pathway.
REACT_310165. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_313751. Cam-PDE 1 activation.
REACT_333484. CaMK IV-mediated phosphorylation of CREB.
REACT_335974. Calmodulin induced events.
REACT_337505. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_337837. Synthesis of IP3 and IP4 in the cytosol.
REACT_340722. FCERI mediated Ca+2 mobilization.
REACT_341785. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_347698. Activation of Ca-permeable Kainate Receptor.
REACT_347820. Translocation of GLUT4 to the plasma membrane.
REACT_348359. DARPP-32 events.
REACT_362366. CLEC7A (Dectin-1) induces NFAT activation.
REACT_362390. RHO GTPases activate PAKs.
REACT_362399. RHO GTPases activate IQGAPs.

Miscellaneous databases

NextBioi35574099.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  2. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiD4ABV5_RAT
AccessioniPrimary (citable) accession number: D4ABV5
Entry historyi
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: June 24, 2015
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.