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P11798

- KCC2A_MOUSE

UniProt

P11798 - KCC2A_MOUSE

Protein

Calcium/calmodulin-dependent protein kinase type II subunit alpha

Gene

Camk2a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    CaM-kinase II (CAMK2) is a prominent kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release. Member of the NMDAR signaling complex in excitatory synapses it may regulate NMDAR-dependent potentiation of the AMPAR and synaptic plasticity By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Autophosphorylation of Thr-286 allows the kinase to switch from a calmodulin-dependent to a calmodulin-independent state.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei42 – 421ATPPROSITE-ProRule annotation
    Active sitei135 – 1351Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi19 – 279ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calmodulin-dependent protein kinase activity Source: UniProtKB-EC
    3. glutamate receptor binding Source: MGI
    4. protein binding Source: IntAct
    5. protein serine/threonine kinase activity Source: MGI

    GO - Biological processi

    1. calcium ion transport Source: MGI
    2. G1/S transition of mitotic cell cycle Source: MGI
    3. peptidyl-serine phosphorylation Source: MGI
    4. positive regulation of calcium ion transport Source: MGI
    5. positive regulation of cardiac muscle cell apoptotic process Source: MGI
    6. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
    7. protein autophosphorylation Source: MGI
    8. regulation of mitochondrial membrane permeability involved in apoptotic process Source: MGI
    9. regulation of neuronal synaptic plasticity Source: MGI
    10. regulation of neurotransmitter secretion Source: MGI
    11. response to ischemia Source: MGI

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.17. 3474.
    ReactomeiREACT_198244. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_198246. CREB phosphorylation through the activation of Ras.
    REACT_198248. CREB phosphorylation through the activation of CaMKII.
    REACT_198660. Interferon gamma signaling.
    REACT_213550. HSF1-dependent transactivation.
    REACT_221970. Ca2+ pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcium/calmodulin-dependent protein kinase type II subunit alpha (EC:2.7.11.17)
    Short name:
    CaM kinase II subunit alpha
    Short name:
    CaMK-II subunit alpha
    Gene namesi
    Name:Camk2a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:88256. Camk2a.

    Subcellular locationi

    Isoform Alpha KAP : Cytoplasm Curated. Cell junctionsynapsepresynaptic cell membrane By similarity. Cell junctionsynapse By similarity
    Note: Postsynaptic lipid rafts.By similarity

    GO - Cellular componenti

    1. calcium- and calmodulin-dependent protein kinase complex Source: UniProtKB
    2. cell junction Source: UniProtKB-KW
    3. mitochondrion Source: GOC
    4. presynaptic membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Membrane, Synapse

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 478478Calcium/calmodulin-dependent protein kinase type II subunit alphaPRO_0000086092Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei13 – 131Phosphotyrosine1 Publication
    Modified residuei286 – 2861Phosphothreonine; by autocatalysis

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP11798.
    PaxDbiP11798.
    PRIDEiP11798.

    PTM databases

    PhosphoSiteiP11798.

    Expressioni

    Tissue specificityi

    Isoform Alpha CaMKII is expressed in brain while isoform Alpha KAP is expressed in skeletal muscle.

    Gene expression databases

    ArrayExpressiP11798.
    BgeeiP11798.
    GenevestigatoriP11798.

    Interactioni

    Subunit structurei

    CAMK2 is composed of four different chains: alpha, beta, gamma, and delta. The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 8 to 12 subunits. Interacts with BAALC, MPDZ, SYN1, CAMK2N2 and SYNGAP1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Actn2Q9JI913EBI-400384,EBI-299169
    Bag6Q9Z1R23EBI-400402,EBI-644645
    Dlg4Q621083EBI-400384,EBI-300895
    Grin2bQ009603EBI-400384,EBI-396905From a different organism.
    Grin2bQ010976EBI-400384,EBI-400125
    Lrrc7P705872EBI-400384,EBI-7798464From a different organism.

    Protein-protein interaction databases

    BioGridi198461. 6 interactions.
    DIPiDIP-31593N.
    IntActiP11798. 26 interactions.
    MINTiMINT-136541.

    Structurei

    Secondary structure

    1
    478
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni338 – 3403
    Helixi341 – 36222
    Helixi366 – 3727
    Beta strandi373 – 3808
    Helixi382 – 3843
    Beta strandi389 – 3924
    Helixi393 – 4008
    Helixi404 – 4063
    Beta strandi410 – 42112
    Beta strandi423 – 43715
    Beta strandi445 – 45814
    Beta strandi461 – 47212

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HKXX-ray2.65A/B/C/D/E/F/G/H/I/J/K/L/M/N336-478[»]
    ProteinModelPortaliP11798.
    SMRiP11798. Positions 7-474.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11798.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 271259Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni290 – 30011Calmodulin-bindingAdd
    BLAST
    Regioni310 – 32011Interaction with BAALCBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00720000108643.
    HOGENOMiHOG000233016.
    HOVERGENiHBG108055.
    KOiK04515.
    OMAiDHQDEEN.
    OrthoDBiEOG7ZD1VM.
    TreeFamiTF315229.

    Family and domain databases

    InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
    IPR013543. Ca/CaM-dep_prot_kinase-assoc.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PANTHERiPTHR24347. PTHR24347. 1 hit.
    PfamiPF08332. CaMKII_AD. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Alpha CaMKII (identifier: P11798-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MATITCTRFT EEYQLFEELG KGAFSVVRRC VKVLAGQEYA AKIINTKKLS    50
    ARDHQKLERE ARICRLLKHP NIVRLHDSIS EEGHHYLIFD LVTGGELFED 100
    IVAREYYSEA DASHCIQQIL EAVLHCHQMG VVHRDLKPEN LLLASKLKGA 150
    AVKLADFGLA IEVEGEQQAW FGFAGTPGYL SPEVLRKDPY GKPVDLWACG 200
    VILYILLVGY PPFWDEDQHR LYQQIKAGAY DFPSPEWDTV TPEAKDLINK 250
    MLTINPSKRI TAAEALKHPW ISHRSTVASC MHRQETVDCL KKFNARRKLK 300
    GAILTTMLAT RNFSGGKSGG NKKNDGVKES SESTNTTIED EDTKVRKQEI 350
    IKVTEQLIEA ISNGDFESYT KMCDPGMTAF EPEALGNLVE GLDFHRFYFE 400
    NLWSRNSKPV HTTILNPHIH LMGDESACIA YIRITQYLDA GGIPRTAQSE 450
    ETRVWHRRDG KWQIVHFHRS GAPSVLPH 478
    Length:478
    Mass (Da):54,115
    Last modified:January 23, 2007 - v2
    Checksum:i306F416CCE9B5F62
    GO
    Isoform Alpha KAP (identifier: P11798-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-289: Missing.
         290-314: LKKFNARRKLKGAILTTMLATRNFS → MLLFLTLWALVPCLVLLTLYFLSST
         328-328: K → KKRKSSSSVQLM

    Note: Has no kinase activity.

    Show »
    Length:200
    Mass (Da):22,584
    Checksum:i3FB8D6A5C891CBD4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 401A → P in CAA32946. (PubMed:2543961)Curated
    Sequence conflicti169 – 1691A → R in CAA32946. (PubMed:2543961)Curated
    Sequence conflicti228 – 2281G → R in CAA32946. (PubMed:2543961)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 289289Missing in isoform Alpha KAP. 1 PublicationVSP_004767Add
    BLAST
    Alternative sequencei290 – 31425LKKFN…TRNFS → MLLFLTLWALVPCLVLLTLY FLSST in isoform Alpha KAP. 1 PublicationVSP_004768Add
    BLAST
    Alternative sequencei328 – 3281K → KKRKSSSSVQLM in isoform Alpha KAP. 1 PublicationVSP_004769

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14836 mRNA. Translation: CAA32946.1.
    X87142 mRNA. Translation: CAA60620.1.
    AK083245 mRNA. Translation: BAC38829.1.
    BC031745 mRNA. Translation: AAH31745.1.
    CCDSiCCDS29276.1. [P11798-1]
    CCDS29277.1. [P11798-2]
    PIRiJC6083.
    S04365.
    RefSeqiNP_001273738.1. NM_001286809.1.
    NP_033922.1. NM_009792.3. [P11798-2]
    NP_803126.1. NM_177407.4. [P11798-1]
    UniGeneiMm.131530.
    Mm.446530.

    Genome annotation databases

    EnsembliENSMUST00000102888; ENSMUSP00000099952; ENSMUSG00000024617. [P11798-1]
    ENSMUST00000115295; ENSMUSP00000110950; ENSMUSG00000024617. [P11798-2]
    GeneIDi12322.
    KEGGimmu:12322.
    UCSCiuc008fbg.2. mouse. [P11798-1]
    uc008fbh.2. mouse. [P11798-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14836 mRNA. Translation: CAA32946.1 .
    X87142 mRNA. Translation: CAA60620.1 .
    AK083245 mRNA. Translation: BAC38829.1 .
    BC031745 mRNA. Translation: AAH31745.1 .
    CCDSi CCDS29276.1. [P11798-1 ]
    CCDS29277.1. [P11798-2 ]
    PIRi JC6083.
    S04365.
    RefSeqi NP_001273738.1. NM_001286809.1.
    NP_033922.1. NM_009792.3. [P11798-2 ]
    NP_803126.1. NM_177407.4. [P11798-1 ]
    UniGenei Mm.131530.
    Mm.446530.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HKX X-ray 2.65 A/B/C/D/E/F/G/H/I/J/K/L/M/N 336-478 [» ]
    ProteinModelPortali P11798.
    SMRi P11798. Positions 7-474.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198461. 6 interactions.
    DIPi DIP-31593N.
    IntActi P11798. 26 interactions.
    MINTi MINT-136541.

    Chemistry

    BindingDBi P11798.

    PTM databases

    PhosphoSitei P11798.

    Proteomic databases

    MaxQBi P11798.
    PaxDbi P11798.
    PRIDEi P11798.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000102888 ; ENSMUSP00000099952 ; ENSMUSG00000024617 . [P11798-1 ]
    ENSMUST00000115295 ; ENSMUSP00000110950 ; ENSMUSG00000024617 . [P11798-2 ]
    GeneIDi 12322.
    KEGGi mmu:12322.
    UCSCi uc008fbg.2. mouse. [P11798-1 ]
    uc008fbh.2. mouse. [P11798-2 ]

    Organism-specific databases

    CTDi 815.
    MGIi MGI:88256. Camk2a.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00720000108643.
    HOGENOMi HOG000233016.
    HOVERGENi HBG108055.
    KOi K04515.
    OMAi DHQDEEN.
    OrthoDBi EOG7ZD1VM.
    TreeFami TF315229.

    Enzyme and pathway databases

    BRENDAi 2.7.11.17. 3474.
    Reactomei REACT_198244. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_198246. CREB phosphorylation through the activation of Ras.
    REACT_198248. CREB phosphorylation through the activation of CaMKII.
    REACT_198660. Interferon gamma signaling.
    REACT_213550. HSF1-dependent transactivation.
    REACT_221970. Ca2+ pathway.

    Miscellaneous databases

    ChiTaRSi CAMK2A. mouse.
    EvolutionaryTracei P11798.
    NextBioi 280898.
    PROi P11798.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11798.
    Bgeei P11798.
    Genevestigatori P11798.

    Family and domain databases

    InterProi IPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
    IPR013543. Ca/CaM-dep_prot_kinase-assoc.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    PANTHERi PTHR24347. PTHR24347. 1 hit.
    Pfami PF08332. CaMKII_AD. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the cDNA for the alpha subunit of calmodulin kinase II from mouse brain."
      Hanley R.M., Payne M.E., Cruzalegui F., Christenson M.A., Means A.R.
      Nucleic Acids Res. 17:3992-3992(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: ICR.
      Tissue: Brain.
    2. "An alternative, nonkinase product of the brain-specifically expressed Ca2+/calmodulin-dependent kinase II alpha isoform gene in skeletal muscle."
      Bayer K.-U., Loehler J., Harbers K.
      Mol. Cell. Biol. 16:29-36(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA KAP).
      Strain: BALB/c.
      Tissue: Skeletal muscle.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Hippocampus.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Eye.
    5. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 9-21; 33-42; 135-146; 260-267; 301-311; 329-344; 353-371; 397-405; 434-445 AND 470-478, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    6. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    7. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.

    Entry informationi

    Entry nameiKCC2A_MOUSE
    AccessioniPrimary (citable) accession number: P11798
    Secondary accession number(s): Q61284, Q6ZWN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 159 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3