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Q96RR4

- KKCC2_HUMAN

UniProt

Q96RR4 - KKCC2_HUMAN

Protein

Calcium/calmodulin-dependent protein kinase kinase 2

Gene

CAMKK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin-binding domain are inactive. Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca2+ signals By similarity. Seems to be involved in hippocampal activation of CREB1 By similarity. May play a role in neurite growth. Isoform 3 may promote neurite elongation, while isoform 1 may promoter neurite branching.By similarity4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Activated by Ca2+/calmodulin. Binding of calmodulin may relieve intrasteric autoinhibition. Autophosphorylation does not alter activity or regulation by Ca2+/calmodulin. In part, activity is independent on Ca2+/calmodulin By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei194 – 1941ATPPROSITE-ProRule annotation
    Active sitei312 – 3121Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi171 – 1799ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium ion binding Source: UniProtKB
    3. calmodulin binding Source: UniProtKB
    4. calmodulin-dependent protein kinase activity Source: UniProtKB-EC
    5. protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. calcium-mediated signaling Source: UniProtKB
    2. MAPK cascade Source: UniProtKB
    3. peptidyl-tyrosine phosphorylation Source: GOC
    4. positive regulation of transcription, DNA-templated Source: UniProtKB
    5. protein autophosphorylation Source: UniProtKB
    6. protein phosphorylation Source: UniProtKB
    7. regulation of protein kinase activity Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ96RR4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcium/calmodulin-dependent protein kinase kinase 2 (EC:2.7.11.17)
    Short name:
    CaM-KK 2
    Short name:
    CaM-kinase kinase 2
    Short name:
    CaMKK 2
    Alternative name(s):
    Calcium/calmodulin-dependent protein kinase kinase beta
    Short name:
    CaM-KK beta
    Short name:
    CaM-kinase kinase beta
    Short name:
    CaMKK beta
    Gene namesi
    Name:CAMKK2
    Synonyms:CAMKKB, KIAA0787
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:1470. CAMKK2.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm 1 Publication. Cell projection 1 Publication
    Note: Predominantly nuclear in unstimulated cells By similarity. Found in the cytoplasm and neurites after forskolin induction.By similarity

    GO - Cellular componenti

    1. cell projection Source: UniProtKB-SubCell
    2. cytoplasm Source: HPA
    3. intracellular Source: UniProtKB
    4. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26052.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 588587Calcium/calmodulin-dependent protein kinase kinase 2PRO_0000086144Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei129 – 1291PhosphoserineBy similarity
    Modified residuei133 – 1331PhosphoserineBy similarity
    Modified residuei495 – 4951Phosphoserine2 Publications

    Post-translational modificationi

    Autophosphorylated and phosphorylated by PKA. Each isoform may show a different pattern of phosphorylation.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96RR4.
    PaxDbiQ96RR4.
    PRIDEiQ96RR4.

    PTM databases

    PhosphoSiteiQ96RR4.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed with higher levels in the brain. Intermediate levels are detected in spleen, prostate, thyroid and leukocytes. The lowest level is in lung.1 Publication

    Inductioni

    Isoform 1 is up-regulated by PKA pathway.1 Publication

    Gene expression databases

    ArrayExpressiQ96RR4.
    BgeeiQ96RR4.
    CleanExiHS_CAMKK2.
    GenevestigatoriQ96RR4.

    Organism-specific databases

    HPAiHPA017389.

    Interactioni

    Subunit structurei

    Interacts with calmodulin.By similarity

    Protein-protein interaction databases

    BioGridi115889. 26 interactions.
    IntActiQ96RR4. 19 interactions.

    Structurei

    Secondary structure

    1
    588
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi165 – 1728
    Beta strandi178 – 1847
    Turni185 – 1884
    Beta strandi189 – 1979
    Helixi232 – 24110
    Beta strandi251 – 2566
    Beta strandi258 – 26811
    Helixi286 – 30520
    Helixi315 – 3173
    Beta strandi318 – 3203
    Beta strandi326 – 3283
    Beta strandi338 – 3414
    Helixi351 – 3533
    Helixi356 – 3583
    Beta strandi366 – 3683
    Helixi369 – 38517
    Helixi395 – 40410
    Beta strandi411 – 4133
    Helixi417 – 42610
    Turni431 – 4333
    Helixi437 – 4404
    Helixi444 – 4474

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZV2X-ray2.40A158-448[»]
    ProteinModelPortaliQ96RR4.
    SMRiQ96RR4. Positions 160-484.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96RR4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini165 – 446282Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni204 – 22623RP domainAdd
    BLAST
    Regioni472 – 4776Autoinhibitory domainBy similarity
    Regioni475 – 50026Calmodulin-bindingBy similarityAdd
    BLAST

    Domaini

    The autoinhibitory domain overlaps with the calmodulin binding region and may be involved in intrasteric autoinhibition.
    The RP domain (arginine/proline-rich) is involved in the recognition of CAMKI and CAMK4 as substrates.By similarity

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG052262.
    KOiK07359.
    OMAiMNGRCIC.
    OrthoDBiEOG7F5114.
    PhylomeDBiQ96RR4.
    TreeFamiTF313013.

    Family and domain databases

    InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
    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.
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96RR4-1) [UniParc]FASTAAdd to Basket

    Also known as: Beta1, CAMKK2+E16

    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

    MSSCVSSQPS SNRAAPQDEL GGRGSSSSES QKPCEALRGL SSLSIHLGME    50
    SFIVVTECEP GCAVDLGLAR DRPLEADGQE VPLDTSGSQA RPHLSGRKLS 100
    LQERSQGGLA AGGSLDMNGR CICPSLPYSP VSSPQSSPRL PRRPTVESHH 150
    VSITGMQDCV QLNQYTLKDE IGKGSYGVVK LAYNENDNTY YAMKVLSKKK 200
    LIRQAGFPRR PPPRGTRPAP GGCIQPRGPI EQVYQEIAIL KKLDHPNVVK 250
    LVEVLDDPNE DHLYMVFELV NQGPVMEVPT LKPLSEDQAR FYFQDLIKGI 300
    EYLHYQKIIH RDIKPSNLLV GEDGHIKIAD FGVSNEFKGS DALLSNTVGT 350
    PAFMAPESLS ETRKIFSGKA LDVWAMGVTL YCFVFGQCPF MDERIMCLHS 400
    KIKSQALEFP DQPDIAEDLK DLITRMLDKN PESRIVVPEI KLHPWVTRHG 450
    AEPLPSEDEN CTLVEVTEEE VENSVKHIPS LATVILVKTM IRKRSFGNPF 500
    EGSRREERSL SAPGNLLTKK PTRECESLSE LKEARQRRQP PGHRPAPRGG 550
    GGSALVRGSP CVESCWAPAP GSPARMHPLR PEEAMEPE 588

    Note: Major isoform.

    Length:588
    Mass (Da):64,746
    Last modified:January 11, 2011 - v2
    Checksum:i04E3583561341167
    GO
    Isoform 2 (identifier: Q96RR4-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta2

    The sequence of this isoform differs from the canonical sequence as follows:
         533-533: E → T
         534-554: Missing.
         555-588: Missing.

    Note: Major isoform.

    Show »
    Length:533
    Mass (Da):58,899
    Checksum:i98FAAB0FB8C4CACF
    GO
    Isoform 3 (identifier: Q96RR4-3) [UniParc]FASTAAdd to Basket

    Also known as: Beta1delta16, CAMKK2-E16

    The sequence of this isoform differs from the canonical sequence as follows:
         520-532: KPTRECESLSELK → QGSEDNLQGTDPP
         533-541: EARQRRQPP → PVGEEEVLL
         542-554: Missing.
         555-588: Missing.

    Note: Contains a phosphoserine at position 522.

    Show »
    Length:541
    Mass (Da):59,602
    Checksum:iD9A56C3D780C0DDE
    GO
    Isoform 4 (identifier: Q96RR4-4) [UniParc]FASTAAdd to Basket

    Also known as: Beta1delta14

    The sequence of this isoform differs from the canonical sequence as follows:
         442-484: Missing.

    Show »
    Length:545
    Mass (Da):59,971
    Checksum:iEE849E31E0416BC3
    GO
    Isoform 5 (identifier: Q96RR4-5) [UniParc]FASTAAdd to Basket

    Also known as: Beta1delta14/16, beta-3x

    The sequence of this isoform differs from the canonical sequence as follows:
         442-484: Missing.
         520-532: KPTRECESLSELK → QGSEDNLQGTDPP
         533-541: EARQRRQPP → PVGEEEVLL
         542-554: Missing.
         555-588: Missing.

    Note: Inactive. Does not activate CAMK1 and CAMK4. Contains a phosphoserine at position 479.

    Show »
    Length:498
    Mass (Da):54,827
    Checksum:i6D051947DDCB69E1
    GO
    Isoform 6 (identifier: Q96RR4-6) [UniParc]FASTAAdd to Basket

    Also known as: Beta2delta14

    The sequence of this isoform differs from the canonical sequence as follows:
         442-484: Missing.
         533-533: E → T
         534-554: Missing.
         555-588: Missing.

    Note: Inactive. Does not activate CAMK1 and CAMK4.

    Show »
    Length:490
    Mass (Da):54,124
    Checksum:i0821956F65E543C4
    GO
    Isoform 7 (identifier: Q96RR4-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         533-554: EARQRRQPPGHRPAPRGGGGSA → GTKKKKGLDSMTSTVAAGWLDRRV
         555-588: Missing.

    Show »
    Length:556
    Mass (Da):61,386
    Checksum:i47E33706CE77489C
    GO

    Sequence cautioni

    The sequence CAD38990.1 differs from that shown. Reason: Intron retention.
    The sequence AAC72943.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA34507.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti206 – 2061G → A in AAD31507. (PubMed:9822657)Curated
    Sequence conflicti331 – 3311F → I in BAF84761. (PubMed:14702039)Curated
    Sequence conflicti347 – 3471T → Y in AAD31507. (PubMed:9822657)Curated
    Sequence conflicti371 – 3711L → K in AAD31507. (PubMed:9822657)Curated
    Sequence conflicti554 – 5541A → H in AAK91829. (PubMed:11395482)Curated
    Sequence conflicti557 – 5571R → N in AAK91829. (PubMed:11395482)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti10 – 101S → N.1 Publication
    Corresponds to variant rs28360477 [ dbSNP | Ensembl ].
    VAR_032788
    Natural varianti85 – 851T → S.4 Publications
    Corresponds to variant rs3817190 [ dbSNP | Ensembl ].
    VAR_020532
    Natural varianti123 – 1231C → Y.1 Publication
    Corresponds to variant rs35403710 [ dbSNP | Ensembl ].
    VAR_040610
    Natural varianti127 – 1271P → L in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
    VAR_040611
    Natural varianti182 – 1821A → T in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040612
    Natural varianti363 – 3631R → C.
    Corresponds to variant rs1132780 [ dbSNP | Ensembl ].
    VAR_020533
    Natural varianti492 – 4921R → H.1 Publication
    Corresponds to variant rs34129994 [ dbSNP | Ensembl ].
    VAR_040613

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei442 – 48443Missing in isoform 4, isoform 5 and isoform 6. 2 PublicationsVSP_012142Add
    BLAST
    Alternative sequencei520 – 53213KPTRE…LSELK → QGSEDNLQGTDPP in isoform 3 and isoform 5. 4 PublicationsVSP_012143Add
    BLAST
    Alternative sequencei533 – 55422EARQR…GGGSA → GTKKKKGLDSMTSTVAAGWL DRRV in isoform 7. 2 PublicationsVSP_012148Add
    BLAST
    Alternative sequencei533 – 5419EARQRRQPP → PVGEEEVLL in isoform 3 and isoform 5. 4 PublicationsVSP_012144
    Alternative sequencei533 – 5331E → T in isoform 2 and isoform 6. 3 PublicationsVSP_012146
    Alternative sequencei534 – 55421Missing in isoform 2 and isoform 6. 3 PublicationsVSP_012147Add
    BLAST
    Alternative sequencei542 – 55413Missing in isoform 3 and isoform 5. 4 PublicationsVSP_012145Add
    BLAST
    Alternative sequencei555 – 58834Missing in isoform 2, isoform 3, isoform 5, isoform 6 and isoform 7. 8 PublicationsVSP_012149Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB081337 mRNA. Translation: BAC19841.1.
    AF287630 mRNA. Translation: AAK64600.1.
    AF287631 mRNA. Translation: AAK64601.1.
    AF321385 mRNA. Translation: AAL37215.1.
    AF321386 mRNA. Translation: AAL37216.1.
    AF321387 mRNA. Translation: AAL37217.1.
    AF321388 mRNA. Translation: AAL37218.1.
    AF321401
    , AF321390, AF321391, AF321392, AF321393, AF321394, AF321395, AF321396, AF321397, AF321398, AF321399, AF321400, AF321575, AF321576, AF321577, AF321578 Genomic DNA. Translation: AAK91830.1.
    AF321402
    , AF321390, AF321391, AF321392, AF321393, AF321394, AF321395, AF321396, AF321397, AF321398, AF321399, AF321400, AF321575, AF321576, AF321577, AF321578 Genomic DNA. Translation: AAK91829.1.
    AF140507 mRNA. Translation: AAD31507.1.
    AB081336 mRNA. Translation: BAC19840.1.
    AB018330 mRNA. Translation: BAA34507.2. Different initiation.
    AK292072 mRNA. Translation: BAF84761.1.
    AC069209 Genomic DNA. No translation available.
    BC000318 mRNA. Translation: AAH00318.2.
    BC026060 mRNA. Translation: AAH26060.1.
    AF101264 mRNA. Translation: AAD04566.1.
    AL834322 mRNA. Translation: CAD38990.1. Sequence problems.
    AF091074 mRNA. Translation: AAC72943.1. Different initiation.
    CCDSiCCDS44999.1. [Q96RR4-2]
    CCDS53837.1. [Q96RR4-6]
    CCDS58283.1. [Q96RR4-7]
    CCDS9216.1. [Q96RR4-1]
    CCDS9217.1. [Q96RR4-4]
    CCDS9218.1. [Q96RR4-3]
    CCDS9219.1. [Q96RR4-5]
    PIRiJE0191.
    RefSeqiNP_001257414.1. NM_001270485.1. [Q96RR4-1]
    NP_001257415.1. NM_001270486.1. [Q96RR4-7]
    NP_006540.3. NM_006549.3. [Q96RR4-1]
    NP_705719.2. NM_153499.2. [Q96RR4-3]
    NP_705720.1. NM_153500.1. [Q96RR4-5]
    NP_757363.1. NM_172214.2. [Q96RR4-2]
    NP_757364.1. NM_172215.2. [Q96RR4-6]
    NP_757365.1. NM_172216.1. [Q96RR4-4]
    NP_757380.1. NM_172226.2. [Q96RR4-3]
    XP_005253880.1. XM_005253823.1. [Q96RR4-2]
    XP_005253881.1. XM_005253824.2. [Q96RR4-5]
    UniGeneiHs.297343.

    Genome annotation databases

    GeneIDi10645.
    KEGGihsa:10645.
    UCSCiuc001tzt.3. human. [Q96RR4-3]
    uc001tzu.3. human. [Q96RR4-1]
    uc001tzw.3. human. [Q96RR4-4]
    uc001tzy.3. human. [Q96RR4-5]
    uc001uaa.2. human. [Q96RR4-7]
    uc001uab.3. human. [Q96RR4-2]
    uc001uac.3. human. [Q96RR4-6]

    Polymorphism databases

    DMDMi317373374.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB081337 mRNA. Translation: BAC19841.1 .
    AF287630 mRNA. Translation: AAK64600.1 .
    AF287631 mRNA. Translation: AAK64601.1 .
    AF321385 mRNA. Translation: AAL37215.1 .
    AF321386 mRNA. Translation: AAL37216.1 .
    AF321387 mRNA. Translation: AAL37217.1 .
    AF321388 mRNA. Translation: AAL37218.1 .
    AF321401
    , AF321390 , AF321391 , AF321392 , AF321393 , AF321394 , AF321395 , AF321396 , AF321397 , AF321398 , AF321399 , AF321400 , AF321575 , AF321576 , AF321577 , AF321578 Genomic DNA. Translation: AAK91830.1 .
    AF321402
    , AF321390 , AF321391 , AF321392 , AF321393 , AF321394 , AF321395 , AF321396 , AF321397 , AF321398 , AF321399 , AF321400 , AF321575 , AF321576 , AF321577 , AF321578 Genomic DNA. Translation: AAK91829.1 .
    AF140507 mRNA. Translation: AAD31507.1 .
    AB081336 mRNA. Translation: BAC19840.1 .
    AB018330 mRNA. Translation: BAA34507.2 . Different initiation.
    AK292072 mRNA. Translation: BAF84761.1 .
    AC069209 Genomic DNA. No translation available.
    BC000318 mRNA. Translation: AAH00318.2 .
    BC026060 mRNA. Translation: AAH26060.1 .
    AF101264 mRNA. Translation: AAD04566.1 .
    AL834322 mRNA. Translation: CAD38990.1 . Sequence problems.
    AF091074 mRNA. Translation: AAC72943.1 . Different initiation.
    CCDSi CCDS44999.1. [Q96RR4-2 ]
    CCDS53837.1. [Q96RR4-6 ]
    CCDS58283.1. [Q96RR4-7 ]
    CCDS9216.1. [Q96RR4-1 ]
    CCDS9217.1. [Q96RR4-4 ]
    CCDS9218.1. [Q96RR4-3 ]
    CCDS9219.1. [Q96RR4-5 ]
    PIRi JE0191.
    RefSeqi NP_001257414.1. NM_001270485.1. [Q96RR4-1 ]
    NP_001257415.1. NM_001270486.1. [Q96RR4-7 ]
    NP_006540.3. NM_006549.3. [Q96RR4-1 ]
    NP_705719.2. NM_153499.2. [Q96RR4-3 ]
    NP_705720.1. NM_153500.1. [Q96RR4-5 ]
    NP_757363.1. NM_172214.2. [Q96RR4-2 ]
    NP_757364.1. NM_172215.2. [Q96RR4-6 ]
    NP_757365.1. NM_172216.1. [Q96RR4-4 ]
    NP_757380.1. NM_172226.2. [Q96RR4-3 ]
    XP_005253880.1. XM_005253823.1. [Q96RR4-2 ]
    XP_005253881.1. XM_005253824.2. [Q96RR4-5 ]
    UniGenei Hs.297343.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ZV2 X-ray 2.40 A 158-448 [» ]
    ProteinModelPortali Q96RR4.
    SMRi Q96RR4. Positions 160-484.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115889. 26 interactions.
    IntActi Q96RR4. 19 interactions.

    Chemistry

    BindingDBi Q96RR4.
    ChEMBLi CHEMBL5284.
    GuidetoPHARMACOLOGYi 1957.

    PTM databases

    PhosphoSitei Q96RR4.

    Polymorphism databases

    DMDMi 317373374.

    Proteomic databases

    MaxQBi Q96RR4.
    PaxDbi Q96RR4.
    PRIDEi Q96RR4.

    Protocols and materials databases

    DNASUi 10645.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 10645.
    KEGGi hsa:10645.
    UCSCi uc001tzt.3. human. [Q96RR4-3 ]
    uc001tzu.3. human. [Q96RR4-1 ]
    uc001tzw.3. human. [Q96RR4-4 ]
    uc001tzy.3. human. [Q96RR4-5 ]
    uc001uaa.2. human. [Q96RR4-7 ]
    uc001uab.3. human. [Q96RR4-2 ]
    uc001uac.3. human. [Q96RR4-6 ]

    Organism-specific databases

    CTDi 10645.
    GeneCardsi GC12M121675.
    H-InvDB HIX0011079.
    HIX0171630.
    HIX0171665.
    HGNCi HGNC:1470. CAMKK2.
    HPAi HPA017389.
    MIMi 615002. gene.
    neXtProti NX_Q96RR4.
    PharmGKBi PA26052.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG052262.
    KOi K07359.
    OMAi MNGRCIC.
    OrthoDBi EOG7F5114.
    PhylomeDBi Q96RR4.
    TreeFami TF313013.

    Enzyme and pathway databases

    SignaLinki Q96RR4.

    Miscellaneous databases

    ChiTaRSi CAMKK2. human.
    EvolutionaryTracei Q96RR4.
    GeneWikii CAMKK2.
    GenomeRNAii 10645.
    NextBioi 40461.
    PROi Q96RR4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96RR4.
    Bgeei Q96RR4.
    CleanExi HS_CAMKK2.
    Genevestigatori Q96RR4.

    Family and domain databases

    InterProi IPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
    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 PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    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. "Human Ca2+/calmodulin-dependent protein kinase kinase beta gene encodes multiple isoforms that display distinct kinase activity."
      Hsu L.-S., Chen G.-D., Lee L.-S., Chi C.-W., Cheng J.-F., Chen J.-Y.
      J. Biol. Chem. 276:31113-31123(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), FUNCTION, VARIANT SER-85.
    2. "Components of a calmodulin-dependent protein kinase cascade. Molecular cloning, functional characterization and cellular localization of Ca2+/calmodulin-dependent protein kinase kinase beta."
      Anderson K.A., Means R.L., Huang Q.-H., Kemp B.E., Goldstein E.G., Selbert M.A., Edelman A.M., Fremeau R.T., Means A.R.
      J. Biol. Chem. 273:31880-31889(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain cortex.
    3. "Identification and characterization of novel components of a Ca2+/calmodulin-dependent protein kinase cascade in HeLa cells."
      Ishikawa Y., Tokumitsu H., Inuzuka H., Murata-Hori M., Hosoya H., Kobayashi R.
      FEBS Lett. 550:57-63(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION IN PHOSPHORYLATION OF CAMK1D.
    4. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7), VARIANT SER-85.
      Tissue: Brain.
    5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Stomach.
    7. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 233-588 (ISOFORM 5), VARIANT SER-85.
      Tissue: Placenta.
    9. "Cloning, expression and chromosomal localization of human Ca2+/calmodulin-dependent protein kinase kinase."
      Hsu L.-S., Tsou A.-P., Chi C.-W., Lee C.-H., Chen J.-Y.
      J. Biomed. Sci. 5:141-149(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 117-588 (ISOFORM 2), FUNCTION IN PHOSPHORYLATION OF CAMK1, TISSUE SPECIFICITY.
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-588 (ISOFORM 7).
      Tissue: Amygdala.
    11. "Full-insert sequence of mapped XREF EST."
      Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 338-533 (ISOFORM 2).
    12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Differential effects of PKA-controlled CaMKK2 variants on neuronal differentiation."
      Cao W., Sohail M., Liu G., Koumbadinga G.A., Lobo V.G., Xie J.
      RNA Biol. 8:1061-1072(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, PHOSPHORYLATION BY PKA, INDUCTION OF ISOFORM 1.
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASN-10; SER-85; TYR-123; LEU-127; THR-182 AND HIS-492.

    Entry informationi

    Entry nameiKKCC2_HUMAN
    AccessioniPrimary (citable) accession number: Q96RR4
    Secondary accession number(s): A8K7Q7
    , O94883, Q8IUG2, Q8IUG3, Q8N3I4, Q8WY03, Q8WY04, Q8WY05, Q8WY06, Q96RP1, Q96RP2, Q96RR3, Q9BWE9, Q9UER3, Q9UES2, Q9Y5N2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3