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Q96RR4 (KKCC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium/calmodulin-dependent protein kinase kinase 2

Short name=CaM-KK 2
Short name=CaM-kinase kinase 2
Short name=CaMKK 2
EC=2.7.11.17
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 names
Name:CAMKK2
Synonyms:CAMKKB, KIAA0787
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length588 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.3 Ref.9 Ref.14

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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.

Subunit structure

Interacts with calmodulin By similarity.

Subcellular location

Nucleus By similarity. Cytoplasm. Cell projection. Note: Predominantly nuclear in unstimulated cells By similarity. Found in the cytoplasm and neurites after forskolin induction. Ref.14

Tissue specificity

Ubiquitously expressed with higher levels in the brain. Intermediate levels are detected in spleen, prostate, thyroid and leukocytes. The lowest level is in lung. Ref.9

Induction

Isoform 1 is up-regulated by PKA pathway. Ref.14

Domain

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.

Post-translational modification

Autophosphorylated and phosphorylated by PKA. Each isoform mayshow a different pattern of phosphorylation. Ref.14

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Sequence caution

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.

The sequence CAD38990.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
   Cellular componentCell projection
Cytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Traceable author statement Ref.1. Source: UniProtKB

calcium-mediated signaling

Traceable author statement Ref.1. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Traceable author statement Ref.1. Source: GOC

positive regulation of transcription, DNA-templated

Traceable author statement Ref.1. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of protein kinase activity

Traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentcell projection

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay. Source: HPA

intracellular

Traceable author statement Ref.1. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion binding

Inferred from direct assay Ref.1. Source: UniProtKB

calmodulin binding

Traceable author statement Ref.1. Source: UniProtKB

calmodulin-dependent protein kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine kinase activity

Traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96RR4-1)

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.
Note: Major isoform.
Isoform 2 (identifier: Q96RR4-2)

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.
Isoform 3 (identifier: Q96RR4-3)

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.
Isoform 4 (identifier: Q96RR4-4)

Also known as: Beta1delta14;

The sequence of this isoform differs from the canonical sequence as follows:
     442-484: Missing.
Note: Inactive. Does not activate CAMK1 and CAMK4. Contains a phosphoserine at position 479.
Isoform 5 (identifier: Q96RR4-5)

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.
Isoform 6 (identifier: Q96RR4-6)

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.
Isoform 7 (identifier: Q96RR4-7)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 588587Calcium/calmodulin-dependent protein kinase kinase 2
PRO_0000086144

Regions

Domain165 – 446282Protein kinase
Nucleotide binding171 – 1799ATP By similarity
Region204 – 22623RP domain
Region472 – 4776Autoinhibitory domain By similarity
Region475 – 50026Calmodulin-binding By similarity

Sites

Active site3121Proton acceptor By similarity
Binding site1941ATP By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.15
Modified residue1291Phosphoserine By similarity
Modified residue1331Phosphoserine By similarity
Modified residue4951Phosphoserine Ref.12

Natural variations

Alternative sequence442 – 48443Missing in isoform 4, isoform 5 and isoform 6.
VSP_012142
Alternative sequence520 – 53213KPTRE…LSELK → QGSEDNLQGTDPP in isoform 3 and isoform 5.
VSP_012143
Alternative sequence533 – 55422EARQR…GGGSA → GTKKKKGLDSMTSTVAAGWL DRRV in isoform 7.
VSP_012148
Alternative sequence533 – 5419EARQRRQPP → PVGEEEVLL in isoform 3 and isoform 5.
VSP_012144
Alternative sequence5331E → T in isoform 2 and isoform 6.
VSP_012146
Alternative sequence534 – 55421Missing in isoform 2 and isoform 6.
VSP_012147
Alternative sequence542 – 55413Missing in isoform 3 and isoform 5.
VSP_012145
Alternative sequence555 – 58834Missing in isoform 2, isoform 3, isoform 5, isoform 6 and isoform 7.
VSP_012149
Natural variant101S → N. Ref.16
Corresponds to variant rs28360477 [ dbSNP | Ensembl ].
VAR_032788
Natural variant851T → S. Ref.1 Ref.4 Ref.8 Ref.16
Corresponds to variant rs3817190 [ dbSNP | Ensembl ].
VAR_020532
Natural variant1231C → Y. Ref.16
Corresponds to variant rs35403710 [ dbSNP | Ensembl ].
VAR_040610
Natural variant1271P → L in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.16
VAR_040611
Natural variant1821A → T in a colorectal adenocarcinoma sample; somatic mutation. Ref.16
VAR_040612
Natural variant3631R → C.
Corresponds to variant rs1132780 [ dbSNP | Ensembl ].
VAR_020533
Natural variant4921R → H. Ref.16
Corresponds to variant rs34129994 [ dbSNP | Ensembl ].
VAR_040613

Experimental info

Sequence conflict2061G → A in AAD31507. Ref.2
Sequence conflict3311F → I in BAF84761. Ref.6
Sequence conflict3471T → Y in AAD31507. Ref.2
Sequence conflict3711L → K in AAD31507. Ref.2
Sequence conflict5541A → H in AAK91829. Ref.1
Sequence conflict5571R → N in AAK91829. Ref.1

Secondary structure

......................................... 588
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Beta1) (CAMKK2+E16) [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: 04E3583561341167

FASTA58864,746
        10         20         30         40         50         60 
MSSCVSSQPS SNRAAPQDEL GGRGSSSSES QKPCEALRGL SSLSIHLGME SFIVVTECEP 

        70         80         90        100        110        120 
GCAVDLGLAR DRPLEADGQE VPLDTSGSQA RPHLSGRKLS LQERSQGGLA AGGSLDMNGR 

       130        140        150        160        170        180 
CICPSLPYSP VSSPQSSPRL PRRPTVESHH VSITGMQDCV QLNQYTLKDE IGKGSYGVVK 

       190        200        210        220        230        240 
LAYNENDNTY YAMKVLSKKK LIRQAGFPRR PPPRGTRPAP GGCIQPRGPI EQVYQEIAIL 

       250        260        270        280        290        300 
KKLDHPNVVK LVEVLDDPNE DHLYMVFELV NQGPVMEVPT LKPLSEDQAR FYFQDLIKGI 

       310        320        330        340        350        360 
EYLHYQKIIH RDIKPSNLLV GEDGHIKIAD FGVSNEFKGS DALLSNTVGT PAFMAPESLS 

       370        380        390        400        410        420 
ETRKIFSGKA LDVWAMGVTL YCFVFGQCPF MDERIMCLHS KIKSQALEFP DQPDIAEDLK 

       430        440        450        460        470        480 
DLITRMLDKN PESRIVVPEI KLHPWVTRHG AEPLPSEDEN CTLVEVTEEE VENSVKHIPS 

       490        500        510        520        530        540 
LATVILVKTM IRKRSFGNPF EGSRREERSL SAPGNLLTKK PTRECESLSE LKEARQRRQP 

       550        560        570        580 
PGHRPAPRGG GGSALVRGSP CVESCWAPAP GSPARMHPLR PEEAMEPE 

« Hide

Isoform 2 (Beta2) [UniParc].

Checksum: 98FAAB0FB8C4CACF
Show »

FASTA53358,899
Isoform 3 (Beta1delta16) (CAMKK2-E16) [UniParc].

Checksum: D9A56C3D780C0DDE
Show »

FASTA54159,602
Isoform 4 (Beta1delta14) [UniParc].

Checksum: EE849E31E0416BC3
Show »

FASTA54559,971
Isoform 5 (Beta1delta14/16) (beta-3x) [UniParc].

Checksum: 6D051947DDCB69E1
Show »

FASTA49854,827
Isoform 6 (Beta2delta14) [UniParc].

Checksum: 0821956F65E543C4
Show »

FASTA49054,124
Isoform 7 [UniParc].

Checksum: 47E33706CE77489C
Show »

FASTA55661,386

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , AF321390, AF321391, AF321392, AF321393, AF321394, AF321395, AF321396, AF321397, AF321398, AF321399, AF321400, AF321575, AF321576, AF321577, AF321578 Genomic DNA. Translation: AAK91830.1.
AF321402 expand/collapse EMBL AC list , 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.
PIRJE0191.
RefSeqNP_001257414.1. NM_001270485.1.
NP_001257415.1. NM_001270486.1.
NP_006540.3. NM_006549.3.
NP_705719.2. NM_153499.2.
NP_705720.1. NM_153500.1.
NP_757363.1. NM_172214.2.
NP_757364.1. NM_172215.2.
NP_757365.1. NM_172216.1.
NP_757380.1. NM_172226.2.
XP_005253879.1. XM_005253822.2.
XP_005253880.1. XM_005253823.1.
XP_005253881.1. XM_005253824.2.
UniGeneHs.297343.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZV2X-ray2.40A158-448[»]
ProteinModelPortalQ96RR4.
SMRQ96RR4. Positions 160-487.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115889. 26 interactions.
IntActQ96RR4. 18 interactions.

Chemistry

BindingDBQ96RR4.
ChEMBLCHEMBL5284.
GuidetoPHARMACOLOGY1957.

PTM databases

PhosphoSiteQ96RR4.

Polymorphism databases

DMDM317373374.

Proteomic databases

PaxDbQ96RR4.
PRIDEQ96RR4.

Protocols and materials databases

DNASU10645.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324774; ENSP00000312741; ENSG00000110931. [Q96RR4-1]
ENST00000337174; ENSP00000336634; ENSG00000110931. [Q96RR4-3]
ENST00000347034; ENSP00000321230; ENSG00000110931. [Q96RR4-4]
ENST00000392473; ENSP00000376265; ENSG00000110931. [Q96RR4-2]
ENST00000392474; ENSP00000376266; ENSG00000110931. [Q96RR4-7]
ENST00000402834; ENSP00000384591; ENSG00000110931. [Q96RR4-1]
ENST00000404169; ENSP00000384600; ENSG00000110931. [Q96RR4-1]
ENST00000412367; ENSP00000388368; ENSG00000110931. [Q96RR4-3]
ENST00000446440; ENSP00000388273; ENSG00000110931. [Q96RR4-6]
ENST00000538733; ENSP00000445944; ENSG00000110931. [Q96RR4-5]
GeneID10645.
KEGGhsa:10645.
UCSCuc001tzt.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

CTD10645.
GeneCardsGC12M121675.
H-InvDBHIX0011079.
HIX0171630.
HIX0171665.
HGNCHGNC:1470. CAMKK2.
HPAHPA017389.
MIM615002. gene.
neXtProtNX_Q96RR4.
PharmGKBPA26052.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG052262.
KOK07359.
OMAMNGRCIC.
OrthoDBEOG7F5114.
PhylomeDBQ96RR4.
TreeFamTF313013.

Enzyme and pathway databases

SignaLinkQ96RR4.

Gene expression databases

ArrayExpressQ96RR4.
BgeeQ96RR4.
CleanExHS_CAMKK2.
GenevestigatorQ96RR4.

Family and domain databases

InterProIPR020636. 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]
PANTHERPTHR24347. PTHR24347. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCAMKK2. human.
EvolutionaryTraceQ96RR4.
GeneWikiCAMKK2.
GenomeRNAi10645.
NextBio40461.
PROQ96RR4.
SOURCESearch...

Entry information

Entry nameKKCC2_HUMAN
AccessionPrimary (citable) accession number: Q96RR4
Secondary accession number(s): A8K7Q7 expand/collapse secondary AC list , O94883, Q8IUG2, Q8IUG3, Q8N3I4, Q8WY03, Q8WY04, Q8WY05, Q8WY06, Q96RP1, Q96RP2, Q96RR3, Q9BWE9, Q9UER3, Q9UES2, Q9Y5N2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM