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Q8C078

- KKCC2_MOUSE

UniProt

Q8C078 - KKCC2_MOUSE

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Protein

Calcium/calmodulin-dependent protein kinase kinase 2

Gene

Camkk2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1, CAMK4 and CAMK1D (By similarity). 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). May play a role in neurite growth. Isoform 2 may promote neurite elongation, while isoform 1 may promoter neurite branching (By similarity). May be involved in hippocampal activation of CREB1.By similarity1 Publication

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-dependent protein kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. protein autophosphorylation Source: UniProtKB
  2. protein phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

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:Kiaa0787
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:2444812. Camkk2.

Subcellular locationi

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

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB-KW
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice are unable to form spatial long-term memory.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 588587Calcium/calmodulin-dependent protein kinase kinase 2PRO_0000086145Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei129 – 1291Phosphoserine1 Publication
Modified residuei133 – 1331Phosphoserine1 Publication
Modified residuei495 – 4951PhosphoserineBy similarity

Post-translational modificationi

Autophosphorylated and phosphorylated by PKA. Each isoform may show a different pattern of phosphorylation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8C078.
PaxDbiQ8C078.
PRIDEiQ8C078.

PTM databases

PhosphoSiteiQ8C078.

Expressioni

Tissue specificityi

Expressed in all tissues tested. A differential expression pattern compared to CAMKK1 is observed in the brain.1 Publication

Gene expression databases

GenevestigatoriQ8C078.

Interactioni

Subunit structurei

Interacts with calmodulin.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PPM1FP495933EBI-937199,EBI-719945From a different organism.

Protein-protein interaction databases

IntActiQ8C078. 3 interactions.
MINTiMINT-4099835.

Structurei

3D structure databases

ProteinModelPortaliQ8C078.
SMRiQ8C078. Positions 79-507.
ModBaseiSearch...
MobiDBiSearch...

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi549 – 5524Poly-Gly

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.
GeneTreeiENSGT00530000063214.
HOGENOMiHOG000007846.
HOVERGENiHBG052262.
InParanoidiQ8C078.
KOiK07359.
OMAiMNGRCIC.
OrthoDBiEOG7F5114.
PhylomeDBiQ8C078.
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.
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 (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8C078-1) [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

        10         20         30         40         50
MSSCVSSQPT SDRVAPQDEL GSGGGSREGQ KPCEALRGLS SLSIHLGMES
60 70 80 90 100
FIVVTECEPG RGVDLNLARD QPPEADGQEL PLEASDPESR SPLSGRKMSL
110 120 130 140 150
QEPSQGGPAS SSNSLDMNGR CICPSLSYSP ASSPQSSPRM PRRPTVESHH
160 170 180 190 200
VSITGLQDCV QLNQYTLKDE IGKGSYGVVK LAYNENDNTY YAMKVLSKKK
210 220 230 240 250
LIRQAGFPRR PPPRGARPAP GGCIQPRGPI EQVYQEIAIL KKLDHPNVVK
260 270 280 290 300
LVEVLDDPNE DHLYMVFELV NQGPVMEVPT LKPLSEDQAR FYFQDLIKGI
310 320 330 340 350
EYLHYQKIIH RDIKPSNLLV GEDGHIKIAD FGVSNEFKGS DALLSNTVGT
360 370 380 390 400
PAFMAPESLS ETRKIFSGKA LDVWAMGVTL YCFVFGQCPF MDERIMCLHS
410 420 430 440 450
KIKSQALEFP DQPDIAEDLK DLITRMLDKN PESRIVVPEI KLHPWVTRHG
460 470 480 490 500
AEPLPSEDEN CTLVEVTEEE VENSVKHIPS LATVILVKTM IRKRSFGNPF
510 520 530 540 550
EGSRREERSL SAPGNLLTKK PTREWEPLSE PKEARQRRQP PGPRAGPCGG
560 570 580
GGSALVKGGP CVESWGAPAP GSPPRMPPLQ PEEVMEPE
Length:588
Mass (Da):64,618
Last modified:December 7, 2004 - v2
Checksum:iAED7433ADB3477A5
GO
Isoform 2 (identifier: Q8C078-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     520-588: KPTREWEPLS...LQPEEVMEPE → QGSEDSPRGPEPAPVGEEEVLL

Note: Contains a phosphoserine at position 522.By similarity

Show »
Length:541
Mass (Da):59,617
Checksum:iFEB2385A4D793FF2
GO
Isoform 3 (identifier: Q8C078-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     498-498: N → T
     499-507: Missing.
     508-588: RSLSAPGNLL...LQPEEVMEPE → RSKVAAGRNV...DGAGVAAWTT

Show »
Length:579
Mass (Da):63,477
Checksum:iA79C6F3E1CE6DDCA
GO
Isoform 4 (identifier: Q8C078-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     485-503: ILVKTMIRKRSFGNPFEGS → VRRAGPLTKNKNRESPRQG
     504-588: Missing.

Show »
Length:503
Mass (Da):55,517
Checksum:i0ADB843145944187
GO
Isoform 5 (identifier: Q8C078-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     533-588: EARQRRQPPG...LQPEEVMEPE → VNACLPACAI...YPGSSGPLDG

Note: No experimental confirmation available.

Show »
Length:625
Mass (Da):68,051
Checksum:i83E6E29CA297E2B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761Y → F in BAC32023. (PubMed:16141072)Curated
Sequence conflicti290 – 2901R → H in BAC27681. (PubMed:16141072)Curated
Sequence conflicti396 – 3983MCL → IWR(PubMed:12654522)Curated
Sequence conflicti401 – 4011K → R(PubMed:12654522)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei485 – 50319ILVKT…PFEGS → VRRAGPLTKNKNRESPRQG in isoform 4. 1 PublicationVSP_012150Add
BLAST
Alternative sequencei498 – 4981N → T in isoform 3. 1 PublicationVSP_012151
Alternative sequencei499 – 5079Missing in isoform 3. 1 PublicationVSP_012152
Alternative sequencei504 – 58885Missing in isoform 4. 1 PublicationVSP_012153Add
BLAST
Alternative sequencei508 – 58881RSLSA…VMEPE → RSKVAAGRNVPCQRLETCSR SKAAKTAPGAQSRPLWGRRK CSCERWSLRGKLGGSGPWLP TTHASTAARGGDGAGVAAWT T in isoform 3. 1 PublicationVSP_012154Add
BLAST
Alternative sequencei520 – 58869KPTRE…VMEPE → QGSEDSPRGPEPAPVGEEEV LL in isoform 2. 1 PublicationVSP_012155Add
BLAST
Alternative sequencei533 – 58856EARQR…VMEPE → VNACLPACAIASPPLGPGGG QLQSKHVGISSRQDVPSAGA AVPGSLRASGFPARGIQGLG SHGVSCMRAGLRCMALHPEC LRTYPGSSGPLDG in isoform 5. 1 PublicationVSP_012156Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF453383 mRNA. Translation: AAN75696.1.
AK031399 mRNA. Translation: BAC27387.1.
AK032070 mRNA. Translation: BAC27681.1.
AK044660 mRNA. Translation: BAC32023.1.
BC023103 mRNA. Translation: AAH23103.1.
AK122370 mRNA. Translation: BAC65652.1.
CCDSiCCDS19655.1. [Q8C078-2]
RefSeqiNP_001186605.1. NM_001199676.1. [Q8C078-1]
NP_663333.1. NM_145358.2. [Q8C078-2]
XP_006530293.1. XM_006530230.1. [Q8C078-5]
XP_006530294.1. XM_006530231.1. [Q8C078-5]
UniGeneiMm.289237.

Genome annotation databases

EnsembliENSMUST00000111668; ENSMUSP00000107297; ENSMUSG00000029471. [Q8C078-2]
GeneIDi207565.
KEGGimmu:207565.
UCSCiuc008zlz.3. mouse. [Q8C078-1]
uc008zma.3. mouse. [Q8C078-2]
uc008zmb.1. mouse. [Q8C078-5]
uc008zmc.2. mouse. [Q8C078-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF453383 mRNA. Translation: AAN75696.1 .
AK031399 mRNA. Translation: BAC27387.1 .
AK032070 mRNA. Translation: BAC27681.1 .
AK044660 mRNA. Translation: BAC32023.1 .
BC023103 mRNA. Translation: AAH23103.1 .
AK122370 mRNA. Translation: BAC65652.1 .
CCDSi CCDS19655.1. [Q8C078-2 ]
RefSeqi NP_001186605.1. NM_001199676.1. [Q8C078-1 ]
NP_663333.1. NM_145358.2. [Q8C078-2 ]
XP_006530293.1. XM_006530230.1. [Q8C078-5 ]
XP_006530294.1. XM_006530231.1. [Q8C078-5 ]
UniGenei Mm.289237.

3D structure databases

ProteinModelPortali Q8C078.
SMRi Q8C078. Positions 79-507.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8C078. 3 interactions.
MINTi MINT-4099835.

PTM databases

PhosphoSitei Q8C078.

Proteomic databases

MaxQBi Q8C078.
PaxDbi Q8C078.
PRIDEi Q8C078.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000111668 ; ENSMUSP00000107297 ; ENSMUSG00000029471 . [Q8C078-2 ]
GeneIDi 207565.
KEGGi mmu:207565.
UCSCi uc008zlz.3. mouse. [Q8C078-1 ]
uc008zma.3. mouse. [Q8C078-2 ]
uc008zmb.1. mouse. [Q8C078-5 ]
uc008zmc.2. mouse. [Q8C078-4 ]

Organism-specific databases

CTDi 10645.
MGIi MGI:2444812. Camkk2.
Rougei Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00530000063214.
HOGENOMi HOG000007846.
HOVERGENi HBG052262.
InParanoidi Q8C078.
KOi K07359.
OMAi MNGRCIC.
OrthoDBi EOG7F5114.
PhylomeDBi Q8C078.
TreeFami TF313013.

Miscellaneous databases

NextBioi 371961.
PROi Q8C078.
SOURCEi Search...

Gene expression databases

Genevestigatori Q8C078.

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.
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

« Hide 'large scale' publications
  1. "Cloning of mouse Ca2+/calmodulin-dependent protein kinase kinase beta (CaMKKbeta) and characterization of CaMKKbeta and CaMKKalpha distribution in the adult mouse brain."
    Vinet J., Carra S., Blom J.M.C., Harvey M., Brunello N., Barden N., Tascedda F.
    Brain Res. Mol. Brain Res. 111:216-221(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  2. "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] (ISOFORMS 1; 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Medulla oblongata, Retina and Testis.
  3. "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 2).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 207-588 (ISOFORM 5).
    Tissue: Brain.
  5. "Loss of Ca2+/calmodulin kinase kinase beta affects the formation of some, but not all, types of hippocampus-dependent long-term memory."
    Peters M., Mizuno K., Ris L., Angelo M., Godaux E., Giese K.P.
    J. Neurosci. 23:9752-9760(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiKKCC2_MOUSE
AccessioniPrimary (citable) accession number: Q8C078
Secondary accession number(s): Q80TS0
, Q8BXM8, Q8C0G3, Q8CH42, Q8QZT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: December 7, 2004
Last modified: October 29, 2014
This is version 119 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3