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Q3TZA2

- CDKL4_MOUSE

UniProt

Q3TZA2 - CDKL4_MOUSE

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Protein
Cyclin-dependent kinase-like 4
Gene
Cdkl4, Gm942
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331ATP By similarity
Active sitei126 – 1261Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 189ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase-like 4 (EC:2.7.11.22)
Gene namesi
Name:Cdkl4
Synonyms:Gm942
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:3587025. Cdkl4.

Subcellular locationi

Cytoplasm Inferred

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 342342Cyclin-dependent kinase-like 4
PRO_0000085825Add
BLAST

Proteomic databases

PaxDbiQ3TZA2.
PRIDEiQ3TZA2.

PTM databases

PhosphoSiteiQ3TZA2.

Expressioni

Gene expression databases

BgeeiQ3TZA2.
CleanExiMM_CDKL4.
GenevestigatoriQ3TZA2.

Structurei

3D structure databases

ProteinModelPortaliQ3TZA2.
SMRiQ3TZA2. Positions 2-290.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 286283Protein kinase
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi45 – 517[NKR]KIAxRE

Domaini

The [NKR]KIAxRE motif seems to be a cyclin-binding region.

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00650000093115.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiB2RSS7.
KOiK08824.
OMAiWATGCVF.
OrthoDBiEOG7992PS.
PhylomeDBiQ3TZA2.
TreeFamiTF101031.

Family and domain databases

InterProiIPR011009. 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]
PfamiPF00069. 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]

Sequencei

Sequence statusi: Complete.

Q3TZA2-1 [UniParc]FASTAAdd to Basket

« Hide

MEKYEKLAKI GEGSYGVVFK CRNKSSGQVV AIKKFVESED DRVVRKIALR    50
EIRMLKQLKH PNLVNLIEVF RRKRKMHLVF EYCDHTLLNE LERNPNGVSD 100
GVIKSVLWQT LQALNFCHKH NCIHRDVKPE NILITKQGMI KICDFGFARI 150
LIPGDAYTDY VATRWYRAPE LLVGDTKYGS SVDVWAVGCV FAELLTGQPL 200
WPGKSDVDQL YLIIRTLGKL IPRHQSIFRS NQFFRGISIP EPEDMETLEE 250
KFSNVQPVAL SFMKGCLKMN PDERLTCAQL LDSAYFESFQ EDQMKRKARS 300
EGRSRRRQQN QLLPLIPGSH ISPTPDGRKQ VVQLKFDHLP NI 342
Length:342
Mass (Da):39,446
Last modified:October 11, 2005 - v1
Checksum:i384426A832F4D7C8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK157995 mRNA. Translation: BAE34307.1.
BC138986 mRNA. Translation: AAI38987.1.
BC138988 mRNA. Translation: AAI38989.1.
CCDSiCCDS28992.1.
RefSeqiNP_001028615.1. NM_001033443.4.
XP_006524589.1. XM_006524526.1.
XP_006524590.1. XM_006524527.1.
XP_006524591.1. XM_006524528.1.
UniGeneiMm.329216.

Genome annotation databases

EnsembliENSMUST00000086545; ENSMUSP00000083732; ENSMUSG00000033966.
GeneIDi381113.
KEGGimmu:381113.
UCSCiuc008dri.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK157995 mRNA. Translation: BAE34307.1 .
BC138986 mRNA. Translation: AAI38987.1 .
BC138988 mRNA. Translation: AAI38989.1 .
CCDSi CCDS28992.1.
RefSeqi NP_001028615.1. NM_001033443.4.
XP_006524589.1. XM_006524526.1.
XP_006524590.1. XM_006524527.1.
XP_006524591.1. XM_006524528.1.
UniGenei Mm.329216.

3D structure databases

ProteinModelPortali Q3TZA2.
SMRi Q3TZA2. Positions 2-290.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q3TZA2.

Proteomic databases

PaxDbi Q3TZA2.
PRIDEi Q3TZA2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000086545 ; ENSMUSP00000083732 ; ENSMUSG00000033966 .
GeneIDi 381113.
KEGGi mmu:381113.
UCSCi uc008dri.2. mouse.

Organism-specific databases

CTDi 344387.
MGIi MGI:3587025. Cdkl4.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00650000093115.
HOGENOMi HOG000233024.
HOVERGENi HBG014652.
InParanoidi B2RSS7.
KOi K08824.
OMAi WATGCVF.
OrthoDBi EOG7992PS.
PhylomeDBi Q3TZA2.
TreeFami TF101031.

Miscellaneous databases

NextBioi 401624.
PROi Q3TZA2.
SOURCEi Search...

Gene expression databases

Bgeei Q3TZA2.
CleanExi MM_CDKL4.
Genevestigatori Q3TZA2.

Family and domain databases

InterProi 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 ]
Pfami 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. "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: Inner ear.
  2. "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: Brain.

Entry informationi

Entry nameiCDKL4_MOUSE
AccessioniPrimary (citable) accession number: Q3TZA2
Secondary accession number(s): B2RSS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: October 11, 2005
Last modified: July 9, 2014
This is version 76 of the entry and version 1 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

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