Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

Cyclin-dependent kinase 5, isoform CRA_c

Gene

Cdk5

Organism
Mus musculus (Mouse)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

CyclinImported, Kinase, Serine/threonine-protein kinaseUniRule annotation, Transferase

Keywords - Ligandi

ATP-bindingUniRule annotation, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Submitted name:
Cyclin-dependent kinase 5, isoform CRA_cImported
Submitted name:
Cyclin-dependent-like kinase 5Imported
Gene namesi
Name:Cdk5Imported
ORF Names:mCG_16479Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:101765. Cdk5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000030814.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 286283Protein kinaseInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG0594. Eukaryota.
ENOG410XPP3. LUCA.
GeneTreeiENSGT00830000128256.
HOVERGENiHBG014652.
KOiK02090.
OMAiVLFGAKM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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.

Q543F6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKYEKLEKI GEGTYGTVFK AKNRETHEIV ALKRVRLDDD DEGVPSSALR
60 70 80 90 100
EICLLKELKH KNIVRLHDVL HSDKKLTLVF EFCDQDLKKY FDSCNGDLDP
110 120 130 140 150
EIVKSFLFQL LKGLGFCHSR NVLHRDLKPQ NLLINRNGEL KLADFGLARA
160 170 180 190 200
FGIPVRCYSA EVVTLWYRPP DVLFGAKLYS TSIDMWSAGC IFAELANAGR
210 220 230 240 250
PLFPGNDVDD QLKRIFRLLG TPTEEQWPAM TKLPDYKPYP MYPATTSLVN
260 270 280 290
VVPKLNATGR DLLQNLLKCN PVQRISAEEA LQHPYFSDFC PP
Length:292
Mass (Da):33,288
Last modified:May 24, 2005 - v1
Checksum:i4CB11CED9017D535
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC113055 Genomic DNA. No translation available.
AK051790 mRNA. Translation: BAC34769.1.
CH466586 Genomic DNA. Translation: EDL03128.1.
RefSeqiNP_031694.1. NM_007668.3.
UniGeneiMm.298798.
Mm.445256.

Genome annotation databases

EnsembliENSMUST00000030814; ENSMUSP00000030814; ENSMUSG00000028969.
GeneIDi12568.
KEGGimmu:12568.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC113055 Genomic DNA. No translation available.
AK051790 mRNA. Translation: BAC34769.1.
CH466586 Genomic DNA. Translation: EDL03128.1.
RefSeqiNP_031694.1. NM_007668.3.
UniGeneiMm.298798.
Mm.445256.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000030814.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030814; ENSMUSP00000030814; ENSMUSG00000028969.
GeneIDi12568.
KEGGimmu:12568.

Organism-specific databases

CTDi1020.
MGIiMGI:101765. Cdk5.

Phylogenomic databases

eggNOGiKOG0594. Eukaryota.
ENOG410XPP3. LUCA.
GeneTreeiENSGT00830000128256.
HOVERGENiHBG014652.
KOiK02090.
OMAiVLFGAKM.

Miscellaneous databases

ChiTaRSiCdk5. mouse.
NextBioi281666.
SOURCEiSearch...

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "High-efficiency full-length cDNA cloning."
    Carninci P., Hayashizaki Y.
    Methods Enzymol. 303:19-44(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6JImported.
    Tissue: Spinal ganglionImported.
  2. "Normalization and subtraction of cap-trapper-selected cDNAs to prepare full-length cDNA libraries for rapid discovery of new genes."
    Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.
    Genome Res. 10:1617-1630(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6JImported.
    Tissue: Spinal ganglionImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6JImported.
    Tissue: Spinal ganglionImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6JImported.
    Tissue: Spinal ganglionImported.
  5. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6JImported.
    Tissue: Spinal ganglionImported.
  6. "Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs."
    The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team
    Nature 420:563-573(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6JImported.
    Tissue: Spinal ganglionImported.
  7. "A comparison of whole-genome shotgun-derived mouse chromosome 16 and the human genome."
    Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R., Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A., Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.
    , Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K., Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J., Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R., Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H., Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A., Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A., Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C., Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C., Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B., Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E., Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R., Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C., Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L., Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S., Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L., Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R., Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R., Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J., Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L., Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C., Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A., Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H., Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L., Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M., Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K., Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S., Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J., Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G., Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.
    Science 296:1661-1671(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: MixedImported.
  8. "The Transcriptional Landscape of the Mammalian Genome."
    The FANTOM Consortium, Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group)
    Science 309:1559-1563(2005)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6JImported.
    Tissue: Spinal ganglionImported.
  9. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6JImported.
    Tissue: Spinal ganglionImported.
  10. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: MixedImported.
  11. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6JImported.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Ensembl
    Submitted (AUG-2015) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: C57BL/6JImported.

Entry informationi

Entry nameiQ543F6_MOUSE
AccessioniPrimary (citable) accession number: Q543F6
Entry historyi
Integrated into UniProtKB/TrEMBL: May 24, 2005
Last sequence update: May 24, 2005
Last modified: May 11, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.