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Protein

Cyclin-dependent kinase 11B

Gene

Cdk11b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Acts as a negative regulator of the normal cell cycle progression. In vitro, this protein kinase has been shown to phosphorylate a number of substrates, including histone h1, casein, and galactosyltransferase. May function in regulating proliferation by the phosphorylation and subsequent plasma membrane targeting of galactosyltransferase.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei108 – 1081ATPPROSITE-ProRule annotation
Active sitei203 – 2031Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi85 – 939ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.22. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 11B
Alternative name(s):
Cell division cycle 2-like protein kinase 1
Cell division protein kinase 11
Cyclin-dependent kinase 11 (EC:2.7.11.22)
Galactosyltransferase-associated protein kinase p58/GTA
PITSLRE serine/threonine-protein kinase CDC2L1
Gene namesi
Name:Cdk11b
Synonyms:Cdc2l1, Cdk11
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628604. Cdk11b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436Cyclin-dependent kinase 11BPRO_0000085710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei123 – 1231Phosphoserine; by CDK7By similarity
Modified residuei129 – 1291Phosphothreonine; by CDK7By similarity
Modified residuei230 – 2301PhosphoserineBy similarity
Modified residuei235 – 2351PhosphotyrosineBy similarity
Modified residuei236 – 2361PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP46892.

PTM databases

PhosphoSiteiP46892.

Expressioni

Gene expression databases

GenevisibleiP46892. RN.

Interactioni

Protein-protein interaction databases

MINTiMINT-4655594.
STRINGi10116.ENSRNOP00000039105.

Structurei

3D structure databases

ProteinModelPortaliP46892.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini79 – 364286Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 4415Calmodulin-bindingSequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi25 – 306Nuclear localization signalSequence Analysis

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG014652.
InParanoidiP46892.
PhylomeDBiP46892.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46892-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSEKSRTTS WLFQSHEVTE ILGRVKKNRK KLVKGLHRAG PPPEKNYLPD
60 70 80 90 100
SPALSPIELK QELPKYLPAL QGCRSVEEFQ CLNRIEEGTY GVVYRAKDKK
110 120 130 140 150
TDEIVALKRL KMEKEKEGFP LTSIREINTI LKAQHPNIVT VREIVVGSNM
160 170 180 190 200
DKIYIVMNYV EHDLKSLMET MKQPFLPGEV KTLMIQLLSG VKHLHDNWIL
210 220 230 240 250
HRDLKTSNLL LTHAGILKVG DFGLAREYGS PLKAYTPVVV TLWYRAPELL
260 270 280 290 300
LGAKEYSTAC DMWSVGCIFG ELLTQKPLFP GKSDIDQINK IFKDIGTPSE
310 320 330 340 350
KIWPGYSELP AVKKMTFSEL PYNNLRKRFG ALLSDQGFDL MNKFLTYYPG
360 370 380 390 400
RRINAEDGLK HEYFRETPLP IDPSMFPTWP AKSEQQCVKR GTSPKPPEGG
410 420 430
LGYSQLGDDD LKETGFHLTT TNDGAVSCRP WCSLLF
Length:436
Mass (Da):49,547
Last modified:November 1, 1995 - v1
Checksum:iD2BA9BC73EAD3D27
GO

Sequence cautioni

The sequence AAA88509.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24388 mRNA. Translation: AAA88509.1. Different initiation.
PIRiS47628.
UniGeneiRn.10204.
Rn.129782.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24388 mRNA. Translation: AAA88509.1. Different initiation.
PIRiS47628.
UniGeneiRn.10204.
Rn.129782.

3D structure databases

ProteinModelPortaliP46892.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4655594.
STRINGi10116.ENSRNOP00000039105.

PTM databases

PhosphoSiteiP46892.

Proteomic databases

PRIDEiP46892.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi628604. Cdk11b.

Phylogenomic databases

HOVERGENiHBG014652.
InParanoidiP46892.
PhylomeDBiP46892.

Enzyme and pathway databases

BRENDAi2.7.11.22. 5301.

Miscellaneous databases

NextBioi623956.
PROiP46892.

Gene expression databases

GenevisibleiP46892. RN.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of the synthesis and expression of the GTA-kinase from transformed and normal rodent cells."
    Kerr M., Fischer J.E., Purushotham K.R., Gao D., Nakagawa Y., Maeda N., Ghanta V., Hiramoto R., Chegini N., Humphreys-Beher M.G.
    Biochim. Biophys. Acta 1218:375-387(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Salivary gland.

Entry informationi

Entry nameiCD11B_RAT
AccessioniPrimary (citable) accession number: P46892
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 24, 2015
This is version 121 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.