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P24788 (CD11B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
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 names
Name:Cdk11b
Synonyms:Cdc2l1, Cdk11
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length784 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

Phosphorylation at Thr-437 or Tyr-438 inactivates the enzyme, while phosphorylation at Thr-584 activates it By similarity.

Post-translational modification

Phosphorylation at Ser-115 creates a binding site for 14-3-3 proteins By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAA03518.1 differs from that shown. Reason: Frameshift at several positions.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: P24788-1)

Also known as: p130PITSLRE;

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.
Isoform 2 (identifier: P24788-2)

Also known as: p58clk-1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-345: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 784784Cyclin-dependent kinase 11B
PRO_0000024313

Regions

Domain427 – 712286Protein kinase
Nucleotide binding433 – 4419ATP By similarity
Compositional bias291 – 30414Poly-Glu
Compositional bias309 – 32517Poly-Glu

Sites

Active site5511Proton acceptor By similarity
Binding site4561ATP By similarity

Amino acid modifications

Modified residue1151Phosphoserine By similarity
Modified residue4711Phosphoserine; by CDK7 By similarity
Modified residue4771Phosphothreonine; by CDK7 By similarity
Modified residue5781Phosphoserine By similarity
Modified residue5831Phosphotyrosine By similarity
Modified residue5841Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 345345Missing in isoform 2.
VSP_018835

Experimental info

Sequence conflict35 – 373LKN → MSQ in AAH52920. Ref.4
Sequence conflict2841Missing in AAA66169. Ref.2
Sequence conflict5601S → T in AAA03518. Ref.1
Sequence conflict6081V → C in AAA03518. Ref.1
Sequence conflict6451T → S in AAA03518. Ref.1
Sequence conflict6681Y → I in AAA03518. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (p130PITSLRE) [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: CDF03AC3957FA351

FASTA78491,513
        10         20         30         40         50         60 
MGDEKDSWKV KTLDEILQEK KRRKEQEEKA EIKRLKNSDD RDSKRDSLEE GELRDHRMEI 

        70         80         90        100        110        120 
TIRNSPYRRE DSMEDRGEED DSLAIKPPQQ MSRKEKAHHR KDEKRKEKRR HRSHSAEGGK 

       130        140        150        160        170        180 
HARVKEKERE HERRKRHREE QDKARREWER QKRREMAREH SRRERDRLEQ LERKRERERK 

       190        200        210        220        230        240 
LREQQKEQRE QKERERRAEE RRKEREARRE VSAHHRTMRE EYSDKGKVGH WSRSPLRPPR 

       250        260        270        280        290        300 
ERFEMGDNRK PVKEEKVEER DLLSDLQDIS DSERKTSSAE SSSAESGSGS EEEEEEEEEE 

       310        320        330        340        350        360 
EEEEGSTSEE SEEEEEEEEE EEEEETGSNS EEASEQSAEE VSDEEMSEDE DRENENHILV 

       370        380        390        400        410        420 
VPESRFDRDS GDSEEGEEEV GEGTPQSSAP TEGDYVPDSP ALSPIELKQE LPKYLPALQG 

       430        440        450        460        470        480 
CRSVEEFQCL NRIEEGTYGV VYRAKDKKTD EIVALKRLKM EKEKEGFPIT SLREINTILK 

       490        500        510        520        530        540 
AQHPNIVTVR EIVVGSNMDK IYIVMNYVEH DLKSLMETMK QPFLPGEVKT LMIQLLSGVK 

       550        560        570        580        590        600 
HLHDNWILHR DLKTSNLLLS HAGILKVGDF GLAREYGSPL KAYTPVVVTL WYRAPELLLG 

       610        620        630        640        650        660 
AKEYSTAVDM WSVGCIFGEL LTQKPLFPGK SDIDQINKIF KDLGTPSEKI WPGYNDLPAV 

       670        680        690        700        710        720 
KKMTFSEYPY NNLRKRFGAL LSDQGFDLMN KFLTYYPGRR INAEDGLKHE YFRETPLPID 

       730        740        750        760        770        780 
PSMFPTWPAK SEQQRVKRGT SPRPPEGGLG YSQLGDDDLK ETGFHLTTTN QGASAAGPGF 


SLKF 

« Hide

Isoform 2 (p58clk-1) [UniParc].

Checksum: A31D79C4919C1A3B
Show »

FASTA43949,509

References

« Hide 'large scale' references
[1]"Regulated expression of a cell division control-related protein kinase during development."
Kidd V.J., Luo W., Xiang J.L., Tu F., Easton J., McCune S., Snead M.L.
Cell Growth Differ. 2:85-93(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"A cyclin-dependent kinase homologue, p130PITSLRE is a phosphotyrosine-independent SH2 ligand."
Malek S.N., Desiderio S.
J. Biol. Chem. 269:33009-33020(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"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. expand/collapse author list , 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] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Stomach.
[4]"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] OF 35-784 (ISOFORM 1).
Tissue: Eye.
[5]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M58633 mRNA. Translation: AAA03518.1. Frameshift.
L37092 mRNA. Translation: AAA66169.1.
AK077668 mRNA. Translation: BAC36942.1.
AK147133 mRNA. Translation: BAE27703.1.
BC052920 mRNA. Translation: AAH52920.1.
CCDSCCDS19033.1. [P24788-1]
PIRA55817.
RefSeqNP_031687.2. NM_007661.3. [P24788-1]
XP_006538570.1. XM_006538507.1. [P24788-1]
XP_006538571.1. XM_006538508.1.
XP_006538572.1. XM_006538509.1.
XP_006538573.1. XM_006538510.1.
XP_006538574.1. XM_006538511.1.
UniGeneMm.267410.

3D structure databases

ProteinModelPortalP24788.
SMRP24788. Positions 405-754.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198625. 2 interactions.
IntActP24788. 2 interactions.
MINTMINT-4090174.

PTM databases

PhosphoSiteP24788.

Proteomic databases

MaxQBP24788.
PaxDbP24788.
PRIDEP24788.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067081; ENSMUSP00000070527; ENSMUSG00000029062. [P24788-1]
ENSMUST00000105600; ENSMUSP00000101225; ENSMUSG00000029062. [P24788-1]
GeneID12537.
KEGGmmu:12537.
UCSCuc008wea.1. mouse. [P24788-1]

Organism-specific databases

CTD984.
MGIMGI:88353. Cdk11b.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000114964.
HOGENOMHOG000233024.
HOVERGENHBG014652.
InParanoidP24788.
KOK08818.
OMADGRKPVK.
OrthoDBEOG74BJS4.
PhylomeDBP24788.
TreeFamTF101035.

Enzyme and pathway databases

BRENDA2.7.11.22. 3474.
ReactomeREACT_188576. Developmental Biology.
REACT_200794. Mus musculus biological processes.

Gene expression databases

ArrayExpressP24788.
BgeeP24788.
CleanExMM_CDC2L1.
GenevestigatorP24788.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDK11B. mouse.
NextBio281574.
PROP24788.
SOURCESearch...

Entry information

Entry nameCD11B_MOUSE
AccessionPrimary (citable) accession number: P24788
Secondary accession number(s): Q3UI03 expand/collapse secondary AC list , Q61399, Q7TST4, Q8BP53
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 4, 2005
Last modified: July 9, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot