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P24788

- CD11B_MOUSE

UniProt

P24788 - CD11B_MOUSE

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Protein

Cyclin-dependent kinase 11B

Gene

Cdk11b

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

Magnesium.

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei456 – 4561ATPPROSITE-ProRule annotation
Active sitei551 – 5511Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi433 – 4419ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. blastocyst development Source: MGI
  2. cell cycle Source: UniProtKB-KW
  3. negative regulation of apoptotic signaling pathway Source: MGI
  4. regulation of mitosis Source: MGI
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. 3474.
ReactomeiREACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:88353. Cdk11b.

Subcellular locationi

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 784784Cyclin-dependent kinase 11BPRO_0000024313Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei115 – 1151PhosphoserineBy similarity
Modified residuei471 – 4711Phosphoserine; by CDK7By similarity
Modified residuei477 – 4771Phosphothreonine; by CDK7By similarity
Modified residuei578 – 5781PhosphoserineBy similarity
Modified residuei583 – 5831PhosphotyrosineBy similarity
Modified residuei584 – 5841PhosphothreonineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP24788.
PaxDbiP24788.
PRIDEiP24788.

PTM databases

PhosphoSiteiP24788.

Expressioni

Gene expression databases

BgeeiP24788.
CleanExiMM_CDC2L1.
ExpressionAtlasiP24788. baseline.
GenevestigatoriP24788.

Interactioni

Protein-protein interaction databases

BioGridi198625. 2 interactions.
IntActiP24788. 2 interactions.
MINTiMINT-4090174.

Structurei

3D structure databases

ProteinModelPortaliP24788.
SMRiP24788. Positions 423-754.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini427 – 712286Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi291 – 30414Poly-GluAdd
BLAST
Compositional biasi309 – 32517Poly-GluAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119154.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP24788.
KOiK08818.
OMAiDGRKPVK.
OrthoDBiEOG74BJS4.
PhylomeDBiP24788.
TreeFamiTF101035.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform 1 (identifier: P24788) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGDEKDSWKV KTLDEILQEK KRRKEQEEKA EIKRLKNSDD RDSKRDSLEE
60 70 80 90 100
GELRDHRMEI TIRNSPYRRE DSMEDRGEED DSLAIKPPQQ MSRKEKAHHR
110 120 130 140 150
KDEKRKEKRR HRSHSAEGGK HARVKEKERE HERRKRHREE QDKARREWER
160 170 180 190 200
QKRREMAREH SRRERDRLEQ LERKRERERK LREQQKEQRE QKERERRAEE
210 220 230 240 250
RRKEREARRE VSAHHRTMRE EYSDKGKVGH WSRSPLRPPR ERFEMGDNRK
260 270 280 290 300
PVKEEKVEER DLLSDLQDIS DSERKTSSAE SSSAESGSGS EEEEEEEEEE
310 320 330 340 350
EEEEGSTSEE SEEEEEEEEE EEEEETGSNS EEASEQSAEE VSDEEMSEDE
360 370 380 390 400
DRENENHILV VPESRFDRDS GDSEEGEEEV GEGTPQSSAP TEGDYVPDSP
410 420 430 440 450
ALSPIELKQE LPKYLPALQG CRSVEEFQCL NRIEEGTYGV VYRAKDKKTD
460 470 480 490 500
EIVALKRLKM EKEKEGFPIT SLREINTILK AQHPNIVTVR EIVVGSNMDK
510 520 530 540 550
IYIVMNYVEH DLKSLMETMK QPFLPGEVKT LMIQLLSGVK HLHDNWILHR
560 570 580 590 600
DLKTSNLLLS HAGILKVGDF GLAREYGSPL KAYTPVVVTL WYRAPELLLG
610 620 630 640 650
AKEYSTAVDM WSVGCIFGEL LTQKPLFPGK SDIDQINKIF KDLGTPSEKI
660 670 680 690 700
WPGYNDLPAV KKMTFSEYPY NNLRKRFGAL LSDQGFDLMN KFLTYYPGRR
710 720 730 740 750
INAEDGLKHE YFRETPLPID PSMFPTWPAK SEQQRVKRGT SPRPPEGGLG
760 770 780
YSQLGDDDLK ETGFHLTTTN QGASAAGPGF SLKF
Length:784
Mass (Da):91,513
Last modified:January 4, 2005 - v2
Checksum:iCDF03AC3957FA351
GO
Isoform 2 (identifier: P24788-2) [UniParc]FASTAAdd to Basket

Also known as: p58clk-1

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

Show »
Length:439
Mass (Da):49,509
Checksum:iA31D79C4919C1A3B
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 373LKN → MSQ in AAH52920. (PubMed:15489334)Curated
Sequence conflicti284 – 2841Missing in AAA66169. (PubMed:7528743)Curated
Sequence conflicti560 – 5601S → T in AAA03518. (PubMed:2069872)Curated
Sequence conflicti608 – 6081V → C in AAA03518. (PubMed:2069872)Curated
Sequence conflicti645 – 6451T → S in AAA03518. (PubMed:2069872)Curated
Sequence conflicti668 – 6681Y → I in AAA03518. (PubMed:2069872)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 345345Missing in isoform 2. 1 PublicationVSP_018835Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS19033.1. [P24788-1]
PIRiA55817.
RefSeqiNP_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.
UniGeneiMm.267410.

Genome annotation databases

EnsembliENSMUST00000067081; ENSMUSP00000070527; ENSMUSG00000029062. [P24788-1]
ENSMUST00000105600; ENSMUSP00000101225; ENSMUSG00000029062. [P24788-1]
GeneIDi12537.
KEGGimmu:12537.
UCSCiuc008wea.1. mouse. [P24788-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS19033.1. [P24788-1 ]
PIRi A55817.
RefSeqi NP_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.
UniGenei Mm.267410.

3D structure databases

ProteinModelPortali P24788.
SMRi P24788. Positions 423-754.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198625. 2 interactions.
IntActi P24788. 2 interactions.
MINTi MINT-4090174.

PTM databases

PhosphoSitei P24788.

Proteomic databases

MaxQBi P24788.
PaxDbi P24788.
PRIDEi P24788.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000067081 ; ENSMUSP00000070527 ; ENSMUSG00000029062 . [P24788-1 ]
ENSMUST00000105600 ; ENSMUSP00000101225 ; ENSMUSG00000029062 . [P24788-1 ]
GeneIDi 12537.
KEGGi mmu:12537.
UCSCi uc008wea.1. mouse. [P24788-1 ]

Organism-specific databases

CTDi 984.
MGIi MGI:88353. Cdk11b.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119154.
HOGENOMi HOG000233024.
HOVERGENi HBG014652.
InParanoidi P24788.
KOi K08818.
OMAi DGRKPVK.
OrthoDBi EOG74BJS4.
PhylomeDBi P24788.
TreeFami TF101035.

Enzyme and pathway databases

BRENDAi 2.7.11.22. 3474.
Reactomei REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Miscellaneous databases

ChiTaRSi CDK11B. mouse.
NextBioi 281574.
PROi P24788.
SOURCEi Search...

Gene expression databases

Bgeei P24788.
CleanExi MM_CDC2L1.
ExpressionAtlasi P24788. baseline.
Genevestigatori P24788.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
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 PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCD11B_MOUSE
AccessioniPrimary (citable) accession number: P24788
Secondary accession number(s): Q3UI03
, Q61399, Q7TST4, Q8BP53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 4, 2005
Last modified: October 29, 2014
This is version 138 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