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P21127 (CD11B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-dependent kinase 11B

EC=2.7.11.22
Alternative name(s):
Cell division cycle 2-like protein kinase 1
Short name=CLK-1
Cell division protein kinase 11B
Galactosyltransferase-associated protein kinase p58/GTA
PITSLRE serine/threonine-protein kinase CDC2L1
p58 CLK-1
Gene names
Name:CDK11B
Synonyms:CDC2L1, CDK11, PITSLREA, PK58
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length795 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Appears to play multiple roles in cell cycle progression, cytokinesis and apoptosis. The p110 isoforms have been suggested to be involved in pre-mRNA splicing, potentially by phosphorylating the splicing protein SFRS7. The p58 isoform mayact as a negative regulator of normal cell cycle progression. Ref.1 Ref.10 Ref.11

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

Phosphorylation at Thr-448 or Tyr-449 inactivates the enzyme, while phosphorylation at Thr-595 activates it By similarity.

Subunit structure

The cleaved p110 isoform, p110C, binds to the serine/threonine kinase PAK1 and RANBP9. p110C interacts with RNPS1. The p58 isoform butnot the p110 isoforms or p110C interacts with CCND3. The p110 isoforms are found in large molecular weight complexes containing CCNL1 and SFRS7. Ref.7 Ref.9 Ref.10 Ref.11

Subcellular location

Cytoplasm. Nucleus Ref.4 Ref.9 Ref.10.

Tissue specificity

Expressed ubiquitously. Some evidence of isoform-specific tissue distribution. Ref.4 Ref.5

Induction

The p58 isoform isspecifically induced in G2/M phase of the cell cycle. Ref.8

Post-translational modification

During apoptosis, induced by Fas or tumor necrosis factor, specific CKD11 p110 isoforms are cleaved by caspases to produce a protein (p110C) that contains the C-terminal kinase domain of the CDK11 proteins.

Phosphorylation at Ser-115 creates a binding site for 14-3-3 proteins. p110C can be autophosphorylated. Ref.9 Ref.12 Ref.15

Miscellaneous

Duplicated gene. CDK11A and CDK11B encode almost identical protein kinases of 110 kDa that contain at their C-termini the open reading frame of a smaller 58 kDa isoform whichis expressed following IRES-mediated alternative initiation of translation.

Sequence similarities

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

Contains 1 protein kinase domain.

Caution

Many references talk about 'p110 isoforms' but it is not yet known if this refers to CDK11A and/or CDK11B or one/some of the isoforms of each.

Sequence caution

The sequence AAC83664.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAF36538.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative initiation
Alternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Non-traceable author statement Ref.5. Source: UniProtKB

cell proliferation

Traceable author statement Ref.4. Source: ProtInc

mitosis

Non-traceable author statement Ref.3. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of cell growth

Inferred from expression pattern Ref.8. Source: UniProtKB

regulation of mRNA processing

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of transcription, DNA-templated

Non-traceable author statement Ref.5. Source: UniProtKB

   Cellular_componentcytoplasm

Traceable author statement Ref.4. Source: ProtInc

nucleus

Inferred from direct assay Ref.4. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.10. Source: UniProtKB

cyclin-dependent protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein kinase activity

Traceable author statement Ref.3Ref.4. Source: ProtInc

protein serine/threonine kinase activity

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EIF3FO003033EBI-1298,EBI-711990
PAK1Q131534EBI-1298,EBI-1307

Alternative products

This entry describes 10 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform SV9 (identifier: P21127-1)

Also known as: p110;

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 SV1 (identifier: P21127-2)

Also known as: Alpha 2-1;

The sequence of this isoform differs from the canonical sequence as follows:
     252-265: GEARPARAQKPAQL → V
Isoform 2 (identifier: P21127-3)

Also known as: Alpha 2-2;

The sequence of this isoform differs from the canonical sequence as follows:
     110-119: Missing.
     165-165: R → RGNDGVCLFR
     252-265: GEARPARAQKPAQL → V
Isoform 3 (identifier: P21127-4)

Also known as: Alpha 1;

The sequence of this isoform differs from the canonical sequence as follows:
     2-335: Missing.
Isoform SV4 (identifier: P21127-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-269: Missing.
Isoform SV5 (identifier: P21127-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.
     35-37: LKN → MSQ
     110-119: Missing.
     252-265: GEARPARAQKPAQL → V
Isoform 8 (identifier: P21127-8)

Also known as: Alpha 2-3;

The sequence of this isoform differs from the canonical sequence as follows:
     110-119: Missing.
     252-265: GEARPARAQKPAQL → V
Isoform SV10 (identifier: P21127-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.
     35-37: LKN → MSQ
     252-265: GEARPARAQKPAQL → V
Isoform SV11 (identifier: P21127-10)

Also known as: Alpha 2-4;

The sequence of this isoform differs from the canonical sequence as follows:
     1-217: Missing.
     252-265: GEARPARAQKPAQL → V
Isoform 7 (identifier: P21127-12)

Also known as: p58;

The sequence of this isoform differs from the canonical sequence as follows:
     1-356: Missing.
Note: Produced by alternative initiation at Met-357 of isoform SV9.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 795795Cyclin-dependent kinase 11B
PRO_0000024311

Regions

Domain438 – 723286Protein kinase
Nucleotide binding444 – 4529ATP By similarity
Compositional bias126 – 393268Glu-rich

Sites

Active site5621Proton acceptor By similarity
Binding site4671ATP By similarity

Amino acid modifications

Modified residue1151Phosphoserine Ref.12
Modified residue4821Phosphoserine; by CDK7 Ref.15
Modified residue4881Phosphothreonine; by CDK7 Ref.15
Modified residue5891Phosphoserine Ref.18
Modified residue5941Phosphotyrosine Ref.17
Modified residue5951Phosphothreonine Ref.14 Ref.17 Ref.18 Ref.19 Ref.20

Natural variations

Alternative sequence1 – 356356Missing in isoform 7.
VSP_018834
Alternative sequence1 – 269269Missing in isoform SV4.
VSP_008275
Alternative sequence1 – 217217Missing in isoform SV11.
VSP_008274
Alternative sequence1 – 3434Missing in isoform SV5 and isoform SV10.
VSP_008273
Alternative sequence2 – 335334Missing in isoform 3.
VSP_008276
Alternative sequence35 – 373LKN → MSQ in isoform SV5 and isoform SV10.
VSP_008277
Alternative sequence110 – 11910Missing in isoform 2, isoform SV5 and isoform 8.
VSP_008278
Alternative sequence1651R → RGNDGVCLFR in isoform 2.
VSP_008279
Alternative sequence252 – 26514GEARP…KPAQL → V in isoform SV1, isoform 2, isoform SV5, isoform 8, isoform SV10 and isoform SV11.
VSP_008280
Natural variant571R → C. Ref.4 Ref.21
Corresponds to variant rs17424353 [ dbSNP | Ensembl ].
VAR_041958
Natural variant931R → W.
Corresponds to variant rs1059831 [ dbSNP | Ensembl ].
VAR_057775
Natural variant1091R → C.
Corresponds to variant rs1059830 [ dbSNP | Ensembl ].
VAR_062199
Natural variant2011R → W. Ref.21
VAR_041959
Natural variant4141S → L. Ref.21
VAR_041960
Natural variant4521V → A. Ref.21
VAR_045577
Natural variant4631I → V. Ref.21
VAR_041961
Natural variant5061G → S. Ref.21
VAR_045578
Natural variant6011L → Q. Ref.3 Ref.21
VAR_041962
Natural variant6411K → N. Ref.21
VAR_041963
Natural variant6701A → V. Ref.21
Corresponds to variant rs1059811 [ dbSNP | Ensembl ].
VAR_041964

Experimental info

Sequence conflict1091Missing in AAA19582. Ref.4
Sequence conflict1091Missing in AAA19583. Ref.4
Sequence conflict1091Missing in AAC72079. Ref.5
Sequence conflict1261E → K in AAA19582. Ref.4
Sequence conflict1261E → K in AAA19583. Ref.4
Sequence conflict1261E → K in AAA19586. Ref.4
Sequence conflict3201S → T Ref.6
Sequence conflict324 – 3263Missing in AAA19582. Ref.4
Sequence conflict324 – 3263Missing in AAA19583. Ref.4
Sequence conflict324 – 3263Missing in AAA19584. Ref.4
Sequence conflict324 – 3263Missing in AAA19586. Ref.4
Sequence conflict4361E → D Ref.3
Sequence conflict5601H → Q Ref.6
Sequence conflict5671N → T Ref.6
Sequence conflict6781E → R Ref.4
Sequence conflict6781E → R Ref.6
Sequence conflict6941D → E Ref.3
Sequence conflict6971F → C Ref.6
Sequence conflict7121I → L Ref.3
Sequence conflict7151E → Q Ref.3
Sequence conflict7921S → R Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform SV9 (p110) [UniParc].

Last modified September 19, 2003. Version 3.
Checksum: C07CEE9A4F7A6804

FASTA79592,707
        10         20         30         40         50         60 
MGDEKDSWKV KTLDEILQEK KRRKEQEEKA EIKRLKNSDD RDSKRDSLEE GELRDHRMEI 

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

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

       190        200        210        220        230        240 
MREQQKEQRE QKERERRAEE RRKEREARRE VSAHHRTMRE DYSDKVKASH WSRSPPRPPR 

       250        260        270        280        290        300 
ERFELGDGRK PGEARPARAQ KPAQLKEEKM EERDLLSDLQ DISDSERKTS SAESSSAESG 

       310        320        330        340        350        360 
SGSEEEEEEE EEEEEEGSTS EESEEEEEEE EEEEEETGSN SEEASEQSAE EVSEEEMSED 

       370        380        390        400        410        420 
EERENENHLL VVPESRFDRD SGESEEAEEE VGEGTPQSSA LTEGDYVPDS PALSPIELKQ 

       430        440        450        460        470        480 
ELPKYLPALQ GCRSVEEFQC LNRIEEGTYG VVYRAKDKKT DEIVALKRLK MEKEKEGFPI 

       490        500        510        520        530        540 
TSLREINTIL KAQHPNIVTV REIVVGSNMD KIYIVMNYVE HDLKSLMETM KQPFLPGEVK 

       550        560        570        580        590        600 
TLMIQLLRGV KHLHDNWILH RDLKTSNLLL SHAGILKVGD FGLAREYGSP LKAYTPVVVT 

       610        620        630        640        650        660 
LWYRAPELLL GAKEYSTAVD MWSVGCIFGE LLTQKPLFPG KSEIDQINKV FKDLGTPSEK 

       670        680        690        700        710        720 
IWPGYSELPA VKKMTFSEHP YNNLRKRFGA LLSDQGFDLM NKFLTYFPGR RISAEDGLKH 

       730        740        750        760        770        780 
EYFRETPLPI DPSMFPTWPA KSEQQRVKRG TSPRPPEGGL GYSQLGDDDL KETGFHLTTT 

       790 
NQGASAAGPG FSLKF 

« Hide

Isoform SV1 (Alpha 2-1) [UniParc].

Checksum: 63A4E5BDBE1411FE
Show »

FASTA78291,331
Isoform 2 (Alpha 2-2) [UniParc].

Checksum: EDEE50FC3D19E26D
Show »

FASTA78191,218
Isoform 3 (Alpha 1) [UniParc].

Checksum: 6D054208C50D621C
Show »

FASTA46151,925
Isoform SV4 [UniParc].

Checksum: 3DFF4854ED82B81B
Show »

FASTA52659,273
Isoform SV5 [UniParc].

Checksum: 0885FB5ECECB398A
Show »

FASTA73886,063
Isoform 8 (Alpha 2-3) [UniParc].

Checksum: 03929873CFBD1CF6
Show »

FASTA77290,256
Isoform SV10 [UniParc].

Checksum: A13766F2F6F8E00A
Show »

FASTA74887,138
Isoform SV11 (Alpha 2-4) [UniParc].

Checksum: 6E088C8322ADB36A
Show »

FASTA56563,937
Isoform 7 (p58) [UniParc].

Checksum: 2008B90F6CE66EF6
Show »

FASTA43949,555

References

« Hide 'large scale' references
[1]"Increased expression of a 58-kDa protein kinase leads to changes in the CHO cell cycle."
Bunnell B.A., Heath L.S., Adams D.E., Lahti J.M., Kidd V.J.
Proc. Natl. Acad. Sci. U.S.A. 87:7467-7471(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), FUNCTION.
Tissue: Liver.
[2]Erratum
Bunnell B.A., Heath L.S., Adams D.E., Lahti J.M., Kidd V.J.
Proc. Natl. Acad. Sci. U.S.A. 88:2612-2612(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"Structure and expression of the human p58clk-1 protein kinase chromosomal gene."
Eipers P.G., Lahti J.M., Kidd V.J.
Genomics 13:613-621(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 7), VARIANT GLN-601.
Tissue: Hematopoietic.
[4]"Molecular cloning and expression of alternatively spliced PITSLRE protein kinase isoforms."
Xiang J., Lahti J.M., Grenet J.A., Easton J.B., Kidd V.J.
J. Biol. Chem. 269:15786-15794(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SV1; 2; 3; 8 AND SV11), VARIANT CYS-57, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Tissue: Cervix carcinoma.
[5]"Duplication of a genomic region containing the Cdc2L1-2 and MMP21-22 genes on human chromosome 1p36.3 and their linkage to D1Z2."
Gururajan R., Lahti J.M., Grenet J.A., Easton J., Gruber I., Ambros P.F., Kidd V.J.
Genome Res. 8:929-939(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS SV1; SV4; SV5; SV9; SV10 AND SV11), TISSUE SPECIFICITY.
Tissue: Cervix carcinoma.
[6]Govindan M.V., Warriar N.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SV11).
Tissue: Placenta.
[7]"The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinases in vivo."
Loyer P., Trembley J.H., Lahti J.M., Kidd V.J.
J. Cell Sci. 111:1495-1506(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNPS1.
[8]"Identification and characterization of a novel cell cycle-regulated internal ribosome entry site."
Cornelis S., Bruynooghe Y., Denecker G., Van Huffel S., Tinton S., Beyaert R.
Mol. Cell 5:597-605(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE INITIATION (ISOFORM 7), INDUCTION.
[9]"The cyclin-dependent kinase 11(p46) isoform interacts with RanBPM."
Mikolajczyk M., Shi J., Vaillancourt R.R., Sachs N.A., Nelson M.
Biochem. Biophys. Res. Commun. 310:14-18(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RANBP9, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION.
[10]"CDK11 complexes promote pre-mRNA splicing."
Hu D., Mayeda A., Trembley J.H., Lahti J.M., Kidd V.J.
J. Biol. Chem. 278:8623-8629(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CCNL1 AND SFRS7.
[11]"The C-terminal kinase domain of the p34cdc2-related PITSLRE protein kinase (p110C) associates with p21-activated kinase 1 and inhibits its activity during anoikis."
Chen S., Yin X., Zhu X., Yan J., Ji S., Chen C., Cai M., Zhang S., Zong H., Hu Y., Yuan Z., Shen Z., Gu J.
J. Biol. Chem. 278:20029-20036(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PAK1.
[12]"The cyclin-dependent kinase 11 interacts with 14-3-3 proteins."
Feng Y., Qi W., Martinez J., Nelson M.A.
Biochem. Biophys. Res. Commun. 331:1503-1509(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-115.
[13]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-595, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Dichotomous but stringent substrate selection by the dual-function Cdk7 complex revealed by chemical genetics."
Larochelle S., Batliner J., Gamble M.J., Barboza N.M., Kraybill B.C., Blethrow J.D., Shokat K.M., Fisher R.P.
Nat. Struct. Mol. Biol. 13:55-62(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-482 AND THR-488 BY CDK7.
[16]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-594 AND THR-595, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589 AND THR-595, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-595, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-595, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-57; TRP-201; LEU-414; ALA-452; VAL-463; SER-506; GLN-601; ASN-641 AND VAL-670.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M37712 mRNA. Translation: AAA36406.1. Sequence problems.
M88563 expand/collapse EMBL AC list , M88553, M88554, M88555, M88558, M88559, M88560, M88561, M88562 Genomic DNA. Translation: AAB59449.1. Sequence problems.
U04815 mRNA. Translation: AAA19581.1.
U04816 mRNA. Translation: AAA19582.1.
U04817 mRNA. Translation: AAA19583.1.
U04818 mRNA. Translation: AAA19584.1.
U04824 mRNA. Translation: AAA19586.1.
AF067512 mRNA. Translation: AAC72077.1.
AF067513 mRNA. Translation: AAC72078.1.
AF067514 mRNA. Translation: AAC72079.1.
AF067515 mRNA. Translation: AAC72080.1.
AF067516 mRNA. Translation: AAC72081.1.
AF067517 mRNA. Translation: AAC72082.1.
AF080683 expand/collapse EMBL AC list , AF080685, AF080686, AF080687, AF080688, AF092429, AF092430, AF080678, AF080679, AF080680, AF080681, AF080682 Genomic DNA. Translation: AAC83662.1.
AF080683 expand/collapse EMBL AC list , AF080685, AF080686, AF080687, AF080688, AF092429, AF092430, AF080678, AF080679, AF080680, AF080681, AF080682 Genomic DNA. Translation: AAC83663.1.
AF080683 expand/collapse EMBL AC list , AF080685, AF080686, AF080687, AF080688, AF092429, AF092430, AF080678, AF080679, AF080680, AF080681, AF080682 Genomic DNA. Translation: AAC83664.1. Sequence problems.
AF080683 expand/collapse EMBL AC list , AF080685, AF080686, AF080687, AF080688, AF092429, AF092430, AF080678, AF080679, AF080680, AF080681, AF080682 Genomic DNA. Translation: AAC83665.1.
AF080683 expand/collapse EMBL AC list , AF092430, AF080678, AF080679, AF080680, AF080681, AF080682 Genomic DNA. Translation: AAC83666.1.
AF174497 mRNA. Translation: AAF36538.1. Different initiation.
PIRA38282.
B54024.
E54024.
F54024.
H54024.
T09568.
RefSeqNP_277021.1. NM_033486.1.
NP_277022.1. NM_033487.1.
NP_277023.1. NM_033488.1.
NP_277024.1. NM_033489.1.
NP_277027.1. NM_033492.1.
NP_277028.1. NM_033493.1.
UniGeneHs.709182.

3D structure databases

ProteinModelPortalP21127.
SMRP21127. Positions 374-765.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107421. 30 interactions.
IntActP21127. 11 interactions.
MINTMINT-1400900.

Chemistry

BindingDBP21127.
ChEMBLCHEMBL5808.
GuidetoPHARMACOLOGY1964.

PTM databases

PhosphoSiteP21127.

Polymorphism databases

DMDM34978359.

Proteomic databases

PRIDEP21127.

Protocols and materials databases

DNASU984.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID984.
KEGGhsa:984.
UCSCuc001ags.1. human. [P21127-1]
uc001agt.1. human. [P21127-10]
uc001agv.1. human. [P21127-2]
uc001agw.1. human. [P21127-6]
uc001agx.1. human. [P21127-8]
uc001agy.1. human. [P21127-3]
uc001aha.1. human. [P21127-9]

Organism-specific databases

CTD984.
GeneCardsGC01M001574.
HGNCHGNC:1729. CDK11B.
HPACAB010467.
HPA025061.
MIM176873. gene.
neXtProtNX_P21127.
PharmGKBPA26262.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG014652.
InParanoidP21127.
KOK08818.
PhylomeDBP21127.

Enzyme and pathway databases

BRENDA2.7.11.22. 2681.
ReactomeREACT_115566. Cell Cycle.
SignaLinkP21127.

Gene expression databases

GenevestigatorP21127.

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. human.
GeneWikiCDC2L1.
GenomeRNAi984.
NextBio4128.
PMAP-CutDBP21127.
PROP21127.
SOURCESearch...

Entry information

Entry nameCD11B_HUMAN
AccessionPrimary (citable) accession number: P21127
Secondary accession number(s): O95265 expand/collapse secondary AC list , Q12817, Q12818, Q12819, Q12820, Q12822, Q8N530, Q9NZS5, Q9UBJ0, Q9UBQ1, Q9UBR0, Q9UNY2, Q9UP57, Q9UP58, Q9UP59
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: September 19, 2003
Last modified: April 16, 2014
This is version 160 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM