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P21127

- CD11B_HUMAN

UniProt

P21127 - CD11B_HUMAN

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Protein

Cyclin-dependent kinase 11B

Gene

CDK11B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 may act as a negative regulator of normal cell cycle progression.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei467 – 4671ATPPROSITE-ProRule annotation
Active sitei562 – 5621Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi444 – 4529ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
  3. poly(A) RNA binding Source: UniProtKB
  4. protein kinase activity Source: ProtInc
  5. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. cell proliferation Source: ProtInc
  3. mitotic nuclear division Source: UniProtKB
  4. protein phosphorylation Source: UniProtKB
  5. regulation of cell growth Source: UniProtKB
  6. regulation of mRNA processing Source: UniProtKB
  7. regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.22. 2681.
ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
SignaLinkiP21127.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CDK11B
Synonyms:CDC2L1, CDK11, PITSLREA, PK58
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:1729. CDK11B.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26262.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 795795Cyclin-dependent kinase 11BPRO_0000024311Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei115 – 1151Phosphoserine1 Publication
Modified residuei482 – 4821Phosphoserine; by CDK71 Publication
Modified residuei488 – 4881Phosphothreonine; by CDK71 Publication
Modified residuei589 – 5891Phosphoserine1 Publication
Modified residuei594 – 5941Phosphotyrosine1 Publication
Modified residuei595 – 5951Phosphothreonine5 Publications

Post-translational modificationi

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.7 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP21127.
PRIDEiP21127.

PTM databases

PhosphoSiteiP21127.

Miscellaneous databases

PMAP-CutDBP21127.

Expressioni

Tissue specificityi

Expressed ubiquitously. Some evidence of isoform-specific tissue distribution.2 Publications

Inductioni

The p58 isoform is specifically induced in G2/M phase of the cell cycle.1 Publication

Gene expression databases

GenevestigatoriP21127.

Organism-specific databases

HPAiCAB010467.
HPA025061.

Interactioni

Subunit structurei

The cleaved p110 isoform, p110C, binds to the serine/threonine kinase PAK1 and RANBP9. p110C interacts with RNPS1. The p58 isoform but not the p110 isoforms or p110C interacts with CCND3. The p110 isoforms are found in large molecular weight complexes containing CCNL1 and SFRS7.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF3FO003033EBI-1298,EBI-711990
PAK1Q131534EBI-1298,EBI-1307

Protein-protein interaction databases

BioGridi107421. 33 interactions.
IntActiP21127. 11 interactions.
MINTiMINT-1400900.

Structurei

3D structure databases

ProteinModelPortaliP21127.
SMRiP21127. Positions 374-765.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini438 – 723286Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi126 – 393268Glu-richAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG014652.
InParanoidiP21127.
KOiK08818.
PhylomeDBiP21127.

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 (10)i

Sequence statusi: Complete.

This entry describes 10 isoformsi produced by alternative splicing and alternative initiation. Align

Isoform SV9 (identifier: P21127-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGDEKDSWKV KTLDEILQEK KRRKEQEEKA EIKRLKNSDD RDSKRDSLEE
60 70 80 90 100
GELRDHRMEI TIRNSPYRRE DSMEDRGEED DSLAIKPPQQ MSRKEKVHHR
110 120 130 140 150
KDEKRKEKRR HRSHSAEGGK HARVKEKERE HERRKRHREE QDKARREWER
160 170 180 190 200
QKRREMAREH SRRERDRLEQ LERKRERERK MREQQKEQRE QKERERRAEE
210 220 230 240 250
RRKEREARRE VSAHHRTMRE DYSDKVKASH WSRSPPRPPR ERFELGDGRK
260 270 280 290 300
PGEARPARAQ KPAQLKEEKM EERDLLSDLQ DISDSERKTS SAESSSAESG
310 320 330 340 350
SGSEEEEEEE EEEEEEGSTS EESEEEEEEE EEEEEETGSN SEEASEQSAE
360 370 380 390 400
EVSEEEMSED EERENENHLL VVPESRFDRD SGESEEAEEE VGEGTPQSSA
410 420 430 440 450
LTEGDYVPDS PALSPIELKQ ELPKYLPALQ GCRSVEEFQC LNRIEEGTYG
460 470 480 490 500
VVYRAKDKKT DEIVALKRLK MEKEKEGFPI TSLREINTIL KAQHPNIVTV
510 520 530 540 550
REIVVGSNMD KIYIVMNYVE HDLKSLMETM KQPFLPGEVK TLMIQLLRGV
560 570 580 590 600
KHLHDNWILH RDLKTSNLLL SHAGILKVGD FGLAREYGSP LKAYTPVVVT
610 620 630 640 650
LWYRAPELLL GAKEYSTAVD MWSVGCIFGE LLTQKPLFPG KSEIDQINKV
660 670 680 690 700
FKDLGTPSEK IWPGYSELPA VKKMTFSEHP YNNLRKRFGA LLSDQGFDLM
710 720 730 740 750
NKFLTYFPGR RISAEDGLKH EYFRETPLPI DPSMFPTWPA KSEQQRVKRG
760 770 780 790
TSPRPPEGGL GYSQLGDDDL KETGFHLTTT NQGASAAGPG FSLKF
Length:795
Mass (Da):92,707
Last modified:September 19, 2003 - v3
Checksum:iC07CEE9A4F7A6804
GO
Isoform SV1 (identifier: P21127-2) [UniParc]FASTAAdd to Basket

Also known as: Alpha 2-1

The sequence of this isoform differs from the canonical sequence as follows:
     252-265: GEARPARAQKPAQL → V

Show »
Length:782
Mass (Da):91,331
Checksum:i63A4E5BDBE1411FE
GO
Isoform 2 (identifier: P21127-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:781
Mass (Da):91,218
Checksum:iEDEE50FC3D19E26D
GO
Isoform 3 (identifier: P21127-4) [UniParc]FASTAAdd to Basket

Also known as: Alpha 1

The sequence of this isoform differs from the canonical sequence as follows:
     2-335: Missing.

Show »
Length:461
Mass (Da):51,925
Checksum:i6D054208C50D621C
GO
Isoform SV4 (identifier: P21127-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-269: Missing.

Show »
Length:526
Mass (Da):59,273
Checksum:i3DFF4854ED82B81B
GO
Isoform SV5 (identifier: P21127-6) [UniParc]FASTAAdd to Basket

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

Show »
Length:738
Mass (Da):86,063
Checksum:i0885FB5ECECB398A
GO
Isoform 8 (identifier: P21127-8) [UniParc]FASTAAdd to Basket

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

Show »
Length:772
Mass (Da):90,256
Checksum:i03929873CFBD1CF6
GO
Isoform SV10 (identifier: P21127-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.
     35-37: LKN → MSQ
     252-265: GEARPARAQKPAQL → V

Show »
Length:748
Mass (Da):87,138
Checksum:iA13766F2F6F8E00A
GO
Isoform SV11 (identifier: P21127-10) [UniParc]FASTAAdd to Basket

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

Show »
Length:565
Mass (Da):63,937
Checksum:i6E088C8322ADB36A
GO
Isoform 7 (identifier: P21127-12) [UniParc]FASTAAdd to Basket

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.

Show »
Length:439
Mass (Da):49,555
Checksum:i2008B90F6CE66EF6
GO

Sequence cautioni

The sequence AAF36538.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAC83664.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091Missing in AAA19582. (PubMed:8195233)Curated
Sequence conflicti109 – 1091Missing in AAA19583. (PubMed:8195233)Curated
Sequence conflicti109 – 1091Missing in AAC72079. (PubMed:9750192)Curated
Sequence conflicti126 – 1261E → K in AAA19582. (PubMed:8195233)Curated
Sequence conflicti126 – 1261E → K in AAA19583. (PubMed:8195233)Curated
Sequence conflicti126 – 1261E → K in AAA19586. (PubMed:8195233)Curated
Sequence conflicti320 – 3201S → T1 PublicationCurated
Sequence conflicti324 – 3263Missing in AAA19582. (PubMed:8195233)Curated
Sequence conflicti324 – 3263Missing in AAA19583. (PubMed:8195233)Curated
Sequence conflicti324 – 3263Missing in AAA19584. (PubMed:8195233)Curated
Sequence conflicti324 – 3263Missing in AAA19586. (PubMed:8195233)Curated
Sequence conflicti436 – 4361E → D(PubMed:1639388)Curated
Sequence conflicti560 – 5601H → Q1 PublicationCurated
Sequence conflicti567 – 5671N → T1 PublicationCurated
Sequence conflicti678 – 6781E → R(PubMed:8195233)Curated
Sequence conflicti678 – 6781E → R1 PublicationCurated
Sequence conflicti694 – 6941D → E(PubMed:1639388)Curated
Sequence conflicti697 – 6971F → C1 PublicationCurated
Sequence conflicti712 – 7121I → L(PubMed:1639388)Curated
Sequence conflicti715 – 7151E → Q(PubMed:1639388)Curated
Sequence conflicti792 – 7921S → R1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571R → C.2 Publications
Corresponds to variant rs17424353 [ dbSNP | Ensembl ].
VAR_041958
Natural varianti93 – 931R → W.
Corresponds to variant rs1059831 [ dbSNP | Ensembl ].
VAR_057775
Natural varianti109 – 1091R → C.
Corresponds to variant rs1059830 [ dbSNP | Ensembl ].
VAR_062199
Natural varianti201 – 2011R → W.1 Publication
VAR_041959
Natural varianti414 – 4141S → L.1 Publication
VAR_041960
Natural varianti452 – 4521V → A.1 Publication
VAR_045577
Natural varianti463 – 4631I → V.1 Publication
VAR_041961
Natural varianti506 – 5061G → S.1 Publication
VAR_045578
Natural varianti601 – 6011L → Q.2 Publications
VAR_041962
Natural varianti641 – 6411K → N.1 Publication
VAR_041963
Natural varianti670 – 6701A → V.1 Publication
Corresponds to variant rs1059811 [ dbSNP | Ensembl ].
VAR_041964

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 356356Missing in isoform 7. 1 PublicationVSP_018834Add
BLAST
Alternative sequencei1 – 269269Missing in isoform SV4. 1 PublicationVSP_008275Add
BLAST
Alternative sequencei1 – 217217Missing in isoform SV11. 3 PublicationsVSP_008274Add
BLAST
Alternative sequencei1 – 3434Missing in isoform SV5 and isoform SV10. 1 PublicationVSP_008273Add
BLAST
Alternative sequencei2 – 335334Missing in isoform 3. 1 PublicationVSP_008276Add
BLAST
Alternative sequencei35 – 373LKN → MSQ in isoform SV5 and isoform SV10. 1 PublicationVSP_008277
Alternative sequencei110 – 11910Missing in isoform 2, isoform SV5 and isoform 8. 2 PublicationsVSP_008278
Alternative sequencei165 – 1651R → RGNDGVCLFR in isoform 2. 1 PublicationVSP_008279
Alternative sequencei252 – 26514GEARP…KPAQL → V in isoform SV1, isoform 2, isoform SV5, isoform 8, isoform SV10 and isoform SV11. 3 PublicationsVSP_008280Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M37712 mRNA. Translation: AAA36406.1. Sequence problems.
M88563
, 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
, AF080685, AF080686, AF080687, AF080688, AF092429, AF092430, AF080678, AF080679, AF080680, AF080681, AF080682 Genomic DNA. Translation: AAC83662.1.
AF080683
, AF080685, AF080686, AF080687, AF080688, AF092429, AF092430, AF080678, AF080679, AF080680, AF080681, AF080682 Genomic DNA. Translation: AAC83663.1.
AF080683
, AF080685, AF080686, AF080687, AF080688, AF092429, AF092430, AF080678, AF080679, AF080680, AF080681, AF080682 Genomic DNA. Translation: AAC83664.1. Sequence problems.
AF080683
, AF080685, AF080686, AF080687, AF080688, AF092429, AF092430, AF080678, AF080679, AF080680, AF080681, AF080682 Genomic DNA. Translation: AAC83665.1.
AF080683
, AF092430, AF080678, AF080679, AF080680, AF080681, AF080682 Genomic DNA. Translation: AAC83666.1.
AF174497 mRNA. Translation: AAF36538.1. Different initiation.
CCDSiCCDS72682.1. [P21127-9]
CCDS72683.1. [P21127-1]
CCDS72684.1. [P21127-2]
PIRiA38282.
B54024.
E54024.
F54024.
H54024.
T09568.
RefSeqiNP_277022.1. NM_033487.2. [P21127-5]
NP_277025.1. NM_033490.2. [P21127-10]
UniGeneiHs.651228.
Hs.709182.

Genome annotation databases

GeneIDi984.
KEGGihsa:984.
UCSCiuc001ags.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]

Polymorphism databases

DMDMi34978359.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M37712 mRNA. Translation: AAA36406.1 . Sequence problems.
M88563
, 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
, AF080685 , AF080686 , AF080687 , AF080688 , AF092429 , AF092430 , AF080678 , AF080679 , AF080680 , AF080681 , AF080682 Genomic DNA. Translation: AAC83662.1 .
AF080683
, AF080685 , AF080686 , AF080687 , AF080688 , AF092429 , AF092430 , AF080678 , AF080679 , AF080680 , AF080681 , AF080682 Genomic DNA. Translation: AAC83663.1 .
AF080683
, AF080685 , AF080686 , AF080687 , AF080688 , AF092429 , AF092430 , AF080678 , AF080679 , AF080680 , AF080681 , AF080682 Genomic DNA. Translation: AAC83664.1 . Sequence problems.
AF080683
, AF080685 , AF080686 , AF080687 , AF080688 , AF092429 , AF092430 , AF080678 , AF080679 , AF080680 , AF080681 , AF080682 Genomic DNA. Translation: AAC83665.1 .
AF080683
, AF092430 , AF080678 , AF080679 , AF080680 , AF080681 , AF080682 Genomic DNA. Translation: AAC83666.1 .
AF174497 mRNA. Translation: AAF36538.1 . Different initiation.
CCDSi CCDS72682.1. [P21127-9 ]
CCDS72683.1. [P21127-1 ]
CCDS72684.1. [P21127-2 ]
PIRi A38282.
B54024.
E54024.
F54024.
H54024.
T09568.
RefSeqi NP_277022.1. NM_033487.2. [P21127-5 ]
NP_277025.1. NM_033490.2. [P21127-10 ]
UniGenei Hs.651228.
Hs.709182.

3D structure databases

ProteinModelPortali P21127.
SMRi P21127. Positions 374-765.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107421. 33 interactions.
IntActi P21127. 11 interactions.
MINTi MINT-1400900.

Chemistry

BindingDBi P21127.
ChEMBLi CHEMBL5808.
GuidetoPHARMACOLOGYi 1964.

PTM databases

PhosphoSitei P21127.

Polymorphism databases

DMDMi 34978359.

Proteomic databases

MaxQBi P21127.
PRIDEi P21127.

Protocols and materials databases

DNASUi 984.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 984.
KEGGi hsa:984.
UCSCi uc001ags.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

CTDi 984.
GeneCardsi GC01M001574.
HGNCi HGNC:1729. CDK11B.
HPAi CAB010467.
HPA025061.
MIMi 176873. gene.
neXtProti NX_P21127.
PharmGKBi PA26262.
GenAtlasi Search...

Phylogenomic databases

HOVERGENi HBG014652.
InParanoidi P21127.
KOi K08818.
PhylomeDBi P21127.

Enzyme and pathway databases

BRENDAi 2.7.11.22. 2681.
Reactomei REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
SignaLinki P21127.

Miscellaneous databases

ChiTaRSi CDK11B. human.
GeneWikii CDC2L1.
GenomeRNAii 984.
NextBioi 4128.
PMAP-CutDB P21127.
PROi P21127.
SOURCEi Search...

Gene expression databases

Genevestigatori P21127.

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. "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. 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. 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. 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.
    , 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.

Entry informationi

Entry nameiCD11B_HUMAN
AccessioniPrimary (citable) accession number: P21127
Secondary accession number(s): O95265
, Q12817, Q12818, Q12819, Q12820, Q12822, Q8N530, Q9NZS5, Q9UBJ0, Q9UBQ1, Q9UBR0, Q9UNY2, Q9UP57, Q9UP58, Q9UP59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: September 19, 2003
Last modified: October 29, 2014
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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 which is expressed following IRES-mediated alternative initiation of translation.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3