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P21127

- CD11B_HUMAN

UniProt

P21127 - CD11B_HUMAN

Protein

Cyclin-dependent kinase 11B

Gene

CDK11B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 3 (19 Sep 2003)
      Previous versions | rss
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    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 binding Source: IntAct
    5. protein kinase activity Source: ProtInc
    6. 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

    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

    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. 30 interactions.
    IntActiP21127. 11 interactions.
    MINTiMINT-1400900.

    Structurei

    3D structure databases

    ProteinModelPortaliP21127.
    SMRiP21127. Positions 374-745.
    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_dom.
    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

    MGDEKDSWKV KTLDEILQEK KRRKEQEEKA EIKRLKNSDD RDSKRDSLEE    50
    GELRDHRMEI TIRNSPYRRE DSMEDRGEED DSLAIKPPQQ MSRKEKVHHR 100
    KDEKRKEKRR HRSHSAEGGK HARVKEKERE HERRKRHREE QDKARREWER 150
    QKRREMAREH SRRERDRLEQ LERKRERERK MREQQKEQRE QKERERRAEE 200
    RRKEREARRE VSAHHRTMRE DYSDKVKASH WSRSPPRPPR ERFELGDGRK 250
    PGEARPARAQ KPAQLKEEKM EERDLLSDLQ DISDSERKTS SAESSSAESG 300
    SGSEEEEEEE EEEEEEGSTS EESEEEEEEE EEEEEETGSN SEEASEQSAE 350
    EVSEEEMSED EERENENHLL VVPESRFDRD SGESEEAEEE VGEGTPQSSA 400
    LTEGDYVPDS PALSPIELKQ ELPKYLPALQ GCRSVEEFQC LNRIEEGTYG 450
    VVYRAKDKKT DEIVALKRLK MEKEKEGFPI TSLREINTIL KAQHPNIVTV 500
    REIVVGSNMD KIYIVMNYVE HDLKSLMETM KQPFLPGEVK TLMIQLLRGV 550
    KHLHDNWILH RDLKTSNLLL SHAGILKVGD FGLAREYGSP LKAYTPVVVT 600
    LWYRAPELLL GAKEYSTAVD MWSVGCIFGE LLTQKPLFPG KSEIDQINKV 650
    FKDLGTPSEK IWPGYSELPA VKKMTFSEHP YNNLRKRFGA LLSDQGFDLM 700
    NKFLTYFPGR RISAEDGLKH EYFRETPLPI DPSMFPTWPA KSEQQRVKRG 750
    TSPRPPEGGL GYSQLGDDDL KETGFHLTTT NQGASAAGPG FSLKF 795
    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.
    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.
    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 374-745.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107421. 30 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_dom.
    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

    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 1, 2014
    This is version 165 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