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Q14004

- CDK13_HUMAN

UniProt

Q14004 - CDK13_HUMAN

Protein

Cyclin-dependent kinase 13

Gene

CDK13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (10 May 2005)
      Previous versions | rss
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    Functioni

    Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef.4 Publications

    Catalytic activityi

    ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.1 Publication
    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei734 – 7341ATPPROSITE-ProRule annotation
    Active sitei837 – 8371Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi711 – 7199ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cyclin binding Source: MGI
    3. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein kinase activity Source: ProtInc
    7. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB

    GO - Biological processi

    1. alternative mRNA splicing, via spliceosome Source: UniProtKB
    2. hemopoiesis Source: UniProtKB
    3. multicellular organismal development Source: ProtInc
    4. phosphorylation of RNA polymerase II C-terminal domain Source: UniProtKB
    5. positive regulation of cell proliferation Source: ProtInc
    6. regulation of mitosis Source: ProtInc
    7. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Host-virus interaction, mRNA processing, mRNA splicing

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ14004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-dependent kinase 13 (EC:2.7.11.22, EC:2.7.11.23)
    Alternative name(s):
    CDC2-related protein kinase 5
    Cell division cycle 2-like protein kinase 5
    Cell division protein kinase 13
    Short name:
    hCDK13
    Cholinesterase-related cell division controller
    Gene namesi
    Name:CDK13
    Synonyms:CDC2L, CDC2L5, CHED, KIAA1791
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:1733. CDK13.

    Subcellular locationi

    Nucleus speckle 1 Publication

    GO - Cellular componenti

    1. cyclin K-CDK13 complex Source: MGI
    2. extracellular space Source: UniProt
    3. nuclear cyclin-dependent protein kinase holoenzyme complex Source: UniProtKB
    4. nuclear speck Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26264.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15121512Cyclin-dependent kinase 13PRO_0000085711Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei315 – 3151Phosphoserine2 Publications
    Modified residuei317 – 3171Phosphoserine2 Publications
    Modified residuei325 – 3251Phosphoserine1 Publication
    Modified residuei340 – 3401Phosphoserine1 Publication
    Modified residuei342 – 3421Phosphoserine1 Publication
    Modified residuei383 – 3831Phosphoserine3 Publications
    Modified residuei395 – 3951Phosphoserine2 Publications
    Modified residuei397 – 3971Phosphoserine2 Publications
    Modified residuei400 – 4001Phosphoserine2 Publications
    Modified residuei437 – 4371Phosphoserine3 Publications
    Modified residuei439 – 4391Phosphoserine3 Publications
    Modified residuei525 – 5251Phosphoserine1 Publication
    Modified residuei556 – 5561N6-acetyllysine1 Publication
    Modified residuei871 – 8711Phosphothreonine3 Publications
    Modified residuei1048 – 10481Phosphoserine1 Publication
    Modified residuei1246 – 12461Phosphothreonine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ14004.
    PaxDbiQ14004.
    PRIDEiQ14004.

    PTM databases

    PhosphoSiteiQ14004.

    Miscellaneous databases

    PMAP-CutDBQ14004.

    Expressioni

    Tissue specificityi

    Expressed in fetal brain, liver, muscle and in adult brain. Also expressed in neuroblastoma and glioblastoma tumors.

    Gene expression databases

    BgeeiQ14004.
    CleanExiHS_CDC2L5.
    GenevestigatoriQ14004.

    Organism-specific databases

    HPAiHPA059241.

    Interactioni

    Subunit structurei

    Interacts with CCNL1 and CCNL2 By similarity. Interacts with CCNK. Interacts with C1QBP. Interacts with HIV-1 Tat.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    C1QBPQ070216EBI-6375898,EBI-347528

    Protein-protein interaction databases

    BioGridi114176. 18 interactions.
    IntActiQ14004. 6 interactions.
    MINTiMINT-1197921.
    STRINGi9606.ENSP00000181839.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14004.
    SMRiQ14004. Positions 677-1024.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini705 – 998294Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG050851.
    InParanoidiQ14004.
    KOiK08819.
    OMAiKERHREH.
    OrthoDBiEOG76DTSM.
    PhylomeDBiQ14004.
    TreeFamiTF101060.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    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.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. 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 splicing. Align

    Isoform 1 (identifier: Q14004-1) [UniParc]FASTAAdd to Basket

    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

    MPSSSDTALG GGGGLSWAEK KLEERRKRRR FLSPQQPPLL LPLLQPQLLQ     50
    PPPPPPPLLF LAAPGTAAAA AAAAAASSSC FSPGPPLEVK RLARGKRRAG 100
    GRQKRRRGPR AGQEAEKRRV FSLPQPQQDG GGGASSGGGV TPLVEYEDVS 150
    SQSEQGLLLG GASAATAATA AGGTGGSGGS PASSSGTQRR GEGSERRPRR 200
    DRRSSSGRSK ERHREHRRRD GQRGGSEASK SRSRHSHSGE ERAEVAKSGS 250
    SSSSGGRRKS ASATSSSSSS RKDRDSKAHR SRTKSSKEPP SAYKEPPKAY 300
    REDKTEPKAY RRRRSLSPLG GRDDSPVSHR ASQSLRSRKS PSPAGGGSSP 350
    YSRRLPRSPS PYSRRRSPSY SRHSSYERGG DVSPSPYSSS SWRRSRSPYS 400
    PVLRRSGKSR SRSPYSSRHS RSRSRHRLSR SRSRHSSISP STLTLKSSLA 450
    AELNKNKKAR AAEAARAAEA AKAAEATKAA EAAAKAAKAS NTSTPTKGNT 500
    ETSASASQTN HVKDVKKIKI EHAPSPSSGG TLKNDKAKTK PPLQVTKVEN 550
    NLIVDKATKK AVIVGKESKS AATKEESVSL KEKTKPLTPS IGAKEKEQHV 600
    ALVTSTLPPL PLPPMLPEDK EADSLRGNIS VKAVKKEVEK KLRCLLADLP 650
    LPPELPGGDD LSKSPEEKKT ATQLHSKRRP KICGPRYGET KEKDIDWGKR 700
    CVDKFDIIGI IGEGTYGQVY KARDKDTGEM VALKKVRLDN EKEGFPITAI 750
    REIKILRQLT HQSIINMKEI VTDKEDALDF KKDKGAFYLV FEYMDHDLMG 800
    LLESGLVHFN ENHIKSFMRQ LMEGLDYCHK KNFLHRDIKC SNILLNNRGQ 850
    IKLADFGLAR LYSSEESRPY TNKVITLWYR PPELLLGEER YTPAIDVWSC 900
    GCILGELFTK KPIFQANQEL AQLELISRIC GSPCPAVWPD VIKLPYFNTM 950
    KPKKQYRRKL REEFVFIPAA ALDLFDYMLA LDPSKRCTAE QALQCEFLRD 1000
    VEPSKMPPPD LPLWQDCHEL WSKKRRRQKQ MGMTDDVSTI KAPRKDLSLG 1050
    LDDSRTNTPQ GVLPSSQLKS QGSSNVAPVK TGPGQHLNHS ELAILLNLLQ 1100
    SKTSVNMADF VQVLNIKVNS ETQQQLNKIN LPAGILATGE KQTDPSTPQQ 1150
    ESSKPLGGIQ PSSQTIQPKV ETDAAQAAVQ SAFAVLLTQL IKAQQSKQKD 1200
    VLLEERENGS GHEASLQLRP PPEPSTPVSG QDDLIQHQDM RILELTPEPD 1250
    RPRILPPDQR PPEPPEPPPV TEEDLDYRTE NQHVPTTSSS LTDPHAGVKA 1300
    ALLQLLAQHQ PQDDPKREGG IDYQAGDTYV STSDYKDNFG SSSFSSAPYV 1350
    SNDGLGSSSA PPLERRSFIG NSDIQSLDNY STASSHSGGP PQPSAFSESF 1400
    PSSVAGYGDI YLNAGPMLFS GDKDHRFEYS HGPIAVLANS SDPSTGPEST 1450
    HPLPAKMHNY NYGGNLQENP SGPSLMHGQT WTSPAQGPGY SQGYRGHIST 1500
    STGRGRGRGL PY 1512
    Length:1,512
    Mass (Da):164,923
    Last modified:May 10, 2005 - v2
    Checksum:i3CA54A3585A2943D
    GO
    Isoform 2 (identifier: Q14004-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1079-1138: Missing.

    Show »
    Length:1,452
    Mass (Da):158,435
    Checksum:i8A8B712D8621EEA3
    GO

    Sequence cautioni

    The sequence AAA58424.1 differs from that shown. Reason: Frameshift at position 1006.
    The sequence AAS07490.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211K → R in CAC10400. (PubMed:11162436)Curated
    Sequence conflicti21 – 211K → R in CAC10401. (PubMed:11162436)Curated
    Sequence conflicti671 – 6711A → T in CAC10400. (PubMed:11162436)Curated
    Sequence conflicti671 – 6711A → T in CAC10401. (PubMed:11162436)Curated
    Sequence conflicti671 – 6711A → T in AAA58424. (PubMed:1731328)Curated
    Sequence conflicti810 – 8101N → Y in AAA58424. (PubMed:1731328)Curated
    Sequence conflicti862 – 8665YSSEE → FSVFF in BAB47420. 1 PublicationCurated
    Sequence conflicti1180 – 11801Q → R in BAD96773. 1 PublicationCurated
    Sequence conflicti1356 – 13561G → E in BAD96773. 1 PublicationCurated

    RNA editingi

    Edited at about 88%.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti103 – 1031Q → R in RNA edited version.
    VAR_066526
    Natural varianti340 – 3401S → F.
    Corresponds to variant rs13622 [ dbSNP | Ensembl ].
    VAR_053926
    Natural varianti356 – 3561P → A.1 Publication
    Corresponds to variant rs17537669 [ dbSNP | Ensembl ].
    VAR_022381
    Natural varianti403 – 4031L → F.1 Publication
    Corresponds to variant rs3735137 [ dbSNP | Ensembl ].
    VAR_022382
    Natural varianti410 – 4101R → Q.1 Publication
    Corresponds to variant rs17496261 [ dbSNP | Ensembl ].
    VAR_022383
    Natural varianti494 – 4941T → A.1 Publication
    Corresponds to variant rs34624759 [ dbSNP | Ensembl ].
    VAR_041965
    Natural varianti500 – 5001T → A.2 Publications
    Corresponds to variant rs3735135 [ dbSNP | Ensembl ].
    VAR_022384
    Natural varianti624 – 6241S → G.1 Publication
    Corresponds to variant rs17496275 [ dbSNP | Ensembl ].
    VAR_022385
    Natural varianti670 – 6701T → R.1 Publication
    Corresponds to variant rs34775357 [ dbSNP | Ensembl ].
    VAR_041966
    Natural varianti700 – 7001R → L.2 Publications
    Corresponds to variant rs1057000 [ dbSNP | Ensembl ].
    VAR_022386
    Natural varianti1062 – 10621V → M.1 Publication
    Corresponds to variant rs17496712 [ dbSNP | Ensembl ].
    VAR_022387
    Natural varianti1170 – 11701V → M.2 Publications
    Corresponds to variant rs3204309 [ dbSNP | Ensembl ].
    VAR_041967

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1079 – 113860Missing in isoform 2. 2 PublicationsVSP_013579Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ297709 mRNA. Translation: CAC10400.1.
    AJ297710 mRNA. Translation: CAC10401.1.
    AY679523 Genomic DNA. Translation: AAT74623.1.
    AC072061 Genomic DNA. Translation: AAS07490.1. Sequence problems.
    AC072061 Genomic DNA. Translation: AAS07491.1.
    AC006023 Genomic DNA. Translation: AAD54514.1.
    M80629 mRNA. Translation: AAA58424.1. Frameshift.
    AK223053 mRNA. Translation: BAD96773.1.
    AB058694 mRNA. Translation: BAB47420.1.
    CCDSiCCDS5461.1. [Q14004-1]
    CCDS5462.1. [Q14004-2]
    PIRiA38197.
    RefSeqiNP_003709.3. NM_003718.4. [Q14004-1]
    NP_112557.2. NM_031267.3. [Q14004-2]
    UniGeneiHs.233552.

    Genome annotation databases

    EnsembliENST00000181839; ENSP00000181839; ENSG00000065883. [Q14004-1]
    ENST00000340829; ENSP00000340557; ENSG00000065883. [Q14004-2]
    GeneIDi8621.
    KEGGihsa:8621.
    UCSCiuc003thh.4. human. [Q14004-1]
    uc003thi.4. human. [Q14004-2]

    Polymorphism databases

    DMDMi66774048.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism, RNA editing

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ297709 mRNA. Translation: CAC10400.1 .
    AJ297710 mRNA. Translation: CAC10401.1 .
    AY679523 Genomic DNA. Translation: AAT74623.1 .
    AC072061 Genomic DNA. Translation: AAS07490.1 . Sequence problems.
    AC072061 Genomic DNA. Translation: AAS07491.1 .
    AC006023 Genomic DNA. Translation: AAD54514.1 .
    M80629 mRNA. Translation: AAA58424.1 . Frameshift.
    AK223053 mRNA. Translation: BAD96773.1 .
    AB058694 mRNA. Translation: BAB47420.1 .
    CCDSi CCDS5461.1. [Q14004-1 ]
    CCDS5462.1. [Q14004-2 ]
    PIRi A38197.
    RefSeqi NP_003709.3. NM_003718.4. [Q14004-1 ]
    NP_112557.2. NM_031267.3. [Q14004-2 ]
    UniGenei Hs.233552.

    3D structure databases

    ProteinModelPortali Q14004.
    SMRi Q14004. Positions 677-1024.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114176. 18 interactions.
    IntActi Q14004. 6 interactions.
    MINTi MINT-1197921.
    STRINGi 9606.ENSP00000181839.

    Chemistry

    BindingDBi Q14004.
    ChEMBLi CHEMBL1795192.
    GuidetoPHARMACOLOGYi 1966.

    PTM databases

    PhosphoSitei Q14004.

    Polymorphism databases

    DMDMi 66774048.

    Proteomic databases

    MaxQBi Q14004.
    PaxDbi Q14004.
    PRIDEi Q14004.

    Protocols and materials databases

    DNASUi 8621.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000181839 ; ENSP00000181839 ; ENSG00000065883 . [Q14004-1 ]
    ENST00000340829 ; ENSP00000340557 ; ENSG00000065883 . [Q14004-2 ]
    GeneIDi 8621.
    KEGGi hsa:8621.
    UCSCi uc003thh.4. human. [Q14004-1 ]
    uc003thi.4. human. [Q14004-2 ]

    Organism-specific databases

    CTDi 8621.
    GeneCardsi GC07P039957.
    HGNCi HGNC:1733. CDK13.
    HPAi HPA059241.
    MIMi 603309. gene.
    neXtProti NX_Q14004.
    PharmGKBi PA26264.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG050851.
    InParanoidi Q14004.
    KOi K08819.
    OMAi KERHREH.
    OrthoDBi EOG76DTSM.
    PhylomeDBi Q14004.
    TreeFami TF101060.

    Enzyme and pathway databases

    SignaLinki Q14004.

    Miscellaneous databases

    GeneWikii CDC2L5.
    GenomeRNAii 8621.
    NextBioi 32303.
    PMAP-CutDB Q14004.
    PROi Q14004.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q14004.
    CleanExi HS_CDC2L5.
    Genevestigatori Q14004.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    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 PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS LEU-700 AND MET-1170.
      Tissue: Placenta.
    2. NIEHS SNPs program
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-356; PHE-403; GLN-410; ALA-500; GLY-624 AND MET-1062.
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Cloning and antisense oligodeoxynucleotide inhibition of a human homolog of cdc2 required in hematopoiesis."
      Lapidot-Lifson Y., Patinkin D., Prody C.A., Ehrlich G., Seidman S., Ben-Aziz R., Benseler F., Eckstein F., Zakut H., Soreq H.
      Proc. Natl. Acad. Sci. U.S.A. 89:579-583(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 361-1078, FUNCTION, VARIANT LEU-700.
      Tissue: Glioblastoma.
    5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 856-1512 (ISOFORM 2).
      Tissue: Thyroid.
    6. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
      DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 860-1512 (ISOFORM 1).
      Tissue: Brain.
    7. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "CDC2L5, a Cdk-like kinase with RS domain, interacts with the ASF/SF2-associated protein p32 and affects splicing in vivo."
      Even Y., Durieux S., Escande M.L., Lozano J.C., Peaucellier G., Weil D., Geneviere A.M.
      J. Cell. Biochem. 99:890-904(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH C1QBP.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    11. "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.
    12. "CDK13, a new potential human immunodeficiency virus type 1 inhibitory factor regulating viral mRNA splicing."
      Berro R., Pedati C., Kehn-Hall K., Wu W., Klase Z., Even Y., Geneviere A.M., Ammosova T., Nekhai S., Kashanchi F.
      J. Virol. 82:7155-7166(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HIV-1 TAT.
    13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-317; SER-325; SER-340; SER-342; SER-383; SER-395; SER-397; SER-400; SER-437; SER-439 AND THR-871, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1048, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-556, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "CDK12 is a transcription elongation-associated CTD kinase, the metazoan ortholog of yeast Ctk1."
      Bartkowiak B., Liu P., Phatnani H.P., Fuda N.J., Cooper J.J., Price D.H., Adelman K., Lis J.T., Greenleaf A.L.
      Genes Dev. 24:2303-2316(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    20. "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 SER-383; SER-437; SER-439; SER-525 AND THR-871, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: RNA EDITING OF POSITION 103.
    23. "The Cyclin K/Cdk12 complex maintains genomic stability via regulation of expression of DNA damage response genes."
      Blazek D., Kohoutek J., Bartholomeeusen K., Johansen E., Hulinkova P., Luo Z., Cimermancic P., Ule J., Peterlin B.M.
      Genes Dev. 25:2158-2172(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CCNK.
    24. "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 SER-315; SER-317; SER-383; SER-395; SER-397; SER-400; SER-437; SER-439; THR-871 AND THR-1246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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] ALA-494; ALA-500; ARG-670 AND MET-1170.

    Entry informationi

    Entry nameiCDK13_HUMAN
    AccessioniPrimary (citable) accession number: Q14004
    Secondary accession number(s): Q53G78
    , Q6DKQ9, Q75MH4, Q75MH5, Q96JN4, Q9H4A0, Q9H4A1, Q9UDR4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 10, 2005
    Last modified: October 1, 2014
    This is version 145 of the entry and version 2 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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