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Q14004

- CDK13_HUMAN

UniProt

Q14004 - CDK13_HUMAN

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Protein

Cyclin-dependent kinase 13

Gene
CDK13, CDC2L, CDC2L5, CHED, KIAA1791
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 7341ATP By similarity
Active sitei837 – 8371Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi711 – 7199ATP By similarity

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
Complete GO annotation...

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
Complete GO annotation...

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.3 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi114176. 18 interactions.
IntActiQ14004. 5 interactions.
MINTiMINT-1197921.
STRINGi9606.ENSP00000181839.

Structurei

3D structure databases

ProteinModelPortaliQ14004.
SMRiQ14004. Positions 677-1024.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini705 – 998294Protein kinaseAdd
BLAST

Sequence similaritiesi

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.

RNA editingi

Edited at about 88%.1 Publication

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. VSP_013579Add
BLAST

Sequence conflict

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

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. 5 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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 144 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

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