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Q14004 (CDK13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 130. Feed History...

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

Names and origin

Protein namesRecommended 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 names
Name:CDK13
Synonyms:CDC2L, CDC2L5, CHED, KIAA1791
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length1512 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.9 Ref.12 Ref.18

Catalytic activity

ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate. Ref.18

ATP + a protein = ADP + a phosphoprotein. Ref.18

Subunit structure

Interacts with CCNL1 and CCNL2 By similarity. Interacts with C1QBP. Interacts with HIV-1 Tat. Ref.9 Ref.12

Subcellular location

Nucleus speckle Ref.9.

Tissue specificity

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

Sequence similarities

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

Contains 1 protein kinase domain.

RNA editing

Edited at position 103.
Edited at about 88%. Ref.21

Sequence caution

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.

Ontologies

Keywords
   Biological processHost-virus interaction
mRNA processing
mRNA splicing
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
RNA editing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processalternative mRNA splicing, via spliceosome

Inferred from sequence or structural similarity. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: GOC

hemopoiesis

Inferred from mutant phenotype Ref.4. Source: UniProtKB

phosphorylation of RNA polymerase II C-terminal domain

Inferred from direct assay Ref.18. Source: UniProtKB

positive regulation of cell proliferation

Traceable author statement Ref.4. Source: ProtInc

regulation of mitosis

Traceable author statement Ref.4. Source: ProtInc

virus-host interaction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcyclin K-CDK13 complex

Inferred from physical interaction PubMed 22012619. Source: MGI

nuclear cyclin-dependent protein kinase holoenzyme complex

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear speck

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from direct assay Ref.18. Source: UniProtKB

cyclin-dependent protein serine/threonine kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

C1QBPQ070216EBI-6375898,EBI-347528

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14004-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q14004-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15121512Cyclin-dependent kinase 13
PRO_0000085711

Regions

Domain705 – 998294Protein kinase
Nucleotide binding711 – 7199ATP By similarity

Sites

Active site8371Proton acceptor By similarity
Binding site7341ATP By similarity

Amino acid modifications

Modified residue3151Phosphoserine Ref.14 Ref.22
Modified residue3171Phosphoserine Ref.14 Ref.22
Modified residue3251Phosphoserine Ref.14
Modified residue3401Phosphoserine Ref.14
Modified residue3421Phosphoserine Ref.14
Modified residue3831Phosphoserine Ref.14 Ref.19 Ref.22
Modified residue3951Phosphoserine Ref.14 Ref.22
Modified residue3971Phosphoserine Ref.14 Ref.22
Modified residue4001Phosphoserine Ref.14 Ref.22
Modified residue4091Phosphoserine By similarity
Modified residue4361Phosphoserine By similarity
Modified residue4371Phosphoserine Ref.14 Ref.19 Ref.22
Modified residue4391Phosphoserine Ref.14 Ref.19 Ref.22
Modified residue5251Phosphoserine Ref.19
Modified residue5561N6-acetyllysine Ref.17
Modified residue8711Phosphothreonine Ref.14 Ref.19 Ref.22
Modified residue10481Phosphoserine Ref.15
Modified residue12461Phosphothreonine Ref.8 Ref.13 Ref.22

Natural variations

Alternative sequence1079 – 113860Missing in isoform 2.
VSP_013579
Natural variant1031Q → R in RNA edited version.
VAR_066526
Natural variant3401S → F.
Corresponds to variant rs13622 [ dbSNP | Ensembl ].
VAR_053926
Natural variant3561P → A. Ref.2
Corresponds to variant rs17537669 [ dbSNP | Ensembl ].
VAR_022381
Natural variant4031L → F. Ref.2
Corresponds to variant rs3735137 [ dbSNP | Ensembl ].
VAR_022382
Natural variant4101R → Q. Ref.2
Corresponds to variant rs17496261 [ dbSNP | Ensembl ].
VAR_022383
Natural variant4941T → A. Ref.23
Corresponds to variant rs34624759 [ dbSNP | Ensembl ].
VAR_041965
Natural variant5001T → A. Ref.2 Ref.23
Corresponds to variant rs3735135 [ dbSNP | Ensembl ].
VAR_022384
Natural variant6241S → G. Ref.2
Corresponds to variant rs17496275 [ dbSNP | Ensembl ].
VAR_022385
Natural variant6701T → R. Ref.23
Corresponds to variant rs34775357 [ dbSNP | Ensembl ].
VAR_041966
Natural variant7001R → L. Ref.1 Ref.4
Corresponds to variant rs1057000 [ dbSNP | Ensembl ].
VAR_022386
Natural variant10621V → M. Ref.2
Corresponds to variant rs17496712 [ dbSNP | Ensembl ].
VAR_022387
Natural variant11701V → M. Ref.1 Ref.23
Corresponds to variant rs3204309 [ dbSNP | Ensembl ].
VAR_041967

Experimental info

Sequence conflict211K → R in CAC10400. Ref.1
Sequence conflict211K → R in CAC10401. Ref.1
Sequence conflict6711A → T in CAC10400. Ref.1
Sequence conflict6711A → T in CAC10401. Ref.1
Sequence conflict6711A → T in AAA58424. Ref.4
Sequence conflict8101N → Y in AAA58424. Ref.4
Sequence conflict862 – 8665YSSEE → FSVFF in BAB47420. Ref.5
Sequence conflict11801Q → R in BAD96773. Ref.5
Sequence conflict13561G → E in BAD96773. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 10, 2005. Version 2.
Checksum: 3CA54A3585A2943D

FASTA1,512164,923
        10         20         30         40         50         60 
MPSSSDTALG GGGGLSWAEK KLEERRKRRR FLSPQQPPLL LPLLQPQLLQ PPPPPPPLLF 

        70         80         90        100        110        120 
LAAPGTAAAA AAAAAASSSC FSPGPPLEVK RLARGKRRAG GRQKRRRGPR AGQEAEKRRV 

       130        140        150        160        170        180 
FSLPQPQQDG GGGASSGGGV TPLVEYEDVS SQSEQGLLLG GASAATAATA AGGTGGSGGS 

       190        200        210        220        230        240 
PASSSGTQRR GEGSERRPRR DRRSSSGRSK ERHREHRRRD GQRGGSEASK SRSRHSHSGE 

       250        260        270        280        290        300 
ERAEVAKSGS SSSSGGRRKS ASATSSSSSS RKDRDSKAHR SRTKSSKEPP SAYKEPPKAY 

       310        320        330        340        350        360 
REDKTEPKAY RRRRSLSPLG GRDDSPVSHR ASQSLRSRKS PSPAGGGSSP YSRRLPRSPS 

       370        380        390        400        410        420 
PYSRRRSPSY SRHSSYERGG DVSPSPYSSS SWRRSRSPYS PVLRRSGKSR SRSPYSSRHS 

       430        440        450        460        470        480 
RSRSRHRLSR SRSRHSSISP STLTLKSSLA AELNKNKKAR AAEAARAAEA AKAAEATKAA 

       490        500        510        520        530        540 
EAAAKAAKAS NTSTPTKGNT ETSASASQTN HVKDVKKIKI EHAPSPSSGG TLKNDKAKTK 

       550        560        570        580        590        600 
PPLQVTKVEN NLIVDKATKK AVIVGKESKS AATKEESVSL KEKTKPLTPS IGAKEKEQHV 

       610        620        630        640        650        660 
ALVTSTLPPL PLPPMLPEDK EADSLRGNIS VKAVKKEVEK KLRCLLADLP LPPELPGGDD 

       670        680        690        700        710        720 
LSKSPEEKKT ATQLHSKRRP KICGPRYGET KEKDIDWGKR CVDKFDIIGI IGEGTYGQVY 

       730        740        750        760        770        780 
KARDKDTGEM VALKKVRLDN EKEGFPITAI REIKILRQLT HQSIINMKEI VTDKEDALDF 

       790        800        810        820        830        840 
KKDKGAFYLV FEYMDHDLMG LLESGLVHFN ENHIKSFMRQ LMEGLDYCHK KNFLHRDIKC 

       850        860        870        880        890        900 
SNILLNNRGQ IKLADFGLAR LYSSEESRPY TNKVITLWYR PPELLLGEER YTPAIDVWSC 

       910        920        930        940        950        960 
GCILGELFTK KPIFQANQEL AQLELISRIC GSPCPAVWPD VIKLPYFNTM KPKKQYRRKL 

       970        980        990       1000       1010       1020 
REEFVFIPAA ALDLFDYMLA LDPSKRCTAE QALQCEFLRD VEPSKMPPPD LPLWQDCHEL 

      1030       1040       1050       1060       1070       1080 
WSKKRRRQKQ MGMTDDVSTI KAPRKDLSLG LDDSRTNTPQ GVLPSSQLKS QGSSNVAPVK 

      1090       1100       1110       1120       1130       1140 
TGPGQHLNHS ELAILLNLLQ SKTSVNMADF VQVLNIKVNS ETQQQLNKIN LPAGILATGE 

      1150       1160       1170       1180       1190       1200 
KQTDPSTPQQ ESSKPLGGIQ PSSQTIQPKV ETDAAQAAVQ SAFAVLLTQL IKAQQSKQKD 

      1210       1220       1230       1240       1250       1260 
VLLEERENGS GHEASLQLRP PPEPSTPVSG QDDLIQHQDM RILELTPEPD RPRILPPDQR 

      1270       1280       1290       1300       1310       1320 
PPEPPEPPPV TEEDLDYRTE NQHVPTTSSS LTDPHAGVKA ALLQLLAQHQ PQDDPKREGG 

      1330       1340       1350       1360       1370       1380 
IDYQAGDTYV STSDYKDNFG SSSFSSAPYV SNDGLGSSSA PPLERRSFIG NSDIQSLDNY 

      1390       1400       1410       1420       1430       1440 
STASSHSGGP PQPSAFSESF PSSVAGYGDI YLNAGPMLFS GDKDHRFEYS HGPIAVLANS 

      1450       1460       1470       1480       1490       1500 
SDPSTGPEST HPLPAKMHNY NYGGNLQENP SGPSLMHGQT WTSPAQGPGY SQGYRGHIST 

      1510 
STGRGRGRGL PY

« Hide

Isoform 2 [UniParc].

Checksum: 8A8B712D8621EEA3
Show »

FASTA1,452158,435

References

« Hide 'large scale' references
[1]"A new subfamily of high molecular mass CDC2-related kinases with PITAI/VRE."
Marques F., Moreau J.L., Peaucellier G., Lozano J.C., Schatt P., Picard A., Callebaut I., Perre E., Geneviere A.M.
Biochem. Biophys. Res. Commun. 279:832-837(2000) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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, MASS SPECTROMETRY.
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT 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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[15]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1048, MASS SPECTROMETRY.
[16]"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.
[17]"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, MASS SPECTROMETRY.
[18]"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.
[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 SER-383; SER-437; SER-439; SER-525 AND THR-871, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Genome-wide evaluation and discovery of vertebrate A-to-I RNA editing sites."
Maas S., Godfried Sie C.P., Stoev I., Dupuis D.E., Latona J., Porman A.M., Evans B., Rekawek P., Kluempers V., Mutter M., Gommans W.M., Lopresti D.
Biochem. Biophys. Res. Commun. 412:407-412(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA EDITING OF POSITION 103.
[22]"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, MASS SPECTROMETRY.
[23]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-494; ALA-500; ARG-670 AND MET-1170.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00029162.
IPI00456970.
PIRA38197.
RefSeqNP_003709.3. NM_003718.4.
NP_112557.2. NM_031267.3.
UniGeneHs.233552.

3D structure databases

ProteinModelPortalQ14004.
ModBaseSearch...

Protein-protein interaction databases

IntActQ14004. 2 interactions.
MINTMINT-1197921.
STRING9606.ENSP00000181839.

PTM databases

PhosphoSiteQ14004.

Polymorphism databases

DMDM66774048.

Proteomic databases

PaxDbQ14004.
PRIDEQ14004.

Protocols and materials databases

DNASU8621.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000181839; ENSP00000181839; ENSG00000065883.
ENST00000340829; ENSP00000340557; ENSG00000065883.
GeneID8621.
KEGGhsa:8621.
UCSCuc003thh.4. human.
uc003thi.4. human.

Organism-specific databases

CTD8621.
GeneCardsGC07P039957.
HGNCHGNC:1733. CDK13.
MIM603309. gene.
neXtProtNX_Q14004.
PharmGKBPA26264.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG050851.
InParanoidQ14004.
KOK08819.
OMAKERHREH.
OrthoDBEOG4TTGH6.
PhylomeDBQ14004.

Gene expression databases

BgeeQ14004.
CleanExHS_CDC2L5.
GenevestigatorQ14004.
GermOnlineENSG00000065883. Homo sapiens.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ14004.
ChEMBLCHEMBL1795192.
GenomeRNAi8621.
NextBio32303.
PMAP-CutDBQ14004.
SOURCESearch...

Entry information

Entry nameCDK13_HUMAN
AccessionPrimary (citable) accession number: Q14004
Secondary accession number(s): Q53G78 expand/collapse secondary AC list , Q6DKQ9, Q75MH4, Q75MH5, Q96JN4, Q9H4A0, Q9H4A1, Q9UDR4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 10, 2005
Last modified: May 1, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

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