Q14004 (CDK13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CDK13
Synonyms:	CDC2L, CDC2L5, CHED, KIAA1791

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1512 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11 Ref.14 Ref.21
Catalytic activity	ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate. Ref.21 ATP + a protein = ADP + a phosphoprotein. Ref.21
Subunit structure	Interacts with CCNL1 and CCNL2 By similarity. Interacts with C1QBP. Interacts with HIV-1 Tat. Ref.11 Ref.14
Subcellular location	Nucleus speckle Ref.11.
Tissue specificity	Expressed in fetal brain, liver, muscle and in adult brain. Also expressed in neuroblastoma and glioblastoma tumors.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19
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.23
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 process	Host-virus interaction mRNA processing mRNA splicing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism RNA editing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	alternative nuclear mRNA splicing, via spliceosome Inferred from sequence or structural similarity. Source: UniProtKB hemopoiesis Inferred from mutant phenotype Ref.4. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW phosphorylation of RNA polymerase II C-terminal domain Inferred from direct assay Ref.21. Source: UniProtKB positive regulation of cell proliferation Traceable author statement. Source: ProtInc regulation of mitosis Traceable author statement. Source: ProtInc
Cellular component	nuclear cyclin-dependent protein kinase holoenzyme complex Inferred from sequence or structural similarity. Source: UniProtKB nuclear speck Inferred from direct assay Ref.11. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II carboxy-terminal domain kinase activity Inferred from direct assay Ref.21. Source: UniProtKB cyclin-dependent protein kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1512	1512	Cyclin-dependent kinase 13		PRO_0000085711
Regions
	Domain	705 – 998	294	Protein kinase
	Nucleotide binding	711 – 719	9	ATP By similarity
Sites
	Active site	837	1	Proton acceptor By similarity
	Binding site	734	1	ATP By similarity
Amino acid modifications
	Modified residue	3	1	Phosphoserine Ref.18
	Modified residue	238	1	Phosphoserine Ref.18
	Modified residue	315	1	Phosphoserine Ref.9 Ref.15 Ref.16 Ref.18
	Modified residue	317	1	Phosphoserine Ref.8 Ref.9 Ref.15 Ref.16 Ref.18
	Modified residue	325	1	Phosphoserine Ref.9 Ref.15 Ref.16 Ref.18
	Modified residue	340	1	Phosphoserine Ref.8 Ref.16
	Modified residue	342	1	Phosphoserine Ref.8 Ref.16 Ref.18
	Modified residue	348	1	Phosphoserine Ref.18
	Modified residue	349	1	Phosphoserine Ref.16
	Modified residue	358	1	Phosphoserine Ref.15 Ref.18
	Modified residue	360	1	Phosphoserine Ref.15 Ref.18
	Modified residue	367	1	Phosphoserine Ref.8
	Modified residue	383	1	Phosphoserine Ref.8 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19
	Modified residue	385	1	Phosphoserine Ref.18
	Modified residue	395	1	Phosphoserine Ref.15 Ref.16 Ref.18
	Modified residue	397	1	Phosphoserine Ref.15 Ref.16 Ref.18
	Modified residue	400	1	Phosphoserine Ref.15 Ref.16
	Modified residue	409	1	Phosphoserine By similarity
	Modified residue	413	1	Phosphoserine Ref.18
	Modified residue	436	1	Phosphoserine Ref.18
	Modified residue	437	1	Phosphoserine Ref.7 Ref.9 Ref.10 Ref.15 Ref.16 Ref.18 Ref.19
	Modified residue	439	1	Phosphoserine Ref.9 Ref.15 Ref.16 Ref.18
	Modified residue	441	1	Phosphoserine Ref.10
	Modified residue	442	1	Phosphothreonine Ref.7
	Modified residue	490	1	Phosphoserine Ref.18
	Modified residue	492	1	Phosphothreonine Ref.18
	Modified residue	494	1	Phosphothreonine Ref.17
	Modified residue	525	1	Phosphoserine Ref.15 Ref.18
	Modified residue	527	1	Phosphoserine Ref.18
	Modified residue	556	1	N6-acetyllysine Ref.20
	Modified residue	662	1	Phosphoserine Ref.18
	Modified residue	664	1	Phosphoserine Ref.15 Ref.18
	Modified residue	863	1	Phosphoserine Ref.18
	Modified residue	870	1	Phosphotyrosine Ref.18
	Modified residue	871	1	Phosphothreonine Ref.15 Ref.16 Ref.18
	Modified residue	1048	1	Phosphoserine Ref.18
	Modified residue	1054	1	Phosphoserine Ref.13 Ref.18
	Modified residue	1056	1	Phosphothreonine Ref.15
	Modified residue	1058	1	Phosphothreonine Ref.18
	Modified residue	1066	1	Phosphoserine Ref.12
	Modified residue	1143	1	Phosphothreonine Ref.18
	Modified residue	1146	1	Phosphoserine Ref.18
	Modified residue	1147	1	Phosphothreonine Ref.18
	Modified residue	1246	1	Phosphothreonine Ref.9 Ref.15 Ref.16 Ref.18
Natural variations
	Alternative sequence	1079 – 1138	60	Missing in isoform 2.		VSP_013579
	Natural variant	103	1	Q → R in RNA edited version.		VAR_066526
	Natural variant	340	1	S → F. Corresponds to variant rs13622 [ dbSNP | Ensembl ].		VAR_053926
	Natural variant	356	1	P → A. Ref.2 Corresponds to variant rs17537669 [ dbSNP | Ensembl ].		VAR_022381
	Natural variant	403	1	L → F. Ref.2 Corresponds to variant rs3735137 [ dbSNP | Ensembl ].		VAR_022382
	Natural variant	410	1	R → Q. Ref.2 Corresponds to variant rs17496261 [ dbSNP | Ensembl ].		VAR_022383
	Natural variant	494	1	T → A. Ref.24 Corresponds to variant rs34624759 [ dbSNP | Ensembl ].		VAR_041965
	Natural variant	500	1	T → A. Ref.2 Ref.24 Corresponds to variant rs3735135 [ dbSNP | Ensembl ].		VAR_022384
	Natural variant	624	1	S → G. Ref.2 Corresponds to variant rs17496275 [ dbSNP | Ensembl ].		VAR_022385
	Natural variant	670	1	T → R. Ref.24 Corresponds to variant rs34775357 [ dbSNP | Ensembl ].		VAR_041966
	Natural variant	700	1	R → L. Ref.1 Ref.4 Corresponds to variant rs1057000 [ dbSNP | Ensembl ].		VAR_022386
	Natural variant	1062	1	V → M. Ref.2 Corresponds to variant rs17496712 [ dbSNP | Ensembl ].		VAR_022387
	Natural variant	1170	1	V → M. Ref.1 Ref.24 Corresponds to variant rs3204309 [ dbSNP | Ensembl ].		VAR_041967
Experimental info
	Sequence conflict	21	1	K → R in CAC10400. Ref.1
	Sequence conflict	21	1	K → R in CAC10401. Ref.1
	Sequence conflict	671	1	A → T in CAC10400. Ref.1
	Sequence conflict	671	1	A → T in CAC10401. Ref.1
	Sequence conflict	671	1	A → T in AAA58424. Ref.4
	Sequence conflict	810	1	N → Y in AAA58424. Ref.4
	Sequence conflict	862 – 866	5	YSSEE → FSVFF in BAB47420. Ref.5
	Sequence conflict	1180	1	Q → R in BAD96773. Ref.5
	Sequence conflict	1356	1	G → E in BAD96773. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 10, 2005. Version 2. Checksum: 3CA54A3585A2943D	FASTA	1,512	164,923
	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
	Isoform 2 [UniParc]. Checksum: 8A8B712D8621EEA3	FASTA	1,452	158,435
	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 QGSSNVAPGE 1090 1100 1110 1120 1130 1140 KQTDPSTPQQ ESSKPLGGIQ PSSQTIQPKV ETDAAQAAVQ SAFAVLLTQL IKAQQSKQKD 1150 1160 1170 1180 1190 1200 VLLEERENGS GHEASLQLRP PPEPSTPVSG QDDLIQHQDM RILELTPEPD RPRILPPDQR 1210 1220 1230 1240 1250 1260 PPEPPEPPPV TEEDLDYRTE NQHVPTTSSS LTDPHAGVKA ALLQLLAQHQ PQDDPKREGG 1270 1280 1290 1300 1310 1320 IDYQAGDTYV STSDYKDNFG SSSFSSAPYV SNDGLGSSSA PPLERRSFIG NSDIQSLDNY 1330 1340 1350 1360 1370 1380 STASSHSGGP PQPSAFSESF PSSVAGYGDI YLNAGPMLFS GDKDHRFEYS HGPIAVLANS 1390 1400 1410 1420 1430 1440 SDPSTGPEST HPLPAKMHNY NYGGNLQENP SGPSLMHGQT WTSPAQGPGY SQGYRGHIST 1450 STGRGRGRGL PY

References

	« Hide 'large scale' referencesShow '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: 11162436] [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. , 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: 12853948] [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: 1731328] [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: 11347906] [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: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND THR-442, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[8]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317; SER-340; SER-342; SER-367 AND SER-383, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-317; SER-325; SER-437; SER-439 AND THR-1246, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-441, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: 16721827] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH C1QBP.
[12]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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: 18480452] [Abstract] Cited for: FUNCTION, INTERACTION WITH HIV-1 TAT.
[15]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-317; SER-325; SER-358; SER-360; SER-383; SER-395; SER-397; SER-400; SER-437; SER-439; SER-525; SER-664; THR-871; THR-1056 AND THR-1246, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-317; SER-325; SER-340; SER-342; SER-349; SER-383; SER-395; SER-397; SER-400; SER-437; SER-439; THR-871 AND THR-1246, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383 AND THR-494, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[18]	"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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-238; SER-315; SER-317; SER-325; SER-342; SER-348; SER-358; SER-360; SER-383; SER-385; SER-395; SER-397; SER-413; SER-436; SER-437; SER-439; SER-490; THR-492; SER-525; SER-527; SER-662; SER-664; SER-863; TYR-870; THR-871; SER-1048; SER-1054; THR-1058; THR-1143; SER-1146; THR-1147 AND THR-1246, MASS SPECTROMETRY.
[19]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383 AND SER-437, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[20]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-556, MASS SPECTROMETRY.
[21]	"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: 20952539] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[22]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]	"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: 21835166] [Abstract] Cited for: RNA EDITING OF POSITION 103.
[24]	"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: 17344846] [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.
IPI	IPI00029162. IPI00456970.
PIR	A38197.
RefSeq	NP_003709.3. NM_003718.4. NP_112557.2. NM_031267.3.
UniGene	Hs.233552.
3D structure databases
ProteinModelPortal	Q14004.
SMR	Q14004. Positions 701-1001.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14004. 1 interaction.
MINT	MINT-1197921.
STRING	Q14004.
PTM databases
PhosphoSite	Q14004.
Polymorphism databases
DMDM	66774048.
Proteomic databases
PRIDE	Q14004.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000181839; ENSP00000181839; ENSG00000065883. ENST00000340829; ENSP00000340557; ENSG00000065883.
GeneID	8621.
KEGG	hsa:8621.
NMPDR	fig|9606.3.peg.28511.
UCSC	uc003thh.2. human. uc003thi.2. human.
Organism-specific databases
CTD	8621.
GeneCards	GC07P039957.
H-InvDB	HIX0006620.
HGNC	HGNC:1733. CDK13.
MIM	603309. gene.
neXtProt	NX_Q14004.
PharmGKB	PA165617810. PA26264.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG12381.
GeneTree	ENSGT00570000079089.
HOVERGEN	HBG050851.
InParanoid	Q14004.
OMA	RHSHSGE.
OrthoDB	EOG4TTGH6.
PhylomeDB	Q14004.
Gene expression databases
ArrayExpress	Q14004.
Bgee	Q14004.
CleanEx	HS_CDC2L5.
Genevestigator	Q14004.
GermOnline	ENSG00000065883. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K08819.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	32303.
PMAP-CutDB	Q14004.
SOURCE	Search...

Entry information

Entry name

CDK13_HUMAN

Accession

Primary (citable) accession number: Q14004
Secondary accession number(s): Q53G78 , 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:	January 25, 2012
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.