Q9NYV4 (CDK12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclin-dependent kinase 12
EC=2.7.11.22
EC=2.7.11.23

Alternative name(s):
Cdc2-related kinase, arginine/serine-rich
Short name=CrkRS
Cell division cycle 2-related protein kinase 7
Short name=CDC2-related protein kinase 7
Cell division protein kinase 12
Short name=hCDK12

Gene names

Name:	CDK12
Synonyms:	CRK7, CRKRS, KIAA0904

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	1490 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, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogn inhibitors. Ref.1 Ref.16 Ref.20
Catalytic activity	ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate. Ref.20 ATP + a protein = ADP + a phosphoprotein. Ref.20
Subunit structure	Interacts with CCNL1 and CCNL2 By similarity.
Subcellular location	Nucleus. Nucleus speckle. Note: Colocalized with nuclear speckles throughout interphase. Ref.1
Tissue specificity	Ubiquitously expressed. Ref.1
Involvement in disease	Note=Chromosomal aberrations involving CDK12 may be a cause gastric cancer. Deletions within 17q12 region producing fusion transcripts with ERBB2, leading to CDK12-ERBB2 fusion leading to trunctated CDK12 protein not in-frame with ERBB2.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence BAA74927.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
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	RNA splicing Inferred from sequence or structural similarity. Source: UniProtKB mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW phosphorylation of RNA polymerase II C-terminal domain Inferred from mutant phenotype Ref.20. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.1. Source: HGNC regulation of MAP kinase activity Inferred from mutant phenotype Ref.16. Source: UniProtKB
Cellular component	nuclear cyclin-dependent protein kinase holoenzyme complex Inferred from sequence or structural similarity. Source: UniProtKB nuclear speck Inferred from direct assay Ref.1. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II carboxy-terminal domain kinase activity Inferred from mutant phenotype Ref.20. Source: UniProtKB cyclin-dependent protein kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NYV4-1)

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: Q9NYV4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1254-1262: Missing.

Isoform 3 (identifier: Q9NYV4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     349-349: Missing.
     1205-1274: DMQNILAVLL...RPPEPPGPPP → ILWYMQRPNC...FLTNPETSVS
     1275-1490: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1490	1490	Cyclin-dependent kinase 12		PRO_0000085715
Regions
	Domain	727 – 1020	294	Protein kinase
	Nucleotide binding	733 – 741	9	ATP By similarity
	Compositional bias	407 – 413	7	Poly-Ala
	Compositional bias	535 – 540	6	Poly-Pro
	Compositional bias	1266 – 1280	15	Poly-Pro
Sites
	Active site	859	1	Proton acceptor By similarity
	Binding site	756	1	ATP By similarity
Amino acid modifications
	Modified residue	14	1	Phosphoserine Ref.17
	Modified residue	24	1	Phosphoserine Ref.13 Ref.17
	Modified residue	25	1	Phosphoserine Ref.13
	Modified residue	29	1	Phosphoserine Ref.17
	Modified residue	32	1	Phosphoserine Ref.13
	Modified residue	57	1	Phosphothreonine Ref.13 Ref.17
	Modified residue	62	1	Phosphoserine Ref.17
	Modified residue	73	1	Phosphotyrosine Ref.13
	Modified residue	77	1	Phosphoserine Ref.9 Ref.13
	Modified residue	78	1	Phosphoserine Ref.9 Ref.13
	Modified residue	80	1	Phosphoserine Ref.9 Ref.13
	Modified residue	82	1	Phosphothreonine Ref.17
	Modified residue	84	1	Phosphoserine Ref.9 Ref.13 Ref.17
	Modified residue	215	1	Phosphoserine Ref.8
	Modified residue	228	1	Phosphoserine Ref.17
	Modified residue	236	1	Phosphoserine Ref.13 Ref.17 Ref.18
	Modified residue	238	1	Phosphoserine Ref.13
	Modified residue	249	1	Phosphoserine Ref.8 Ref.13 Ref.14 Ref.17
	Modified residue	265	1	Phosphoserine Ref.8
	Modified residue	274	1	Phosphoserine Ref.9 Ref.11 Ref.13 Ref.17
	Modified residue	276	1	Phosphoserine Ref.9 Ref.11 Ref.13 Ref.17
	Modified residue	279	1	Phosphotyrosine By similarity
	Modified residue	291	1	Phosphoserine Ref.13 Ref.17
	Modified residue	293	1	Phosphoserine Ref.8 Ref.13 Ref.17
	Modified residue	301	1	Phosphoserine Ref.13 Ref.14 Ref.17
	Modified residue	303	1	Phosphoserine Ref.8 Ref.13 Ref.14 Ref.17
	Modified residue	318	1	Phosphoserine Ref.14
	Modified residue	319	1	Phosphotyrosine By similarity
	Modified residue	320	1	Phosphoserine Ref.14
	Modified residue	323	1	Phosphoserine Ref.14 Ref.17
	Modified residue	325	1	Phosphoserine Ref.14 Ref.17
	Modified residue	332	1	Phosphoserine Ref.14 Ref.17
	Modified residue	333	1	Phosphoserine Ref.14 Ref.17
	Modified residue	334	1	Phosphoserine Ref.14 Ref.17
	Modified residue	341	1	Phosphoserine Ref.13
	Modified residue	343	1	Phosphoserine Ref.13 Ref.14
	Modified residue	345	1	Phosphoserine Ref.14
	Modified residue	382	1	Phosphoserine Ref.14 Ref.17
	Modified residue	383	1	Phosphoserine Ref.11 Ref.13 Ref.14 Ref.17 Ref.18
	Modified residue	385	1	Phosphoserine Ref.11 Ref.13 Ref.14 Ref.17 Ref.18
	Modified residue	393	1	Phosphoserine Ref.17
	Modified residue	400	1	Phosphoserine Ref.13 Ref.14
	Modified residue	420	1	Phosphoserine Ref.17
	Modified residue	423	1	Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.17
	Modified residue	434	1	Phosphoserine Ref.17
	Modified residue	504	1	N6-acetyllysine Ref.19
	Modified residue	514	1	Phosphothreonine Ref.13 Ref.17
	Modified residue	681	1	Phosphoserine Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18
	Modified residue	685	1	Phosphoserine Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18
	Modified residue	692	1	Phosphothreonine Ref.8 Ref.10 Ref.13 Ref.14 Ref.15 Ref.17
	Modified residue	892	1	Phosphotyrosine Ref.17
	Modified residue	893	1	Phosphothreonine Ref.11 Ref.13 Ref.17
	Modified residue	1053	1	Phosphoserine Ref.17
	Modified residue	1070	1	Phosphothreonine Ref.17
	Modified residue	1074	1	Phosphothreonine Ref.17
	Modified residue	1076	1	Phosphothreonine Ref.15 Ref.17
	Modified residue	1082	1	Phosphoserine Ref.15 Ref.17
	Modified residue	1083	1	Phosphoserine Ref.8 Ref.12 Ref.13 Ref.15 Ref.17
	Modified residue	1244	1	Phosphothreonine Ref.13 Ref.17 Ref.18
Natural variations
	Alternative sequence	349	1	Missing in isoform 3.		VSP_040908
	Alternative sequence	1205 – 1274	70	DMQNI…PGPPP → ILWYMQRPNCKTMGSWGQEP LGPAAQEQAFTGGAQLSLLL MENSIGGLQESHQEGEEGEE FLTNPETSVS in isoform 3.		VSP_040909
	Alternative sequence	1254 – 1262	9	Missing in isoform 2.		VSP_030284
	Alternative sequence	1275 – 1490	216	Missing in isoform 3.		VSP_040910
	Natural variant	530	1	P → A. Ref.23 Corresponds to variant rs56121596 [ dbSNP | Ensembl ].		VAR_041968
	Natural variant	912	1	R → H in a colorectal adenocarcinoma sample; somatic mutation. Ref.23		VAR_041969
	Natural variant	1189	1	L → Q. Ref.23 Corresponds to variant rs56362165 [ dbSNP | Ensembl ].		VAR_041970
	Natural variant	1275	1	P → L. Ref.23 Corresponds to variant rs34070318 [ dbSNP | Ensembl ].		VAR_041971
Experimental info
	Sequence conflict	133	1	S → G in BAG63886. Ref.4
	Sequence conflict	268	1	S → G in BAG63886. Ref.4
	Sequence conflict	639	1	D → G in AAF36401. Ref.1
	Sequence conflict	737	1	T → I in BAG63886. Ref.4
	Sequence conflict	745	1	K → R in AAF36401. Ref.1
	Sequence conflict	822	1	G → V in BAG63886. Ref.4
	Sequence conflict	1195	1	T → M in AAF36401. Ref.1
	Sequence conflict	1195	1	T → M in BAA74927. Ref.2
	Sequence conflict	1195	1	T → M in AAI50266. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 5, 2010. Version 2. Checksum: D6B04B998ECDE58E	FASTA	1,490	164,155
	10 20 30 40 50 60 MPNSERHGGK KDGSGGASGT LQPSSGGGSS NSRERHRLVS KHKRHKSKHS KDMGLVTPEA 70 80 90 100 110 120 ASLGTVIKPL VEYDDISSDS DTFSDDMAFK LDRRENDERR GSDRSDRLHK HRHHQHRRSR 130 140 150 160 170 180 DLLKAKQTEK EKSQEVSSKS GSMKDRISGS SKRSNEETDD YGKAQVAKSS SKESRSSKLH 190 200 210 220 230 240 KEKTRKEREL KSGHKDRSKS HRKRETPKSY KTVDSPKRRS RSPHRKWSDS SKQDDSPSGA 250 260 270 280 290 300 SYGQDYDLSP SRSHTSSNYD SYKKSPGSTS RRQSVSPPYK EPSAYQSSTR SPSPYSRRQR 310 320 330 340 350 360 SVSPYSRRRS SSYERSGSYS GRSPSPYGRR RSSSPFLSKR SLSRSPLPSR KSMKSRSRSP 370 380 390 400 410 420 AYSRHSSSHS KKKRSSSRSR HSSISPVRLP LNSSLGAELS RKKKERAAAA AAAKMDGKES 430 440 450 460 470 480 KGSPVFLPRK ENSSVEAKDS GLESKKLPRS VKLEKSAPDT ELVNVTHLNT EVKNSSDTGK 490 500 510 520 530 540 VKLDENSEKH LVKDLKAQGT RDSKPIALKE EIVTPKETET SEKETPPPLP TIASPPPPLP 550 560 570 580 590 600 TTTPPPQTPP LPPLPPIPAL PQQPPLPPSQ PAFSQVPASS TSTLPPSTHS KTSAVSSQAN 610 620 630 640 650 660 SQPPVQVSVK TQVSVTAAIP HLKTSTLPPL PLPPLLPGDD DMDSPKETLP SKPVKKEKEQ 670 680 690 700 710 720 RTRHLLTDLP LPPELPGGDL SPPDSPEPKA ITPPQQPYKK RPKICCPRYG ERRQTESDWG 730 740 750 760 770 780 KRCVDKFDII GIIGEGTYGQ VYKAKDKDTG ELVALKKVRL DNEKEGFPIT AIREIKILRQ 790 800 810 820 830 840 LIHRSVVNMK EIVTDKQDAL DFKKDKGAFY LVFEYMDHDL MGLLESGLVH FSEDHIKSFM 850 860 870 880 890 900 KQLMEGLEYC HKKNFLHRDI KCSNILLNNS GQIKLADFGL ARLYNSEESR PYTNKVITLW 910 920 930 940 950 960 YRPPELLLGE ERYTPAIDVW SCGCILGELF TKKPIFQANL ELAQLELISR LCGSPCPAVW 970 980 990 1000 1010 1020 PDVIKLPYFN TMKPKKQYRR RLREEFSFIP SAALDLLDHM LTLDPSKRCT AEQTLQSDFL 1030 1040 1050 1060 1070 1080 KDVELSKMAP PDLPHWQDCH ELWSKKRRRQ RQSGVVVEEP PPSKTSRKET TSGTSTEPVK 1090 1100 1110 1120 1130 1140 NSSPAPPQPA PGKVESGAGD AIGLADITQQ LNQSELAVLL NLLQSQTDLS IPQMAQLLNI 1150 1160 1170 1180 1190 1200 HSNPEMQQQL EALNQSISAL TEATSQQQDS ETMAPEESLK EAPSAPVILP SAEQTTLEAS 1210 1220 1230 1240 1250 1260 STPADMQNIL AVLLSQLMKT QEPAGSLEEN NSDKNSGPQG PRRTPTMPQE EAAACPPHIL 1270 1280 1290 1300 1310 1320 PPEKRPPEPP GPPPPPPPPP LVEGDLSSAP QELNPAVTAA LLQLLSQPEA EPPGHLPHEH 1330 1340 1350 1360 1370 1380 QALRPMEYST RPRPNRTYGN TDGPETGFSA IDTDERNSGP ALTESLVQTL VKNRTFSGSL 1390 1400 1410 1420 1430 1440 SHLGESSSYQ GTGSVQFPGD QDLRFARVPL ALHPVVGQPF LKAEGSSNSV VHAETKLQNY 1450 1460 1470 1480 1490 GELGPGTTGA SSSGAGLHWG GPTQSSAYGK LYRGPTRVPP RGGRGRGVPY
	Isoform 2 [UniParc]. Checksum: D0CF4B898D3032D4	FASTA	1,481	163,228
	10 20 30 40 50 60 MPNSERHGGK KDGSGGASGT LQPSSGGGSS NSRERHRLVS KHKRHKSKHS KDMGLVTPEA 70 80 90 100 110 120 ASLGTVIKPL VEYDDISSDS DTFSDDMAFK LDRRENDERR GSDRSDRLHK HRHHQHRRSR 130 140 150 160 170 180 DLLKAKQTEK EKSQEVSSKS GSMKDRISGS SKRSNEETDD YGKAQVAKSS SKESRSSKLH 190 200 210 220 230 240 KEKTRKEREL KSGHKDRSKS HRKRETPKSY KTVDSPKRRS RSPHRKWSDS SKQDDSPSGA 250 260 270 280 290 300 SYGQDYDLSP SRSHTSSNYD SYKKSPGSTS RRQSVSPPYK EPSAYQSSTR SPSPYSRRQR 310 320 330 340 350 360 SVSPYSRRRS SSYERSGSYS GRSPSPYGRR RSSSPFLSKR SLSRSPLPSR KSMKSRSRSP 370 380 390 400 410 420 AYSRHSSSHS KKKRSSSRSR HSSISPVRLP LNSSLGAELS RKKKERAAAA AAAKMDGKES 430 440 450 460 470 480 KGSPVFLPRK ENSSVEAKDS GLESKKLPRS VKLEKSAPDT ELVNVTHLNT EVKNSSDTGK 490 500 510 520 530 540 VKLDENSEKH LVKDLKAQGT RDSKPIALKE EIVTPKETET SEKETPPPLP TIASPPPPLP 550 560 570 580 590 600 TTTPPPQTPP LPPLPPIPAL PQQPPLPPSQ PAFSQVPASS TSTLPPSTHS KTSAVSSQAN 610 620 630 640 650 660 SQPPVQVSVK TQVSVTAAIP HLKTSTLPPL PLPPLLPGDD DMDSPKETLP SKPVKKEKEQ 670 680 690 700 710 720 RTRHLLTDLP LPPELPGGDL SPPDSPEPKA ITPPQQPYKK RPKICCPRYG ERRQTESDWG 730 740 750 760 770 780 KRCVDKFDII GIIGEGTYGQ VYKAKDKDTG ELVALKKVRL DNEKEGFPIT AIREIKILRQ 790 800 810 820 830 840 LIHRSVVNMK EIVTDKQDAL DFKKDKGAFY LVFEYMDHDL MGLLESGLVH FSEDHIKSFM 850 860 870 880 890 900 KQLMEGLEYC HKKNFLHRDI KCSNILLNNS GQIKLADFGL ARLYNSEESR PYTNKVITLW 910 920 930 940 950 960 YRPPELLLGE ERYTPAIDVW SCGCILGELF TKKPIFQANL ELAQLELISR LCGSPCPAVW 970 980 990 1000 1010 1020 PDVIKLPYFN TMKPKKQYRR RLREEFSFIP SAALDLLDHM LTLDPSKRCT AEQTLQSDFL 1030 1040 1050 1060 1070 1080 KDVELSKMAP PDLPHWQDCH ELWSKKRRRQ RQSGVVVEEP PPSKTSRKET TSGTSTEPVK 1090 1100 1110 1120 1130 1140 NSSPAPPQPA PGKVESGAGD AIGLADITQQ LNQSELAVLL NLLQSQTDLS IPQMAQLLNI 1150 1160 1170 1180 1190 1200 HSNPEMQQQL EALNQSISAL TEATSQQQDS ETMAPEESLK EAPSAPVILP SAEQTTLEAS 1210 1220 1230 1240 1250 1260 STPADMQNIL AVLLSQLMKT QEPAGSLEEN NSDKNSGPQG PRRTPTMPQE EAAEKRPPEP 1270 1280 1290 1300 1310 1320 PGPPPPPPPP PLVEGDLSSA PQELNPAVTA ALLQLLSQPE AEPPGHLPHE HQALRPMEYS 1330 1340 1350 1360 1370 1380 TRPRPNRTYG NTDGPETGFS AIDTDERNSG PALTESLVQT LVKNRTFSGS LSHLGESSSY 1390 1400 1410 1420 1430 1440 QGTGSVQFPG DQDLRFARVP LALHPVVGQP FLKAEGSSNS VVHAETKLQN YGELGPGTTG 1450 1460 1470 1480 ASSSGAGLHW GGPTQSSAYG KLYRGPTRVP PRGGRGRGVP Y
	Isoform 3 [UniParc]. Checksum: 85B012B87EDC02F1	FASTA	1,273	141,449
	10 20 30 40 50 60 MPNSERHGGK KDGSGGASGT LQPSSGGGSS NSRERHRLVS KHKRHKSKHS KDMGLVTPEA 70 80 90 100 110 120 ASLGTVIKPL VEYDDISSDS DTFSDDMAFK LDRRENDERR GSDRSDRLHK HRHHQHRRSR 130 140 150 160 170 180 DLLKAKQTEK EKSQEVSSKS GSMKDRISGS SKRSNEETDD YGKAQVAKSS SKESRSSKLH 190 200 210 220 230 240 KEKTRKEREL KSGHKDRSKS HRKRETPKSY KTVDSPKRRS RSPHRKWSDS SKQDDSPSGA 250 260 270 280 290 300 SYGQDYDLSP SRSHTSSNYD SYKKSPGSTS RRQSVSPPYK EPSAYQSSTR SPSPYSRRQR 310 320 330 340 350 360 SVSPYSRRRS SSYERSGSYS GRSPSPYGRR RSSSPFLSKR SLSRSPLPRK SMKSRSRSPA 370 380 390 400 410 420 YSRHSSSHSK KKRSSSRSRH SSISPVRLPL NSSLGAELSR KKKERAAAAA AAKMDGKESK 430 440 450 460 470 480 GSPVFLPRKE NSSVEAKDSG LESKKLPRSV KLEKSAPDTE LVNVTHLNTE VKNSSDTGKV 490 500 510 520 530 540 KLDENSEKHL VKDLKAQGTR DSKPIALKEE IVTPKETETS EKETPPPLPT IASPPPPLPT 550 560 570 580 590 600 TTPPPQTPPL PPLPPIPALP QQPPLPPSQP AFSQVPASST STLPPSTHSK TSAVSSQANS 610 620 630 640 650 660 QPPVQVSVKT QVSVTAAIPH LKTSTLPPLP LPPLLPGDDD MDSPKETLPS KPVKKEKEQR 670 680 690 700 710 720 TRHLLTDLPL PPELPGGDLS PPDSPEPKAI TPPQQPYKKR PKICCPRYGE RRQTESDWGK 730 740 750 760 770 780 RCVDKFDIIG IIGEGTYGQV YKAKDKDTGE LVALKKVRLD NEKEGFPITA IREIKILRQL 790 800 810 820 830 840 IHRSVVNMKE IVTDKQDALD FKKDKGAFYL VFEYMDHDLM GLLESGLVHF SEDHIKSFMK 850 860 870 880 890 900 QLMEGLEYCH KKNFLHRDIK CSNILLNNSG QIKLADFGLA RLYNSEESRP YTNKVITLWY 910 920 930 940 950 960 RPPELLLGEE RYTPAIDVWS CGCILGELFT KKPIFQANLE LAQLELISRL CGSPCPAVWP 970 980 990 1000 1010 1020 DVIKLPYFNT MKPKKQYRRR LREEFSFIPS AALDLLDHML TLDPSKRCTA EQTLQSDFLK 1030 1040 1050 1060 1070 1080 DVELSKMAPP DLPHWQDCHE LWSKKRRRQR QSGVVVEEPP PSKTSRKETT SGTSTEPVKN 1090 1100 1110 1120 1130 1140 SSPAPPQPAP GKVESGAGDA IGLADITQQL NQSELAVLLN LLQSQTDLSI PQMAQLLNIH 1150 1160 1170 1180 1190 1200 SNPEMQQQLE ALNQSISALT EATSQQQDSE TMAPEESLKE APSAPVILPS AEQTTLEASS 1210 1220 1230 1240 1250 1260 TPAILWYMQR PNCKTMGSWG QEPLGPAAQE QAFTGGAQLS LLLMENSIGG LQESHQEGEE 1270 GEEFLTNPET SVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CrkRS: a novel conserved Cdc2-related protein kinase that colocalises with SC35 speckles." Ko T.K., Kelly E., Pines J. J. Cell Sci. 114:2591-2603(2001) [PubMed: 11683387] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
[2]	"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:355-364(1998) [PubMed: 10048485] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[3]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed: 12168954] [Abstract] Cited for: SEQUENCE REVISION.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Testis.
[5]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[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-215; SER-249; SER-265; SER-293; SER-303; SER-423; THR-692 AND SER-1083, 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-77; SER-78; SER-80; SER-84; SER-274; SER-276; SER-423; SER-681 AND SER-685, 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-423 AND THR-692, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; SER-276; SER-383; SER-385; SER-423; SER-681; SER-685 AND THR-893, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1083, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-25; SER-32; THR-57; TYR-73; SER-77; SER-78; SER-80; SER-84; SER-236; SER-238; SER-249; SER-274; SER-276; SER-291; SER-293; SER-301; SER-303; SER-341; SER-343; SER-383; SER-385; SER-400; SER-423; THR-514; SER-681; SER-685; THR-692; THR-893; SER-1083 AND THR-1244, 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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; SER-301; SER-303; SER-318; SER-320; SER-323; SER-325; SER-332; SER-333; SER-334; SER-343; SER-345; SER-382; SER-383; SER-385; SER-400; SER-423; SER-681; SER-685 AND THR-692, MASS SPECTROMETRY. 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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-681; SER-685; THR-692; THR-1076; SER-1082 AND SER-1083, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"CRK7 modifies the MAPK pathway and influences the response to endocrine therapy." Iorns E., Martens-de Kemp S.R., Lord C.J., Ashworth A. Carcinogenesis 30:1696-1701(2009) [PubMed: 19651820] [Abstract] Cited for: FUNCTION.
[17]	"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-14; SER-24; SER-29; THR-57; SER-62; THR-82; SER-84; SER-228; SER-236; SER-249; SER-274; SER-276; SER-291; SER-293; SER-301; SER-303; SER-323; SER-325; SER-332; SER-333; SER-334; SER-382; SER-383; SER-385; SER-393; SER-420; SER-423; SER-434; THR-514; SER-681; SER-685; THR-692; TYR-892; THR-893; SER-1053; THR-1070; THR-1074; THR-1076; SER-1082; SER-1083 AND THR-1244, MASS SPECTROMETRY.
[18]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-383; SER-385; SER-681; SER-685 AND THR-1244, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"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-504, MASS SPECTROMETRY.
[20]	"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.
[21]	"Genetic and structural variation in the gastric cancer kinome revealed through targeted deep sequencing." Zang Z.J., Ong C.K., Cutcutache I., Yu W., Zhang S.L., Huang D., Ler L.D., Dykema K., Gan A., Tao J., Lim S., Liu Y., Futreal P.A., Grabsch H., Furge K.A., Goh L.K., Rozen S., Teh B.T., Tan P. Cancer Res. 71:29-39(2011) [PubMed: 21097718] [Abstract] Cited for: CHROMOSOMAL REARRANGEMENT WITH ERBB2, POSSIBLE INVOLVEMENT IN GASTRIC CANCER.
[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]	"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-530; HIS-912; GLN-1189 AND LEU-1275.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF227198 mRNA. Translation: AAF36401.1. AB020711 mRNA. Translation: BAA74927.2. Different initiation. AK302645 mRNA. Translation: BAG63886.1. AC009283 Genomic DNA. No translation available. CH471152 Genomic DNA. Translation: EAW60577.1. BC140854 mRNA. Translation: AAI40855.1. BC150265 mRNA. Translation: AAI50266.1.
IPI	IPI00021175. IPI00868781. IPI00910891.
RefSeq	NP_055898.1. NM_015083.1. NP_057591.2. NM_016507.2.
UniGene	Hs.416108.
3D structure databases
ProteinModelPortal	Q9NYV4.
SMR	Q9NYV4. Positions 723-1023.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NYV4. 2 interactions.
MINT	MINT-1191969.
STRING	Q9NYV4.
PTM databases
PhosphoSite	Q9NYV4.
Polymorphism databases
DMDM	308153421.
Proteomic databases
PRIDE	Q9NYV4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000300647; ENSP00000300647; ENSG00000167258. ENST00000430627; ENSP00000407720; ENSG00000167258. ENST00000447079; ENSP00000398880; ENSG00000167258.
GeneID	51755.
KEGG	hsa:51755.
UCSC	uc002hrw.2. human. uc010cvv.1. human.
Organism-specific databases
CTD	51755.
GeneCards	GC17P037618.
H-InvDB	HIX0013777.
HGNC	HGNC:24224. CDK12.
HPA	HPA008038.
neXtProt	NX_Q9NYV4.
PharmGKB	PA142672078. PA165431656.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG09762.
GeneTree	ENSGT00570000079089.
HOGENOM	HBG282140.
HOVERGEN	HBG050852.
InParanoid	Q9NYV4.
OMA	DSYKKSP.
OrthoDB	EOG498V0D.
PhylomeDB	Q9NYV4.
Enzyme and pathway databases
BRENDA	2.7.11.22. 2681.
Gene expression databases
ArrayExpress	Q9NYV4.
Bgee	Q9NYV4.
CleanEx	HS_CRKRS.
Genevestigator	Q9NYV4.
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	55858.

Entry information

Entry name

CDK12_HUMAN

Accession

Primary (citable) accession number: Q9NYV4
Secondary accession number(s): A7E2B2 , B4DYX4, B9EIQ6, O94978

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	October 5, 2010
Last modified:	January 25, 2012
This is version 106 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.