D2H526 (CDK12_AILME) 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):
Cell division protein kinase 12

Gene names

Name:	CDK12
ORF Names:	PANDA_004952

Organism

Ailuropoda melanoleuca (Giant panda) [Reference proteome]

Taxonomic identifier

9646 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Carnivora › Caniformia › Ursidae › Ailuropoda

Protein attributes

Sequence length	1491 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 By similarity.
Catalytic activity	ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate. ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with CCNL1 and CCNL2 By similarity.
Subcellular location	Nucleus By similarity. Nucleus speckle By similarity. Note: Colocalized with nuclear speckles throughout interphase By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from sequence or structural similarity. Source: UniProtKB cell cycle Inferred from electronic annotation. Source: GOC mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW phosphorylation of RNA polymerase II C-terminal domain Inferred from sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from electronic annotation. Source: Compara regulation of MAP kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	nuclear cyclin-dependent protein kinase holoenzyme complex Inferred from sequence or structural similarity. Source: UniProtKB nuclear speck Inferred from sequence or structural similarity. Source: UniProtKB nucleolus Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II carboxy-terminal domain kinase activity Inferred from sequence or structural similarity. Source: UniProtKB cyclin-dependent protein serine/threonine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1491	1491	Cyclin-dependent kinase 12		PRO_0000406957
Regions
	Domain	728 – 1021	294	Protein kinase
	Nucleotide binding	734 – 742	9	ATP By similarity
	Compositional bias	137 – 395	259	Ser-rich
	Compositional bias	408 – 414	7	Poly-Ala
	Compositional bias	527 – 708	182	Pro-rich
	Compositional bias	1239 – 1281	43	Pro-rich
Sites
	Active site	860	1	Proton acceptor By similarity
	Binding site	757	1	ATP By similarity
Amino acid modifications
	Modified residue	57	1	Phosphothreonine By similarity
	Modified residue	73	1	Phosphotyrosine By similarity
	Modified residue	237	1	Phosphoserine By similarity
	Modified residue	250	1	Phosphoserine By similarity
	Modified residue	275	1	Phosphoserine By similarity
	Modified residue	277	1	Phosphoserine By similarity
	Modified residue	280	1	Phosphotyrosine By similarity
	Modified residue	302	1	Phosphoserine By similarity
	Modified residue	304	1	Phosphoserine By similarity
	Modified residue	311	1	Phosphoserine By similarity
	Modified residue	313	1	Phosphoserine By similarity
	Modified residue	319	1	Phosphoserine By similarity
	Modified residue	320	1	Phosphotyrosine By similarity
	Modified residue	324	1	Phosphoserine By similarity
	Modified residue	326	1	Phosphoserine By similarity
	Modified residue	333	1	Phosphoserine By similarity
	Modified residue	334	1	Phosphoserine By similarity
	Modified residue	335	1	Phosphoserine By similarity
	Modified residue	339	1	Phosphoserine By similarity
	Modified residue	346	1	Phosphoserine By similarity
	Modified residue	384	1	Phosphoserine By similarity
	Modified residue	386	1	Phosphoserine By similarity
	Modified residue	401	1	Phosphoserine By similarity
	Modified residue	421	1	Phosphoserine By similarity
	Modified residue	424	1	Phosphoserine By similarity
	Modified residue	515	1	Phosphothreonine By similarity
	Modified residue	682	1	Phosphoserine By similarity
	Modified residue	686	1	Phosphoserine By similarity
	Modified residue	693	1	Phosphothreonine By similarity
	Modified residue	894	1	Phosphothreonine By similarity
	Modified residue	1054	1	Phosphoserine By similarity
	Modified residue	1084	1	Phosphoserine By similarity
	Modified residue	1245	1	Phosphothreonine By similarity

Sequences

	Sequence		Length	Mass (Da)
	D2H526 [UniParc]. Last modified February 9, 2010. Version 1. Checksum: BA53304B554D1195	FASTA	1,491	164,479
	10 20 30 40 50 60 MPNPERHGGK KDGSGGASGT LQPSSGGGSS NSRERHRLVS KHKRHKSKHS KDMGLVTPEA 70 80 90 100 110 120 APLGTIIKPL VEYDDISSDS DTFSDDMAFK LDRRENDERR GTDRSDRLHK HRHHQHRRSR 130 140 150 160 170 180 DLLKTKQTEK EKNQEVSSKS GSMKDRISGS SKRSNEENED YGKAQISKSS SNKESRSSKL 190 200 210 220 230 240 HKEKTRKERE LKSGHKDRSK SHRKRETPKS YKTVDSPKRR SRSPHRKWSD SPKQDDSPSG 250 260 270 280 290 300 ASYGQDYDLS PPRSHTSSNY DSYKKSPGST SRRQSISPPY KEPSAYQSST RSPSPYSRRQ 310 320 330 340 350 360 RSVSPYSRRR SSSYERSGSY SGRSPSPYGR RRSSSPFMSK RSLSRSPLPS RKSMKSRSRS 370 380 390 400 410 420 PAYSRHSSSH SKKKRSGSRS RHSSISPVRL PLNSSLGAEL SRKKKERAAA AAAAKMDGKE 430 440 450 460 470 480 SKGSPIFLPR KENSLVEAKD SGLESKKLTR GVKLEKSAPD TELVNIPHLN TEVKNSLDTG 490 500 510 520 530 540 KVKLDENSEK HPIKDLKAQG SRDSKPIALK EEIVTPKETE TSEKETPPPV PAVTSPPPPL 550 560 570 580 590 600 PTTSPPPQTP PLPPLPPLPA IPQQPPLPPP QPAFSHVLAS STSTLPPSTH PRTSTLSSQA 610 620 630 640 650 660 NSQPLAQVSV KTQVSVTAAI PHLKTSTLPP LPLPPLLPGD DDMDSPKETP PSKPVKKEKE 670 680 690 700 710 720 QRPRHLLTDL PLPPELPGGD PSPPDSPEPK AVTPPQQPYK KRPKICCPRY GERRQTESDW 730 740 750 760 770 780 GKRCVDKFDI IGIIGEGTYG QVYKAKDKDT GELVALKKVR LDNEKEGFPI TAIREIKILR 790 800 810 820 830 840 QLIHRSVVNM KEIVTDKQDA LDFKKDKGAF YLVFEYMDHD LMGLLESGLV HFSEDHIKSF 850 860 870 880 890 900 MKQLMEGLDY CHKKNFLHRD IKCSNILLNN SGQIKLADFG LARLYNSEES RPYTNKVITL 910 920 930 940 950 960 WYRPPELLLG EERYTPAIDV WSCGCILGEL FTKKPIFQAN LELAQLELIS RLCGSPCPAV 970 980 990 1000 1010 1020 WPDVIKLPYF NTMKPKKQYR RRLREEFSFI PSAALDLLDH MLTLDPSKRC TAEQTLQSDF 1030 1040 1050 1060 1070 1080 LKDVELSKMD PPDLPHWQDC HELWSKKRRR QRQSGVVIEE PPPSKASRKE TTSGTSAEPV 1090 1100 1110 1120 1130 1140 KNSSPAPPQP ASGKVEPGTG DAIGLGDITQ QLNQSELAVL LNLLQSQTDL SIPQMAQLLN 1150 1160 1170 1180 1190 1200 IHSNPEMQQQ LEALNQSISA LTEATSQQQD SEHMAPEESL KEAPPALVVQ PSAEQTTSEA 1210 1220 1230 1240 1250 1260 SSTPADMQNM LAVLLSQLMK TQEPAGSLEE NNSDKNSGPQ GPRRTPTMPQ EEAAACPPHI 1270 1280 1290 1300 1310 1320 LPPEKRPPEP PGPPPPPPPP PLIEGDLSSA PQELNPAVTA ALLQLLSQPE AEPPGHLPHE 1330 1340 1350 1360 1370 1380 HQALRPMEYS TRPHPNRTYG NTDGPETGFS ATDTDERNSG PALTESLTQT LVKNRTFSGS 1390 1400 1410 1420 1430 1440 VSHLGESSSY QGTGSVQFPG DQDLRFARVP LPLHSVVGQP FLKAEGSSNS VVHAETKLQN 1450 1460 1470 1480 1490 YGELGPGTTG ASSSGAGLNW GGSAQSSAYG KLYRGPTRVP PRGGRGRGVP Y

References

[1]

"The sequence and de novo assembly of the giant panda genome." Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J. , Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J., Wang J. Nature 463:311-317(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	GL192497 Genomic DNA. Translation: EFB19924.1.
RefSeq	XP_002916839.1. XM_002916793.1.
3D structure databases
ProteinModelPortal	D2H526.
ModBase	Search...
Proteomic databases
PRIDE	D2H526.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSAMET00000004348; ENSAMEP00000004181; ENSAMEG00000003944.
GeneID	100467815.
KEGG	aml:100467815.
Organism-specific databases
CTD	51755.
Phylogenomic databases
GeneTree	ENSGT00690000102025.
HOGENOM	HOG000049118.
KO	K08819.
OMA	LPHEHQA.
Family and domain databases
InterPro	IPR011009. 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]
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...

Entry information

Entry name

CDK12_AILME

Accession

Primary (citable) accession number: D2H526

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 5, 2011
Last sequence update:	February 9, 2010
Last modified:	May 1, 2013
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program