Q86UE8 (TLK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase tousled-like 2
EC=2.7.11.1

Alternative name(s):
HsHPK
PKU-alpha
Tousled-like kinase 2

Gene names

Name:

TLK2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	772 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation. Phosphorylates the chromatin assembly factors ASF1A AND ASF1B. Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly. Negative regulator of amino acid starvation-induced autophagy. Ref.1 Ref.2 Ref.7 Ref.8 Ref.9 Ref.14 Ref.18
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.1 Ref.2 Ref.8
Cofactor	Magnesium. Ref.1 Ref.2 Ref.8
Enzyme regulation	Cell cycle-regulated, with maximal activity in the S-phase. Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase, probably by CHEK1, possibly at Ser-750. This inhibition is cell cycle checkpoint- and ATM-dependent. Ref.2 Ref.8 Ref.9 Ref.14
Subunit structure	Monomer and heterodimer with TLK1. Interacts with ASF1A and ASF1B. Association with 14-3-3 proteins such as YWHAZ regulates subcellular location. May also interact with FEZ1/LZTS1 and FEZ2. Ref.2 Ref.6 Ref.7 Ref.10
Subcellular location	Nucleus. Cytoplasm › perinuclear region. Cytoplasm › cytoskeleton. Note: Colocalizes with the cytoplasmic intermediate filament system during the G1 phase of the cell cycle. Present in the perinuclear region at S phase and in the nucleus at late G2. Ref.1 Ref.2 Ref.6
Tissue specificity	Ubiquitous. Detected in placenta, fetal liver, kidney, pancreas, heart and skeletal muscle. Highly expressed in testis. Detected in spleen, thymus, colon, ovary, small intestine, prostate and peripheral blood leukocytes. Ref.1 Ref.5
Post-translational modification	Phosphorylated at Ser-750, probably by CHEK1. Ref.9
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain.
Sequence caution	The sequence AAF03095.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH44925.2 differs from that shown. Reason: Erroneous initiation. The sequence BAA20561.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell cycle DNA damage
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chromatin regulator Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cellular response to gamma radiation Inferred from direct assay Ref.8. Source: UniProtKB chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW chromosome segregation Inferred from mutant phenotype PubMed 20705056. Source: UniProtKB intracellular signal transduction Inferred from direct assay Ref.8. Source: UniProtKB negative regulation of autophagy Non-traceable author statement Ref.18. Source: BHF-UCL negative regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from mutant phenotype Ref.14. Source: UniProtKB peptidyl-serine phosphorylation Inferred from direct assay Ref.14. Source: UniProtKB regulation of chromatin assembly or disassembly Inferred from direct assay Ref.8. Source: UniProtKB response to DNA damage stimulus Inferred from direct assay Ref.8. Source: UniProtKB
Cellular_component	intermediate filament Inferred from direct assay Ref.6. Source: UniProtKB nucleus Inferred from direct assay Ref.6Ref.1. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	ATP binding Inferred from direct assay Ref.8. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IRF4	Q15306	2	EBI-1047967,EBI-751345
IRF7	Q92985	2	EBI-1047967,EBI-968267

Alternative products

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

Isoform 1 (identifier: Q86UE8-1)

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.

Note: No experimental confirmation available.

Isoform 2 Ref.2 (identifier: Q86UE8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     375-396: Missing.

Isoform 3 Ref.1 (identifier: Q86UE8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     90-121: Missing.
     375-396: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 772	772	Serine/threonine-protein kinase tousled-like 2		PRO_0000086754
Regions
	Domain	462 – 741	280	Protein kinase
	Nucleotide binding	468 – 476	9	ATP By similarity UniProtKB O96017
	Coiled coil	225 – 276	52	Potential
	Coiled coil	317 – 347	31	Potential
	Coiled coil	403 – 451	49	Potential
Sites
	Active site	592	1	Proton acceptor Ref.2
	Binding site	491	1	ATP By similarity UniProtKB O96017
Amino acid modifications
	Modified residue	94	1	Phosphoserine Ref.13
	Modified residue	99	1	Phosphoserine Ref.12 Ref.15
	Modified residue	134	1	Phosphoserine Ref.13
	Modified residue	750	1	Phosphoserine; by CHEK1 Probable UniProtKB Q9UKI8
Natural variations
	Alternative sequence	90 – 121	32	Missing in isoform 3. Ref.1		VSP_050572
	Alternative sequence	375 – 396	22	Missing in isoform 2 and isoform 3. Ref.1 Ref.2		VSP_050573
	Natural variant	6	1	H → R. Ref.1 Ref.19 Corresponds to variant rs45550140 [ dbSNP | Ensembl ].		VAR_041216
	Natural variant	54	1	E → D. Ref.19		VAR_041217
	Natural variant	95	1	A → G. Ref.19		VAR_041218
	Natural variant	108	1	A → G. Ref.19		VAR_041219
	Natural variant	109	1	R → L. Ref.19		VAR_041220
	Natural variant	173	1	F → L in a gastric adenocarcinoma sample; somatic mutation. Ref.19		VAR_041221
	Natural variant	262	1	R → Q. Ref.19		VAR_041222
Experimental info
	Mutagenesis	613	1	D → A: Loss of kinase activity. Ref.2 Ref.7
	Sequence conflict	1	1	M → I in BAA20561. Ref.1
	Sequence conflict	161	1	T → P in BAA20561. Ref.1
	Sequence conflict	207	1	Q → R in AAF03095. Ref.2
	Sequence conflict	562	1	M → I in BAA20561. Ref.1
	Sequence conflict	727	1	E → R in AAF03095. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 22, 2003. Version 2. Checksum: 765EE37ED4A4ADEC	FASTA	772	87,661
	10 20 30 40 50 60 MMEELHSLDP RRQELLEARF TGVGVSKGPL NSESSNQSLC SVGSLSDKEV ETPEKKQNDQ 70 80 90 100 110 120 RNRKRKAEPY ETSQGKGTPR GHKISDYFEF AGGSAPGTSP GRSVPPVARS SPQHSLSNPL 130 140 150 160 170 180 PRRVEQPLYG LDGSAAKEAT EEQSALPTLM SVMLAKPRLD TEQLAQRGAG LCFTFVSAQQ 190 200 210 220 230 240 NSPSSTGSGN TEHSCSSQKQ ISIQHRQTQS DLTIEKISAL ENSKNSDLEK KEGRIDDLLR 250 260 270 280 290 300 ANCDLRRQID EQQKMLEKYK ERLNRCVTMS KKLLIEKSKQ EKMACRDKSM QDRLRLGHFT 310 320 330 340 350 360 TVRHGASFTE QWTDGYAFQN LIKQQERINS QREEIERQRK MLAKRKPPAM GQAPPATNEQ 370 380 390 400 410 420 KQRKSKTNGA ENETPSSGNT ELKDTAPALG AHSLLRLTLA EYHEQEEIFK LRLGHLKKEE 430 440 450 460 470 480 AEIQAELERL ERVRNLHIRE LKRIHNEDNS QFKDHPTLND RYLLLHLLGR GGFSEVYKAF 490 500 510 520 530 540 DLTEQRYVAV KIHQLNKNWR DEKKENYHKH ACREYRIHKE LDHPRIVKLY DYFSLDTDSF 550 560 570 580 590 600 CTVLEYCEGN DLDFYLKQHK LMSEKEARSI IMQIVNALKY LNEIKPPIIH YDLKPGNILL 610 620 630 640 650 660 VNGTACGEIK ITDFGLSKIM DDDSYNSVDG MELTSQGAGT YWYLPPECFV VGKEPPKISN 670 680 690 700 710 720 KVDVWSVGVI FYQCLYGRKP FGHNQSQQDI LQENTILKAT EVQFPPKPVV TPEAKAFIRR 730 740 750 760 770 CLAYRKEDRI DVQQLACDPY LLPHIRKSVS TSSPAGAAIA STSGASNNSS SN
	Isoform 2 [UniParc]. Checksum: DECCDBF95115C286	FASTA	750	85,444
	10 20 30 40 50 60 MMEELHSLDP RRQELLEARF TGVGVSKGPL NSESSNQSLC SVGSLSDKEV ETPEKKQNDQ 70 80 90 100 110 120 RNRKRKAEPY ETSQGKGTPR GHKISDYFEF AGGSAPGTSP GRSVPPVARS SPQHSLSNPL 130 140 150 160 170 180 PRRVEQPLYG LDGSAAKEAT EEQSALPTLM SVMLAKPRLD TEQLAQRGAG LCFTFVSAQQ 190 200 210 220 230 240 NSPSSTGSGN TEHSCSSQKQ ISIQHRQTQS DLTIEKISAL ENSKNSDLEK KEGRIDDLLR 250 260 270 280 290 300 ANCDLRRQID EQQKMLEKYK ERLNRCVTMS KKLLIEKSKQ EKMACRDKSM QDRLRLGHFT 310 320 330 340 350 360 TVRHGASFTE QWTDGYAFQN LIKQQERINS QREEIERQRK MLAKRKPPAM GQAPPATNEQ 370 380 390 400 410 420 KQRKSKTNGA ENETLTLAEY HEQEEIFKLR LGHLKKEEAE IQAELERLER VRNLHIRELK 430 440 450 460 470 480 RIHNEDNSQF KDHPTLNDRY LLLHLLGRGG FSEVYKAFDL TEQRYVAVKI HQLNKNWRDE 490 500 510 520 530 540 KKENYHKHAC REYRIHKELD HPRIVKLYDY FSLDTDSFCT VLEYCEGNDL DFYLKQHKLM 550 560 570 580 590 600 SEKEARSIIM QIVNALKYLN EIKPPIIHYD LKPGNILLVN GTACGEIKIT DFGLSKIMDD 610 620 630 640 650 660 DSYNSVDGME LTSQGAGTYW YLPPECFVVG KEPPKISNKV DVWSVGVIFY QCLYGRKPFG 670 680 690 700 710 720 HNQSQQDILQ ENTILKATEV QFPPKPVVTP EAKAFIRRCL AYRKEDRIDV QQLACDPYLL 730 740 750 PHIRKSVSTS SPAGAAIAST SGASNNSSSN
	Isoform 3 [UniParc]. Checksum: 60E703322E8F2D2D	FASTA	718	82,348
	10 20 30 40 50 60 MMEELHSLDP RRQELLEARF TGVGVSKGPL NSESSNQSLC SVGSLSDKEV ETPEKKQNDQ 70 80 90 100 110 120 RNRKRKAEPY ETSQGKGTPR GHKISDYFER RVEQPLYGLD GSAAKEATEE QSALPTLMSV 130 140 150 160 170 180 MLAKPRLDTE QLAQRGAGLC FTFVSAQQNS PSSTGSGNTE HSCSSQKQIS IQHRQTQSDL 190 200 210 220 230 240 TIEKISALEN SKNSDLEKKE GRIDDLLRAN CDLRRQIDEQ QKMLEKYKER LNRCVTMSKK 250 260 270 280 290 300 LLIEKSKQEK MACRDKSMQD RLRLGHFTTV RHGASFTEQW TDGYAFQNLI KQQERINSQR 310 320 330 340 350 360 EEIERQRKML AKRKPPAMGQ APPATNEQKQ RKSKTNGAEN ETLTLAEYHE QEEIFKLRLG 370 380 390 400 410 420 HLKKEEAEIQ AELERLERVR NLHIRELKRI HNEDNSQFKD HPTLNDRYLL LHLLGRGGFS 430 440 450 460 470 480 EVYKAFDLTE QRYVAVKIHQ LNKNWRDEKK ENYHKHACRE YRIHKELDHP RIVKLYDYFS 490 500 510 520 530 540 LDTDSFCTVL EYCEGNDLDF YLKQHKLMSE KEARSIIMQI VNALKYLNEI KPPIIHYDLK 550 560 570 580 590 600 PGNILLVNGT ACGEIKITDF GLSKIMDDDS YNSVDGMELT SQGAGTYWYL PPECFVVGKE 610 620 630 640 650 660 PPKISNKVDV WSVGVIFYQC LYGRKPFGHN QSQQDILQEN TILKATEVQF PPKPVVTPEA 670 680 690 700 710 KAFIRRCLAY RKEDRIDVQQ LACDPYLLPH IRKSVSTSSP AGAAIASTSG ASNNSSSN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and chromosomal mapping of genes encoding novel protein kinases termed PKU-alpha and PKU-beta, which have nuclear localization signal." Yamakawa A., Kameoka Y., Hashimoto K., Yoshitake Y., Nishikawa K., Tanihara K., Date T. Gene 202:193-201(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT ARG-6, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Placenta and Testis.
[2]	"Mammalian homologues of the plant tousled gene code for cell-cycle-regulated kinases with maximal activities linked to ongoing DNA replication." Sillje H.H.W., Takahashi K., Tanaka K., Van Houwe G., Nigg E.A. EMBO J. 18:5691-5702(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, MUTAGENESIS OF ASP-613, SUBCELLULAR LOCATION, INTERACTION WITH TLK1, ENZYME REGULATION. Tissue: Placenta.
[3]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Testis.
[5]	"From mosquito to man: identification of a novel protein kinase, HsHPK, which is highly expressed in human hepatoma tissues." Huang A.M., Chang T.J., Cho W.L., Chou C.K. J. Biomed. Sci. 5:135-140(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 189-772 (ISOFORM 2/3), TISSUE SPECIFICITY.
[6]	"Nuclear localization of protein kinase U-alpha is regulated by 14-3-3." Zhang S., Xing H., Muslin A.J. J. Biol. Chem. 274:24865-24872(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH YWHAZ.
[7]	"Identification of human Asf1 chromatin assembly factors as substrates of Tousled-like kinases." Sillje H.H.W., Nigg E.A. Curr. Biol. 11:1068-1073(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ASF1A AND ASF1B, MUTAGENESIS OF ASP-613.
[8]	"Human tousled like kinases are targeted by an ATM- and Chk1-dependent DNA damage checkpoint." Groth A., Lukas J., Nigg E.A., Sillje H.H.W., Wernstedt C., Bartek J., Hansen K. EMBO J. 22:1676-1687(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION.
[9]	"Suppression of tousled-like kinase activity after DNA damage or replication block requires ATM, NBS1 and Chk1." Krause D.R., Jonnalagadda J.C., Gatei M.H., Sillje H.H.W., Zhou B.-B., Nigg E.A., Khanna K. Oncogene 22:5927-5937(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-750, FUNCTION, ENZYME REGULATION.
[10]	"FEZ1 dimerization and interaction with transcription regulatory proteins involves its coiled-coil region." Assmann E.M., Alborghetti M.R., Camargo M.E.R., Kobarg J. J. Biol. Chem. 281:9869-9881(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FEZ1 AND FEZ2.
[11]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[12]	"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-99, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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-94 AND SER-134, MASS SPECTROMETRY.
[14]	"Phosphorylation-mediated control of histone chaperone ASF1 levels by Tousled-like kinases." Pilyugin M., Demmers J., Verrijzer C.P., Karch F., Moshkin Y.M. PLoS ONE 4:E8328-E8328(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS ASF1A AND ASF1B KINASE, ENZYME REGULATION.
[15]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"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].
[17]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"Genome-wide siRNA screen reveals amino acid starvation-induced autophagy requires SCOC and WAC." McKnight N.C., Jefferies H.B., Alemu E.A., Saunders R.E., Howell M., Johansen T., Tooze S.A. EMBO J. 31:1931-1946(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-6; ASP-54; GLY-95; GLY-108; LEU-109; LEU-173 AND GLN-262.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB004884 mRNA. Translation: BAA20561.1. Different initiation. AF162667 mRNA. Translation: AAF03095.1. Different initiation. CH471109 Genomic DNA. Translation: EAW94346.1. CH471109 Genomic DNA. Translation: EAW94348.1. BC044925 mRNA. Translation: AAH44925.2. Different initiation.
IPI	IPI00337659. IPI00337660. IPI00385652.
RefSeq	NP_001106178.1. NM_001112707.1. NP_006843.2. NM_006852.3.
UniGene	Hs.445078.
3D structure databases
ProteinModelPortal	Q86UE8.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q86UE8. 3 interactions.
STRING	9606.ENSP00000275780.
PTM databases
PhosphoSite	Q86UE8.
Polymorphism databases
DMDM	34222826.
Proteomic databases
PaxDb	Q86UE8.
PRIDE	Q86UE8.
Protocols and materials databases
DNASU	11011.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000326270; ENSP00000316512; ENSG00000146872. ENST00000343388; ENSP00000340800; ENSG00000146872. ENST00000346027; ENSP00000275780; ENSG00000146872. ENST00000542523; ENSP00000442311; ENSG00000146872.
GeneID	11011.
KEGG	hsa:11011.
UCSC	uc002izx.4. human. uc002izz.4. human. uc010ddp.3. human.
Organism-specific databases
CTD	11011.
GeneCards	GC17P060556.
H-InvDB	HIX0027107.
HGNC	HGNC:11842. TLK2.
MIM	608439. gene.
neXtProt	NX_Q86UE8.
PharmGKB	PA36544.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000259522.
HOVERGEN	HBG007938.
InParanoid	Q86UE8.
KO	K08864.
OMA	LVYRKED.
OrthoDB	EOG4M65H4.
PhylomeDB	Q86UE8.
Gene expression databases
Bgee	Q86UE8.
CleanEx	HS_TLK2.
Genevestigator	Q86UE8.
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. IPR027086. TLK. [Graphical view]
PANTHER	PTHR22974:SF1. PTHR22974:SF1. 1 hit.
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
BindingDB	Q86UE8.
ChEMBL	CHEMBL5404.
ChiTaRS	TLK2. human.
GenomeRNAi	11011.
NextBio	41827.
SOURCE	Search...

Entry information

Entry name

TLK2_HUMAN

Accession

Primary (citable) accession number: Q86UE8
Secondary accession number(s): D3DU07, Q9UKI7, Q9Y4F7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 22, 2003
Last sequence update:	August 22, 2003
Last modified:	May 1, 2013
This is version 112 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.