Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q86UE8 (TLK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length772 AA.
Sequence statusComplete.
Protein existenceEvidence 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.15 Ref.19

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.15

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. Cytoplasmperinuclear region. Cytoplasmcytoskeleton. 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 processCell cycle
DNA damage
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionChromatin regulator
Kinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to DNA damage stimulus

Inferred from direct assay Ref.8. Source: UniProtKB

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.19. Source: BHF-UCL

negative regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.15. Source: UniProtKB

peptidyl-serine phosphorylation

Inferred from direct assay Ref.15. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.8. Source: UniProtKB

regulation of chromatin assembly or disassembly

Inferred from direct assay Ref.8. Source: UniProtKB

   Cellular_componentintermediate filament

Inferred from direct assay Ref.6. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.6Ref.1. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.8. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 21903422. Source: IntAct

protein serine/threonine kinase activity

Inferred from direct assay Ref.8. Source: UniProtKB

Complete GO annotation...

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 772772Serine/threonine-protein kinase tousled-like 2
PRO_0000086754

Regions

Domain462 – 741280Protein kinase
Nucleotide binding468 – 4769ATP By similarity UniProtKB O96017
Coiled coil225 – 27652 Potential
Coiled coil317 – 34731 Potential
Coiled coil403 – 45149 Potential

Sites

Active site5921Proton acceptor Ref.2
Binding site4911ATP By similarity UniProtKB O96017

Amino acid modifications

Modified residue941Phosphoserine Ref.14
Modified residue991Phosphoserine Ref.12 Ref.16
Modified residue1341Phosphoserine Ref.14
Modified residue7501Phosphoserine; by CHEK1 Probable UniProtKB Q9UKI8

Natural variations

Alternative sequence90 – 12132Missing in isoform 3. Ref.1
VSP_050572
Alternative sequence375 – 39622Missing in isoform 2 and isoform 3. Ref.1 Ref.2
VSP_050573
Natural variant61H → R. Ref.1 Ref.20
Corresponds to variant rs45550140 [ dbSNP | Ensembl ].
VAR_041216
Natural variant541E → D. Ref.20
VAR_041217
Natural variant951A → G. Ref.20
VAR_041218
Natural variant1081A → G. Ref.20
VAR_041219
Natural variant1091R → L. Ref.20
VAR_041220
Natural variant1731F → L in a gastric adenocarcinoma sample; somatic mutation. Ref.20
VAR_041221
Natural variant2621R → Q. Ref.20
VAR_041222

Experimental info

Mutagenesis6131D → A: Loss of kinase activity. Ref.2 Ref.7
Sequence conflict11M → I in BAA20561. Ref.1
Sequence conflict1611T → P in BAA20561. Ref.1
Sequence conflict2071Q → R in AAF03095. Ref.2
Sequence conflict5621M → I in BAA20561. Ref.1
Sequence conflict7271E → R in AAF03095. Ref.2

Sequences

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

Last modified August 22, 2003. Version 2.
Checksum: 765EE37ED4A4ADEC

FASTA77287,661
        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 

« Hide

Isoform 2 [UniParc].

Checksum: DECCDBF95115C286
Show »

FASTA75085,444
Isoform 3 [UniParc].

Checksum: 60E703322E8F2D2D
Show »

FASTA71882,348

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"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].
[18]"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].
[19]"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.
[20]"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] 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.
CCDSCCDS11633.1. [Q86UE8-2]
CCDS45753.1. [Q86UE8-3]
CCDS62283.1. [Q86UE8-1]
RefSeqNP_001271262.1. NM_001284333.1. [Q86UE8-1]
NP_001271292.1. NM_001284363.1. [Q86UE8-3]
NP_006843.2. NM_006852.3. [Q86UE8-2]
XP_005257026.1. XM_005256969.1. [Q86UE8-2]
XP_005257027.1. XM_005256970.2. [Q86UE8-2]
XP_005257028.1. XM_005256971.2. [Q86UE8-3]
XP_006721710.1. XM_006721647.1. [Q86UE8-2]
XP_006721711.1. XM_006721648.1. [Q86UE8-3]
UniGeneHs.445078.

3D structure databases

ProteinModelPortalQ86UE8.
SMRQ86UE8. Positions 458-769.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116201. 14 interactions.
IntActQ86UE8. 3 interactions.
MINTMINT-5006424.
STRING9606.ENSP00000275780.

Chemistry

BindingDBQ86UE8.
ChEMBLCHEMBL5404.
GuidetoPHARMACOLOGY2243.

PTM databases

PhosphoSiteQ86UE8.

Polymorphism databases

DMDM34222826.

Proteomic databases

MaxQBQ86UE8.
PaxDbQ86UE8.
PRIDEQ86UE8.

Protocols and materials databases

DNASU11011.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326270; ENSP00000316512; ENSG00000146872. [Q86UE8-1]
ENST00000343388; ENSP00000340800; ENSG00000146872. [Q86UE8-3]
ENST00000346027; ENSP00000275780; ENSG00000146872. [Q86UE8-2]
ENST00000542523; ENSP00000442311; ENSG00000146872. [Q86UE8-3]
GeneID11011.
KEGGhsa:11011.
UCSCuc002izz.4. human. [Q86UE8-2]
uc002jaa.4. human. [Q86UE8-3]
uc010ddp.3. human. [Q86UE8-1]

Organism-specific databases

CTD11011.
GeneCardsGC17P060556.
H-InvDBHIX0027107.
HGNCHGNC:11842. TLK2.
HPAHPA056342.
MIM608439. gene.
neXtProtNX_Q86UE8.
PharmGKBPA36544.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000259522.
HOVERGENHBG007938.
InParanoidQ86UE8.
KOK08864.
OMALVYRKED.
PhylomeDBQ86UE8.
TreeFamTF315233.

Enzyme and pathway databases

SignaLinkQ86UE8.

Gene expression databases

ArrayExpressQ86UE8.
BgeeQ86UE8.
CleanExHS_TLK2.
GenevestigatorQ86UE8.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR027086. TLK2.
[Graphical view]
PANTHERPTHR22974:SF20. PTHR22974:SF20. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTLK2. human.
GeneWikiTLK2.
GenomeRNAi11011.
NextBio41827.
PROQ86UE8.
SOURCESearch...

Entry information

Entry nameTLK2_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 125 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

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM