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Q86UE8

- TLK2_HUMAN

UniProt

Q86UE8 - TLK2_HUMAN

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Protein

Serine/threonine-protein kinase tousled-like 2

Gene
TLK2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.7 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.3 Publications

Cofactori

Magnesium.3 Publications

Enzyme regulationi

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.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei491 – 4911ATP By similarityBy similarity
Active sitei592 – 5921Proton acceptor1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi468 – 4769ATP By similarityBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. protein binding Source: IntAct
  3. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cellular response to DNA damage stimulus Source: UniProtKB
  3. cellular response to gamma radiation Source: UniProtKB
  4. chromatin modification Source: UniProtKB-KW
  5. chromosome segregation Source: UniProtKB
  6. intracellular signal transduction Source: UniProtKB
  7. negative regulation of autophagy Source: BHF-UCL
  8. negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  9. peptidyl-serine phosphorylation Source: UniProtKB
  10. protein phosphorylation Source: UniProtKB
  11. regulation of chromatin assembly or disassembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, DNA damage

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ86UE8.

Names & Taxonomyi

Protein namesi
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 namesi
Name:TLK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:11842. TLK2.

Subcellular locationi

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 G2.3 Publications

GO - Cellular componenti

  1. intermediate filament Source: UniProtKB
  2. nucleolus Source: HPA
  3. nucleus Source: UniProtKB
  4. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi613 – 6131D → A: Loss of kinase activity. 2 Publications

Organism-specific databases

PharmGKBiPA36544.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 772772Serine/threonine-protein kinase tousled-like 2PRO_0000086754Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei94 – 941Phosphoserine1 Publication
Modified residuei99 – 991Phosphoserine2 Publications
Modified residuei134 – 1341Phosphoserine1 Publication
Modified residuei750 – 7501Phosphoserine; by CHEK1 InferredBy similarity

Post-translational modificationi

Phosphorylated at Ser-750, probably by CHEK1.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ86UE8.
PaxDbiQ86UE8.
PRIDEiQ86UE8.

PTM databases

PhosphoSiteiQ86UE8.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

ArrayExpressiQ86UE8.
BgeeiQ86UE8.
CleanExiHS_TLK2.
GenevestigatoriQ86UE8.

Organism-specific databases

HPAiHPA056342.

Interactioni

Subunit structurei

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 FEZ2.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IRF4Q153062EBI-1047967,EBI-751345
IRF7Q929852EBI-1047967,EBI-968267

Protein-protein interaction databases

BioGridi116201. 14 interactions.
IntActiQ86UE8. 3 interactions.
MINTiMINT-5006424.
STRINGi9606.ENSP00000275780.

Structurei

3D structure databases

ProteinModelPortaliQ86UE8.
SMRiQ86UE8. Positions 458-769.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini462 – 741280Protein kinaseAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili225 – 27652 Reviewed predictionAdd
BLAST
Coiled coili317 – 34731 Reviewed predictionAdd
BLAST
Coiled coili403 – 45149 Reviewed predictionAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000259522.
HOVERGENiHBG007938.
InParanoidiQ86UE8.
KOiK08864.
OMAiLVYRKED.
PhylomeDBiQ86UE8.
TreeFamiTF315233.

Family and domain databases

InterProiIPR011009. 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]
PANTHERiPTHR22974:SF20. PTHR22974:SF20. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q86UE8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MMEELHSLDP RRQELLEARF TGVGVSKGPL NSESSNQSLC SVGSLSDKEV    50
ETPEKKQNDQ RNRKRKAEPY ETSQGKGTPR GHKISDYFEF AGGSAPGTSP 100
GRSVPPVARS SPQHSLSNPL PRRVEQPLYG LDGSAAKEAT EEQSALPTLM 150
SVMLAKPRLD TEQLAQRGAG LCFTFVSAQQ NSPSSTGSGN TEHSCSSQKQ 200
ISIQHRQTQS DLTIEKISAL ENSKNSDLEK KEGRIDDLLR ANCDLRRQID 250
EQQKMLEKYK ERLNRCVTMS KKLLIEKSKQ EKMACRDKSM QDRLRLGHFT 300
TVRHGASFTE QWTDGYAFQN LIKQQERINS QREEIERQRK MLAKRKPPAM 350
GQAPPATNEQ KQRKSKTNGA ENETPSSGNT ELKDTAPALG AHSLLRLTLA 400
EYHEQEEIFK LRLGHLKKEE AEIQAELERL ERVRNLHIRE LKRIHNEDNS 450
QFKDHPTLND RYLLLHLLGR GGFSEVYKAF DLTEQRYVAV KIHQLNKNWR 500
DEKKENYHKH ACREYRIHKE LDHPRIVKLY DYFSLDTDSF CTVLEYCEGN 550
DLDFYLKQHK LMSEKEARSI IMQIVNALKY LNEIKPPIIH YDLKPGNILL 600
VNGTACGEIK ITDFGLSKIM DDDSYNSVDG MELTSQGAGT YWYLPPECFV 650
VGKEPPKISN KVDVWSVGVI FYQCLYGRKP FGHNQSQQDI LQENTILKAT 700
EVQFPPKPVV TPEAKAFIRR CLAYRKEDRI DVQQLACDPY LLPHIRKSVS 750
TSSPAGAAIA STSGASNNSS SN 772

Note: No experimental confirmation available.

Length:772
Mass (Da):87,661
Last modified:August 22, 2003 - v2
Checksum:i765EE37ED4A4ADEC
GO
Isoform 21 Publication (identifier: Q86UE8-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:750
Mass (Da):85,444
Checksum:iDECCDBF95115C286
GO
Isoform 31 Publication (identifier: Q86UE8-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:718
Mass (Da):82,348
Checksum:i60E703322E8F2D2D
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61H → R.2 Publications
Corresponds to variant rs45550140 [ dbSNP | Ensembl ].
VAR_041216
Natural varianti54 – 541E → D.1 Publication
VAR_041217
Natural varianti95 – 951A → G.1 Publication
VAR_041218
Natural varianti108 – 1081A → G.1 Publication
VAR_041219
Natural varianti109 – 1091R → L.1 Publication
VAR_041220
Natural varianti173 – 1731F → L in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041221
Natural varianti262 – 2621R → Q.1 Publication
VAR_041222

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei90 – 12132Missing in isoform 3. 1 PublicationVSP_050572Add
BLAST
Alternative sequencei375 – 39622Missing in isoform 2 and isoform 3. 2 PublicationsVSP_050573Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → I in BAA20561. 1 Publication
Sequence conflicti161 – 1611T → P in BAA20561. 1 Publication
Sequence conflicti207 – 2071Q → R in AAF03095. 1 Publication
Sequence conflicti562 – 5621M → I in BAA20561. 1 Publication
Sequence conflicti727 – 7271E → R in AAF03095. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS11633.1. [Q86UE8-2]
CCDS45753.1. [Q86UE8-3]
CCDS62283.1. [Q86UE8-1]
RefSeqiNP_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]
UniGeneiHs.445078.

Genome annotation databases

EnsembliENST00000326270; ENSP00000316512; ENSG00000146872. [Q86UE8-1]
ENST00000343388; ENSP00000340800; ENSG00000146872. [Q86UE8-3]
ENST00000346027; ENSP00000275780; ENSG00000146872. [Q86UE8-2]
ENST00000542523; ENSP00000442311; ENSG00000146872. [Q86UE8-3]
GeneIDi11011.
KEGGihsa:11011.
UCSCiuc002izz.4. human. [Q86UE8-2]
uc002jaa.4. human. [Q86UE8-3]
uc010ddp.3. human. [Q86UE8-1]

Polymorphism databases

DMDMi34222826.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS11633.1. [Q86UE8-2 ]
CCDS45753.1. [Q86UE8-3 ]
CCDS62283.1. [Q86UE8-1 ]
RefSeqi NP_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 ]
UniGenei Hs.445078.

3D structure databases

ProteinModelPortali Q86UE8.
SMRi Q86UE8. Positions 458-769.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116201. 14 interactions.
IntActi Q86UE8. 3 interactions.
MINTi MINT-5006424.
STRINGi 9606.ENSP00000275780.

Chemistry

BindingDBi Q86UE8.
ChEMBLi CHEMBL5404.
GuidetoPHARMACOLOGYi 2243.

PTM databases

PhosphoSitei Q86UE8.

Polymorphism databases

DMDMi 34222826.

Proteomic databases

MaxQBi Q86UE8.
PaxDbi Q86UE8.
PRIDEi Q86UE8.

Protocols and materials databases

DNASUi 11011.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000326270 ; ENSP00000316512 ; ENSG00000146872 . [Q86UE8-1 ]
ENST00000343388 ; ENSP00000340800 ; ENSG00000146872 . [Q86UE8-3 ]
ENST00000346027 ; ENSP00000275780 ; ENSG00000146872 . [Q86UE8-2 ]
ENST00000542523 ; ENSP00000442311 ; ENSG00000146872 . [Q86UE8-3 ]
GeneIDi 11011.
KEGGi hsa:11011.
UCSCi uc002izz.4. human. [Q86UE8-2 ]
uc002jaa.4. human. [Q86UE8-3 ]
uc010ddp.3. human. [Q86UE8-1 ]

Organism-specific databases

CTDi 11011.
GeneCardsi GC17P060556.
H-InvDB HIX0027107.
HGNCi HGNC:11842. TLK2.
HPAi HPA056342.
MIMi 608439. gene.
neXtProti NX_Q86UE8.
PharmGKBi PA36544.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000259522.
HOVERGENi HBG007938.
InParanoidi Q86UE8.
KOi K08864.
OMAi LVYRKED.
PhylomeDBi Q86UE8.
TreeFami TF315233.

Enzyme and pathway databases

SignaLinki Q86UE8.

Miscellaneous databases

ChiTaRSi TLK2. human.
GeneWikii TLK2.
GenomeRNAii 11011.
NextBioi 41827.
PROi Q86UE8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q86UE8.
Bgeei Q86UE8.
CleanExi HS_TLK2.
Genevestigatori Q86UE8.

Family and domain databases

InterProi IPR011009. 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 ]
PANTHERi PTHR22974:SF20. PTHR22974:SF20. 1 hit.
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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.
    , 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.

Entry informationi

Entry nameiTLK2_HUMAN
AccessioniPrimary (citable) accession number: Q86UE8
Secondary accession number(s): D3DU07, Q9UKI7, Q9Y4F7
Entry historyi
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 statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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