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Q9UKI8

- TLK1_HUMAN

UniProt

Q9UKI8 - TLK1_HUMAN

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Protein

Serine/threonine-protein kinase tousled-like 1

Gene

TLK1

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

Functioni

Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly. Isoform 3 phosphorylates and enhances the stability of the t-SNARE SNAP23, augmenting its assembly with syntaxin. Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10'.6 Publications

Catalytic activityi

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

Cofactori

Magnesium.3 Publications

Enzyme regulationi

Cell-cycle regulated, maximal activity in S-phase. Inactivated by phosphorylation at Ser-743, potentially by CHEK1.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei485 – 4851ATPPROSITE-ProRule annotation
Active sitei586 – 5861Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi462 – 4709ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. 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-KW
  3. chromatin modification Source: UniProtKB-KW
  4. intracellular protein transport Source: UniProtKB
  5. intracellular signal transduction Source: UniProtKB
  6. protein phosphorylation Source: UniProtKB
  7. 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

SignaLinkiQ9UKI8.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase tousled-like 1 (EC:2.7.11.1)
Alternative name(s):
PKU-beta
Tousled-like kinase 1
Gene namesi
Name:TLK1
Synonyms:KIAA0137
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:11841. TLK1.

Subcellular locationi

Nucleus 4 Publications

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi607 – 6071D → A: Loss of kinase activity. 2 Publications
Mutagenesisi743 – 7431S → A: Loss of kinase inhibition in response to DNA damage. 1 Publication
Mutagenesisi743 – 7431S → D: Loss of kinase inhibition in response to DNA damage. 1 Publication
Mutagenesisi743 – 7431S → E: Loss of kinase inhibition in response to DNA damage. 1 Publication

Organism-specific databases

PharmGKBiPA36543.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 766766Serine/threonine-protein kinase tousled-like 1PRO_0000086752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei159 – 1591Phosphoserine2 Publications
Modified residuei743 – 7431Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UKI8.
PaxDbiQ9UKI8.
PRIDEiQ9UKI8.

Expressioni

Tissue specificityi

Widely expressed. Present in fetal placenta, liver, kidney and pancreas but not heart or skeletal muscle. Also found in adult cell lines. Isoform 3 is ubiquitously expressed in all tissues examined.2 Publications

Gene expression databases

BgeeiQ9UKI8.
CleanExiHS_TLK1.
ExpressionAtlasiQ9UKI8. baseline and differential.
GenevestigatoriQ9UKI8.

Organism-specific databases

HPAiHPA016043.

Interactioni

Subunit structurei

Heterodimerizes with TLK2. Interacts with ASF1A and ASF1B.2 Publications

Protein-protein interaction databases

BioGridi115206. 15 interactions.
IntActiQ9UKI8. 7 interactions.
MINTiMINT-112025.
STRINGi9606.ENSP00000411099.

Structurei

3D structure databases

ProteinModelPortaliQ9UKI8.
SMRiQ9UKI8. Positions 427-764.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini456 – 734279Protein kinasePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili230 – 28152Sequence AnalysisAdd
BLAST
Coiled coili397 – 44549Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00620000087848.
HOGENOMiHOG000259522.
HOVERGENiHBG007938.
InParanoidiQ9UKI8.
KOiK08864.
OMAiDVQFPVK.
OrthoDBiEOG78H3SF.
PhylomeDBiQ9UKI8.
TreeFamiTF315233.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q9UKI8-1) [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

        10         20         30         40         50
MSVQSSSGSL EGPPSWSQLS TSPTPGSAAA ARSLLNHTPP SGRPREGAMD
60 70 80 90 100
ELHSLDPRRQ ELLEARFTGV ASGSTGSTGS CSVGAKASTN NESSNHSFGS
110 120 130 140 150
LGSLSDKESE TPEKKQSESS RGRKRKAENQ NESSQGKSIG GRGHKISDYF
160 170 180 190 200
EYQGGNGSSP VRGIPPAIRS PQNSHSHSTP SSSVRPNSPS PTALAFGDHP
210 220 230 240 250
IVQPKQLSFK IIQTDLTMLK LAALESNKIQ DLEKKEGRID DLLRANCDLR
260 270 280 290 300
RQIDEQQKLL EKYKERLNKC ISMSKKLLIE KSTQEKLSSR EKSMQDRLRL
310 320 330 340 350
GHFTTVRHGA SFTEQWTDGF AFQNLVKQQE WVNQQREDIE RQRKLLAKRK
360 370 380 390 400
PPTANNSQAP STNSEPKQRK NKAVNGAEND PFVRPNLPQL LTLAEYHEQE
410 420 430 440 450
EIFKLRLGHL KKEEAEIQAE LERLERVRNL HIRELKRINN EDNSQFKDHP
460 470 480 490 500
TLNERYLLLH LLGRGGFSEV YKAFDLYEQR YAAVKIHQLN KSWRDEKKEN
510 520 530 540 550
YHKHACREYR IHKELDHPRI VKLYDYFSLD TDTFCTVLEY CEGNDLDFYL
560 570 580 590 600
KQHKLMSEKE ARSIVMQIVN ALRYLNEIKP PIIHYDLKPG NILLVDGTAC
610 620 630 640 650
GEIKITDFGL SKIMDDDSYG VDGMDLTSQG AGTYWYLPPE CFVVGKEPPK
660 670 680 690 700
ISNKVDVWSV GVIFFQCLYG RKPFGHNQSQ QDILQENTIL KATEVQFPVK
710 720 730 740 750
PVVSSEAKAF IRRCLAYRKE DRFDVHQLAN DPYLLPHMRR SNSSGNLHMA
760
GLTASPTPPS SSIITY
Length:766
Mass (Da):86,700
Last modified:August 22, 2003 - v2
Checksum:iA65AE0A2A7C7FF2F
GO
Isoform 21 Publication (identifier: Q9UKI8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     136-136: G → GFPNLPVFQSLAYWEMGRTAGG

Show »
Length:787
Mass (Da):89,023
Checksum:i87275865796F5A54
GO
Isoform 31 Publication (identifier: Q9UKI8-3) [UniParc]FASTAAdd to Basket

Also known as: SNAK1 Publication

, TLK1B

The sequence of this isoform differs from the canonical sequence as follows:
     1-217: Missing.

Show »
Length:549
Mass (Da):63,994
Checksum:iED6FBF1F77E7E90F
GO
Isoform 4 (identifier: Q9UKI8-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MSVQSSSGSLEGPP → MAVLFLYDLKTTGK
     15-110: Missing.

Note: No experimental confirmation available.

Show »
Length:670
Mass (Da):77,110
Checksum:iBFA0D9CF3CEFB7C1
GO
Isoform 5 (identifier: Q9UKI8-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: Missing.

Note: No experimental confirmation available.

Show »
Length:718
Mass (Da):81,927
Checksum:i73E77AF8D34C531D
GO

Sequence cautioni

The sequence AAF03094.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAA09486.2 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 881S → T in AAF03094. (PubMed:10523312)Curated
Sequence conflicti102 – 1021G → E in BAA20562. (PubMed:9427565)Curated
Sequence conflicti230 – 2301Q → L in BAA20562. (PubMed:9427565)Curated
Sequence conflicti261 – 2611E → D in BAA20562. (PubMed:9427565)Curated
Sequence conflicti416 – 4161E → G in BAA20562. (PubMed:9427565)Curated
Sequence conflicti439 – 4391N → H in BAA20562. (PubMed:9427565)Curated
Sequence conflicti471 – 4711Y → D in BAA20562. (PubMed:9427565)Curated
Sequence conflicti477 – 4771Y → S in BAA20562. (PubMed:9427565)Curated
Sequence conflicti625 – 6251D → V in BAA20562. (PubMed:9427565)Curated
Sequence conflicti665 – 6651F → Y in BAA20562. (PubMed:9427565)Curated
Sequence conflicti730 – 7301N → C in BAA20562. (PubMed:9427565)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti121 – 1211R → C.1 Publication
VAR_041215

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 217217Missing in isoform 3. 1 PublicationVSP_050570Add
BLAST
Alternative sequencei1 – 4848Missing in isoform 5. 1 PublicationVSP_043504Add
BLAST
Alternative sequencei1 – 1414MSVQS…LEGPP → MAVLFLYDLKTTGK in isoform 4. 1 PublicationVSP_043505Add
BLAST
Alternative sequencei15 – 11096Missing in isoform 4. 1 PublicationVSP_043506Add
BLAST
Alternative sequencei136 – 1361G → GFPNLPVFQSLAYWEMGRTA GG in isoform 2. 1 PublicationVSP_050571

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB004885 mRNA. Translation: BAA20562.1.
AF162666 mRNA. Translation: AAF03094.1. Different initiation.
AF246219 mRNA. Translation: AAF71263.1.
D50927 mRNA. Translation: BAA09486.2. Different initiation.
AK090779 mRNA. Translation: BAG52227.1.
AK301857 mRNA. Translation: BAG63299.1.
AC007739 Genomic DNA. No translation available.
AC009953 Genomic DNA. No translation available.
AC010092 Genomic DNA. No translation available.
BC032657 mRNA. Translation: AAH32657.1.
CCDSiCCDS2241.1. [Q9UKI8-1]
CCDS46447.1. [Q9UKI8-5]
CCDS46448.1. [Q9UKI8-4]
RefSeqiNP_001130026.1. NM_001136554.1. [Q9UKI8-5]
NP_001130027.1. NM_001136555.1. [Q9UKI8-4]
NP_036422.3. NM_012290.4. [Q9UKI8-1]
XP_005247038.1. XM_005246981.1. [Q9UKI8-3]
UniGeneiHs.744917.

Genome annotation databases

GeneIDi9874.
KEGGihsa:9874.
UCSCiuc002ugn.2. human. [Q9UKI8-1]
uc002ugo.2. human. [Q9UKI8-2]
uc010zdn.1. human. [Q9UKI8-4]

Polymorphism databases

DMDMi34223086.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB004885 mRNA. Translation: BAA20562.1 .
AF162666 mRNA. Translation: AAF03094.1 . Different initiation.
AF246219 mRNA. Translation: AAF71263.1 .
D50927 mRNA. Translation: BAA09486.2 . Different initiation.
AK090779 mRNA. Translation: BAG52227.1 .
AK301857 mRNA. Translation: BAG63299.1 .
AC007739 Genomic DNA. No translation available.
AC009953 Genomic DNA. No translation available.
AC010092 Genomic DNA. No translation available.
BC032657 mRNA. Translation: AAH32657.1 .
CCDSi CCDS2241.1. [Q9UKI8-1 ]
CCDS46447.1. [Q9UKI8-5 ]
CCDS46448.1. [Q9UKI8-4 ]
RefSeqi NP_001130026.1. NM_001136554.1. [Q9UKI8-5 ]
NP_001130027.1. NM_001136555.1. [Q9UKI8-4 ]
NP_036422.3. NM_012290.4. [Q9UKI8-1 ]
XP_005247038.1. XM_005246981.1. [Q9UKI8-3 ]
UniGenei Hs.744917.

3D structure databases

ProteinModelPortali Q9UKI8.
SMRi Q9UKI8. Positions 427-764.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115206. 15 interactions.
IntActi Q9UKI8. 7 interactions.
MINTi MINT-112025.
STRINGi 9606.ENSP00000411099.

Chemistry

BindingDBi Q9UKI8.
ChEMBLi CHEMBL5388.
GuidetoPHARMACOLOGYi 2242.

Polymorphism databases

DMDMi 34223086.

Proteomic databases

MaxQBi Q9UKI8.
PaxDbi Q9UKI8.
PRIDEi Q9UKI8.

Protocols and materials databases

DNASUi 9874.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 9874.
KEGGi hsa:9874.
UCSCi uc002ugn.2. human. [Q9UKI8-1 ]
uc002ugo.2. human. [Q9UKI8-2 ]
uc010zdn.1. human. [Q9UKI8-4 ]

Organism-specific databases

CTDi 9874.
GeneCardsi GC02M171812.
HGNCi HGNC:11841. TLK1.
HPAi HPA016043.
MIMi 608438. gene.
neXtProti NX_Q9UKI8.
PharmGKBi PA36543.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00620000087848.
HOGENOMi HOG000259522.
HOVERGENi HBG007938.
InParanoidi Q9UKI8.
KOi K08864.
OMAi DVQFPVK.
OrthoDBi EOG78H3SF.
PhylomeDBi Q9UKI8.
TreeFami TF315233.

Enzyme and pathway databases

SignaLinki Q9UKI8.

Miscellaneous databases

ChiTaRSi TLK1. human.
GeneWikii TLK1.
GenomeRNAii 9874.
NextBioi 37219.
PROi Q9UKI8.
SOURCEi Search...

Gene expression databases

Bgeei Q9UKI8.
CleanExi HS_TLK1.
ExpressionAtlasi Q9UKI8. baseline and differential.
Genevestigatori Q9UKI8.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
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 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Placenta1 Publication and Testis1 Publication.
  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 1), FUNCTION, MUTAGENESIS OF ASP-607, SUBCELLULAR LOCATION, INTERACTION WITH TLK2, ENZYME REGULATION.
    Tissue: PlacentaImported.
  3. "Phosphorylation of SNAP-23 by the novel kinase SNAK regulates t-SNARE complex assembly."
    Cabaniols J.-P., Ravichandran V., Roche P.A.
    Mol. Biol. Cell 10:4033-4041(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Placenta1 Publication.
  4. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
    DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow1 Publication.
  5. "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] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  6. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
    Tissue: Amygdala and Testis.
  7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: UterusImported.
  9. "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-607.
  10. "A translationally regulated Tousled kinase phosphorylates histone H3 and confers radioresistance when overexpressed."
    Li Y., DeFatta R., Anthony C., Sunavala G., De Benedetti A.
    Oncogene 20:726-738(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION OF HISTONE H3.
  11. "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, MUTAGENESIS OF SER-743, PHOSPHORYLATION AT SER-743, ENZYME REGULATION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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: VARIANT [LARGE SCALE ANALYSIS] CYS-121.

Entry informationi

Entry nameiTLK1_HUMAN
AccessioniPrimary (citable) accession number: Q9UKI8
Secondary accession number(s): B3KR15
, B4DX87, Q14150, Q8N591, Q9NYH2, Q9Y4F6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: August 22, 2003
Last modified: October 29, 2014
This is version 140 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 2
    Human chromosome 2: 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