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Q9UKI8 (TLK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase tousled-like 1

EC=2.7.11.1
Alternative name(s):
PKU-beta
Tousled-like kinase 1
Gene names
Name:TLK1
Synonyms:KIAA0137
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length766 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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'. Ref.1 Ref.2 Ref.3 Ref.9 Ref.10 Ref.11

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.1 Ref.2 Ref.3

Cofactor

Magnesium. Ref.1 Ref.2 Ref.3

Enzyme regulation

Cell-cycle regulated, maximal activity in S-phase. Inactivated by phosphorylation at Ser-743, potentially by CHEK1. Ref.2 Ref.11

Subunit structure

Heterodimerizes with TLK2. Interacts with ASF1A and ASF1B. Ref.2 Ref.9

Subcellular location

Nucleus Ref.1 Ref.2 Ref.3 Ref.10.

Tissue specificity

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. Ref.1 Ref.3

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Sequence caution

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

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

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.2 (identifier: Q9UKI8-1)

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.
Isoform 2 Ref.1 (identifier: Q9UKI8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     136-136: G → GFPNLPVFQSLAYWEMGRTAGG
Isoform 3 Ref.3 (identifier: Q9UKI8-3)

Also known as: SNAK; TLK1B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-217: Missing.
Isoform 4 (identifier: Q9UKI8-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MSVQSSSGSLEGPP → MAVLFLYDLKTTGK
     15-110: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q9UKI8-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 766766Serine/threonine-protein kinase tousled-like 1
PRO_0000086752

Regions

Domain456 – 734279Protein kinase
Nucleotide binding462 – 4709ATP By similarity UniProtKB O96017
Coiled coil230 – 28152 Potential
Coiled coil397 – 44549 Potential

Sites

Active site5861Proton acceptor Ref.2
Binding site4851ATP By similarity UniProtKB O96017

Amino acid modifications

Modified residue1591Phosphoserine Ref.14 Ref.15
Modified residue7431Phosphoserine Ref.11

Natural variations

Alternative sequence1 – 217217Missing in isoform 3. Ref.3
VSP_050570
Alternative sequence1 – 4848Missing in isoform 5.
VSP_043504
Alternative sequence1 – 1414MSVQS…LEGPP → MAVLFLYDLKTTGK in isoform 4.
VSP_043505
Alternative sequence15 – 11096Missing in isoform 4.
VSP_043506
Alternative sequence1361G → GFPNLPVFQSLAYWEMGRTA GG in isoform 2. Ref.1
VSP_050571
Natural variant1211R → C. Ref.18
VAR_041215

Experimental info

Mutagenesis6071D → A: Loss of kinase activity. Ref.2 Ref.9
Mutagenesis7431S → A: Loss of kinase inhibition in response to DNA damage. Ref.11
Mutagenesis7431S → D: Loss of kinase inhibition in response to DNA damage. Ref.11
Mutagenesis7431S → E: Loss of kinase inhibition in response to DNA damage. Ref.11
Sequence conflict881S → T in AAF03094. Ref.2
Sequence conflict1021G → E in BAA20562. Ref.1
Sequence conflict2301Q → L in BAA20562. Ref.1
Sequence conflict2611E → D in BAA20562. Ref.1
Sequence conflict4161E → G in BAA20562. Ref.1
Sequence conflict4391N → H in BAA20562. Ref.1
Sequence conflict4711Y → D in BAA20562. Ref.1
Sequence conflict4771Y → S in BAA20562. Ref.1
Sequence conflict6251D → V in BAA20562. Ref.1
Sequence conflict6651F → Y in BAA20562. Ref.1
Sequence conflict7301N → C in BAA20562. Ref.1

Sequences

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

Last modified August 22, 2003. Version 2.
Checksum: A65AE0A2A7C7FF2F

FASTA76686,700
        10         20         30         40         50         60 
MSVQSSSGSL EGPPSWSQLS TSPTPGSAAA ARSLLNHTPP SGRPREGAMD ELHSLDPRRQ 

        70         80         90        100        110        120 
ELLEARFTGV ASGSTGSTGS CSVGAKASTN NESSNHSFGS LGSLSDKESE TPEKKQSESS 

       130        140        150        160        170        180 
RGRKRKAENQ NESSQGKSIG GRGHKISDYF EYQGGNGSSP VRGIPPAIRS PQNSHSHSTP 

       190        200        210        220        230        240 
SSSVRPNSPS PTALAFGDHP IVQPKQLSFK IIQTDLTMLK LAALESNKIQ DLEKKEGRID 

       250        260        270        280        290        300 
DLLRANCDLR RQIDEQQKLL EKYKERLNKC ISMSKKLLIE KSTQEKLSSR EKSMQDRLRL 

       310        320        330        340        350        360 
GHFTTVRHGA SFTEQWTDGF AFQNLVKQQE WVNQQREDIE RQRKLLAKRK PPTANNSQAP 

       370        380        390        400        410        420 
STNSEPKQRK NKAVNGAEND PFVRPNLPQL LTLAEYHEQE EIFKLRLGHL KKEEAEIQAE 

       430        440        450        460        470        480 
LERLERVRNL HIRELKRINN EDNSQFKDHP TLNERYLLLH LLGRGGFSEV YKAFDLYEQR 

       490        500        510        520        530        540 
YAAVKIHQLN KSWRDEKKEN YHKHACREYR IHKELDHPRI VKLYDYFSLD TDTFCTVLEY 

       550        560        570        580        590        600 
CEGNDLDFYL KQHKLMSEKE ARSIVMQIVN ALRYLNEIKP PIIHYDLKPG NILLVDGTAC 

       610        620        630        640        650        660 
GEIKITDFGL SKIMDDDSYG VDGMDLTSQG AGTYWYLPPE CFVVGKEPPK ISNKVDVWSV 

       670        680        690        700        710        720 
GVIFFQCLYG RKPFGHNQSQ QDILQENTIL KATEVQFPVK PVVSSEAKAF IRRCLAYRKE 

       730        740        750        760 
DRFDVHQLAN DPYLLPHMRR SNSSGNLHMA GLTASPTPPS SSIITY 

« Hide

Isoform 2 [UniParc].

Checksum: 87275865796F5A54
Show »

FASTA78789,023
Isoform 3 (SNAK) (TLK1B) [UniParc].

Checksum: ED6FBF1F77E7E90F
Show »

FASTA54963,994
Isoform 4 [UniParc].

Checksum: BFA0D9CF3CEFB7C1
Show »

FASTA67077,110
Isoform 5 [UniParc].

Checksum: 73E77AF8D34C531D
Show »

FASTA71881,927

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 2), 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 1), FUNCTION, MUTAGENESIS OF ASP-607, SUBCELLULAR LOCATION, INTERACTION WITH TLK2, ENZYME REGULATION.
Tissue: Placenta.
[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: Placenta.
[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 marrow.
[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. expand/collapse author list , 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. expand/collapse author list , 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: Uterus.
[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]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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: 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]"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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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. 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: VARIANT [LARGE SCALE ANALYSIS] CYS-121.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2241.1. [Q9UKI8-1]
CCDS46447.1. [Q9UKI8-5]
CCDS46448.1. [Q9UKI8-4]
RefSeqNP_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]
UniGeneHs.744917.

3D structure databases

ProteinModelPortalQ9UKI8.
SMRQ9UKI8. Positions 427-764.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115206. 15 interactions.
IntActQ9UKI8. 7 interactions.
MINTMINT-112025.
STRING9606.ENSP00000411099.

Chemistry

BindingDBQ9UKI8.
ChEMBLCHEMBL5388.
GuidetoPHARMACOLOGY2242.

Polymorphism databases

DMDM34223086.

Proteomic databases

MaxQBQ9UKI8.
PaxDbQ9UKI8.
PRIDEQ9UKI8.

Protocols and materials databases

DNASU9874.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360843; ENSP00000354089; ENSG00000198586. [Q9UKI8-2]
ENST00000431350; ENSP00000411099; ENSG00000198586. [Q9UKI8-1]
ENST00000434911; ENSP00000409222; ENSG00000198586. [Q9UKI8-4]
ENST00000442919; ENSP00000402165; ENSG00000198586. [Q9UKI8-5]
ENST00000521943; ENSP00000428113; ENSG00000198586. [Q9UKI8-5]
GeneID9874.
KEGGhsa:9874.
UCSCuc002ugn.2. human. [Q9UKI8-1]
uc002ugo.2. human. [Q9UKI8-2]
uc010zdn.1. human. [Q9UKI8-4]

Organism-specific databases

CTD9874.
GeneCardsGC02M171812.
HGNCHGNC:11841. TLK1.
HPAHPA016043.
MIM608438. gene.
neXtProtNX_Q9UKI8.
PharmGKBPA36543.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000259522.
HOVERGENHBG007938.
KOK08864.
OMADVQFPVK.
OrthoDBEOG78H3SF.
PhylomeDBQ9UKI8.
TreeFamTF315233.

Enzyme and pathway databases

SignaLinkQ9UKI8.

Gene expression databases

ArrayExpressQ9UKI8.
BgeeQ9UKI8.
CleanExHS_TLK1.
GenevestigatorQ9UKI8.

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.
[Graphical view]
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

ChiTaRSTLK1. human.
GeneWikiTLK1.
GenomeRNAi9874.
NextBio37219.
PROQ9UKI8.
SOURCESearch...

Entry information

Entry nameTLK1_HUMAN
AccessionPrimary (citable) accession number: Q9UKI8
Secondary accession number(s): B3KR15 expand/collapse secondary AC list , B4DX87, Q14150, Q8N591, Q9NYH2, Q9Y4F6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: August 22, 2003
Last modified: July 9, 2014
This is version 138 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 2

Human chromosome 2: entries, gene names and cross-references to MIM