Q9UKI8 (TLK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	766 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cell cycle DNA damage
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chromatin regulator Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW intracellular protein transport Inferred from direct assay Ref.3. Source: UniProtKB intracellular signal transduction Inferred from direct assay Ref.11. Source: UniProtKB regulation of chromatin assembly or disassembly Inferred from direct assay Ref.11. Source: UniProtKB response to DNA damage stimulus Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from direct assay Ref.2. Source: UniProtKB
Molecular_function	ATP binding Inferred from direct assay Ref.11. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.11. Source: UniProtKB
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 766	766	Serine/threonine-protein kinase tousled-like 1		PRO_0000086752
Regions
	Domain	456 – 734	279	Protein kinase
	Nucleotide binding	462 – 470	9	ATP By similarity UniProtKB O96017
	Coiled coil	230 – 281	52	Potential
	Coiled coil	397 – 445	49	Potential
Sites
	Active site	586	1	Proton acceptor Ref.2
	Binding site	485	1	ATP By similarity UniProtKB O96017
Amino acid modifications
	Modified residue	159	1	Phosphoserine Ref.14 Ref.15
	Modified residue	743	1	Phosphoserine Ref.11
Natural variations
	Alternative sequence	1 – 217	217	Missing in isoform 3. Ref.3		VSP_050570
	Alternative sequence	1 – 48	48	Missing in isoform 5.		VSP_043504
	Alternative sequence	1 – 14	14	MSVQS…LEGPP → MAVLFLYDLKTTGK in isoform 4.		VSP_043505
	Alternative sequence	15 – 110	96	Missing in isoform 4.		VSP_043506
	Alternative sequence	136	1	G → GFPNLPVFQSLAYWEMGRTA GG in isoform 2. Ref.1		VSP_050571
	Natural variant	121	1	R → C. Ref.17		VAR_041215
Experimental info
	Mutagenesis	607	1	D → A: Loss of kinase activity. Ref.2 Ref.9
	Mutagenesis	743	1	S → A: Loss of kinase inhibition in response to DNA damage. Ref.11
	Mutagenesis	743	1	S → D: Loss of kinase inhibition in response to DNA damage. Ref.11
	Mutagenesis	743	1	S → E: Loss of kinase inhibition in response to DNA damage. Ref.11
	Sequence conflict	88	1	S → T in AAF03094. Ref.2
	Sequence conflict	102	1	G → E in BAA20562. Ref.1
	Sequence conflict	230	1	Q → L in BAA20562. Ref.1
	Sequence conflict	261	1	E → D in BAA20562. Ref.1
	Sequence conflict	416	1	E → G in BAA20562. Ref.1
	Sequence conflict	439	1	N → H in BAA20562. Ref.1
	Sequence conflict	471	1	Y → D in BAA20562. Ref.1
	Sequence conflict	477	1	Y → S in BAA20562. Ref.1
	Sequence conflict	625	1	D → V in BAA20562. Ref.1
	Sequence conflict	665	1	F → Y in BAA20562. Ref.1
	Sequence conflict	730	1	N → C in BAA20562. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 22, 2003. Version 2. Checksum: A65AE0A2A7C7FF2F	FASTA	766	86,700
	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
	Isoform 2 [UniParc]. Checksum: 87275865796F5A54	FASTA	787	89,023
	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 NESSQGFPNL PVFQSLAYWE MGRTAGGKSI GGRGHKISDY FEYQGGNGSS 190 200 210 220 230 240 PVRGIPPAIR SPQNSHSHST PSSSVRPNSP SPTALAFGDH PIVQPKQLSF KIIQTDLTML 250 260 270 280 290 300 KLAALESNKI QDLEKKEGRI DDLLRANCDL RRQIDEQQKL LEKYKERLNK CISMSKKLLI 310 320 330 340 350 360 EKSTQEKLSS REKSMQDRLR LGHFTTVRHG ASFTEQWTDG FAFQNLVKQQ EWVNQQREDI 370 380 390 400 410 420 ERQRKLLAKR KPPTANNSQA PSTNSEPKQR KNKAVNGAEN DPFVRPNLPQ LLTLAEYHEQ 430 440 450 460 470 480 EEIFKLRLGH LKKEEAEIQA ELERLERVRN LHIRELKRIN NEDNSQFKDH PTLNERYLLL 490 500 510 520 530 540 HLLGRGGFSE VYKAFDLYEQ RYAAVKIHQL NKSWRDEKKE NYHKHACREY RIHKELDHPR 550 560 570 580 590 600 IVKLYDYFSL DTDTFCTVLE YCEGNDLDFY LKQHKLMSEK EARSIVMQIV NALRYLNEIK 610 620 630 640 650 660 PPIIHYDLKP GNILLVDGTA CGEIKITDFG LSKIMDDDSY GVDGMDLTSQ GAGTYWYLPP 670 680 690 700 710 720 ECFVVGKEPP KISNKVDVWS VGVIFFQCLY GRKPFGHNQS QQDILQENTI LKATEVQFPV 730 740 750 760 770 780 KPVVSSEAKA FIRRCLAYRK EDRFDVHQLA NDPYLLPHMR RSNSSGNLHM AGLTASPTPP SSSIITY
	Isoform 3 (SNAK) (TLK1B) [UniParc]. Checksum: ED6FBF1F77E7E90F	FASTA	549	63,994
	10 20 30 40 50 60 MLKLAALESN KIQDLEKKEG RIDDLLRANC DLRRQIDEQQ KLLEKYKERL NKCISMSKKL 70 80 90 100 110 120 LIEKSTQEKL SSREKSMQDR LRLGHFTTVR HGASFTEQWT DGFAFQNLVK QQEWVNQQRE 130 140 150 160 170 180 DIERQRKLLA KRKPPTANNS QAPSTNSEPK QRKNKAVNGA ENDPFVRPNL PQLLTLAEYH 190 200 210 220 230 240 EQEEIFKLRL GHLKKEEAEI QAELERLERV RNLHIRELKR INNEDNSQFK DHPTLNERYL 250 260 270 280 290 300 LLHLLGRGGF SEVYKAFDLY EQRYAAVKIH QLNKSWRDEK KENYHKHACR EYRIHKELDH 310 320 330 340 350 360 PRIVKLYDYF SLDTDTFCTV LEYCEGNDLD FYLKQHKLMS EKEARSIVMQ IVNALRYLNE 370 380 390 400 410 420 IKPPIIHYDL KPGNILLVDG TACGEIKITD FGLSKIMDDD SYGVDGMDLT SQGAGTYWYL 430 440 450 460 470 480 PPECFVVGKE PPKISNKVDV WSVGVIFFQC LYGRKPFGHN QSQQDILQEN TILKATEVQF 490 500 510 520 530 540 PVKPVVSSEA KAFIRRCLAY RKEDRFDVHQ LANDPYLLPH MRRSNSSGNL HMAGLTASPT PPSSSIITY
	Isoform 4 [UniParc]. Checksum: BFA0D9CF3CEFB7C1	FASTA	670	77,110
	10 20 30 40 50 60 MAVLFLYDLK TTGKTPEKKQ SESSRGRKRK AENQNESSQG KSIGGRGHKI SDYFEYQGGN 70 80 90 100 110 120 GSSPVRGIPP AIRSPQNSHS HSTPSSSVRP NSPSPTALAF GDHPIVQPKQ LSFKIIQTDL 130 140 150 160 170 180 TMLKLAALES NKIQDLEKKE GRIDDLLRAN CDLRRQIDEQ QKLLEKYKER LNKCISMSKK 190 200 210 220 230 240 LLIEKSTQEK LSSREKSMQD RLRLGHFTTV RHGASFTEQW TDGFAFQNLV KQQEWVNQQR 250 260 270 280 290 300 EDIERQRKLL AKRKPPTANN SQAPSTNSEP KQRKNKAVNG AENDPFVRPN LPQLLTLAEY 310 320 330 340 350 360 HEQEEIFKLR LGHLKKEEAE IQAELERLER VRNLHIRELK RINNEDNSQF KDHPTLNERY 370 380 390 400 410 420 LLLHLLGRGG FSEVYKAFDL YEQRYAAVKI HQLNKSWRDE KKENYHKHAC REYRIHKELD 430 440 450 460 470 480 HPRIVKLYDY FSLDTDTFCT VLEYCEGNDL DFYLKQHKLM SEKEARSIVM QIVNALRYLN 490 500 510 520 530 540 EIKPPIIHYD LKPGNILLVD GTACGEIKIT DFGLSKIMDD DSYGVDGMDL TSQGAGTYWY 550 560 570 580 590 600 LPPECFVVGK EPPKISNKVD VWSVGVIFFQ CLYGRKPFGH NQSQQDILQE NTILKATEVQ 610 620 630 640 650 660 FPVKPVVSSE AKAFIRRCLA YRKEDRFDVH QLANDPYLLP HMRRSNSSGN LHMAGLTASP 670 TPPSSSIITY
	Isoform 5 [UniParc]. Checksum: 73E77AF8D34C531D	FASTA	718	81,927
	10 20 30 40 50 60 MDELHSLDPR RQELLEARFT GVASGSTGST GSCSVGAKAS TNNESSNHSF GSLGSLSDKE 70 80 90 100 110 120 SETPEKKQSE SSRGRKRKAE NQNESSQGKS IGGRGHKISD YFEYQGGNGS SPVRGIPPAI 130 140 150 160 170 180 RSPQNSHSHS TPSSSVRPNS PSPTALAFGD HPIVQPKQLS FKIIQTDLTM LKLAALESNK 190 200 210 220 230 240 IQDLEKKEGR IDDLLRANCD LRRQIDEQQK LLEKYKERLN KCISMSKKLL IEKSTQEKLS 250 260 270 280 290 300 SREKSMQDRL RLGHFTTVRH GASFTEQWTD GFAFQNLVKQ QEWVNQQRED IERQRKLLAK 310 320 330 340 350 360 RKPPTANNSQ APSTNSEPKQ RKNKAVNGAE NDPFVRPNLP QLLTLAEYHE QEEIFKLRLG 370 380 390 400 410 420 HLKKEEAEIQ AELERLERVR NLHIRELKRI NNEDNSQFKD HPTLNERYLL LHLLGRGGFS 430 440 450 460 470 480 EVYKAFDLYE QRYAAVKIHQ LNKSWRDEKK ENYHKHACRE YRIHKELDHP RIVKLYDYFS 490 500 510 520 530 540 LDTDTFCTVL EYCEGNDLDF YLKQHKLMSE KEARSIVMQI VNALRYLNEI KPPIIHYDLK 550 560 570 580 590 600 PGNILLVDGT ACGEIKITDF GLSKIMDDDS YGVDGMDLTS QGAGTYWYLP PECFVVGKEP 610 620 630 640 650 660 PKISNKVDVW SVGVIFFQCL YGRKPFGHNQ SQQDILQENT ILKATEVQFP VKPVVSSEAK 670 680 690 700 710 AFIRRCLAYR KEDRFDVHQL ANDPYLLPHM RRSNSSGNLH MAGLTASPTP PSSSIITY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and chromosomal mapping of genes encoding novel protein kinases termed PKU-alpha and PKU-beta, which have nuclear localization signal." Yamakawa A., Kameoka Y., Hashimoto K., Yoshitake Y., Nishikawa K., Tanihara K., Date T. Gene 202:193-201(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 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. , 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: 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"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.
+	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.
IPI	IPI00333559. IPI00339361. IPI00746072.
RefSeq	NP_001130026.1. NM_001136554.1. NP_001130027.1. NM_001136555.1. NP_036422.3. NM_012290.4.
UniGene	Hs.731668.
3D structure databases
ProteinModelPortal	Q9UKI8.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UKI8. 7 interactions.
MINT	MINT-112025.
STRING	9606.ENSP00000411099.
Polymorphism databases
DMDM	34223086.
Proteomic databases
PaxDb	Q9UKI8.
PRIDE	Q9UKI8.
Protocols and materials databases
DNASU	9874.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000360843; ENSP00000354089; ENSG00000198586. ENST00000431350; ENSP00000411099; ENSG00000198586. ENST00000434911; ENSP00000409222; ENSG00000198586. ENST00000442919; ENSP00000402165; ENSG00000198586. ENST00000521943; ENSP00000428113; ENSG00000198586.
GeneID	9874.
KEGG	hsa:9874.
UCSC	uc002ugn.2. human. uc002ugo.2. human.
Organism-specific databases
CTD	9874.
GeneCards	GC02M171812.
HGNC	HGNC:11841. TLK1.
HPA	HPA016043.
MIM	608438. gene.
neXtProt	NX_Q9UKI8.
PharmGKB	PA36543.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000259522.
HOVERGEN	HBG007938.
KO	K08864.
OMA	ANSEPKQ.
OrthoDB	EOG4T1HKZ.
Gene expression databases
ArrayExpress	Q9UKI8.
Bgee	Q9UKI8.
CleanEx	HS_TLK1.
Genevestigator	Q9UKI8.
GermOnline	ENSG00000198586. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. IPR027086. TLK. [Graphical view]
PANTHER	PTHR22974:SF1. PTHR22974:SF1. 1 hit.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9UKI8.
ChEMBL	CHEMBL5388.
ChiTaRS	TLK1. human.
GenomeRNAi	9874.
NextBio	37219.
SOURCE	Search...

Entry information

Entry name

TLK1_HUMAN

Accession

Primary (citable) accession number: Q9UKI8
Secondary accession number(s): B3KR15 , B4DX87, Q14150, Q8N591, Q9NYH2, Q9Y4F6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 22, 2003
Last sequence update:	August 22, 2003
Last modified:	May 1, 2013
This is version 125 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.