Q6IQ55 (TTBK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tau-tubulin kinase 2
EC=2.7.11.1

Gene names

Name:	TTBK2
Synonyms:	KIAA0847

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	1244 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine kinase that acts as a key regulator of ciliogenesis: controls the initiation of ciliogenesis by binding to the distal end of the basal body and promoting the removal of CCP110, which caps the mother centriole, leading to the recruitment of IFT proteins, which build the ciliary axoneme. Has some substrate preference for proteins that are already phosphorylated on a Tyr residue at the +2 position relative to the phosphorylation site. Able to phosphorylate tau on serines in vitro. Ref.6 Ref.9
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.6
Subunit structure	Interacts with CEP164. Ref.8
Subcellular location	Cell projection › cilium By similarity. Cytoplasm › cytoskeleton › cilium basal body By similarity. Cytoplasm › cytoskeleton › centrosome › centriole. Cytoplasm › cytosol. Nucleus. Note: Localizes to the transition zone in primary cilia in response to cell cycle signals that promote ciliogenesis By similarity. May also be present in cytosol and, at lower level in the nucleus. Ref.6 Ref.9
Involvement in disease	Spinocerebellar ataxia 11 (SCA11) [MIM:604432]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA11 is an autosomal dominant cerebellar ataxia (ADCA).It is a relatively benign, late-onset, slowly progressive neurologic disorder. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5
Sequence similarities	Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Contains 1 protein kinase domain.
Biophysicochemical properties	Kinetic parameters: KM=18 µM for RRKDLHDDEEDEAMSIYpA peptide Ref.6 KM=141 µM for RRKDLHDDEEDEAMSIYA peptide Vmax=76 µmol/min/mg enzyme with RRKDLHDDEEDEAMSIYpA peptide as substrate Vmax=66 µmol/min/mg enzyme with RRKDLHDDEEDEAMSIYA peptide as substrate

Ontologies

Keywords
Biological process	Cilium biogenesis/degradation
Cellular component	Cell projection Cilium Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Neurodegeneration Spinocerebellar ataxia
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell death Inferred from electronic annotation. Source: UniProtKB-KW cilium assembly Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-serine phosphorylation Inferred from direct assay Ref.6. Source: UniProtKB smoothened signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	centriole Inferred from electronic annotation. Source: UniProtKB-SubCell ciliary transition zone Inferred from sequence or structural similarity. Source: UniProtKB cilium basal body Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from direct assay Ref.6. Source: UniProtKB nucleus Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CEP164	Q9UPV0	4	EBI-1050303,EBI-3937015

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q6IQ55-1)

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 (identifier: Q6IQ55-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: MSGGGEQLDILSVGILVKERWKVLRKIGGGGFGEIYDALDMLTRENVALKVESAQQPKQVLKMEVAVLKKLQ → MES
     1233-1244: QGKSKPASKLSR → PREE

Note: No experimental confirmation available.

Isoform 3 (identifier: Q6IQ55-3)

The sequence of this isoform differs from the canonical sequence as follows:
     470-478: CLEKMQKDT → WYKIVYFSF
     479-1244: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1244	1244	Tau-tubulin kinase 2		PRO_0000234342
Regions
	Domain	21 – 284	264	Protein kinase
	Nucleotide binding	27 – 35	9	ATP By similarity
	Compositional bias	307 – 314	8	Poly-Thr
	Compositional bias	1150 – 1203	54	Ser-rich
Sites
	Active site	141	1	Proton acceptor By similarity
	Binding site	50	1	ATP By similarity
Amino acid modifications
	Modified residue	786	1	Phosphoserine Ref.7
Natural variations
	Alternative sequence	1 – 72	72	MSGGG…LKKLQ → MES in isoform 2.		VSP_018272
	Alternative sequence	470 – 478	9	CLEKMQKDT → WYKIVYFSF in isoform 3.		VSP_018273
	Alternative sequence	479 – 1244	766	Missing in isoform 3.		VSP_018274
	Alternative sequence	1233 – 1244	12	QGKSK…SKLSR → PREE in isoform 2.		VSP_018275
	Natural variant	8	1	L → P. Ref.3 Ref.10 Ref.11 Corresponds to variant rs6493068 [ dbSNP | Ensembl ].		VAR_041261
	Natural variant	120	1	R → Q. Ref.10 Corresponds to variant rs35328266 [ dbSNP | Ensembl ].		VAR_041262
	Natural variant	313	1	T → A. Ref.10 Corresponds to variant rs56017612 [ dbSNP | Ensembl ].		VAR_041263
	Natural variant	440	1	V → M. Ref.10 Corresponds to variant rs56311523 [ dbSNP | Ensembl ].		VAR_041264
	Natural variant	500	1	R → P. Ref.10 Corresponds to variant rs56039839 [ dbSNP | Ensembl ].		VAR_041265
	Natural variant	635	1	D → G in a lung small cell carcinoma sample; somatic mutation. Ref.10		VAR_041266
	Natural variant	842	1	E → G Found in a patient with SCA11; unknown pathological significance. Ref.11 Corresponds to variant rs202004988 [ dbSNP | Ensembl ].		VAR_069052
	Natural variant	1062	1	T → I. Ref.10 Corresponds to variant rs55833708 [ dbSNP | Ensembl ].		VAR_041267
	Natural variant	1084	1	T → M. Ref.10 Corresponds to variant rs34348991 [ dbSNP | Ensembl ].		VAR_041268
	Natural variant	1097	1	V → A. Ref.10 Corresponds to variant rs55796513 [ dbSNP | Ensembl ].		VAR_041269
	Natural variant	1110	1	R → H Found in a patient with SCA11; unknown pathological significance. Ref.11		VAR_069053
	Natural variant	1122	1	P → R. Ref.10 Corresponds to variant rs56142516 [ dbSNP | Ensembl ].		VAR_041270
	Natural variant	1241	1	K → T. Ref.10 Corresponds to variant rs36104367 [ dbSNP | Ensembl ].		VAR_041271
Experimental info
	Mutagenesis	50	1	K → E or A: Leads to inactivation/destabilization of the protein. Ref.6
	Mutagenesis	143	1	K → E or A: Leads to inactivation/destabilization of the protein. Ref.6
	Mutagenesis	163	1	D → A: Abolishes serine/threonine-protein kinase activity. Ref.6
	Mutagenesis	181	1	R → E or A: Impaired serine/threonine-protein kinase activity. Ref.6
	Mutagenesis	184	1	A → E or G: Impaired serine/threonine-protein kinase activity. Ref.6
	Sequence conflict	309	1	T → I in BAD18523. Ref.1
	Sequence conflict	456	1	T → A in BAD18523. Ref.1
	Sequence conflict	557	1	K → N in BAD18523. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: EAB8FC28370966DE	FASTA	1,244	137,412
	10 20 30 40 50 60 MSGGGEQLDI LSVGILVKER WKVLRKIGGG GFGEIYDALD MLTRENVALK VESAQQPKQV 70 80 90 100 110 120 LKMEVAVLKK LQGKDHVCRF IGCGRNDRFN YVVMQLQGRN LADLRRSQSR GTFTISTTLR 130 140 150 160 170 180 LGRQILESIE SIHSVGFLHR DIKPSNFAMG RFPSTCRKCY MLDFGLARQF TNSCGDVRPP 190 200 210 220 230 240 RAVAGFRGTV RYASINAHRN REMGRHDDLW SLFYMLVEFV VGQLPWRKIK DKEQVGSIKE 250 260 270 280 290 300 RYDHRLMLKH LPPEFSIFLD HISSLDYFTK PDYQLLTSVF DNSIKTFGVI ESDPFDWEKT 310 320 330 340 350 360 GNDGSLTTTT TSTTPQLHTR LTPAAIGIAN ATPIPGDLLR ENTDEVFPDE QLSDGENGIP 370 380 390 400 410 420 VGVSPDKLPG SLGHPRPQEK DVWEEMDANK NKIKLGICKA ATEEENSHGQ ANGLLNAPSL 430 440 450 460 470 480 GSPIRVRSEI TQPDRDIPLV RKLRSIHSFE LEKRLTLEPK PDTDKFLETC LEKMQKDTSA 490 500 510 520 530 540 GKESILPALL HKPCVPAVSR TDHIWHYDEE YLPDASKPAS ANTPEQADGG GSNGFIAVNL 550 560 570 580 590 600 SSCKQEIDSK EWVIVDKEQD LQDFRTNEAV GHKTTGSPSD EEPEVLQVLE ASPQDEKLQL 610 620 630 640 650 660 GPWAENDHLK KETSGVVLAL SAEGPPTAAS EQYTDRLELQ PGAASQFIAA TPTSLMEAQA 670 680 690 700 710 720 EGPLTAITIP RPSVASTQST SGSFHCGQQP EKKDLQPMEP TVELYSPREN FSGLVVTEGE 730 740 750 760 770 780 PPSGGSRTDL GLQIDHIGHD MLPNIRESNK SQDLGPKELP DHNRLVVREF ENLPGETEEK 790 800 810 820 830 840 SILLESDNED EKLSRGQHCI EISSLPGDLV IVEKDHSATT EPLDVTKTQT FSVVPNQDKN 850 860 870 880 890 900 NEIMKLLTVG TSEISSRDID PHVEGQIGQV AEMQKNKISK DDDIMSEDLP GHQGDLSTFL 910 920 930 940 950 960 HQEGKREKIT PRNGELFHCV SENEHGAPTR KDMVRSSFVT RHSRIPVLAQ EIDSTLESSS 970 980 990 1000 1010 1020 PVSAKEKLLQ KKAYQPDLVK LLVEKRQFKS FLGDLSSASD KLLEEKLATV PAPFCEEEVL 1030 1040 1050 1060 1070 1080 TPFSRLTVDS HLSRSAEDSF LSPIISQSRK SKIPRPVSWV NTDQVNSSTS SQFFPRPPPG 1090 1100 1110 1120 1130 1140 KPPTRPGVEA RLRRYKVLGS SNSDSDLFSR LAQILQNGSQ KPRSTTQCKS PGSPHNPKTP 1150 1160 1170 1180 1190 1200 PKSPVVPRRS PSASPRSSSL PRTSSSSPSR AGRPHHDQRS SSPHLGRSKS PPSHSGSSSS 1210 1220 1230 1240 RRSCQQEHCK PSKNGLKGSG SLHHHSASTK TPQGKSKPAS KLSR
	Isoform 2 [UniParc]. Checksum: 5517B88C9E5E86E9	FASTA	1,167	129,110
	10 20 30 40 50 60 MESGKDHVCR FIGCGRNDRF NYVVMQLQGR NLADLRRSQS RGTFTISTTL RLGRQILESI 70 80 90 100 110 120 ESIHSVGFLH RDIKPSNFAM GRFPSTCRKC YMLDFGLARQ FTNSCGDVRP PRAVAGFRGT 130 140 150 160 170 180 VRYASINAHR NREMGRHDDL WSLFYMLVEF VVGQLPWRKI KDKEQVGSIK ERYDHRLMLK 190 200 210 220 230 240 HLPPEFSIFL DHISSLDYFT KPDYQLLTSV FDNSIKTFGV IESDPFDWEK TGNDGSLTTT 250 260 270 280 290 300 TTSTTPQLHT RLTPAAIGIA NATPIPGDLL RENTDEVFPD EQLSDGENGI PVGVSPDKLP 310 320 330 340 350 360 GSLGHPRPQE KDVWEEMDAN KNKIKLGICK AATEEENSHG QANGLLNAPS LGSPIRVRSE 370 380 390 400 410 420 ITQPDRDIPL VRKLRSIHSF ELEKRLTLEP KPDTDKFLET CLEKMQKDTS AGKESILPAL 430 440 450 460 470 480 LHKPCVPAVS RTDHIWHYDE EYLPDASKPA SANTPEQADG GGSNGFIAVN LSSCKQEIDS 490 500 510 520 530 540 KEWVIVDKEQ DLQDFRTNEA VGHKTTGSPS DEEPEVLQVL EASPQDEKLQ LGPWAENDHL 550 560 570 580 590 600 KKETSGVVLA LSAEGPPTAA SEQYTDRLEL QPGAASQFIA ATPTSLMEAQ AEGPLTAITI 610 620 630 640 650 660 PRPSVASTQS TSGSFHCGQQ PEKKDLQPME PTVELYSPRE NFSGLVVTEG EPPSGGSRTD 670 680 690 700 710 720 LGLQIDHIGH DMLPNIRESN KSQDLGPKEL PDHNRLVVRE FENLPGETEE KSILLESDNE 730 740 750 760 770 780 DEKLSRGQHC IEISSLPGDL VIVEKDHSAT TEPLDVTKTQ TFSVVPNQDK NNEIMKLLTV 790 800 810 820 830 840 GTSEISSRDI DPHVEGQIGQ VAEMQKNKIS KDDDIMSEDL PGHQGDLSTF LHQEGKREKI 850 860 870 880 890 900 TPRNGELFHC VSENEHGAPT RKDMVRSSFV TRHSRIPVLA QEIDSTLESS SPVSAKEKLL 910 920 930 940 950 960 QKKAYQPDLV KLLVEKRQFK SFLGDLSSAS DKLLEEKLAT VPAPFCEEEV LTPFSRLTVD 970 980 990 1000 1010 1020 SHLSRSAEDS FLSPIISQSR KSKIPRPVSW VNTDQVNSST SSQFFPRPPP GKPPTRPGVE 1030 1040 1050 1060 1070 1080 ARLRRYKVLG SSNSDSDLFS RLAQILQNGS QKPRSTTQCK SPGSPHNPKT PPKSPVVPRR 1090 1100 1110 1120 1130 1140 SPSASPRSSS LPRTSSSSPS RAGRPHHDQR SSSPHLGRSK SPPSHSGSSS SRRSCQQEHC 1150 1160 KPSKNGLKGS GSLHHHSAST KTPPREE
	Isoform 3 [UniParc]. Checksum: 2F3AF5039B6F021A	FASTA	478	54,037
	10 20 30 40 50 60 MSGGGEQLDI LSVGILVKER WKVLRKIGGG GFGEIYDALD MLTRENVALK VESAQQPKQV 70 80 90 100 110 120 LKMEVAVLKK LQGKDHVCRF IGCGRNDRFN YVVMQLQGRN LADLRRSQSR GTFTISTTLR 130 140 150 160 170 180 LGRQILESIE SIHSVGFLHR DIKPSNFAMG RFPSTCRKCY MLDFGLARQF TNSCGDVRPP 190 200 210 220 230 240 RAVAGFRGTV RYASINAHRN REMGRHDDLW SLFYMLVEFV VGQLPWRKIK DKEQVGSIKE 250 260 270 280 290 300 RYDHRLMLKH LPPEFSIFLD HISSLDYFTK PDYQLLTSVF DNSIKTFGVI ESDPFDWEKT 310 320 330 340 350 360 GNDGSLTTTT TSTTPQLHTR LTPAAIGIAN ATPIPGDLLR ENTDEVFPDE QLSDGENGIP 370 380 390 400 410 420 VGVSPDKLPG SLGHPRPQEK DVWEEMDANK NKIKLGICKA ATEEENSHGQ ANGLLNAPSL 430 440 450 460 470 GSPIRVRSEI TQPDRDIPLV RKLRSIHSFE LEKRLTLEPK PDTDKFLETW YKIVYFSF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] (ISOFORM 2). Tissue: Cerebellum.
[2]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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] (ISOFORMS 1 AND 3), VARIANT PRO-8. Tissue: Testis.
[4]	"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 600-1244 (ISOFORM 1). Tissue: Brain.
[5]	"Mutations in TTBK2, encoding a kinase implicated in tau phosphorylation, segregate with spinocerebellar ataxia type 11." Houlden H., Johnson J., Gardner-Thorpe C., Lashley T., Hernandez D., Worth P., Singleton A.B., Hilton D.A., Holton J., Revesz T., Davis M.B., Giunti P., Wood N.W. Nat. Genet. 39:1434-1436(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SCA11.
[6]	"TTBK2 kinase substrate specificity and the impact of spinocerebellar-ataxia-causing mutations on expression, activity, localization and development." Bouskila M., Esoof N., Gay L., Fang E.H., Deak M., Begley M.J., Cantley L.C., Prescott A., Storey K.G., Alessi D.R. Biochem. J. 437:157-167(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-50; LYS-143; ASP-163; ARG-181 AND ALA-184.
[7]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-786, MASS SPECTROMETRY.
[8]	"Exome capture reveals ZNF423 and CEP164 mutations, linking renal ciliopathies to DNA damage response signaling." Chaki M., Airik R., Ghosh A.K., Giles R.H., Chen R., Slaats G.G., Wang H., Hurd T.W., Zhou W., Cluckey A., Gee H.Y., Ramaswami G., Hong C.J., Hamilton B.A., Cervenka I., Ganji R.S., Bryja V., Arts H.H. , van Reeuwijk J., Oud M.M., Letteboer S.J., Roepman R., Husson H., Ibraghimov-Beskrovnaya O., Yasunaga T., Walz G., Eley L., Sayer J.A., Schermer B., Liebau M.C., Benzing T., Le Corre S., Drummond I., Janssen S., Allen S.J., Natarajan S., O'Toole J.F., Attanasio M., Saunier S., Antignac C., Koenekoop R.K., Ren H., Lopez I., Nayir A., Stoetzel C., Dollfus H., Massoudi R., Gleeson J.G., Andreoli S.P., Doherty D.G., Lindstrad A., Golzio C., Katsanis N., Pape L., Abboud E.B., Al-Rajhi A.A., Lewis R.A., Omran H., Lee E.Y., Wang S., Sekiguchi J.M., Saunders R., Johnson C.A., Garner E., Vanselow K., Andersen J.S., Shlomai J., Nurnberg G., Nurnberg P., Levy S., Smogorzewska A., Otto E.A., Hildebrandt F. Cell 150:533-548(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CEP164.
[9]	"The spinocerebellar ataxia-associated gene tau tubulin kinase 2 controls the initiation of ciliogenesis." Goetz S.C., Liem K.F. Jr., Anderson K.V. Cell 151:847-858(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]	"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] PRO-8; GLN-120; ALA-313; MET-440; PRO-500; GLY-635; ILE-1062; MET-1084; ALA-1097; ARG-1122 AND THR-1241.
[11]	"Missense exchanges in the TTBK2 gene mutated in SCA11." Edener U., Kurth I., Meiner A., Hoffmann F., Hubner C.A., Bernard V., Gillessen-Kaesbach G., Zuhlke C. J. Neurol. 256:1856-1859(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PRO-8; GLY-842 AND HIS-1110.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK131372 mRNA. Translation: BAD18523.1. AC068727 Genomic DNA. No translation available. AC090510 Genomic DNA. No translation available. BC041876 mRNA. Translation: AAH41876.1. BC071556 mRNA. Translation: AAH71556.1. AB020654 mRNA. Translation: BAA74870.1.
IPI	IPI00217145. IPI00743279. IPI00743694.
RefSeq	NP_775771.3. NM_173500.3.
UniGene	Hs.646511. Hs.727864.
3D structure databases
ProteinModelPortal	Q6IQ55.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6IQ55. 3 interactions.
STRING	9606.ENSP00000267890.
PTM databases
PhosphoSite	Q6IQ55.
Polymorphism databases
DMDM	116242833.
Proteomic databases
PaxDb	Q6IQ55.
PRIDE	Q6IQ55.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000267890; ENSP00000267890; ENSG00000128881. ENST00000567840; ENSP00000455734; ENSG00000128881.
GeneID	146057.
KEGG	hsa:146057.
UCSC	uc001zqo.2. human. uc001zqp.3. human.
Organism-specific databases
CTD	146057.
GeneCards	GC15M043030.
H-InvDB	HIX0012177.
HGNC	HGNC:19141. TTBK2.
HPA	HPA018113.
MIM	604432. phenotype. 611695. gene.
neXtProt	NX_Q6IQ55.
Orphanet	98767. Spinocerebellar ataxia type 11.
PharmGKB	PA134913925.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000232043.
HOVERGEN	HBG061812.
KO	K08815.
Gene expression databases
ArrayExpress	Q6IQ55.
Bgee	Q6IQ55.
CleanEx	HS_TTBK2.
Genevestigator	Q6IQ55.
GermOnline	ENSG00000128881. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. [Graphical view]
Pfam	PF00069. Pkinase. 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. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	146057.
NextBio	85251.
SOURCE	Search...

Entry information

Entry name

TTBK2_HUMAN

Accession

Primary (citable) accession number: Q6IQ55
Secondary accession number(s): O94932, Q6ZN52, Q8IVV1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 100 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.