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Q6IQ55 (TTBK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tau-tubulin kinase 2

EC=2.7.11.1
Gene names
Name:TTBK2
Synonyms:KIAA0847
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1244 AA.
Sequence statusComplete.
Protein existenceEvidence 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 projectioncilium By similarity. Cytoplasmcytoskeletoncilium basal body By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. Cytoplasmcytosol. 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 processCilium biogenesis/degradation
   Cellular componentCell projection
Cilium
Cytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseNeurodegeneration
Spinocerebellar ataxia
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell 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_componentcentriole

Inferred from electronic annotation. Source: UniProtKB-SubCell

ciliary basal body

Inferred from sequence or structural similarity. Source: UniProtKB

ciliary transition zone

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay Ref.6. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CEP164Q9UPV04EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12441244Tau-tubulin kinase 2
PRO_0000234342

Regions

Domain21 – 284264Protein kinase
Nucleotide binding27 – 359ATP By similarity
Compositional bias307 – 3148Poly-Thr
Compositional bias1150 – 120354Ser-rich

Sites

Active site1411Proton acceptor By similarity
Binding site501ATP By similarity

Amino acid modifications

Modified residue7861Phosphoserine Ref.7

Natural variations

Alternative sequence1 – 7272MSGGG…LKKLQ → MES in isoform 2.
VSP_018272
Alternative sequence470 – 4789CLEKMQKDT → WYKIVYFSF in isoform 3.
VSP_018273
Alternative sequence479 – 1244766Missing in isoform 3.
VSP_018274
Alternative sequence1233 – 124412QGKSK…SKLSR → PREE in isoform 2.
VSP_018275
Natural variant81L → P. Ref.3 Ref.10 Ref.11
Corresponds to variant rs6493068 [ dbSNP | Ensembl ].
VAR_041261
Natural variant1201R → Q. Ref.10
Corresponds to variant rs35328266 [ dbSNP | Ensembl ].
VAR_041262
Natural variant3131T → A. Ref.10
Corresponds to variant rs56017612 [ dbSNP | Ensembl ].
VAR_041263
Natural variant4401V → M. Ref.10
Corresponds to variant rs56311523 [ dbSNP | Ensembl ].
VAR_041264
Natural variant5001R → P. Ref.10
Corresponds to variant rs56039839 [ dbSNP | Ensembl ].
VAR_041265
Natural variant6351D → G in a lung small cell carcinoma sample; somatic mutation. Ref.10
VAR_041266
Natural variant8421E → G Found in a patient with SCA11; unknown pathological significance. Ref.11
Corresponds to variant rs202004988 [ dbSNP | Ensembl ].
VAR_069052
Natural variant10621T → I. Ref.10
Corresponds to variant rs55833708 [ dbSNP | Ensembl ].
VAR_041267
Natural variant10841T → M. Ref.10
Corresponds to variant rs34348991 [ dbSNP | Ensembl ].
VAR_041268
Natural variant10971V → A. Ref.10
Corresponds to variant rs55796513 [ dbSNP | Ensembl ].
VAR_041269
Natural variant11101R → H Found in a patient with SCA11; unknown pathological significance. Ref.11
VAR_069053
Natural variant11221P → R. Ref.10
Corresponds to variant rs56142516 [ dbSNP | Ensembl ].
VAR_041270
Natural variant12411K → T. Ref.10
Corresponds to variant rs36104367 [ dbSNP | Ensembl ].
VAR_041271

Experimental info

Mutagenesis501K → E or A: Leads to inactivation/destabilization of the protein. Ref.6
Mutagenesis1431K → E or A: Leads to inactivation/destabilization of the protein. Ref.6
Mutagenesis1631D → A: Abolishes serine/threonine-protein kinase activity. Ref.6
Mutagenesis1811R → E or A: Impaired serine/threonine-protein kinase activity. Ref.6
Mutagenesis1841A → E or G: Impaired serine/threonine-protein kinase activity. Ref.6
Sequence conflict3091T → I in BAD18523. Ref.1
Sequence conflict4561T → A in BAD18523. Ref.1
Sequence conflict5571K → N in BAD18523. Ref.1

Sequences

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

Last modified October 17, 2006. Version 2.
Checksum: EAB8FC28370966DE

FASTA1,244137,412
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 5517B88C9E5E86E9
Show »

FASTA1,167129,110
Isoform 3 [UniParc].

Checksum: 2F3AF5039B6F021A
Show »

FASTA47854,037

References

« Hide '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. 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] (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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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. expand/collapse author list , 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. 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: 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.

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.
CCDSCCDS42029.1. [Q6IQ55-1]
RefSeqNP_775771.3. NM_173500.3. [Q6IQ55-1]
UniGeneHs.646511.
Hs.727864.
Hs.733489.

3D structure databases

ProteinModelPortalQ6IQ55.
SMRQ6IQ55. Positions 9-301.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126962. 8 interactions.
IntActQ6IQ55. 3 interactions.
STRING9606.ENSP00000267890.

PTM databases

PhosphoSiteQ6IQ55.

Polymorphism databases

DMDM116242833.

Proteomic databases

MaxQBQ6IQ55.
PaxDbQ6IQ55.
PRIDEQ6IQ55.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000267890; ENSP00000267890; ENSG00000128881. [Q6IQ55-1]
ENST00000567840; ENSP00000455734; ENSG00000128881. [Q6IQ55-3]
GeneID146057.
KEGGhsa:146057.
UCSCuc001zqo.2. human. [Q6IQ55-1]
uc001zqp.3. human. [Q6IQ55-3]

Organism-specific databases

CTD146057.
GeneCardsGC15M043030.
GeneReviewsTTBK2.
H-InvDBHIX0012177.
HGNCHGNC:19141. TTBK2.
HPAHPA018113.
MIM604432. phenotype.
611695. gene.
neXtProtNX_Q6IQ55.
Orphanet98767. Spinocerebellar ataxia type 11.
PharmGKBPA134913925.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000232043.
HOVERGENHBG061812.
KOK08815.
OMAHCKPSKN.
OrthoDBEOG7RFTGM.
PhylomeDBQ6IQ55.
TreeFamTF351646.

Enzyme and pathway databases

SignaLinkQ6IQ55.

Gene expression databases

ArrayExpressQ6IQ55.
BgeeQ6IQ55.
CleanExHS_TTBK2.
GenevestigatorQ6IQ55.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTTBK2.
GenomeRNAi146057.
NextBio85251.
PROQ6IQ55.
SOURCESearch...

Entry information

Entry nameTTBK2_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 113 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 15

Human chromosome 15: entries, gene names and cross-references to MIM