| Tag | Content |
|---|
| CPLM ID | CPLM-014971 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Tau-tubulin kinase 2 |
Protein Synonyms/Alias | |
Gene Name | TTBK2 |
Gene Synonyms/Alias | KIAA0847 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 985 | LVKLLVEKRQFKSFL | ubiquitination | [1] |
|
Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | 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. |
Sequence Annotation | DOMAIN 21 284 Protein kinase.
NP_BIND 27 35 ATP (By similarity).
ACT_SITE 141 141 Proton acceptor (By similarity).
BINDING 50 50 ATP (By similarity).
MOD_RES 786 786 Phosphoserine. |
Keyword | Alternative splicing; ATP-binding; Cell projection; Cilium; Cilium biogenesis/degradation; Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Neurodegeneration; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Spinocerebellar ataxia; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1244 AA |
Protein Sequence | MSGGGEQLDI LSVGILVKER WKVLRKIGGG GFGEIYDALD MLTRENVALK VESAQQPKQV 60
LKMEVAVLKK LQGKDHVCRF IGCGRNDRFN YVVMQLQGRN LADLRRSQSR GTFTISTTLR 120
LGRQILESIE SIHSVGFLHR DIKPSNFAMG RFPSTCRKCY MLDFGLARQF TNSCGDVRPP 180
RAVAGFRGTV RYASINAHRN REMGRHDDLW SLFYMLVEFV VGQLPWRKIK DKEQVGSIKE 240
RYDHRLMLKH LPPEFSIFLD HISSLDYFTK PDYQLLTSVF DNSIKTFGVI ESDPFDWEKT 300
GNDGSLTTTT TSTTPQLHTR LTPAAIGIAN ATPIPGDLLR ENTDEVFPDE QLSDGENGIP 360
VGVSPDKLPG SLGHPRPQEK DVWEEMDANK NKIKLGICKA ATEEENSHGQ ANGLLNAPSL 420
GSPIRVRSEI TQPDRDIPLV RKLRSIHSFE LEKRLTLEPK PDTDKFLETC LEKMQKDTSA 480
GKESILPALL HKPCVPAVSR TDHIWHYDEE YLPDASKPAS ANTPEQADGG GSNGFIAVNL 540
SSCKQEIDSK EWVIVDKEQD LQDFRTNEAV GHKTTGSPSD EEPEVLQVLE ASPQDEKLQL 600
GPWAENDHLK KETSGVVLAL SAEGPPTAAS EQYTDRLELQ PGAASQFIAA TPTSLMEAQA 660
EGPLTAITIP RPSVASTQST SGSFHCGQQP EKKDLQPMEP TVELYSPREN FSGLVVTEGE 720
PPSGGSRTDL GLQIDHIGHD MLPNIRESNK SQDLGPKELP DHNRLVVREF ENLPGETEEK 780
SILLESDNED EKLSRGQHCI EISSLPGDLV IVEKDHSATT EPLDVTKTQT FSVVPNQDKN 840
NEIMKLLTVG TSEISSRDID PHVEGQIGQV AEMQKNKISK DDDIMSEDLP GHQGDLSTFL 900
HQEGKREKIT PRNGELFHCV SENEHGAPTR KDMVRSSFVT RHSRIPVLAQ EIDSTLESSS 960
PVSAKEKLLQ KKAYQPDLVK LLVEKRQFKS FLGDLSSASD KLLEEKLATV PAPFCEEEVL 1020
TPFSRLTVDS HLSRSAEDSF LSPIISQSRK SKIPRPVSWV NTDQVNSSTS SQFFPRPPPG 1080
KPPTRPGVEA RLRRYKVLGS SNSDSDLFSR LAQILQNGSQ KPRSTTQCKS PGSPHNPKTP 1140
PKSPVVPRRS PSASPRSSSL PRTSSSSPSR AGRPHHDQRS SSPHLGRSKS PPSHSGSSSS 1200
RRSCQQEHCK PSKNGLKGSG SLHHHSASTK TPQGKSKPAS KLSR 1244 |
Gene Ontology | GO:0005814; C:centriole; IEA:UniProtKB-SubCell. GO:0035869; C:ciliary transition zone; ISS:UniProtKB. GO:0036064; C:cilium basal body; ISS:UniProtKB. GO:0005829; C:cytosol; IDA:UniProtKB. GO:0005634; C:nucleus; IDA:UniProtKB. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. GO:0008219; P:cell death; IEA:UniProtKB-KW. GO:0042384; P:cilium assembly; ISS:UniProtKB. GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB. GO:0007224; P:smoothened signaling pathway; ISS:UniProtKB. |
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