CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015782
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase TAO1 
Protein Synonyms/Alias
 Kinase from chicken homolog B; hKFC-B; MARK Kinase; MARKK; Prostate-derived sterile 20-like kinase 2; PSK-2; PSK2; Prostate-derived STE20-like kinase 2; Thousand and one amino acid protein kinase 1; TAOK1; hTAOK1 
Gene Name
 TAOK1 
Gene Synonyms/Alias
 KIAA1361; MAP3K16; MARKK 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
69SGKQSTEKWQDIIKEubiquitination[1]
484QLMTLENKLKAEMDEubiquitination[2]
818LLNAYQSKIKMQAEAubiquitination[1, 3, 4]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 
Functional Description
 Serine/threonine-protein kinase involved in various processes such as p38/MAPK14 stress-activated MAPK cascade, DNA damage response and regulation of cytoskeleton stability. Phosphorylates MAP2K3, MAP2K6 and MARK2. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade by mediating phosphorylation and subsequent activation of the upstream MAP2K3 and MAP2K6 kinases. Involved in G-protein coupled receptor signaling to p38/MAPK14. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of MAP2K3 and MAP2K6. Acts as a regulator of cytoskeleton stability by phosphorylating 'Thr-208' of MARK2, leading to activate MARK2 kinase activity and subsequent phosphorylation and detachment of MAPT/TAU from microtubules. Also acts as a regulator of apoptosis: regulates apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation via activation of the MAPK8/JNK cascade. 
Sequence Annotation
 DOMAIN 28 281 Protein kinase.
 NP_BIND 34 42 ATP (By similarity).
 ACT_SITE 151 151 Proton acceptor (By similarity).
 BINDING 57 57 ATP (Probable).
 MOD_RES 9 9 Phosphoserine.
 MOD_RES 421 421 Phosphoserine.
 MOD_RES 445 445 Phosphoserine.
 MOD_RES 669 669 Phosphothreonine.
 MOD_RES 965 965 Phosphoserine.  
Keyword
 Alternative splicing; Apoptosis; ATP-binding; Coiled coil; Complete proteome; Cytoplasm; DNA damage; DNA repair; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1001 AA 
Protein Sequence
MPSTNRAGSL KDPEIAELFF KEDPEKLFTD LREIGHGSFG AVYFARDVRT NEVVAIKKMS 60
YSGKQSTEKW QDIIKEVKFL QRIKHPNSIE YKGCYLREHT AWLVMEYCLG SASDLLEVHK 120
KPLQEVEIAA ITHGALQGLA YLHSHTMIHR DIKAGNILLT EPGQVKLADF GSASMASPAN 180
SFVGTPYWMA PEVILAMDEG QYDGKVDVWS LGITCIELAE RKPPLFNMNA MSALYHIAQN 240
ESPTLQSNEW SDYFRNFVDS CLQKIPQDRP TSEELLKHIF VLRERPETVL IDLIQRTKDA 300
VRELDNLQYR KMKKLLFQEA HNGPAVEAQE EEEEQDHGVG RTGTVNSVGS NQSIPSMSIS 360
ASSQSSSVNS LPDVSDDKSE LDMMEGDHTV MSNSSVIHLK PEEENYREEG DPRTRASDPQ 420
SPPQVSRHKS HYRNREHFAT IRTASLVTRQ MQEHEQDSEL REQMSGYKRM RRQHQKQLMT 480
LENKLKAEMD EHRLRLDKDL ETQRNNFAAE MEKLIKKHQA AMEKEAKVMS NEEKKFQQHI 540
QAQQKKELNS FLESQKREYK LRKEQLKEEL NENQSTPKKE KQEWLSKQKE NIQHFQAEEE 600
ANLLRRQRQY LELECRRFKR RMLLGRHNLE QDLVREELNK RQTQKDLEHA MLLRQHESMQ 660
ELEFRHLNTI QKMRCELIRL QHQTELTNQL EYNKRREREL RRKHVMEVRQ QPKSLKSKEL 720
QIKKQFQDTC KIQTRQYKAL RNHLLETTPK SEHKAVLKRL KEEQTRKLAI LAEQYDHSIN 780
EMLSTQALRL DEAQEAECQV LKMQLQQELE LLNAYQSKIK MQAEAQHDRE LRELEQRVSL 840
RRALLEQKIE EEMLALQNER TERIRSLLER QAREIEAFDS ESMRLGFSNM VLSNLSPEAF 900
SHSYPGASGW SHNPTGGPGP HWGHPMGGPP QAWGHPMQGG PQPWGHPSGP MQGVPRGSSM 960
GVRNSPQALR RTASGGRTEQ GMSRSTSVTS QISNGSHMSY T 1001 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005524; F:ATP binding; NAS:HGNC.
 GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0097194; P:execution phase of apoptosis; IDA:UniProtKB.
 GO:0031572; P:G2 DNA damage checkpoint; IMP:UniProtKB.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
 GO:0051493; P:regulation of cytoskeleton organization; ISS:UniProtKB. 
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. 
Pfam
 PF00069; Pkinase 
SMART
 SM00220; S_TKc 
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS