CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018059
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 TBC domain-containing protein kinase-like protein 
Protein Synonyms/Alias
  
Gene Name
 TBCK 
Gene Synonyms/Alias
 TBCKL; HSPC302 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
271PDQLMKDKVFSEVSPubiquitination[1]
285PLYTPFTKPASLFSSubiquitination[1]
343LEKELVNKEIIRSKPubiquitination[1]
349NKEIIRSKPPICTLPubiquitination[1]
433LPLIIREKDTEYQLNubiquitination[1]
450ILFDRLLKAYPYKKNubiquitination[1]
456LKAYPYKKNQIWKEAubiquitination[1]
461YKKNQIWKEARVDIPubiquitination[1]
495AKYDAIDKDTPIPTDubiquitination[1]
706NLFCWTPKSATYRQHubiquitination[1]
756SIPLNDLKSEVSPRIubiquitination[1]
879ILDGGINKIKPTGLLubiquitination[1]
881DGGINKIKPTGLLTIubiquitination[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
  
Sequence Annotation
 DOMAIN 1 273 Protein kinase.
 DOMAIN 466 651 Rab-GAP TBC.
 DOMAIN 790 889 Rhodanese.  
Keyword
 Alternative splicing; Complete proteome; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 893 AA 
Protein Sequence
MFPLKDAEMG AFTFFASALP HDVCGSNGLP LTPNSIKILG RFQILKTITH PRLCQYVDIS 60
RGKHERLVVV AEHCERSLED LLRERKPVSC STVLCIAFEV LQGLQYMNKH GIVHRALSPH 120
NILLDRKGHI KLAKFGLYHM TAHGDDVDFP IGYPSYLAPE VIAQGIFKTT DHMPSKKPLP 180
SGPKSDVWSL GIILFELCVG RKLFQSLDIS ERLKFLLTLD CVDDTLIVLA EEHGCLDIIK 240
ELPETVIDLL NKCLTFHPSK RPTPDQLMKD KVFSEVSPLY TPFTKPASLF SSSLRCADLT 300
LPEDISQLCK DINNDYLAER SIEEVYYLWC LAGGDLEKEL VNKEIIRSKP PICTLPNFLF 360
EDGESFGQGR DRSSLLDDTT VTLSLCQLRN RLKDVGGEAF YPLLEDDQSN LPHSNSNNEL 420
SAAATLPLII REKDTEYQLN RIILFDRLLK AYPYKKNQIW KEARVDIPPL MRGLTWAALL 480
GVEGAIHAKY DAIDKDTPIP TDRQIEVDIP RCHQYDELLS SPEGHAKFRR VLKAWVVSHP 540
DLVYWQGLDS LCAPFLYLNF NNEALAYACM SAFIPKYLYN FFLKDNSHVI QEYLTVFSQM 600
IAFHDPELSN HLNEIGFIPD LYAIPWFLTM FTHVFPLHKI FHLWDTLLLG NSSFPFCIGV 660
AILQQLRDRL LANGFNECIL LFSDLPEIDI ERCVRESINL FCWTPKSATY RQHAQPPKPS 720
SDSSGGRSSA PYFSAECPDP PKTDLSRESI PLNDLKSEVS PRISAEDLID LCELTVTGHF 780
KTPSKKTKSS KPKLLVVDIR NSEDFIRGHI SGSINIPFSA AFTAEGELTQ GPYTAMLQNF 840
KGKVIVIVGH VAKHTAEFAA HLVKMKYPRI CILDGGINKI KPTGLLTIPS PQI 893 
Gene Ontology
 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
 GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
 GO:0032851; P:positive regulation of Rab GTPase activity; IEA:GOC. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR000195; Rab-GTPase-TBC_dom.
 IPR001763; Rhodanese-like_dom. 
Pfam
 PF00069; Pkinase
 PF00566; RabGAP-TBC
 PF00581; Rhodanese 
SMART
 SM00450; RHOD
 SM00164; TBC 
PROSITE
 PS50011; PROTEIN_KINASE_DOM
 PS50206; RHODANESE_3
 PS50086; TBC_RABGAP 
PRINTS