CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000339
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cyclin-G-associated kinase 
Protein Synonyms/Alias
  
Gene Name
 GAK 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
78LLSNEEEKNRAIIQEubiquitination[1]
91QEVCFMKKLSGHPNIubiquitination[1]
175PIIHRDLKVENLLLSubiquitination[1, 2, 3]
325AARNVNPKSPITELLubiquitination[1, 2, 3]
390ERLFTNLKDTSSKVIubiquitination[1, 3, 4]
405QSVANYAKGDLDISYubiquitination[1]
432EGVESALKNNIEDVRubiquitination[1, 2]
445VRLFLDSKHPGHYAVubiquitination[1]
590TPVPLFSKQRSGCRPubiquitination[1]
617STSQEYDKMRDFKIEubiquitination[1]
682PRNATTVKFAKYDLDubiquitination[1]
1265VAPEQVKKHYRRAVLubiquitination[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]
 [2] 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]
 [3] 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]
 [4] 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] 
Functional Description
 Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin- coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1. 
Sequence Annotation
 DOMAIN 40 314 Protein kinase.
 DOMAIN 399 566 Phosphatase tensin-type.
 DOMAIN 572 710 C2 tensin-type.
 DOMAIN 1247 1311 J.
 ACT_SITE 173 173 Proton acceptor (By similarity).
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 16 16 Phosphoserine.
 MOD_RES 456 456 Phosphoserine.
 MOD_RES 770 770 Phosphoserine.
 MOD_RES 826 826 Phosphoserine.
 MOD_RES 829 829 Phosphoserine.
 MOD_RES 834 834 Phosphoserine.
 MOD_RES 939 939 Phosphoserine.
 MOD_RES 1096 1096 Phosphoserine.
 MOD_RES 1176 1176 Phosphoserine.
 MOD_RES 1185 1185 Phosphoserine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell junction; Complete proteome; Cytoplasm; Golgi apparatus; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1311 AA 
Protein Sequence
MSLLQSALDF LAGPGSLGGA SGRDQSDFVG QTVELGELRL RVRRVLAEGG FAFVYEAQDV 60
GSGREYALKR LLSNEEEKNR AIIQEVCFMK KLSGHPNIVQ FCSAASIGKE ESDTGQAEFL 120
LLTELCKGQL VEFLKKMESR GPLSCDTVLK IFYQTCRAVQ HMHRQKPPII HRDLKVENLL 180
LSNQGTIKLC DFGSATTISH YPDYSWSAQR RALVEEEITR NTTPMYRTPE IIDLYSNFPI 240
GEKQDIWALG CILYLLCFRQ HPFEDGAKLR IVNGKYSIPP HDTQYTVFHS LIRAMLQVNP 300
EERLSIAEVV HQLQEIAAAR NVNPKSPITE LLEQNGGYGS ATLSRGPPPP VGPAGSGYSG 360
GLALAEYDQP YGGFLDILRG GTERLFTNLK DTSSKVIQSV ANYAKGDLDI SYITSRIAVM 420
SFPAEGVESA LKNNIEDVRL FLDSKHPGHY AVYNLSPRTY RPSRFHNRVS ECGWAARRAP 480
HLHTLYNICR NMHAWLRQDH KNVCVVHCMD GRAASAVAVC SFLCFCRLFS TAEAAVYMFS 540
MKRCPPGIWP SHKRYIEYMC DMVAEEPITP HSKPILVRAV VMTPVPLFSK QRSGCRPFCE 600
VYVGDERVAS TSQEYDKMRD FKIEDGKAVI PLGVTVQGDV LIVIYHARST LGGRLQAKMA 660
SMKMFQIQFH TGFVPRNATT VKFAKYDLDA CDIQEKYPDL FQVNLEVEVE PRDRPSREAP 720
PWENSSMRGL NPKILFSSRE EQQDILSKFG KPELPRQPGS TAQYDAGAGS PEAEPTDSDS 780
PPSSSADASR FLHTLDWQEE KEAETGAENA SSKESESALM EDRDESEVSD EGGSPISSEG 840
QEPRADPEPP GLAAGLVQQD LVFEVETPAV LPEPVPQEDG VDLLGLHSEV GAGPAVPPQA 900
CKAPSSNTDL LSCLLGPPEA ASQGPPEDLL SEDPLLLASP APPLSVQSTP RGGPPAAADP 960
FGPLLPSSGN NSQPCSNPDL FGEFLNSDSV TVPPSFPSAH SAPPPSCSAD FLHLGDLPGE 1020
PSKMTASSSN PDLLGGWAAW TETAASAVAP TPATEGPLFS PGGQPAPCGS QASWTKSQNP 1080
DPFADLGDLS SGLQGSPAGF PPGGFIPKTA TTPKGSSSWQ TSRPPAQGAS WPPQAKPPPK 1140
ACTQPRPNYA SNFSVIGARE ERGVRAPSFA QKPKVSENDF EDLLSNQGFS SRSDKKGPKT 1200
IAEMRKQDLA KDTDPLKLKL LDWIEGKERN IRALLSTLHT VLWDGESRWT PVGMADLVAP 1260
EQVKKHYRRA VLAVHPDKAA GQPYEQHAKM IFMELNDAWS EFENQGSRPL F 1311 
Gene Ontology
 GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004674; F:protein serine/threonine kinase activity; TAS:ProtInc.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW. 
Interpro
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR001623; DnaJ_domain.
 IPR011009; Kinase-like_dom.
 IPR014019; Phosphatase_tensin-typ.
 IPR000719; Prot_kinase_cat_dom.
 IPR008271; Ser/Thr_kinase_AS.
 IPR014020; Tensin_phosphatase_C2-dom. 
Pfam
 PF00226; DnaJ
 PF00069; Pkinase
 PF10409; PTEN_C2 
SMART
 SM00271; DnaJ 
PROSITE
 PS51182; C2_TENSIN
 PS00636; DNAJ_1
 PS50076; DNAJ_2
 PS51181; PPASE_TENSIN
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS