CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021356
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Homeodomain-interacting protein kinase 3 
Protein Synonyms/Alias
 Androgen receptor-interacting nuclear protein kinase; ANPK; Fas-interacting serine/threonine-protein kinase; FIST; Homolog of protein kinase YAK1 
Gene Name
 HIPK3 
Gene Synonyms/Alias
 DYRK6; FIST3; PKY 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
353GSASHVSKTVCSTYLubiquitination[1]
428QLLNVGTKSTRFFCKubiquitination[1, 2, 3]
435KSTRFFCKETDMSHSubiquitination[1]
447SHSGWRLKTLEEHEAubiquitination[2]
459HEAETGMKSKEARKYubiquitination[1, 2, 3]
461AETGMKSKEARKYIFubiquitination[1]
503REFVSLLKKMLLIDAubiquitination[1]
504EFVSLLKKMLLIDADubiquitination[1]
528NHPFVNMKHLLDFPHubiquitination[1]
813SPKIINGKDVEEVSCubiquitination[1, 3]
852SDSSVSDKQRQTIIIubiquitination[1]
891RHSLRECKGSLDCEAubiquitination[1, 3]
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] 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 transcription regulation, apoptosis and steroidogenic gene expression. Phosphorylates JUN and RUNX2. Seems to negatively regulate apoptosis by promoting FADD phosphorylation. Enhances androgen receptor-mediated transcription. May act as a transcriptional corepressor for NK homeodomain transcription factors. The phosphorylation of NR5A1 activates SF1 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. In osteoblasts, supports transcription activation: phosphorylates RUNX2 that synergizes with SPEN/MINT to enhance FGFR2-mediated activation of the osteocalcin FGF- responsive element (OCFRE). 
Sequence Annotation
 DOMAIN 197 525 Protein kinase.
 NP_BIND 203 211 ATP (By similarity).
 REGION 767 944 Interaction with AR (By similarity).
 REGION 796 891 Interaction with FAS (By similarity).
 REGION 855 1011 Required for localization to nuclear
 REGION 866 918 SUMO interaction motifs (SIM); required
 REGION 870 880 Interaction with UBL1 (Probable).
 ACT_SITE 322 322 Proton acceptor (By similarity).
 BINDING 226 226 ATP (By similarity).
 MOD_RES 359 359 Phosphotyrosine (By similarity).
 CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1208 1208 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Alternative splicing; Apoptosis; ATP-binding; Complete proteome; Cytoplasm; Isopeptide bond; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transcription; Transcription regulation; Transferase; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1215 AA 
Protein Sequence
MASQVLVYPP YVYQTQSSAF CSVKKLKVEP SSCVFQERNY PRTYVNGRNF GNSHPPTKGS 60
AFQTKIPFNR PRGHNFSLQT SAVVLKNTAG ATKVIAAQAQ QAHVQAPQIG AWRNRLHFLE 120
GPQRCGLKRK SEELDNHSSA MQIVDELSIL PAMLQTNMGN PVTVVTATTG SKQNCTTGEG 180
DYQLVQHEVL CSMKNTYEVL DFLGRGTFGQ VVKCWKRGTN EIVAIKILKN HPSYARQGQI 240
EVSILARLST ENADEYNFVR AYECFQHRNH TCLVFEMLEQ NLYDFLKQNK FSPLPLKVIR 300
PILQQVATAL KKLKSLGLIH ADLKPENIML VDPVRQPYRV KVIDFGSASH VSKTVCSTYL 360
QSRYYRAPEI ILGLPFCEAI DMWSLGCVIA ELFLGWPLYP GALEYDQIRY ISQTQGLPGE 420
QLLNVGTKST RFFCKETDMS HSGWRLKTLE EHEAETGMKS KEARKYIFNS LDDVAHVNTV 480
MDLEGSDLLA EKADRREFVS LLKKMLLIDA DLRITPAETL NHPFVNMKHL LDFPHSNHVK 540
SCFHIMDICK SHLNSCDTNN HNKTSLLRPV ASSSTATLTA NFTKIGTLRS QALTTSAHSV 600
VHHGIPLQAG TAQFGCGDAF QQTLIICPPA IQGIPATHGK PTSYSIRVDN TVPLVTQAPA 660
VQPLQIRPGV LSQTWSGRTQ QMLVPAWQQV TPLAPATTTL TSESVAGSHR LGDWGKMISC 720
SNHYNSVMPQ PLLTNQITLS APQPVSVGIA HVVWPQPATT KKNKQCQNRG ILVKLMEWEP 780
GREEINAFSW SNSLQNTNIP HSAFISPKII NGKDVEEVSC IETQDNQNSE GEARNCCETS 840
IRQDSDSSVS DKQRQTIIIA DSPSPAVSVI TISSDTDEEE TSQRHSLREC KGSLDCEACQ 900
STLNIDRMCS LSSPDSTLST SSSGQSSPSP CKRPNSMSDE EQESSCDTVD GSPTSDSSGH 960
DSPFAESTFV EDTHENTELV SSADTETKPA VCSVVVPPVE LENGLNADEH MANTDSICQP 1020
LIKGRSAPGR LNQPSAVGTR QQKLTSAFQQ QHLNFSQVQH FGSGHQEWNG NFGHRRQQAY 1080
IPTSVTSNPF TLSHGSPNHT AVHAHLAGNT HLGGQPTLLP YPSSATLSSA APVAHLLASP 1140
CTSRPMLQHP TYNISHPSGI VHQVPVGLNP RLLPSPTIHQ TQYKPIFPPH SYIAASPAYT 1200
GFPLSPTKLS QYPYM 1215 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0016605; C:PML body; IEA:Compara.
 GO:0005524; F:ATP binding; NAS:UniProtKB.
 GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0009299; P:mRNA transcription; IDA:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
 GO:0043508; P:negative regulation of JUN kinase activity; ISS:UniProtKB.
 GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
 GO:0018107; P:peptidyl-threonine phosphorylation; ISS:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. 
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