PDPK2_HUMAN
ID PDPK2_HUMAN Reviewed; 396 AA.
AC Q6A1A2;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Putative 3-phosphoinositide-dependent protein kinase 2;
DE EC=2.7.11.1;
DE AltName: Full=3-phosphoinositide-dependent protein kinase 2 pseudogene {ECO:0000305};
GN Name=PDPK2P {ECO:0000312|HGNC:HGNC:49897};
GN Synonyms=PDPK2 {ECO:0000303|Ref.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Pingzhang W., Xin W., Tianjing C., Jun W., Ying L.;
RT "A novel member of human 3-phosphoinositide dependent protein kinase-1
RT family, PDPK2.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylates and activates not only PKB/AKT, but also PKA,
CC PKC-zeta, RPS6KA1 and RPS6KB1. May play a general role in signaling
CC processes and in development (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- DOMAIN: The PIF-pocket is a small lobe in the catalytic domain required
CC by the enzyme for the binding to the hydrophobic motif of its
CC substrates. It is an allosteric regulatory site that can accommodate
CC small compounds acting as allosteric inhibitors.
CC {ECO:0000250|UniProtKB:O15530}.
CC -!- PTM: Phosphorylated on tyrosine and serine/threonine. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PDPK1 subfamily. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; AJ785968; CAH05056.1; -; mRNA.
DR AlphaFoldDB; Q6A1A2; -.
DR SMR; Q6A1A2; -.
DR IntAct; Q6A1A2; 2.
DR GlyGen; Q6A1A2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6A1A2; -.
DR BioMuta; HGNC:49897; -.
DR DMDM; 74757401; -.
DR jPOST; Q6A1A2; -.
DR MassIVE; Q6A1A2; -.
DR MaxQB; Q6A1A2; -.
DR PeptideAtlas; Q6A1A2; -.
DR PRIDE; Q6A1A2; -.
DR GeneCards; PDPK2P; -.
DR HGNC; HGNC:49897; PDPK2P.
DR neXtProt; NX_Q6A1A2; -.
DR InParanoid; Q6A1A2; -.
DR PhylomeDB; Q6A1A2; -.
DR SignaLink; Q6A1A2; -.
DR SIGNOR; Q6A1A2; -.
DR ChiTaRS; PDPK2P; human.
DR Pharos; Q6A1A2; Tdark.
DR PRO; PR:Q6A1A2; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q6A1A2; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR CDD; cd05581; STKc_PDK1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR039046; PDPK1.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 5: Uncertain;
KW ATP-binding; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..396
FT /note="Putative 3-phosphoinositide-dependent protein kinase
FT 2"
FT /id="PRO_0000341967"
FT DOMAIN 55..315
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..130
FT /note="PIF-pocket"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 65..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 133..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
SQ SEQUENCE 396 AA; 44765 MW; A0661913B473D8DF CRC64;
MVRTQTESST PPGIPGGSRQ GPAMDGTAAE PRPGAGSLQH AQPPPQPRKK RPEDFKFGKI
LGEGSFSTVV LARELATSRE YAIKILEKRH IIKENKVPYV TRERDVMSRL DHPFFVKLYF
TFQDDEKLYF GLSYAKNGEL LKYIRKIGSF DETCTRFYTA EIVSALEYLH GKGIIHRDLK
PENILLNEDM YIQITDFGTA KVLSPESKQA RANSFVGTAQ YVSPELLTEK SACKSSDLWA
LGCIIYQLVA GLPPFRAGNE YLIFQKIIKL EYDFPEKFFP KARDLVEKLL VLDATKRLGC
EEMEGYGPLK AHPFFESVTW ENLHQQTPPK LTAYLPAMSE DDEDCYGNVS WPGWRARQVA
LGPPCTGLHA RAPDPRVICS RKGRVSVPLR QACWWL
