PRKY_HUMAN
ID PRKY_HUMAN Reviewed; 277 AA.
AC O43930; O15348; O15349;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Putative serine/threonine-protein kinase PRKY;
DE EC=2.7.11.1;
GN Name=PRKY;
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 [GENOMIC DNA], AND CHROMOSOMAL TRANSLOCATION WITH PRKX.
RX PubMed=9302280; DOI=10.1093/hmg/6.11.1985;
RA Schiebel K., Winkelmann M., Mertz A., Xu X., Page D.C., Weil D., Petit C.,
RA Rappold G.A.;
RT "Abnormal XY interchange between a novel isolated protein kinase gene,
RT PRKY, and its homologue, PRKX, accounts for one third of all (Y+)XX males
RT and (Y-)XY females.";
RL Hum. Mol. Genet. 6:1985-1989(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 68-178.
RC TISSUE=Fetal brain;
RX PubMed=9154127; DOI=10.1159/000134514;
RA Schiebel K., Mertz A., Winkelmann M., Glaeser B., Schempp W., Rappold G.;
RT "FISH localization of the human Y-homologue of protein kinase PRKX to
RT Yp11.2 and two pseudogenes to 15q26 and Xq12->13.";
RL Cytogenet. Cell Genet. 76:49-52(1997).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12815422; DOI=10.1038/nature01722;
RA Skaletsky H., Kuroda-Kawaguchi T., Minx P.J., Cordum H.S., Hillier L.W.,
RA Brown L.G., Repping S., Pyntikova T., Ali J., Bieri T., Chinwalla A.,
RA Delehaunty A., Delehaunty K., Du H., Fewell G., Fulton L., Fulton R.,
RA Graves T.A., Hou S.-F., Latrielle P., Leonard S., Mardis E., Maupin R.,
RA McPherson J., Miner T., Nash W., Nguyen C., Ozersky P., Pepin K., Rock S.,
RA Rohlfing T., Scott K., Schultz B., Strong C., Tin-Wollam A., Yang S.-P.,
RA Waterston R.H., Wilson R.K., Rozen S., Page D.C.;
RT "The male-specific region of the human Y chromosome is a mosaic of discrete
RT sequence classes.";
RL Nature 423:825-837(2003).
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 -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12815422}.
CC -!- DISEASE: Note=A chromosomal aberration involving PRKY is a cause of sex
CC reversal disorder. Translocation t(X;Y)(p22;p11) with PRKX. Chromosomal
CC translocations proximal to PRKY account for about 30% of the cases of
CC sex reversal disorder in XX males and XY females.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cAMP subfamily. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. Highly similar to PRKX
CC in the pseudoautosomal region of the X chromosome, the transcripts
CC specific of that gene are potential candidates for nonsense-mediated
CC decay. {ECO:0000305}.
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DR EMBL; Y13927; CAA74244.1; -; Genomic_DNA.
DR EMBL; Y13928; CAA74244.1; JOINED; Genomic_DNA.
DR EMBL; Y13929; CAA74244.1; JOINED; Genomic_DNA.
DR EMBL; Y13930; CAA74244.1; JOINED; Genomic_DNA.
DR EMBL; Y13931; CAA74244.1; JOINED; Genomic_DNA.
DR EMBL; Y13932; CAA74244.1; JOINED; Genomic_DNA.
DR EMBL; Y15801; CAA75792.1; -; mRNA.
DR EMBL; BC074851; AAH74851.1; -; mRNA.
DR EMBL; BC074852; AAH74852.1; -; mRNA.
DR EMBL; Y10484; CAA71508.1; -; mRNA.
DR EMBL; Y10485; CAA71509.1; -; mRNA.
DR AlphaFoldDB; O43930; -.
DR SMR; O43930; -.
DR IntAct; O43930; 3.
DR iPTMnet; O43930; -.
DR PhosphoSitePlus; O43930; -.
DR BioMuta; HGNC:9444; -.
DR jPOST; O43930; -.
DR MassIVE; O43930; -.
DR MaxQB; O43930; -.
DR PeptideAtlas; O43930; -.
DR PRIDE; O43930; -.
DR ProteomicsDB; 49242; -.
DR GeneCards; PRKY; -.
DR HGNC; HGNC:9444; PRKY.
DR MIM; 400008; gene.
DR neXtProt; NX_O43930; -.
DR VEuPathDB; HostDB:ENSG00000099725; -.
DR InParanoid; O43930; -.
DR OMA; WACGILC; -.
DR PhylomeDB; O43930; -.
DR PathwayCommons; O43930; -.
DR SignaLink; O43930; -.
DR ChiTaRS; PRKY; human.
DR Pharos; O43930; Tdark.
DR PRO; PR:O43930; -.
DR Proteomes; UP000005640; Chromosome Y.
DR RNAct; O43930; protein.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:ProtInc.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 5: Uncertain;
KW ATP-binding; Chromosomal rearrangement; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..277
FT /note="Putative serine/threonine-protein kinase PRKY"
FT /id="PRO_0000086584"
FT DOMAIN 49..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 55..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q922R0"
FT CONFLICT 69..70
FT /note="KT -> FR (in Ref. 3; CAA71508)"
FT /evidence="ECO:0000305"
FT CONFLICT 88..90
FT /note="RKQ -> NSG (in Ref. 3; CAA71509)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 31708 MW; 8DC7B21124BF8EAF CRC64;
MEAPGPAQAA AAESNSREVT EDAADWAPAL CPSPEARSPE APAYRLQDCD ALVTMGTGTF
GRVHLVKEKT AKHFFALKVM SIPDVIRRKQ EQHVHNEKSV LKEVSHPFLI RLFWTWHEER
FLYMLMEYVP GGELFSYLRN RGHFSSTTGL FYSAEIICAI EYLHSKEIVY RDLKPENILL
DRDGHIKLTD FGFAKKLVDR TWTLCGTPEY LAPEVIQSKG HGRAVDWWAL GILIFEMLSG
FPPFFDDNPF GIYQKILAGK LYFPRHLDFH VKTGRMM
