ID G1QPM5_NOMLE Unreviewed; 2642 AA.
AC G1QPM5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=WNK1 {ECO:0000313|Ensembl:ENSNLEP00000002891.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000002891.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000002891.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000002891.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR EMBL; ADFV01077999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01078006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003273724.1; XM_003273676.3.
DR Ensembl; ENSNLET00000003040.2; ENSNLEP00000002891.2; ENSNLEG00000002228.3.
DR GeneID; 100594288; -.
DR CTD; 65125; -.
DR eggNOG; KOG0584; Eukaryota.
DR GeneTree; ENSGT00940000155474; -.
DR HOGENOM; CLU_000550_0_1_1; -.
DR OrthoDB; 5478852at2759; -.
DR Proteomes; UP000001073; Chromosome 23.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0042592; P:homeostatic process; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14030; STKc_WNK1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR13902; SERINE/THREONINE-PROTEIN KINASE WNK WITH NO LYSINE -RELATED; 1.
DR PANTHER; PTHR13902:SF46; SERINE_THREONINE-PROTEIN KINASE WNK1; 1.
DR Pfam; PF12202; OSR1_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 221..479
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1530..1561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1717..1741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1803..1822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1994..2020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2128..2207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2281..2329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2372..2456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2592..2613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1376
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1994..2008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2129..2145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2146..2166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2177..2207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2285..2322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2393..2456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2642 AA; 279669 MW; 9E584F1D057B1434 CRC64;
MSGGAAEKQS STPGSLFLSP PAPAPKNGSS SDSSVGEKLG AAAADAVTGR TEEYRRRRHT
MDKDSRGAAA TTTTTEHRFF RRSVICDSNA TALELPGLPL SLPQPSIPAA VPQSAPPEPH
REETVTATAT SQVAQQPPAA AAPGEQAVAG PAPSTVPSST SKDRPVSQPS LVGSKEEPPP
ARSGSGGGSA KEPQEERSQQ QDDIEELETK AVGMSNDGRF LKFDIEIGRG SFKTVYKGLD
TETTVEVAWC ELQDRKLTKS ERQRFKEEAE MLKGLQHPNI VRFYDSWEST VKGKKCIVLV
TELMTSGTLK TYLKRFKVMK IKVLRSWCRQ ILKGLQFLHT RTPPIIHRDL KCDNIFITGP
TGSVKIGDLG LATLKRASFA KSVIGTPEFM APEMYEEKYD ESVDVYAFGM CMLEMATSEY
PYSECQNAAQ IYRRVTSGVK PASFDKVAIP EVKEIIEGCI RQNKDERYSI KDLLNHAFFQ
EETGVRVELA EEDDGEKIAI KLWLRIEDIK KLKGKYKDNE AIEFSFDLER DVPEDVAQEM
VESGYVCEGD HKTMAKAIKD RVSLIKRKRE QRQLVREEQE KKKQEESSLK QLVEQSSASQ
TGVKQLPSAS TGIPTASTTS ASVSTQVEPE EPEADQHQQL QYQQPSISVL SDGTVDSGQG
SSVFTESRVS SQQTVSYGSQ HEQAHSTGTV PGHIPSTVQA QSQPHGVYPP SSVPQSMAHP
CGGTPTYPES QISFPTIHER PVSFSPPPTC PPKVAISQRR KSTSFLEAQT HHFQPLLRTV
GQSLLPPGGS PTNWTPEAAV MLGTTASRVT GESCEIQVHP MFEPSQVYSD YRPGLVLPEE
AHYFIPQEAV YVAGVHYQAR VAEQYEGIPY NSSVLSSPMK QIPEQKPVQG GPTSSSVFEF
PSGQAFLVGH LQNLRLDSGL SPGSPLSSIS APISTDATRL KFHPVFVPHS APAVLTHNNE
SRSNCVFEFH VHTPSSSSGE GGGILPQRVY RNRQVAVDLN QEELPPQSVG LHGYLQPVTE
EKHNYHAPEL TVSVVEPIGQ NWPIGSPEYS SDSSQITSSD PSDFQSPPPT GGAAAPFGSD
VSLPFIHLPQ TVLQESPLFF CFPQGTTSQQ VLTASFSSGG SALHPQAQGQ SQGQPSSSSL
TGVSSSQPIQ HPQQQQGIQQ TAPPQQTVQY SLSQTSTSSE ATTAQPVSQP QAPQVLPQVS
AGKQGFPPRL PPQYPGDSNI APSSNVASVC IHSAVLSPPM PTEVLATPGY FPTVVQPYVE
SNLLVPMGGV GGQVQVSQPG VSLAQAPTTS SQQAVLESTQ GVSQVAPTEP VPVAQPQPTQ
PTTLASSIDS AHSDVASGMS DGNENVPSSS GRHEGRTTKR HYRKSVRSRS RHEKSSRPKL
RILNVSNKGD RVVECQLETH NRKMVTFKFD LDGDNPEEIA TIMVNNDFIL AIERESFVDQ
VREIIEKADE MLSEDVSVEP EGDQGLESLQ GKDDYGFSGS QKLEGEFKQP IPASSMPQQI
GIPTSSLTQV VHSAGRRFIV SPVPESRLRE SKVFPSETTD TVAASTSQSP GMNLSHSASS
LSLQQAFSEL RRAQMTEGPN TAPPNFSHTG PTFPVVPPFL SGIAGVPTTA AATVPVPATS
SPPNDISTSV IQSEVTVPTE EGIAGVATSM GVVTSGGLPI PPVSKSPVVS SVVSSITIPA
VVSTSTTSPS LQVPTSTSEN IVSSTALYPS VTVSATSASA GGSTATPGPK PPGVVSQQAA
GSTTAGATLT SVSATTSFPS TASQLSIQLS SSTSTPTLAE TVVVSAHSLD KTSHSSTTGL
AFSLSAPSSS SSPGAAVSSS ISQPGGLHPL VIPSVTASTP ILPQAAGPTS TPLLPQVPSI
PPLVQPVANV PAVQQTLIHT QPQPALLPNQ PHTHCPEIDS DTQPKAPGID DIKTLEEKLR
SLFSEHSSSG AQHASVSLET SLVIESTVTP GIPTTAVAPS KLLTSTTSTC LPPTNLPLGT
VALPVTPVVT PGQVSTPVST TTSGVKPGTA PSKPPLTKAP VLPVGTELPA GTLSSEQLPP
FPGPSLIQSQ QPLEDLDAQL RRTLSPEIIT VTSAVGPVSV VAPTAITEAG AQPQKDVSQV
KEGPVLATSS GAGVFKMGRF QVSVAADDAQ KEGKNKSEDA KSVHFESSTS ESSVLSSSSP
ESTLVKPEPN GITIPGISSD VPESTHKTAA SEAKSDTGQP TKVGRFQVTT TANKVGRFSV
SKTEDKITDT KKEGPVASPP FMDLEQAVLP AVIPKKEKPE LSEPSHLNGP SSDLEAAFLS
RDVDDGSGSP NSPHQLSSKS LPIQNLSQSL SNSFNSSYMS SDNESDIEDE DLKLELRRLR
DKHLKEIQDL QSRQKHEIES LYTKLGKVPP AVIIPPAAPL SGRRRRPTKS KGSKSSRSSS
LGNKSPQLSG NLSGQSAASV LHPQQTLHPP GNIPESGQNQ LLQPLKPSPS SDNLYSAFTS
DGAISVPSLS APGQGTSSTN TVGATVNSQA AQAQPPAMTS SRKGTFTDDL HKLVDNWARD
AMNLSGRRGS KGHMNYEGPG MARKFSAPGQ LCISMTSNLG GSAPISAASA TSLGHFTKSM
CPPQQYGFPA TPFGAQWSGT GGPAPQPLGQ FQPVGTASLQ NFNISNLQKS ISNPPGSNLR
TT
//
