ID Q5SXG3_MOUSE Unreviewed; 1337 AA.
AC Q5SXG3;
DT 21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 161.
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=Mink1 {ECO:0000313|Ensembl:ENSMUSP00000072649.8,
GN ECO:0000313|MGI:MGI:1355329};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000072649.8, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:16452087}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [2] {ECO:0007829|PubMed:19144319}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000072649.8, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000072649.8,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5] {ECO:0007829|PubMed:24129315}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24129315;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [6] {ECO:0000313|Ensembl:ENSMUSP00000072649.8}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000072649.8};
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};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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DR RefSeq; NP_001039424.1; NM_001045959.1.
DR SMR; Q5SXG3; -.
DR jPOST; Q5SXG3; -.
DR MaxQB; Q5SXG3; -.
DR ProteomicsDB; 355755; -.
DR Antibodypedia; 5678; 261 antibodies from 32 providers.
DR DNASU; 50932; -.
DR Ensembl; ENSMUST00000072873.14; ENSMUSP00000072649.8; ENSMUSG00000020827.19.
DR GeneID; 50932; -.
DR UCSC; uc007jvk.1; mouse.
DR AGR; MGI:1355329; -.
DR CTD; 50488; -.
DR MGI; MGI:1355329; Mink1.
DR VEuPathDB; HostDB:ENSMUSG00000020827; -.
DR GeneTree; ENSGT00950000183196; -.
DR OrthoDB; 2904475at2759; -.
DR PhylomeDB; Q5SXG3; -.
DR TreeFam; TF105138; -.
DR BioGRID-ORCS; 50932; 3 hits in 83 CRISPR screens.
DR ChiTaRS; Mink1; mouse.
DR Proteomes; UP000000589; Chromosome 11.
DR Bgee; ENSMUSG00000020827; Expressed in visual cortex and 243 other cell types or tissues.
DR ExpressionAtlas; Q5SXG3; baseline and differential.
DR Genevisible; Q5SXG3; MM.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd06636; STKc_MAP4K4_6_N; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Proteomics identification {ECO:0007829|EPD:Q5SXG3,
KW ECO:0007829|MaxQB:Q5SXG3};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 25..289
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1024..1311
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 299..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..335
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..575
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..665
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..735
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..849
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1337 AA; 150405 MW; 77412FB60B4FE27B CRC64;
MGDPAPARSL DDIDLSALRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL AAIKVMDVTE
DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKSPPGNDDQ LWLVMEFCGA GSVTDLVKNT
KGNALKEDCI AYICREILRG LAHLHAHKVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR
TVGRRNTFIG TPYWMAPEVI ACDENPDATY DYRSDIWSLG ITAIEMAEGA PPLCDMHPMR
ALFLIPRNPP PRLKSKKWSK KFTDFIDTCL IKTYLSRPPT EQLLKFPFIR DQPTERQVRI
QLKDHIDRSR KKRGEKEETE YEYSGSEEED DSHGEEGEPS SIMNVPGEST LRREFLRLQQ
ENKSNSEALK QQQQLQQQQQ RDPEAHIKHL LHQRQRRIEE QKEERRRVEE QQRREREQRK
LQEKEQQRRL EDMQALRREE ERRQAEREQE YKRKQLEEQR QSERLQRQLQ QEHAYLKSLQ
QQQQQQQLQK QQQQQQQILP GDRKPLYHYG RGINPADKPA WAREVEERAR MNKQQNSPLA
KAKPSSAGPE PPISQASPSP PGPLSQTPPM QRPVEPQEGP HKSLVAHRVP LKPYAAPVPR
SQSLQDQPTR NLAAFPASHD PDPAAVPTPT ATPSARGAVI RQNSDPTSEG PGPSPNPPSW
VRPDNEAPPK VPQRTSSIAT ALNTSGAGGS RPAQAVRARP RSNSAWQIYL QRRAERGTPK
PPGPPAQPPG PPNASSNPDL RRSDPGWERS DSVLPASHGH LPQAGSLERN RNRVGASTKL
DSSPVLSPGN KAKPEDHRSR PGRPADFVLL KERTLDEAPK PPKKAMDYSS SSEEVESSEE
EEEEGDGEPS EGSRDTPGGR SDGDTDSVST MVVHDVEEIS GTQPSYGGGT MVVQRTPEEE
RSLLLADSNG YTNLPDVVQP SHSPTENSKG QSPPTKDGGS DYQSRGLVKA PGKSSFTMFV
DLGIYQPGGS GDTIPITALV GGEGGRLDQL QFDVRKGSVV NVNPTNTRAH SETPEIRKYK
KRFNSEILCA ALWGVNLLVG TENGLMLLDR SGQGKVYGLI GRRRFQQMDV LEGLNLLITI
SGKRNKLRVY YLSWLRNKIL HNDPEVEKKQ GWTTVGDMEG CGHYRVVKYE RIKFLVIALK
NSVEVYAWAP KPYHKFMAFK SFADLPHRPL LVDLTVEEGQ RLKVIYGSSA GFHAVDVDSG
NSYDIYIPVH IQSQITPHAI IFLPNTDGME MLLCYEDEGV YVNTYGRIIK DVVLQWGEMP
TSVAYICSNQ IMGWGEKAIE IRSVETGHLD GVFMHKRAQR LKFLCERNDK VFFASVRSGG
SSQVYFMTLN RNCIMNW
//
