STK31_MOUSE
ID STK31_MOUSE Reviewed; 1018 AA.
AC Q99MW1; B2RQM2; E9QLI8;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Serine/threonine-protein kinase 31;
DE EC=2.7.11.1;
GN Name=Stk31;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=11279525; DOI=10.1038/86927;
RA Wang P.J., McCarrey J.R., Yang F., Page D.C.;
RT "An abundance of X-linked genes expressed in spermatogonia.";
RL Nat. Genet. 27:422-426(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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).
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: Testis specific. Expressed only in male germ cells.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Ser-855 is present instead of the conserved Asp which is
CC expected to be an active site residue. {ECO:0000305}.
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DR EMBL; AF285580; AAK31959.1; -; mRNA.
DR EMBL; AC153385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC137989; AAI37990.1; -; mRNA.
DR CCDS; CCDS39487.1; -.
DR RefSeq; NP_084192.2; NM_029916.2.
DR AlphaFoldDB; Q99MW1; -.
DR SMR; Q99MW1; -.
DR BioGRID; 218727; 1.
DR STRING; 10090.ENSMUSP00000024171; -.
DR iPTMnet; Q99MW1; -.
DR PhosphoSitePlus; Q99MW1; -.
DR EPD; Q99MW1; -.
DR MaxQB; Q99MW1; -.
DR PaxDb; Q99MW1; -.
DR PRIDE; Q99MW1; -.
DR ProteomicsDB; 257453; -.
DR Antibodypedia; 12132; 240 antibodies from 29 providers.
DR DNASU; 77485; -.
DR Ensembl; ENSMUST00000024171; ENSMUSP00000024171; ENSMUSG00000023403.
DR GeneID; 77485; -.
DR KEGG; mmu:77485; -.
DR UCSC; uc009bws.2; mouse.
DR CTD; 56164; -.
DR MGI; MGI:1924735; Stk31.
DR VEuPathDB; HostDB:ENSMUSG00000023403; -.
DR eggNOG; ENOG502QPJA; Eukaryota.
DR GeneTree; ENSGT00390000007287; -.
DR InParanoid; Q99MW1; -.
DR OMA; HRAWNQQ; -.
DR OrthoDB; 104495at2759; -.
DR PhylomeDB; Q99MW1; -.
DR TreeFam; TF105335; -.
DR BioGRID-ORCS; 77485; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Stk31; mouse.
DR PRO; PR:Q99MW1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q99MW1; protein.
DR Bgee; ENSMUSG00000023403; Expressed in spermatocyte and 25 other tissues.
DR ExpressionAtlas; Q99MW1; baseline and differential.
DR Genevisible; Q99MW1; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 2.40.50.90; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00567; TUDOR; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF50199; SSF50199; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1018
FT /note="Serine/threonine-protein kinase 31"
FT /id="PRO_0000086716"
FT DOMAIN 78..137
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 711..1018
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 988..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 298..358
FT /evidence="ECO:0000255"
FT COMPBIAS 988..1012
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 717..725
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 738
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 500
FT /note="Y -> F (in Ref. 1; AAK31959 and 3; AAI37990)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="S -> I (in Ref. 1; AAK31959 and 3; AAI37990)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1018 AA; 115018 MW; DFF8CC620D58B13B CRC64;
MWGQRLFAGT AVAQSVSFPG LVQMDEDTHY NKVEDVVGSH VEDAVTFWAQ NVSKNKDIMK
IGCSLSEVCP LANSVFGNLD PKKIYGGLFS EDKCWYRCKV LKTISDDKCL VRYIDYGNTE
ILNRSDIVEI PPELQFSSIA KKYRLWGLQI PSGQEVTQFD QGRTFLGSLI FEKEIKMRIK
ATYQDGTVIA QAEYGTVDIG EEVAKKGFAE KCRLTSGIDA CEAKKPDPNQ LALRSLKNPI
PLWGRRSNQS TFSRPKGHFN GRLTLDVKYE TSAGNHVTFP KESLAAGDFN LGSNVSLAKI
KQDQKLIEEN EKLKTEKEVL LENYKALELK VEQTAQELQQ EKTATMDLTK HLESTLKTCV
GTRLKNLAAK VELLKEIRHI NISIRFGNDL SDAMQVLDEG SFTTLASLNE LEKIWAEYNV
AQEKIQTCLN ENEGNILIAE RNEVQQKLFV AVDVFILEVD DLPLDKRLKT LQDLATSLES
VYGKAKEGTN NSEETLRKFY DWQCTKREEF ASIRSETEAS LQHLVAWFQS SQKVFDLSLD
EPLTSEDLIG NIDEILEKTE SCVCKELELS LIEQGVIDKE IILSTYSQVL QKIHSEEKFI
ATLLSKYKDS VEFKKQMIDC LNKNPNVDYL LSIKKTLKGL KAQLRWKLVE KSNLEESDDH
DGTEIEKIKQ EITQLRNSVF QEIYHEREEY EKLNSLTQKW FPELPLLYPE IGLLKYMNSG
GLLTMSLERD LLDTEPMKEL SSKRPLVCSE VNGQPVLLKG YSVDVDTEGR VIQRAASYHR
ACGYAKEESG LLPLIFLFLC KSDPVAYLMV PYYPKANLSA VQASMPLTSE EALKVMKGVA
RGLHTLHSAN IIHGSLHQNN VFALNREQGI VGDYDFTKSE SQRASVNAMV GGLSLLSPEL
KTGKPPSASS DLYAYGCLFL WLSVQNQEFE TNEDGIPKVD QFHLDDNVKS LLCSLIYFRS
SMTAEQVLNA ECFLLPKGKS VPIPEKEIEC TQHSREDESK MESLDRYSEK TRNGEANP
