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RecName: Full=Dual specificity mitogen-activated protein kinase kinase dSOR1; Short=Downstream of RAF; Short=MAPKK

UniProtKB/Swiss-Prot: Q24324.2

Identical Proteins FASTA Graphics 

LOCUS       DSOR1_DROME              396 aa            linear   INV 27-NOV-2024
DEFINITION  RecName: Full=Dual specificity mitogen-activated protein kinase
            kinase dSOR1; Short=Downstream of RAF; Short=MAPKK.
ACCESSION   Q24324
VERSION     Q24324.2
DBSOURCE    UniProtKB: locus DSOR1_DROME, accession Q24324;
            class: standard.
            extra accessions:Q8ISE0,Q9W360
            created: Nov 1, 1997.
            sequence updated: Aug 16, 2005.
            annotation updated: Nov 27, 2024.
            xrefs: D13782.1, BAA02925.1, AY135075.1, AAN17587.1, AY135076.1,
            AAN17588.1, AY135077.1, AAN17589.1, AY135078.1, AAN17590.1,
            AY135079.1, AAN17591.1, AY135080.1, AAN17592.1, AY135081.1,
            AAN17593.1, AY135082.1, AAN17594.1, AY135083.1, AAN17595.1,
            AY135084.1, AAN17596.1, AY135085.1, AAN17597.1, AY135086.1,
            AAN17598.1, AY135087.1, AAN17599.1, AY135088.1, AAN17600.1,
            AY135089.1, AAN17601.1, AY135090.1, AAN17602.1, AY135091.1,
            AAN17603.1, AY135092.1, AAN17604.1, AY135093.1, AAN17605.1,
            AE014298.5, AAF46475.1, AY058692.1, AAL13921.1, A45176,
            NP_001285044.1, NP_511098.1, 8BW9_C
            xrefs (non-sequence databases): PDBsum:8BW9, AlphaFoldDB:Q24324,
            EMDB:EMD-16281, SMR:Q24324, BioGRID:58322, DIP:DIP-29770N,
            IntAct:Q24324, MINT:Q24324, STRING:7227.FBpp0071248,
            iPTMnet:Q24324, PaxDb:7227-FBpp0071248, EnsemblMetazoa:FBtr0071313,
            EnsemblMetazoa:FBpp0071248, EnsemblMetazoa:FBgn0010269,
            GeneID:31872, KEGG:dme:Dmel_CG15793, AGR:FB:FBgn0010269, CTD:31872,
            FlyBase:FBgn0010269, VEuPathDB:VectorBase:FBgn0010269,
            eggNOG:KOG0581, GeneTree:ENSGT00940000153487, InParanoid:Q24324,
            OMA:ENKYHDL, OrthoDB:2900742at2759, PhylomeDB:Q24324,
            BRENDA:2.4.1.222, BRENDA:2.7.12.2, Reactome:R-DME-110056,
            Reactome:R-DME-112411, Reactome:R-DME-170968,
            Reactome:R-DME-209190, Reactome:R-DME-209214,
            Reactome:R-DME-432553, Reactome:R-DME-445144,
            Reactome:R-DME-5673000, Reactome:R-DME-5674135,
            Reactome:R-DME-5674499, SignaLink:Q24324, BioGRID-ORCS:31872,
            GenomeRNAi:31872, PRO:PR:Q24324, Proteomes:UP000000803,
            Bgee:FBgn0010269, ExpressionAtlas:Q24324, GO:0000793, GO:0005829,
            GO:0005524, GO:0019900, GO:0004708, GO:0106310, GO:0004674,
            GO:0004713, GO:0007298, GO:0071481, GO:0051607, GO:0008340,
            GO:0009953, GO:0007173, GO:0070371, GO:0008543, GO:0042386,
            GO:0008286, GO:0000165, GO:0033314, GO:0007095, GO:0042461,
            GO:0006468, GO:0007465, GO:0045500, GO:0007430, GO:0007362,
            GO:0008293, GO:0048010, CDD:cd06615, FunFam:1.10.510.10:FF:000115,
            FunFam:3.30.200.20:FF:000100, Gene3D:1.10.510.10,
            InterPro:IPR011009, InterPro:IPR050915, InterPro:IPR000719,
            InterPro:IPR017441, InterPro:IPR008271, PANTHER:PTHR47448,
            PANTHER:PTHR47448:SF1, Pfam:PF00069, SMART:SM00220,
            SUPFAM:SSF56112, PROSITE:PS00107, PROSITE:PS50011, PROSITE:PS00108
KEYWORDS    3D-structure; ATP-binding; Developmental protein; Kinase;
            Nucleotide-binding; Phosphoprotein; Reference proteome;
            Serine/threonine-protein kinase; Transferase; Tyrosine-protein
            kinase.
SOURCE      Drosophila melanogaster (fruit fly)
  ORGANISM  Drosophila melanogaster
            Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
            Pterygota; Neoptera; Endopterygota; Diptera; Brachycera;
            Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Tsuda,L., Inoue,Y.H., Yoo,M.A., Mizuno,M., Hata,M., Lim,Y.M.,
            Adachi-Yamada,T., Ryo,H., Masamune,Y. and Nishida,Y.
  TITLE     A protein kinase similar to MAP kinase activator acts downstream of
            the raf kinase in Drosophila
  JOURNAL   Cell 72 (3), 407-414 (1993)
   PUBMED   8381718
  REMARK    NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL
            STAGE.
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Riley,R.M., Jin,W. and Gibson,G.
  TITLE     Contrasting selection pressures on components of the Ras-mediated
            signal transduction pathway in Drosophila
  JOURNAL   Mol Ecol 12 (5), 1315-1323 (2003)
   PUBMED   12694293
  REMARK    NUCLEOTIDE SEQUENCE [GENOMIC DNA].;
            STRAIN=5-17-88#b1, 5-17-88a#4, 5-17-88a#6, 5-17-88b#1, 5-17-88b#5,
            7-21-88#b2, 7-21-88b#1, 7-21-88b#2, 7-21-88b#4, AA1, AA16, AA18,
            AA20, AA3, CA2, M2, PYR2, Reids2, and wild5b
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Adams,M.D., Celniker,S.E., Holt,R.A., Evans,C.A., Gocayne,J.D.,
            Amanatides,P.G., Scherer,S.E., Li,P.W., Hoskins,R.A., Galle,R.F.,
            George,R.A., Lewis,S.E., Richards,S., Ashburner,M., Henderson,S.N.,
            Sutton,G.G., Wortman,J.R., Yandell,M.D., Zhang,Q., Chen,L.X.,
            Brandon,R.C., Rogers,Y.H., Blazej,R.G., Champe,M., Pfeiffer,B.D.,
            Wan,K.H., Doyle,C., Baxter,E.G., Helt,G., Nelson,C.R., Gabor,G.L.,
            Abril,J.F., Agbayani,A., An,H.J., Andrews-Pfannkoch,C., Baldwin,D.,
            Ballew,R.M., Basu,A., Baxendale,J., Bayraktaroglu,L., Beasley,E.M.,
            Beeson,K.Y., Benos,P.V., Berman,B.P., Bhandari,D., Bolshakov,S.,
            Borkova,D., Botchan,M.R., Bouck,J., Brokstein,P., Brottier,P.,
            Burtis,K.C., Busam,D.A., Butler,H., Cadieu,E., Center,A.,
            Chandra,I., Cherry,J.M., Cawley,S., Dahlke,C., Davenport,L.B.,
            Davies,P., de Pablos,B., Delcher,A., Deng,Z., Mays,A.D., Dew,I.,
            Dietz,S.M., Dodson,K., Doup,L.E., Downes,M., Dugan-Rocha,S.,
            Dunkov,B.C., Dunn,P., Durbin,K.J., Evangelista,C.C., Ferraz,C.,
            Ferriera,S., Fleischmann,W., Fosler,C., Gabrielian,A.E., Garg,N.S.,
            Gelbart,W.M., Glasser,K., Glodek,A., Gong,F., Gorrell,J.H., Gu,Z.,
            Guan,P., Harris,M., Harris,N.L., Harvey,D., Heiman,T.J.,
            Hernandez,J.R., Houck,J., Hostin,D., Houston,K.A., Howland,T.J.,
            Wei,M.H., Ibegwam,C., Jalali,M., Kalush,F., Karpen,G.H., Ke,Z.,
            Kennison,J.A., Ketchum,K.A., Kimmel,B.E., Kodira,C.D., Kraft,C.,
            Kravitz,S., Kulp,D., Lai,Z., Lasko,P., Lei,Y., Levitsky,A.A.,
            Li,J., Li,Z., Liang,Y., Lin,X., Liu,X., Mattei,B., McIntosh,T.C.,
            McLeod,M.P., McPherson,D., Merkulov,G., Milshina,N.V., Mobarry,C.,
            Morris,J., Moshrefi,A., Mount,S.M., Moy,M., Murphy,B., Murphy,L.,
            Muzny,D.M., Nelson,D.L., Nelson,D.R., Nelson,K.A., Nixon,K.,
            Nusskern,D.R., Pacleb,J.M., Palazzolo,M., Pittman,G.S., Pan,S.,
            Pollard,J., Puri,V., Reese,M.G., Reinert,K., Remington,K.,
            Saunders,R.D., Scheeler,F., Shen,H., Shue,B.C., Siden-Kiamos,I.,
            Simpson,M., Skupski,M.P., Smith,T., Spier,E., Spradling,A.C.,
            Stapleton,M., Strong,R., Sun,E., Svirskas,R., Tector,C., Turner,R.,
            Venter,E., Wang,A.H., Wang,X., Wang,Z.Y., Wassarman,D.A.,
            Weinstock,G.M., Weissenbach,J., Williams,S.M., WoodageT,
            Worley,K.C., Wu,D., Yang,S., Yao,Q.A., Ye,J., Yeh,R.F.,
            Zaveri,J.S., Zhan,M., Zhang,G., Zhao,Q., Zheng,L., Zheng,X.H.,
            Zhong,F.N., Zhong,W., Zhou,X., Zhu,S., Zhu,X., Smith,H.O.,
            Gibbs,R.A., Myers,E.W., Rubin,G.M. and Venter,J.C.
  TITLE     The genome sequence of Drosophila melanogaster
  JOURNAL   Science 287 (5461), 2185-2195 (2000)
   PUBMED   10731132
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].;
            STRAIN=Berkeley
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Misra,S., Crosby,M.A., Mungall,C.J., Matthews,B.B., Campbell,K.S.,
            Hradecky,P., Huang,Y., Kaminker,J.S., Millburn,G.H., Prochnik,S.E.,
            Smith,C.D., Tupy,J.L., Whitfied,E.J., Bayraktaroglu,L.,
            Berman,B.P., Bettencourt,B.R., Celniker,S.E., de Grey,A.D.,
            Drysdale,R.A., Harris,N.L., Richter,J., Russo,S., Schroeder,A.J.,
            Shu,S.Q., Stapleton,M., Yamada,C., Ashburner,M., Gelbart,W.M.,
            Rubin,G.M. and Lewis,S.E.
  TITLE     Annotation of the Drosophila melanogaster euchromatic genome: a
            systematic review
  JOURNAL   Genome Biol 3 (12), RESEARCH0083 (2002)
   PUBMED   12537572
  REMARK    GENOME REANNOTATION.;
            STRAIN=Berkeley
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Stapleton,M., Carlson,J., Brokstein,P., Yu,C., Champe,M.,
            George,R., Guarin,H., Kronmiller,B., Pacleb,J., Park,S., Wan,K.,
            Rubin,G.M. and Celniker,S.E.
  TITLE     A Drosophila full-length cDNA resource
  JOURNAL   Genome Biol 3 (12), RESEARCH0080 (2002)
   PUBMED   12537569
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            STRAIN=Berkeley; TISSUE=Embryo
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Lavoie,H., Sahmi,M., Maisonneuve,P., Marullo,S.A., Thevakumaran,N.,
            Jin,T., Kurinov,I., Sicheri,F. and Therrien,M.
  TITLE     MEK drives BRAF activation through allosteric control of KSR
            proteins
  JOURNAL   Nature 554 (7693), 549-553 (2018)
   PUBMED   29433126
  REMARK    INTERACTION WITH KSR AND RAF, AND PHOSPHORYLATION AT SER-237 AND
            SER-241.
COMMENT     On or before Jan 24, 2006 this sequence version replaced
            gi:75016286, gi:75027901, gi:2499636.
            [FUNCTION] Required downstream of Raf in the sevenless (sev), torso
            (tor), and Drosophila EGF receptor homolog (DER) signal
            transduction pathways. Involved in both positive regulation (at the
            posterior terminus) and negative regulation (at the anterior
            domain) of tll, as in other terminal class gene products, maybe via
            the ERK-A kinase. {ECO:0000269|PubMed:8381718}.
            [CATALYTIC ACTIVITY] Reaction=L-seryl-[protein] + ATP =
            O-phospho-L-seryl-[protein] + ADP + H(+); Xref=Rhea:RHEA:17989,
            Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378,
            ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
            ChEBI:CHEBI:456216; EC=2.7.12.2.
            [CATALYTIC ACTIVITY] Reaction=L-threonyl-[protein] + ATP =
            O-phospho-L-threonyl-[protein] + ADP + H(+); Xref=Rhea:RHEA:46608,
            Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378,
            ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
            ChEBI:CHEBI:456216; EC=2.7.12.2.
            [CATALYTIC ACTIVITY] Reaction=L-tyrosyl-[protein] + ATP =
            O-phospho-L-tyrosyl-[protein] + ADP + H(+); Xref=Rhea:RHEA:10596,
            Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378,
            ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620,
            ChEBI:CHEBI:456216; EC=2.7.12.2.
            [SUBUNIT] Interacts with Raf and ksr; Dsor1 binding to ksr probably
            promotes ksr and Raf dimerization and ksr-mediated Raf
            transactivation. {ECO:0000269|PubMed:29433126}.
            [INTERACTION] Q24324; P11346: Raf; NbExp=4; IntAct=EBI-671282,
            EBI-664624.
            [DEVELOPMENTAL STAGE] Expressed both maternally and zygotically.
            {ECO:0000269|PubMed:8381718}.
            [PTM] Phosphorylation on Ser/Thr by MAP kinase kinase kinases
            regulates positively the kinase activity. {ECO:0000250}.
            [SIMILARITY] Belongs to the protein kinase superfamily. STE Ser/Thr
            protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
            [SEQUENCE CAUTION] Sequence=BAA02925.1; Type=Erroneous gene model
            prediction; Evidence={ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Drosophila melanogaster"
                     /db_xref="taxon:7227"
     gene            1..396
                     /gene="Dsor1"
                     /locus_tag="CG15793"
     Protein         1..396
                     /product="Dual specificity mitogen-activated protein
                     kinase kinase dSOR1"
                     /EC_number="2.7.12.2"
                     /note="Downstream of RAF; MAPKK"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..396
                     /region_name="Mature chain"
                     /note="Dual specificity mitogen-activated protein kinase
                     kinase dSOR1. /id=PRO_0000085928."
     Region          25..44
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          29..43
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          84..86
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Region          85..382
                     /region_name="PKc_MEK"
                     /note="Catalytic domain of the dual-specificity Protein
                     Kinase, Mitogen-Activated Protein (MAP)/Extracellular
                     signal-Regulated Kinase (ERK) Kinase; cd06615"
                     /db_xref="CDD:132946"
     Region          87..364
                     /region_name="Domain"
                     /note="Protein kinase.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00159."
     Site            order(93..97,101,114,116,146,162..165,168..169,172,209,
                     211..214,216,226..227,230,242..245,247,274,283)
                     /site_type="active"
                     /db_xref="CDD:132946"
     Site            order(93..97,99,101,114,116,146,162..165,168..169,
                     171..172,211,213..214,216,227)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:132946"
     Region          95..99
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Site            order(96..97,209,211..213,230,242..245,247,274,283)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:132946"
     Site            order(97,116,134,137,146,160,162,227..231,234,238)
                     /site_type="other"
                     /note="noncompetitive inhibitor binding site [chemical
                     binding]"
                     /db_xref="CDD:132946"
     Site            order(100,120..121,156,249,253..256,314,317..318,321..322)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:132946"
     Region          116..119
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Region          124..131
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Region          135..138
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Region          148..154
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Region          157..163
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Region          170..177
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Region          182..203
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Site            209
                     /site_type="active"
                     /note="Proton acceptor.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00159,
                     ECO:0000255|PROSITE-ProRule:PRU10027."
     Region          219..221
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Site            226..247
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:132946"
     Region          232..236
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine; by RAF.
                     /evidence=ECO:0000269|PubMed:29433126."
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine; by RAF.
                     /evidence=ECO:0000269|PubMed:29433126."
     Region          251..256
                     /region_name="Hydrogen bonded turn"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Region          262..277
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Region          313..322
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Region          335..344
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Region          349..351
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Region          355..358
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Region          362..369
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Region          374..381
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:8BW9."
     Region          394
                     /region_name="Variant"
                     /note="S -> L (in strain: Reids2)."
ORIGIN      
        1 msknklnlvl ppvnteatva aatvaptppf ktpsgtdths llgkpktsid altetlegld
       61 mgdterkrik mflsqkekig elsdedlekl gelgsgnggv vmkvrhthth limarklihl
      121 evkpaikkqi lrelkvlhec nfphivgfyg afysdgeisi cmeymdggsl dlilkragri
      181 pesilgritl avlkglsylr dnhaiihrdv kpsnilvnss geikicdfgv sgqlidsman
      241 sfvgtrsyms perlqgthys vqsdiwslgl slvemaigmy pipppntatl esifadnaee
      301 sgqptdepra maifelldyi vnepppkleh kifstefkdf vdiclkkqpd eradlktlls
      361 hpwirkaele evdisgwvck tmdlppstpk rntspn
//
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