ID   MOS_HUMAN               Reviewed;         346 AA.
AC   P00540; Q3KPG9; Q3KPH0;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 205.
DE   RecName: Full=Proto-oncogene serine/threonine-protein kinase mos {ECO:0000305};
DE            EC=2.7.11.1;
DE   AltName: Full=Oocyte maturation factor mos;
DE   AltName: Full=Proto-oncogene c-Mos;
GN   Name=MOS {ECO:0000312|HGNC:HGNC:7199};
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].
RC   TISSUE=Placenta;
RX   PubMed=6287464; DOI=10.1073/pnas.79.13.4078;
RA   Watson R., Oskarsson M., Vande Woude G.F.;
RT   "Human DNA sequence homologous to the transforming gene (mos) of Moloney
RT   murine sarcoma virus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 79:4078-4082(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-105.
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   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH MAP2K1,
RP   INVOLVEMENT IN OZEMA20, VARIANTS OZEMA20 LYS-95; THR-139; HIS-246 AND
RP   320-CYS--GLY-346 DEL, AND CHARACTERIZATION OF VARIANTS OZEMA20 LYS-95;
RP   THR-139; HIS-246 AND 320-CYS--GLY-346 DEL.
RX   PubMed=34779126; DOI=10.15252/emmm.202114887;
RA   Zhang Y.L., Zheng W., Ren P., Hu H., Tong X., Zhang S.P., Li X., Wang H.,
RA   Jiang J.C., Jin J., Yang W., Cao L., He Y., Ma Y., Zhang Y., Gu Y., Hu L.,
RA   Luo K., Gong F., Lu G.X., Lin G., Fan H.Y., Zhang S.;
RT   "Biallelic mutations in MOS cause female infertility characterized by human
RT   early embryonic arrest and fragmentation.";
RL   EMBO Mol. Med. 13:e14887-e14887(2021).
RN   [4]
RP   VARIANTS [LARGE SCALE ANALYSIS] LEU-96; SER-105; THR-123 AND PRO-300.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
RN   [5]
RP   VARIANT OZEMA20 MET-197.
RX   PubMed=36403623; DOI=10.1080/09513590.2022.2147158;
RA   Jiao G., Lian H., Xing J., Chen L., Du Z., Liu X.;
RT   "MOS mutation causes female infertility with large polar body oocytes.";
RL   Gynecol. Endocrinol. 38:1158-1163(2022).
RN   [6]
RP   VARIANTS OZEMA20 LYS-95 AND HIS-319, CHARACTERIZATION OF VARIANTS OZEMA20
RP   LYS-95 AND HIS-319, AND FUNCTION.
RX   PubMed=34997960; DOI=10.1093/humrep/deab281;
RA   Zeng Y., Shi J., Xu S., Shi R., Wu T., Li H., Xue X., Zhu Y., Chen B.,
RA   Sang Q., Wang L.;
RT   "Bi-allelic mutations in MOS cause female infertility characterized by
RT   preimplantation embryonic arrest.";
RL   Hum. Reprod. 37:612-620(2022).
RN   [7]
RP   VARIANTS OZEMA20 LEU-199; CYS-264 AND VAL-292, CHARACTERIZATION LEU-199;
RP   CYS-264 AND VAL-292, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   MAP2K1.
RX   PubMed=35670744; DOI=10.1093/humrep/deac120;
RA   Zhang Y.L., Zheng W., Ren P., Jin J., Hu Z., Liu Q., Fan H.Y., Gong F.,
RA   Lu G.X., Lin G., Zhang S., Tong X.;
RT   "Biallelic variants in MOS cause large polar body in oocyte and human
RT   female infertility.";
RL   Hum. Reprod. 37:1932-1944(2022).
CC   -!- FUNCTION: Serine/threonine kinase involved in the regulation of MAPK
CC       signaling. Is an activator of the ERK1/2 signaling cascade playing an
CC       essential role in the stimulation of oocyte maturation.
CC       {ECO:0000269|PubMed:34779126, ECO:0000269|PubMed:34997960,
CC       ECO:0000269|PubMed:35670744}.
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   -!- SUBUNIT: Interacts with MAP2K1/MEK1. {ECO:0000269|PubMed:34779126,
CC       ECO:0000269|PubMed:35670744}.
CC   -!- INTERACTION:
CC       P00540; P35609: ACTN2; NbExp=3; IntAct=EBI-1757866, EBI-77797;
CC       P00540; Q9NWX5: ASB6; NbExp=3; IntAct=EBI-1757866, EBI-6425205;
CC       P00540; Q8WXE1: ATRIP; NbExp=3; IntAct=EBI-1757866, EBI-747353;
CC       P00540; Q8TD16-2: BICD2; NbExp=3; IntAct=EBI-1757866, EBI-11975051;
CC       P00540; Q96GS4: BORCS6; NbExp=4; IntAct=EBI-1757866, EBI-10193358;
CC       P00540; Q13137: CALCOCO2; NbExp=8; IntAct=EBI-1757866, EBI-739580;
CC       P00540; Q8NA61: CBY2; NbExp=3; IntAct=EBI-1757866, EBI-741724;
CC       P00540; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-1757866, EBI-11524851;
CC       P00540; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-1757866, EBI-10171570;
CC       P00540; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-1757866, EBI-10171416;
CC       P00540; O95273: CCNDBP1; NbExp=3; IntAct=EBI-1757866, EBI-748961;
CC       P00540; Q16543: CDC37; NbExp=2; IntAct=EBI-1757866, EBI-295634;
CC       P00540; Q8WWB3: DYDC1; NbExp=3; IntAct=EBI-1757866, EBI-740680;
CC       P00540; Q86YF9: DZIP1; NbExp=3; IntAct=EBI-1757866, EBI-998108;
CC       P00540; Q13451: FKBP5; NbExp=3; IntAct=EBI-1757866, EBI-306914;
CC       P00540; P14136: GFAP; NbExp=3; IntAct=EBI-1757866, EBI-744302;
CC       P00540; Q08379: GOLGA2; NbExp=6; IntAct=EBI-1757866, EBI-618309;
CC       P00540; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-1757866, EBI-11163335;
CC       P00540; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-1757866, EBI-5916454;
CC       P00540; O75791: GRAP2; NbExp=3; IntAct=EBI-1757866, EBI-740418;
CC       P00540; Q9NSC5: HOMER3; NbExp=8; IntAct=EBI-1757866, EBI-748420;
CC       P00540; P07900: HSP90AA1; NbExp=2; IntAct=EBI-1757866, EBI-296047;
CC       P00540; P08238: HSP90AB1; NbExp=2; IntAct=EBI-1757866, EBI-352572;
CC       P00540; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-1757866, EBI-11522367;
CC       P00540; Q8NC69: KCTD6; NbExp=3; IntAct=EBI-1757866, EBI-2511344;
CC       P00540; Q92845: KIFAP3; NbExp=3; IntAct=EBI-1757866, EBI-954040;
CC       P00540; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-1757866, EBI-2125614;
CC       P00540; A1A4E9: KRT13; NbExp=3; IntAct=EBI-1757866, EBI-10171552;
CC       P00540; P19012: KRT15; NbExp=6; IntAct=EBI-1757866, EBI-739566;
CC       P00540; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-1757866, EBI-3044087;
CC       P00540; Q15323: KRT31; NbExp=3; IntAct=EBI-1757866, EBI-948001;
CC       P00540; Q14525: KRT33B; NbExp=3; IntAct=EBI-1757866, EBI-1049638;
CC       P00540; O76011: KRT34; NbExp=3; IntAct=EBI-1757866, EBI-1047093;
CC       P00540; Q6A162: KRT40; NbExp=3; IntAct=EBI-1757866, EBI-10171697;
CC       P00540; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-1757866, EBI-11749135;
CC       P00540; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-1757866, EBI-741037;
CC       P00540; P36507: MAP2K2; NbExp=3; IntAct=EBI-1757866, EBI-1056930;
CC       P00540; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1757866, EBI-16439278;
CC       P00540; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-1757866, EBI-10172526;
CC       P00540; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-1757866, EBI-2548751;
CC       P00540; Q96QG7: MTMR9; NbExp=6; IntAct=EBI-1757866, EBI-744593;
CC       P00540; Q5JR59-3: MTUS2; NbExp=4; IntAct=EBI-1757866, EBI-11522433;
CC       P00540; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-1757866, EBI-22310682;
CC       P00540; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-1757866, EBI-79165;
CC       P00540; Q15172: PPP2R5A; NbExp=5; IntAct=EBI-1757866, EBI-641666;
CC       P00540; O43586: PSTPIP1; NbExp=3; IntAct=EBI-1757866, EBI-1050964;
CC       P00540; P53992: SEC24C; NbExp=4; IntAct=EBI-1757866, EBI-81134;
CC       P00540; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-1757866, EBI-2212028;
CC       P00540; Q9UNE7: STUB1; NbExp=2; IntAct=EBI-1757866, EBI-357085;
CC       P00540; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-1757866, EBI-11952721;
CC       P00540; Q13077: TRAF1; NbExp=6; IntAct=EBI-1757866, EBI-359224;
CC       P00540; Q12933: TRAF2; NbExp=3; IntAct=EBI-1757866, EBI-355744;
CC       P00540; P14373: TRIM27; NbExp=3; IntAct=EBI-1757866, EBI-719493;
CC       P00540; Q8N6Y0: USHBP1; NbExp=6; IntAct=EBI-1757866, EBI-739895;
CC       P00540; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-1757866, EBI-2515601;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:35670744}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in oocytes. Lower expression is
CC       detected in early embryo. {ECO:0000269|PubMed:34779126}.
CC   -!- DEVELOPMENTAL STAGE: Expression decreases after fertilization and is
CC       slightly increased in four-cell stage embryos. Expression gradually
CC       decreases from eight-cell to blastocyst embryos.
CC       {ECO:0000269|PubMed:34779126}.
CC   -!- DISEASE: Oocyte/zygote/embryo maturation arrest 20 (OZEMA20)
CC       [MIM:620383]: An autosomal recessive, female infertility disorder
CC       characterized by early embryonic arrest and fragmentation. Early embryo
CC       fragmentation is defined by the presence of anucleate cell fragments
CC       derived from the blastomeres. Excessive embryo fragmentation is
CC       associated with deleterious outcomes, including decreased implantation
CC       rate. {ECO:0000269|PubMed:34779126, ECO:0000269|PubMed:34997960,
CC       ECO:0000269|PubMed:35670744, ECO:0000269|PubMed:36403623}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; J00119; AAA52029.1; -; Genomic_DNA.
DR   EMBL; BC069569; AAH69569.1; -; mRNA.
DR   EMBL; BC069590; AAH69590.1; -; mRNA.
DR   EMBL; BC106737; AAI06738.1; -; mRNA.
DR   EMBL; BC106738; AAI06739.1; -; mRNA.
DR   CCDS; CCDS6164.1; -.
DR   PIR; A00649; TVHUMS.
DR   RefSeq; NP_005363.1; NM_005372.1.
DR   AlphaFoldDB; P00540; -.
DR   SMR; P00540; -.
DR   BioGRID; 110483; 74.
DR   IntAct; P00540; 84.
DR   MINT; P00540; -.
DR   STRING; 9606.ENSP00000310722; -.
DR   ChEMBL; CHEMBL1075184; -.
DR   iPTMnet; P00540; -.
DR   PhosphoSitePlus; P00540; -.
DR   BioMuta; MOS; -.
DR   DMDM; 125497; -.
DR   MassIVE; P00540; -.
DR   PaxDb; 9606-ENSP00000310722; -.
DR   PeptideAtlas; P00540; -.
DR   ProteomicsDB; 51265; -.
DR   Antibodypedia; 24550; 308 antibodies from 27 providers.
DR   DNASU; 4342; -.
DR   Ensembl; ENST00000311923.1; ENSP00000310722.1; ENSG00000172680.1.
DR   GeneID; 4342; -.
DR   KEGG; hsa:4342; -.
DR   MANE-Select; ENST00000311923.1; ENSP00000310722.1; NM_005372.1; NP_005363.1.
DR   UCSC; uc011leb.2; human.
DR   AGR; HGNC:7199; -.
DR   CTD; 4342; -.
DR   DisGeNET; 4342; -.
DR   GeneCards; MOS; -.
DR   HGNC; HGNC:7199; MOS.
DR   HPA; ENSG00000172680; Not detected.
DR   MalaCards; MOS; -.
DR   MIM; 190060; gene.
DR   MIM; 620383; phenotype.
DR   neXtProt; NX_P00540; -.
DR   OpenTargets; ENSG00000172680; -.
DR   PharmGKB; PA30907; -.
DR   VEuPathDB; HostDB:ENSG00000172680; -.
DR   eggNOG; KOG0192; Eukaryota.
DR   GeneTree; ENSGT00940000160233; -.
DR   HOGENOM; CLU_000288_7_35_1; -.
DR   InParanoid; P00540; -.
DR   OMA; WQMTTKE; -.
DR   OrthoDB; 54134at2759; -.
DR   PhylomeDB; P00540; -.
DR   TreeFam; TF331103; -.
DR   BRENDA; 2.7.10.2; 2681.
DR   PathwayCommons; P00540; -.
DR   SignaLink; P00540; -.
DR   SIGNOR; P00540; -.
DR   BioGRID-ORCS; 4342; 19 hits in 1185 CRISPR screens.
DR   GeneWiki; MOS_(gene); -.
DR   GenomeRNAi; 4342; -.
DR   Pharos; P00540; Tbio.
DR   PRO; PR:P00540; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; P00540; Protein.
DR   Bgee; ENSG00000172680; Expressed in oocyte and 13 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; ISS:UniProtKB.
DR   GO; GO:0004672; F: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; ISS:UniProtKB.
DR   GO; GO:0006325; P:chromatin organization; ISS:UniProtKB.
DR   GO; GO:0051296; P:establishment of meiotic spindle orientation; ISS:UniProtKB.
DR   GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0000212; P:meiotic spindle organization; ISS:UniProtKB.
DR   GO; GO:1902103; P:negative regulation of metaphase/anaphase transition of meiotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0001556; P:oocyte maturation; IMP:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0040020; P:regulation of meiotic nuclear division; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd13979; STKc_Mos; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; PTHR23257:SF706; PROTO-ONCOGENE SERINE_THREONINE-PROTEIN KINASE MOS; 1.
DR   PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000654; Integrin-linked_kinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; P00540; HS.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Disease variant; Kinase; Nucleotide-binding;
KW   Proto-oncogene; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..346
FT                   /note="Proto-oncogene serine/threonine-protein kinase mos"
FT                   /id="PRO_0000086344"
FT   DOMAIN          60..341
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        201
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         66..74
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   VARIANT         95
FT                   /note="N -> K (in OZEMA20; likely pathogenic; loss of
FT                   function in oocyte maturation activation; results in
FT                   severely decreased activation of the ERK1/ERK2 cascade)"
FT                   /evidence="ECO:0000269|PubMed:34779126,
FT                   ECO:0000269|PubMed:34997960"
FT                   /id="VAR_088642"
FT   VARIANT         96
FT                   /note="R -> L (in dbSNP:rs34532635)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040813"
FT   VARIANT         105
FT                   /note="A -> S (in dbSNP:rs35392772)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040814"
FT   VARIANT         123
FT                   /note="A -> T (in a lung adenocarcinoma sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040815"
FT   VARIANT         139
FT                   /note="M -> T (in OZEMA20; uncertain significance; results
FT                   in decreased activation of the ERK1/ERK2 cascade)"
FT                   /evidence="ECO:0000269|PubMed:34779126"
FT                   /id="VAR_088643"
FT   VARIANT         197
FT                   /note="I -> M (in OZEMA20; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36403623"
FT                   /id="VAR_088644"
FT   VARIANT         199
FT                   /note="H -> L (in OZEMA20; likely pathogenic; loss of
FT                   function in oocyte maturation activation; loss of
FT                   activation of the ERK1/ERK2 cascade; no effect on
FT                   localization to cytoplasm)"
FT                   /evidence="ECO:0000269|PubMed:35670744"
FT                   /id="VAR_088645"
FT   VARIANT         246
FT                   /note="R -> H (in OZEMA20; uncertain significance; results
FT                   in decreased activation of the ERK1/ERK2 cascade)"
FT                   /evidence="ECO:0000269|PubMed:34779126"
FT                   /id="VAR_088646"
FT   VARIANT         264
FT                   /note="S -> C (in OZEMA20; likely pathogenic; loss of
FT                   function in oocyte maturation activation; loss of
FT                   activation of the ERK1/ERK2 cascade; no effect on
FT                   localization to cytoplasm)"
FT                   /evidence="ECO:0000269|PubMed:35670744"
FT                   /id="VAR_088647"
FT   VARIANT         292
FT                   /note="A -> V (in OZEMA20; likely pathogenic; loss of
FT                   function in oocyte maturation activation; decreased
FT                   activation of the ERK1/ERK2 cascade; no effect on
FT                   localization to cytoplasm)"
FT                   /evidence="ECO:0000269|PubMed:35670744"
FT                   /id="VAR_088648"
FT   VARIANT         300
FT                   /note="S -> P (in dbSNP:rs56300224)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040816"
FT   VARIANT         319
FT                   /note="R -> H (in OZEMA20; likely pathogenic; results in
FT                   decreased activation of the ERK1/ERK2 cascade)"
FT                   /evidence="ECO:0000269|PubMed:34997960"
FT                   /id="VAR_088649"
FT   VARIANT         320..346
FT                   /note="Missing (in OZEMA20; likely pathogenic; loss of
FT                   function in oocyte maturation activation; loss of
FT                   activation of the ERK1/ERK2 cascade; severely decreased
FT                   interaction with MAP2K1)"
FT                   /evidence="ECO:0000269|PubMed:34779126"
FT                   /id="VAR_088650"
SQ   SEQUENCE   346 AA;  37820 MW;  68B1AB906ED4B308 CRC64;
     MPSPLALRPY LRSEFSPSVD ARPCSSPSEL PAKLLLGATL PRAPRLPRRL AWCSIDWEQV
     CLLQRLGAGG FGSVYKATYR GVPVAIKQVN KCTKNRLASR RSFWAELNVA RLRHDNIVRV
     VAASTRTPAG SNSLGTIIME FGGNVTLHQV IYGAAGHPEG DAGEPHCRTG GQLSLGKCLK
     YSLDVVNGLL FLHSQSIVHL DLKPANILIS EQDVCKISDF GCSEKLEDLL CFQTPSYPLG
     GTYTHRAPEL LKGEGVTPKA DIYSFAITLW QMTTKQAPYS GERQHILYAV VAYDLRPSLS
     AAVFEDSLPG QRLGDVIQRC WRPSAAQRPS ARLLLVDLTS LKAELG
//