ID   SCML2_HUMAN             Reviewed;         700 AA.
AC   Q9UQR0; Q5JXE6; Q86U98; Q8IWD0; Q8NDP2; Q9UGC5;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 190.
DE   RecName: Full=Sex comb on midleg-like protein 2;
GN   Name=SCML2;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=10331946; DOI=10.1006/geno.1999.5755;
RA   Montini E., Buchner G., Spalluto C., Andolfi G., Caruso A., de Dunnen J.T.,
RA   Trump D., Rocchi M., Ballabio A., Franco B.;
RT   "Identification of SCML2, a second human gene homologous to the Drosophila
RT   Sex comb on midleg (Scm): a new gene cluster on Xp22.";
RL   Genomics 58:65-72(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis, and Uterus;
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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256; SER-267; SER-299;
RP   SER-300; THR-305; SER-499; THR-503; SER-511; SER-583; SER-590 AND SER-594,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499; SER-511 AND SER-590, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499; THR-503; SER-511 AND
RP   SER-590, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499; SER-511 AND SER-590, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256; SER-261; SER-267;
RP   SER-499; SER-511; SER-522; SER-570; SER-583 AND SER-590, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [15]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-536, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [16]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-518; LYS-536; LYS-599 AND
RP   LYS-605, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 33-243.
RX   PubMed=12952983; DOI=10.1074/jbc.m306469200;
RA   Sathyamurthy A., Allen M.D., Murzin A.G., Bycroft M.;
RT   "Crystal structure of the malignant brain tumor (MBT) repeats in sex comb
RT   on midleg-like 2 (SCML2).";
RL   J. Biol. Chem. 278:46968-46973(2003).
CC   -!- FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins act by
CC       forming multiprotein complexes, which are required to maintain the
CC       transcriptionally repressive state of homeotic genes throughout
CC       development (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9UQR0; Q9H9S4: CAB39L; NbExp=3; IntAct=EBI-2513111, EBI-1047244;
CC       Q9UQR0; P24941: CDK2; NbExp=3; IntAct=EBI-2513111, EBI-375096;
CC       Q9UQR0; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-2513111, EBI-739832;
CC       Q9UQR0; O43639: NCK2; NbExp=3; IntAct=EBI-2513111, EBI-713635;
CC       Q9UQR0; P78317: RNF4; NbExp=3; IntAct=EBI-2513111, EBI-2340927;
CC       Q9UQR0; Q5VUG0: SFMBT2; NbExp=3; IntAct=EBI-2513111, EBI-12025260;
CC       Q9UQR0; A0A286YEY3: SRGAP2B; NbExp=3; IntAct=EBI-2513111, EBI-17766455;
CC       Q9UQR0-1; P24941: CDK2; NbExp=7; IntAct=EBI-16087037, EBI-375096;
CC       Q9UQR0-1; P38936: CDKN1A; NbExp=3; IntAct=EBI-16087037, EBI-375077;
CC       Q9UQR0-1; P46527: CDKN1B; NbExp=2; IntAct=EBI-16087037, EBI-519280;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UQR0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UQR0-2; Sequence=VSP_010277;
CC   -!- TISSUE SPECIFICITY: Highly expressed in placenta, thymus and testis.
CC       Detected at lower levels in brain, liver, skeletal muscle, pancreas and
CC       ovary. {ECO:0000269|PubMed:10331946}.
CC   -!- SIMILARITY: Belongs to the SCM family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH51913.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Y18004; CAB38943.1; -; mRNA.
DR   EMBL; AL833937; CAD38792.1; -; mRNA.
DR   EMBL; AL096763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL031007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z93023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC040497; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CH471074; EAW98937.1; -; Genomic_DNA.
DR   EMBL; BC051913; AAH51913.1; ALT_INIT; mRNA.
DR   EMBL; BC064617; AAH64617.1; -; mRNA.
DR   CCDS; CCDS14185.1; -. [Q9UQR0-1]
DR   RefSeq; NP_006080.1; NM_006089.2. [Q9UQR0-1]
DR   RefSeq; XP_016884708.1; XM_017029219.1. [Q9UQR0-1]
DR   RefSeq; XP_016884709.1; XM_017029220.1. [Q9UQR0-1]
DR   PDB; 1OI1; X-ray; 1.78 A; A=24-243.
DR   PDB; 2BIV; X-ray; 1.70 A; A/B/C=1-243.
DR   PDB; 2MEM; NMR; -; A=354-468.
DR   PDB; 2VYT; X-ray; 1.90 A; A/B=24-243.
DR   PDB; 4EDU; X-ray; 2.58 A; A=29-243.
DR   PDBsum; 1OI1; -.
DR   PDBsum; 2BIV; -.
DR   PDBsum; 2MEM; -.
DR   PDBsum; 2VYT; -.
DR   PDBsum; 4EDU; -.
DR   AlphaFoldDB; Q9UQR0; -.
DR   BMRB; Q9UQR0; -.
DR   SMR; Q9UQR0; -.
DR   BioGRID; 115661; 64.
DR   DIP; DIP-53760N; -.
DR   IntAct; Q9UQR0; 29.
DR   MINT; Q9UQR0; -.
DR   STRING; 9606.ENSP00000251900; -.
DR   GlyCosmos; Q9UQR0; 2 sites, 1 glycan.
DR   GlyGen; Q9UQR0; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q9UQR0; -.
DR   MetOSite; Q9UQR0; -.
DR   PhosphoSitePlus; Q9UQR0; -.
DR   SwissPalm; Q9UQR0; -.
DR   BioMuta; SCML2; -.
DR   DMDM; 47117338; -.
DR   EPD; Q9UQR0; -.
DR   jPOST; Q9UQR0; -.
DR   MassIVE; Q9UQR0; -.
DR   MaxQB; Q9UQR0; -.
DR   PaxDb; 9606-ENSP00000251900; -.
DR   PeptideAtlas; Q9UQR0; -.
DR   ProteomicsDB; 85572; -. [Q9UQR0-1]
DR   ProteomicsDB; 85573; -. [Q9UQR0-2]
DR   Pumba; Q9UQR0; -.
DR   ABCD; Q9UQR0; 11 sequenced antibodies.
DR   Antibodypedia; 475; 225 antibodies from 28 providers.
DR   DNASU; 10389; -.
DR   Ensembl; ENST00000251900.9; ENSP00000251900.4; ENSG00000102098.19. [Q9UQR0-1]
DR   Ensembl; ENST00000398048.4; ENSP00000381126.4; ENSG00000102098.19. [Q9UQR0-2]
DR   GeneID; 10389; -.
DR   KEGG; hsa:10389; -.
DR   MANE-Select; ENST00000251900.9; ENSP00000251900.4; NM_006089.3; NP_006080.1.
DR   UCSC; uc004cyl.3; human. [Q9UQR0-1]
DR   AGR; HGNC:10581; -.
DR   CTD; 10389; -.
DR   DisGeNET; 10389; -.
DR   GeneCards; SCML2; -.
DR   HGNC; HGNC:10581; SCML2.
DR   HPA; ENSG00000102098; Tissue enhanced (testis).
DR   MIM; 300208; gene.
DR   neXtProt; NX_Q9UQR0; -.
DR   OpenTargets; ENSG00000102098; -.
DR   PharmGKB; PA34999; -.
DR   VEuPathDB; HostDB:ENSG00000102098; -.
DR   eggNOG; KOG3766; Eukaryota.
DR   GeneTree; ENSGT00940000159407; -.
DR   HOGENOM; CLU_015000_1_0_1; -.
DR   InParanoid; Q9UQR0; -.
DR   OMA; TEEPICC; -.
DR   OrthoDB; 2908161at2759; -.
DR   PhylomeDB; Q9UQR0; -.
DR   TreeFam; TF106488; -.
DR   PathwayCommons; Q9UQR0; -.
DR   SignaLink; Q9UQR0; -.
DR   BioGRID-ORCS; 10389; 11 hits in 782 CRISPR screens.
DR   ChiTaRS; SCML2; human.
DR   EvolutionaryTrace; Q9UQR0; -.
DR   GenomeRNAi; 10389; -.
DR   Pharos; Q9UQR0; Tbio.
DR   PRO; PR:Q9UQR0; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q9UQR0; Protein.
DR   Bgee; ENSG00000102098; Expressed in diaphragm and 177 other cell types or tissues.
DR   ExpressionAtlas; Q9UQR0; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IMP:GO_Central.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central.
DR   CDD; cd20109; MBT_SCML2_rpt2; 1.
DR   CDD; cd09578; SAM_Scm; 1.
DR   Gene3D; 2.30.30.140; -; 2.
DR   Gene3D; 3.90.1150.190; SLED domain; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR004092; Mbt.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR047531; SAM_Scm-like.
DR   InterPro; IPR033763; SCML2_RBR.
DR   InterPro; IPR021987; SLED.
DR   InterPro; IPR038348; SLED_sf.
DR   PANTHER; PTHR12247; POLYCOMB GROUP PROTEIN; 1.
DR   PANTHER; PTHR12247:SF84; SEX COMB ON MIDLEG-LIKE PROTEIN 2; 1.
DR   Pfam; PF02820; MBT; 2.
DR   Pfam; PF17208; RBR; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   Pfam; PF12140; SLED; 1.
DR   SMART; SM00561; MBT; 2.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR   PROSITE; PS51079; MBT; 2.
DR   Genevisible; Q9UQR0; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..700
FT                   /note="Sex comb on midleg-like protein 2"
FT                   /id="PRO_0000097628"
FT   REPEAT          33..131
FT                   /note="MBT 1"
FT   REPEAT          139..240
FT                   /note="MBT 2"
FT   DOMAIN          631..700
FT                   /note="SAM"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          253..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..495
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..589
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         256
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         261
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         267
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         299
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         300
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         305
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         499
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         503
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         511
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         522
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         570
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         583
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         590
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         594
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   CROSSLNK        518
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        536
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        599
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        605
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..562
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_010277"
FT   HELIX           35..42
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   HELIX           49..51
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   STRAND          76..89
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   STRAND          92..97
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   STRAND          106..109
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:4EDU"
FT   HELIX           120..123
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   HELIX           141..149
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   HELIX           157..159
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   STRAND          177..181
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   STRAND          189..198
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   STRAND          201..206
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   HELIX           211..213
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   STRAND          215..218
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   HELIX           229..233
FT                   /evidence="ECO:0007829|PDB:2BIV"
FT   STRAND          356..359
FT                   /evidence="ECO:0007829|PDB:2MEM"
FT   STRAND          369..371
FT                   /evidence="ECO:0007829|PDB:2MEM"
FT   HELIX           373..378
FT                   /evidence="ECO:0007829|PDB:2MEM"
FT   STRAND          383..387
FT                   /evidence="ECO:0007829|PDB:2MEM"
FT   HELIX           388..402
FT                   /evidence="ECO:0007829|PDB:2MEM"
FT   HELIX           406..409
FT                   /evidence="ECO:0007829|PDB:2MEM"
FT   STRAND          422..427
FT                   /evidence="ECO:0007829|PDB:2MEM"
FT   STRAND          430..435
FT                   /evidence="ECO:0007829|PDB:2MEM"
FT   HELIX           442..455
FT                   /evidence="ECO:0007829|PDB:2MEM"
SQ   SEQUENCE   700 AA;  77257 MW;  05E086D4928DEE73 CRC64;
     MGQTVNEDSM DVKKENQEKT PQSSTSSVQR DDFHWEEYLK ETGSISAPSE CFRQSQIPPV
     NDFKVGMKLE ARDPRNATSV CIATVIGITG ARLRLRLDGS DNRNDFWRLV DSPDIQPVGT
     CEKEGDLLQP PLGYQMNTSS WPMFLLKTLN GSEMASATLF KKEPPKPPLN NFKVGMKLEA
     IDKKNPYLIC PATIGDVKGD EVHITFDGWS GAFDYWCKYD SRDIFPAGWC RLTGDVLQPP
     GTSVPIVKNI AKTESSPSEA SQHSMQSPQK TTLILPTQQV RRSSRIKPPG PTAVPKRSSS
     VKNITPRKKG PNSGKKEKPL PVICSTSAAS LKSLTRDRGM LYKDVASGPC KIVMSTVCVY
     VNKHGNFGPH LDPKRIQQLP DHFGPGPVNV VLRRIVQACV DCALETKTVF GYLKPDNRGG
     EVITASFDGE THSIQLPPVN SASFALRFLE NFCHSLQCDN LLSSQPFSSS RGHTHSSAEH
     DKNQSAKEDV TERQSTKRSP QQTVPYVVPL SPKLPKTKEY ASEGEPLFAG GSAIPKEENL
     SEDSKSSSLN SGNYLNPACR NPMYIHTSVS QDFSRSVPGT TSSPLVGDIS PKSSPHEVKF
     QMQRKSEAPS YIAVPDPSVL KQGFSKDPST WSVDEVIQFM KHTDPQISGP LADLFRQHEI
     DGKALFLLKS DVMMKYMGLK LGPALKLCYY IEKLKEGKYS
//