SCML2_HUMAN
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 03-AUG-2022, entry version 182.
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; 50.
DR DIP; DIP-53760N; -.
DR IntAct; Q9UQR0; 27.
DR MINT; Q9UQR0; -.
DR STRING; 9606.ENSP00000251900; -.
DR GlyGen; Q9UQR0; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9UQR0; -.
DR MetOSite; Q9UQR0; -.
DR PhosphoSitePlus; Q9UQR0; -.
DR BioMuta; SCML2; -.
DR DMDM; 47117338; -.
DR EPD; Q9UQR0; -.
DR jPOST; Q9UQR0; -.
DR MassIVE; Q9UQR0; -.
DR MaxQB; Q9UQR0; -.
DR PaxDb; Q9UQR0; -.
DR PeptideAtlas; Q9UQR0; -.
DR PRIDE; Q9UQR0; -.
DR ProteomicsDB; 85572; -. [Q9UQR0-1]
DR ProteomicsDB; 85573; -. [Q9UQR0-2]
DR ABCD; Q9UQR0; 12 sequenced antibodies.
DR Antibodypedia; 475; 195 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 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; PKPVPNC; -.
DR OrthoDB; 229086at2759; -.
DR PhylomeDB; Q9UQR0; -.
DR TreeFam; TF106488; -.
DR PathwayCommons; Q9UQR0; -.
DR SignaLink; Q9UQR0; -.
DR BioGRID-ORCS; 10389; 10 hits in 707 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 175 other tissues.
DR ExpressionAtlas; Q9UQR0; baseline and differential.
DR Genevisible; Q9UQR0; HS.
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 transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.90.1150.190; -; 1.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR033763; SCML2_RBR.
DR InterPro; IPR021987; SLED.
DR InterPro; IPR038348; SLED_sf.
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; SSF47769; 1.
DR PROSITE; PS51079; MBT; 2.
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
