MSD2_HUMAN
ID MSD2_HUMAN Reviewed; 559 AA.
AC Q6P1R3; B3KRY6; Q9H042; Q9H5K8;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Myb/SANT-like DNA-binding domain-containing protein 2;
GN Name=MSANTD2; Synonyms=C11orf61;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Hepatoma, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymph node;
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 MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-48, AND
RP IDENTIFICATION 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 [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-268, 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 [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-268, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-268 AND LYS-343, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-268 AND LYS-343, AND
RP 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).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6P1R3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P1R3-2; Sequence=VSP_022705;
CC Name=3;
CC IsoId=Q6P1R3-3; Sequence=VSP_022706;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK026995; BAB15618.1; -; mRNA.
DR EMBL; AK092413; BAG52548.1; -; mRNA.
DR EMBL; AL512691; CAC21648.1; -; mRNA.
DR EMBL; BC064919; AAH64919.1; -; mRNA.
DR CCDS; CCDS73408.1; -. [Q6P1R3-2]
DR CCDS; CCDS76491.1; -. [Q6P1R3-1]
DR CCDS; CCDS8454.1; -. [Q6P1R3-3]
DR RefSeq; NP_001294956.1; NM_001308027.1. [Q6P1R3-1]
DR RefSeq; NP_001299848.1; NM_001312919.1.
DR RefSeq; NP_001299849.1; NM_001312920.1. [Q6P1R3-2]
DR RefSeq; NP_001299850.1; NM_001312921.1. [Q6P1R3-2]
DR RefSeq; NP_078907.2; NM_024631.3. [Q6P1R3-3]
DR RefSeq; XP_006718968.1; XM_006718905.1. [Q6P1R3-2]
DR RefSeq; XP_006718969.1; XM_006718906.3. [Q6P1R3-2]
DR RefSeq; XP_016873784.1; XM_017018295.1.
DR RefSeq; XP_016873785.1; XM_017018296.1. [Q6P1R3-2]
DR RefSeq; XP_016873786.1; XM_017018297.1. [Q6P1R3-2]
DR RefSeq; XP_016873787.1; XM_017018298.1. [Q6P1R3-2]
DR RefSeq; XP_016873788.1; XM_017018299.1.
DR AlphaFoldDB; Q6P1R3; -.
DR BioGRID; 122807; 13.
DR IntAct; Q6P1R3; 12.
DR STRING; 9606.ENSP00000239614; -.
DR iPTMnet; Q6P1R3; -.
DR PhosphoSitePlus; Q6P1R3; -.
DR BioMuta; MSANTD2; -.
DR DMDM; 74737168; -.
DR EPD; Q6P1R3; -.
DR jPOST; Q6P1R3; -.
DR MassIVE; Q6P1R3; -.
DR MaxQB; Q6P1R3; -.
DR PeptideAtlas; Q6P1R3; -.
DR PRIDE; Q6P1R3; -.
DR ProteomicsDB; 66869; -. [Q6P1R3-1]
DR ProteomicsDB; 66870; -. [Q6P1R3-2]
DR ProteomicsDB; 66871; -. [Q6P1R3-3]
DR Antibodypedia; 49903; 32 antibodies from 11 providers.
DR DNASU; 79684; -.
DR Ensembl; ENST00000239614.8; ENSP00000239614.4; ENSG00000120458.13. [Q6P1R3-3]
DR Ensembl; ENST00000374979.8; ENSP00000364118.3; ENSG00000120458.13. [Q6P1R3-1]
DR Ensembl; ENST00000526629.1; ENSP00000435705.1; ENSG00000120458.13. [Q6P1R3-2]
DR GeneID; 79684; -.
DR KEGG; hsa:79684; -.
DR MANE-Select; ENST00000374979.8; ENSP00000364118.3; NM_001308027.2; NP_001294956.1.
DR UCSC; uc001qay.2; human. [Q6P1R3-1]
DR CTD; 79684; -.
DR DisGeNET; 79684; -.
DR GeneCards; MSANTD2; -.
DR HGNC; HGNC:26266; MSANTD2.
DR HPA; ENSG00000120458; Low tissue specificity.
DR neXtProt; NX_Q6P1R3; -.
DR OpenTargets; ENSG00000120458; -.
DR PharmGKB; PA143485356; -.
DR VEuPathDB; HostDB:ENSG00000120458; -.
DR eggNOG; ENOG502QU4E; Eukaryota.
DR GeneTree; ENSGT00390000013593; -.
DR HOGENOM; CLU_028535_1_0_1; -.
DR InParanoid; Q6P1R3; -.
DR OMA; FSQEDWG; -.
DR OrthoDB; 747790at2759; -.
DR PhylomeDB; Q6P1R3; -.
DR TreeFam; TF331593; -.
DR PathwayCommons; Q6P1R3; -.
DR SignaLink; Q6P1R3; -.
DR BioGRID-ORCS; 79684; 12 hits in 1078 CRISPR screens.
DR ChiTaRS; MSANTD2; human.
DR GenomeRNAi; 79684; -.
DR Pharos; Q6P1R3; Tdark.
DR PRO; PR:Q6P1R3; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6P1R3; protein.
DR Bgee; ENSG00000120458; Expressed in caput epididymis and 191 other tissues.
DR ExpressionAtlas; Q6P1R3; baseline and differential.
DR Genevisible; Q6P1R3; HS.
DR InterPro; IPR042792; MSANTD2.
DR InterPro; IPR044822; Myb_DNA-bind_4.
DR PANTHER; PTHR46933; PTHR46933; 1.
DR Pfam; PF13837; Myb_DNA-bind_4; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..559
FT /note="Myb/SANT-like DNA-binding domain-containing protein
FT 2"
FT /id="PRO_0000274301"
FT DOMAIN 103..173
FT /note="Myb-like"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZR2"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZR2"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZR2"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZR2"
FT CROSSLNK 268
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 343
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..230
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_022705"
FT VAR_SEQ 171..222
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022706"
FT CONFLICT 370
FT /note="N -> D (in Ref. 1; BAB15618)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="E -> K (in Ref. 1; BAB15618)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 61319 MW; 92063815ADDE0E5F CRC64;
MAAPCGSELP ANSPLKIPKM EVLSPASPGG LSDGNPSLSD PSTPRGASPL GPGSAAGSGA
AASGGLGLGL GGRSAASSSV SFSPGGGGGG AAAAAAAACR GMSWTPAETN ALIAVWGNER
LVEARYQQLE GAGTVFGSKA PGPAMYERVS RALAELGYER TPSQCRERIK TLRRCYSRVK
EHGVGKRKSS YTFEQLEQVF GQGGWDAQPC QPVLINSSGL YQELESDGST MEDYSQEDWG
NHSQDLHGYP TDQELDEIPV TKRTLKIKQE SSEEAQKRDI MQNIVQILES VQLKWELFQS
WTDFSRLHLS NKLAIFGIGY NTRWKEDIRY HYAEISSQVP LGKRLREYFN SEKPEGRIIM
TRVQKMNWKN VYYKFLEITI SEARCLELHM EIDWIPIAHS KPTGGNVVQY LLPGGIPKSP
GLYAIGYEEC IERPLSPHME QSSLDPGKEG RVDLETLSAQ ASLQVEIEPT RIIYCYLGIA
EVRTLQQCLF LHFQANTKTF SKDWVGINGF LSQNCIVDPG VSPKSIYIKF VEVERDFLSA
GSLVECLEKA IGYPLKFNN
