MYSM1_HUMAN
ID MYSM1_HUMAN Reviewed; 828 AA.
AC Q5VVJ2; A8KA54; B3KX65; Q68DD3; Q6AI53; Q7Z3G8; Q96PX3;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Deubiquitinase MYSM1;
DE Short=2A-DUB;
DE EC=3.4.19.- {ECO:0000269|PubMed:33086059};
DE AltName: Full=Myb-like, SWIRM and MPN domain-containing protein 1;
GN Name=MYSM1; Synonyms=KIAA1915;
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] (ISOFORM 2), AND VARIANT ALA-264.
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 144-828 (ISOFORM 1), AND VARIANT ALA-264.
RC TISSUE=Trachea;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-133 (ISOFORM 1).
RC TISSUE=Fetal skin, and Liver;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN COMPLEX, AND MUTAGENESIS
RP OF ASP-669.
RX PubMed=17707232; DOI=10.1016/j.molcel.2007.07.024;
RA Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H.,
RA Tempst P., Glass C.K., Rosenfeld M.G.;
RT "A histone H2A deubiquitinase complex coordinating histone acetylation and
RT H1 dissociation in transcriptional regulation.";
RL Mol. Cell 27:609-621(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION BY
RP 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-218, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218 AND THR-236, 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 [9]
RP FUNCTION.
RX PubMed=22169041; DOI=10.1016/j.immuni.2011.11.010;
RA Jiang X.X., Nguyen Q., Chou Y., Wang T., Nandakumar V., Yates P., Jones L.,
RA Wang L., Won H., Lee H.R., Jung J.U., Mueschen M., Huang X.F., Chen S.Y.;
RT "Control of B cell development by the histone H2A deubiquitinase MYSM1.";
RL Immunity 35:883-896(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, AND IDENTIFICATION BY
RP 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 [11]
RP INVOLVEMENT IN BMFS4, AND VARIANT BMFS4 390-GLU--MET-828 DEL.
RX PubMed=24288411; DOI=10.1182/blood-2013-09-527127;
RA Alsultan A., Shamseldin H.E., Osman M.E., Aljabri M., Alkuraya F.S.;
RT "MYSM1 is mutated in a family with transient transfusion-dependent anemia,
RT mild thrombocytopenia, and low NK- and B-cell counts.";
RL Blood 122:3844-3845(2013).
RN [12]
RP FUNCTION, AND INTERACTION WITH NFIL3.
RX PubMed=24062447; DOI=10.1073/pnas.1308888110;
RA Nandakumar V., Chou Y., Zang L., Huang X.F., Chen S.Y.;
RT "Epigenetic control of natural killer cell maturation by histone H2A
RT deubiquitinase, MYSM1.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E3927-E3936(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-218; SER-242 AND
RP SER-267, AND 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 [14]
RP FUNCTION, INVOLVEMENT IN BMFS4, AND VARIANT BMFS4 ARG-656.
RX PubMed=26220525; DOI=10.1016/j.jaci.2015.06.008;
RA Le Guen T., Touzot F., Andre-Schmutz I., Lagresle-Peyrou C., France B.,
RA Kermasson L., Lambert N., Picard C., Nitschke P., Carpentier W.,
RA Bole-Feysot C., Lim A., Cavazzana M., Callebaut I., Soulier J., Jabado N.,
RA Fischer A., de Villartay J.P., Revy P.;
RT "An in vivo genetic reversion highlights the crucial role of Myb-Like,
RT SWIRM, and MPN domains 1 (MYSM1) in human hematopoiesis and lymphocyte
RT differentiation.";
RL J. Allergy Clin. Immunol. 136:1619-1626(2015).
RN [15]
RP FUNCTION, INVOLVEMENT IN BMFS4, AND VARIANT BMFS4 390-GLU--MET-828 DEL.
RX PubMed=28115216; DOI=10.1016/j.jaci.2016.10.053;
RA Bahrami E., Witzel M., Racek T., Puchalka J., Hollizeck S.,
RA Greif-Kohistani N., Kotlarz D., Horny H.P., Feederle R., Schmidt H.,
RA Sherkat R., Steinemann D., Goehring G., Schlegelbeger B., Albert M.H.,
RA Al-Herz W., Klein C.;
RT "Myb-like, SWIRM, and MPN domains 1 (MYSM1) deficiency: Genotoxic stress-
RT associated bone marrow failure and developmental aberrations.";
RL J. Allergy Clin. Immunol. 140:1112-1119(2017).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-187, AND IDENTIFICATION BY MASS
RP 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 FUNCTION, INDUCTION BY INTRACELLULAR DNA, AND CATALYTIC ACTIVITY.
RX PubMed=33086059; DOI=10.1016/j.celrep.2020.108297;
RA Tian M., Liu W., Zhang Q., Huang Y., Li W., Wang W., Zhao P., Huang S.,
RA Song Y., Shereen M.A., Qin M., Liu Y., Wu K., Wu J.;
RT "MYSM1 Represses Innate Immunity and Autoimmunity through Suppressing the
RT cGAS-STING Pathway.";
RL Cell Rep. 33:108297-108297(2020).
RN [18]
RP STRUCTURE BY NMR OF 117-181 AND OF 367-470, AND INTERACTION WITH DNA.
RX PubMed=17428495; DOI=10.1016/j.jmb.2007.03.027;
RA Yoneyama M., Tochio N., Umehara T., Koshiba S., Inoue M., Yabuki T.,
RA Aoki M., Seki E., Matsuda T., Watanabe S., Tomo Y., Nishimura Y.,
RA Harada T., Terada T., Shirouzu M., Hayashizaki Y., Ohara O., Tanaka A.,
RA Kigawa T., Yokoyama S.;
RT "Structural and functional differences of SWIRM domain subtypes.";
RL J. Mol. Biol. 369:222-238(2007).
CC -!- FUNCTION: Metalloprotease with deubiquitinase activity that plays
CC important regulator roles in hematopoietic stem cell function, blood
CC cell production and immune response (PubMed:24062447, PubMed:26220525,
CC PubMed:28115216). Participates in the normal programming of B-cell
CC responses to antigen after the maturation process (By similarity).
CC Within the cytoplasm, plays critical roles in the repression of innate
CC immunity and autoimmunity (PubMed:33086059). Removes 'Lys-63'-linked
CC polyubiquitins from TRAF3 and TRAF6 complexes (By similarity).
CC Attenuates NOD2-mediated inflammation and tissue injury by promoting
CC 'Lys-63'-linked deubiquitination of RIPK2 component (By similarity).
CC Suppresses the CGAS-STING1 signaling pathway by cleaving STING1 'Lys-
CC 63'-linked ubiquitin chains (PubMed:33086059). In the nucleus, acts as
CC a hematopoietic transcription regulator derepressing a range of genes
CC essential for normal stem cell differentiation including EBF1 and PAX5
CC in B-cells, ID2 in NK-cell progenitor or FLT3 in dendritic cell
CC precursors (PubMed:24062447). Deubiquitinates monoubiquitinated histone
CC H2A, a specific tag for epigenetic transcriptional repression, leading
CC to dissociation of histone H1 from the nucleosome (PubMed:17707232).
CC {ECO:0000250|UniProtKB:Q69Z66, ECO:0000269|PubMed:17707232,
CC ECO:0000269|PubMed:22169041, ECO:0000269|PubMed:24062447,
CC ECO:0000269|PubMed:26220525, ECO:0000269|PubMed:28115216,
CC ECO:0000269|PubMed:33086059}.
CC -!- SUBUNIT: Component of a large chromatin remodeling complex, at least
CC composed of MYSM1, PCAF, RBM10 and KIF11/TRIP5. Binds histones
CC (PubMed:17707232). Interacts with NFIL3; this interaction is critical
CC for their correct recruitment to the ID2 locus during natural killer
CC cell maturation (PubMed:24062447). {ECO:0000269|PubMed:17707232,
CC ECO:0000269|PubMed:24062447}.
CC -!- INTERACTION:
CC Q5VVJ2; Q5T2T1: MPP7; NbExp=3; IntAct=EBI-12262412, EBI-2514004;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624,
CC ECO:0000269|PubMed:17707232}. Cytoplasm {ECO:0000250|UniProtKB:Q69Z66}.
CC Note=Localizes to the cytoplasm in response to bacterial infection.
CC {ECO:0000250|UniProtKB:Q69Z66}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5VVJ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VVJ2-2; Sequence=VSP_018211;
CC Name=3;
CC IsoId=Q5VVJ2-3; Sequence=VSP_018210;
CC -!- INDUCTION: By DNA from viral infection and intracellular DNA.
CC {ECO:0000269|PubMed:33086059}.
CC -!- DOMAIN: Contains an N-terminal SANT domain that mediates histone/DNA
CC binding, a central SWIRM domain to mediate interaction with chromatin
CC associated proteins, and a C-terminal MPN domain that contains the
CC metalloprotease activity. {ECO:0000269|PubMed:17707232}.
CC -!- DISEASE: Bone marrow failure syndrome 4 (BMFS4) [MIM:618116]: A form of
CC bone marrow failure syndrome, a heterogeneous group of life-threatening
CC disorders characterized by hematopoietic defects in association with a
CC range of variable extra-hematopoietic manifestations. BMFS4 is
CC characterized by early-onset anemia, leukopenia, decreased B cells, and
CC developmental aberrations including facial dysmorphism, mild skeletal
CC anomalies, and neurodevelopmental delay. BMFS4 inheritance is autosomal
CC recessive. {ECO:0000269|PubMed:24288411, ECO:0000269|PubMed:26220525,
CC ECO:0000269|PubMed:28115216}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. MYSM1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB67808.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAG54377.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB067502; BAB67808.1; ALT_INIT; mRNA.
DR EMBL; AK126835; BAG54377.1; ALT_INIT; mRNA.
DR EMBL; AK292919; BAF85608.1; -; mRNA.
DR EMBL; BX537912; CAD97896.1; -; mRNA.
DR EMBL; CR627323; CAH10370.1; -; mRNA.
DR EMBL; CR749450; CAH18287.1; -; mRNA.
DR EMBL; AL035411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS41343.1; -. [Q5VVJ2-1]
DR RefSeq; NP_001078956.1; NM_001085487.2. [Q5VVJ2-1]
DR RefSeq; XP_016855684.1; XM_017000195.1.
DR RefSeq; XP_016855685.1; XM_017000196.1.
DR RefSeq; XP_016855686.1; XM_017000197.1.
DR PDB; 2CU7; NMR; -; A=117-181.
DR PDB; 2DCE; NMR; -; A=367-470.
DR PDBsum; 2CU7; -.
DR PDBsum; 2DCE; -.
DR AlphaFoldDB; Q5VVJ2; -.
DR BMRB; Q5VVJ2; -.
DR SMR; Q5VVJ2; -.
DR BioGRID; 125363; 45.
DR CORUM; Q5VVJ2; -.
DR DIP; DIP-58941N; -.
DR IntAct; Q5VVJ2; 4.
DR STRING; 9606.ENSP00000418734; -.
DR MEROPS; M67.005; -.
DR iPTMnet; Q5VVJ2; -.
DR PhosphoSitePlus; Q5VVJ2; -.
DR BioMuta; MYSM1; -.
DR DMDM; 74756898; -.
DR EPD; Q5VVJ2; -.
DR jPOST; Q5VVJ2; -.
DR MassIVE; Q5VVJ2; -.
DR MaxQB; Q5VVJ2; -.
DR PaxDb; Q5VVJ2; -.
DR PeptideAtlas; Q5VVJ2; -.
DR PRIDE; Q5VVJ2; -.
DR ProteomicsDB; 65467; -. [Q5VVJ2-1]
DR ProteomicsDB; 65468; -. [Q5VVJ2-2]
DR ProteomicsDB; 65469; -. [Q5VVJ2-3]
DR Antibodypedia; 46901; 281 antibodies from 30 providers.
DR DNASU; 114803; -.
DR Ensembl; ENST00000472487.6; ENSP00000418734.1; ENSG00000162601.11. [Q5VVJ2-1]
DR Ensembl; ENST00000622766.1; ENSP00000478391.1; ENSG00000162601.11. [Q5VVJ2-3]
DR GeneID; 114803; -.
DR KEGG; hsa:114803; -.
DR MANE-Select; ENST00000472487.6; ENSP00000418734.1; NM_001085487.3; NP_001078956.1.
DR UCSC; uc001cza.4; human. [Q5VVJ2-1]
DR CTD; 114803; -.
DR DisGeNET; 114803; -.
DR GeneCards; MYSM1; -.
DR HGNC; HGNC:29401; MYSM1.
DR HPA; ENSG00000162601; Low tissue specificity.
DR MalaCards; MYSM1; -.
DR MIM; 612176; gene.
DR MIM; 618116; phenotype.
DR neXtProt; NX_Q5VVJ2; -.
DR OpenTargets; ENSG00000162601; -.
DR Orphanet; 508542; Congenital progressive bone marrow failure-B-cell immunodeficiency-skeletal dysplasia syndrome.
DR PharmGKB; PA142671301; -.
DR VEuPathDB; HostDB:ENSG00000162601; -.
DR eggNOG; KOG1279; Eukaryota.
DR eggNOG; KOG1555; Eukaryota.
DR GeneTree; ENSGT00940000157721; -.
DR HOGENOM; CLU_018854_0_0_1; -.
DR InParanoid; Q5VVJ2; -.
DR OMA; SWRTDNS; -.
DR OrthoDB; 590811at2759; -.
DR PhylomeDB; Q5VVJ2; -.
DR TreeFam; TF324811; -.
DR PathwayCommons; Q5VVJ2; -.
DR Reactome; R-HSA-5689901; Metalloprotease DUBs.
DR SignaLink; Q5VVJ2; -.
DR BioGRID-ORCS; 114803; 32 hits in 1144 CRISPR screens.
DR ChiTaRS; MYSM1; human.
DR EvolutionaryTrace; Q5VVJ2; -.
DR GenomeRNAi; 114803; -.
DR Pharos; Q5VVJ2; Tbio.
DR PRO; PR:Q5VVJ2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5VVJ2; protein.
DR Bgee; ENSG00000162601; Expressed in calcaneal tendon and 172 other tissues.
DR ExpressionAtlas; Q5VVJ2; baseline and differential.
DR Genevisible; Q5VVJ2; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IMP:UniProtKB.
DR GO; GO:0043473; P:pigmentation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
DR GO; GO:0051797; P:regulation of hair follicle development; IEA:Ensembl.
DR GO; GO:1903706; P:regulation of hemopoiesis; IMP:UniProtKB.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR033497; MYSM1.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR12802:SF67; PTHR12802:SF67; 1.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF04433; SWIRM; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS50249; MPN; 1.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Chromatin regulator;
KW Cytoplasm; Disease variant; DNA-binding; Hydrolase; Immunity;
KW Isopeptide bond; Metal-binding; Metalloprotease; Nucleus; Phosphoprotein;
KW Protease; Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Ubl conjugation pathway; Zinc.
FT CHAIN 1..828
FT /note="Deubiquitinase MYSM1"
FT /id="PRO_0000234073"
FT DOMAIN 116..167
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 372..470
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT DOMAIN 577..709
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 656..669
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 774..778
FT /note="LXXLL motif"
FT BINDING 656
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 658
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 669
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 236
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 187
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..594
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_018210"
FT VAR_SEQ 1..253
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11572484"
FT /id="VSP_018211"
FT VARIANT 200
FT /note="C -> S (in dbSNP:rs17118103)"
FT /id="VAR_051814"
FT VARIANT 264
FT /note="T -> A (in dbSNP:rs12139511)"
FT /evidence="ECO:0000269|PubMed:11572484,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_051815"
FT VARIANT 390..828
FT /note="Missing (in BMFS4)"
FT /evidence="ECO:0000269|PubMed:24288411,
FT ECO:0000269|PubMed:28115216"
FT /id="VAR_081184"
FT VARIANT 656
FT /note="H -> R (in BMFS4; dbSNP:rs1557507208)"
FT /evidence="ECO:0000269|PubMed:26220525"
FT /id="VAR_081185"
FT VARIANT 825
FT /note="E -> K (in dbSNP:rs232777)"
FT /id="VAR_051816"
FT MUTAGEN 669
FT /note="D->N: Abolishes H2A deubiquitination."
FT /evidence="ECO:0000269|PubMed:17707232"
FT CONFLICT 231
FT /note="E -> G (in Ref. 2; BAG54377)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="G -> D (in Ref. 2; BAG54377)"
FT /evidence="ECO:0000305"
FT CONFLICT 782
FT /note="R -> G (in Ref. 3; CAH18287)"
FT /evidence="ECO:0000305"
FT HELIX 123..135
FT /evidence="ECO:0007829|PDB:2CU7"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:2CU7"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:2CU7"
FT HELIX 152..166
FT /evidence="ECO:0007829|PDB:2CU7"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:2DCE"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:2DCE"
FT HELIX 406..423
FT /evidence="ECO:0007829|PDB:2DCE"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:2DCE"
FT TURN 433..437
FT /evidence="ECO:0007829|PDB:2DCE"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:2DCE"
FT HELIX 443..456
FT /evidence="ECO:0007829|PDB:2DCE"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:2DCE"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:2DCE"
SQ SEQUENCE 828 AA; 95032 MW; 9EE635A30AF3B089 CRC64;
MAAEEADVDI EGDVVAAAGA QPGSGENTAS VLQKDHYLDS SWRTENGLIP WTLDNTISEE
NRAVIEKMLL EEEYYLSKKS QPEKVWLDQK EDDKKYMKSL QKTAKIMVHS PTKPASYSVK
WTIEEKELFE QGLAKFGRRW TKISKLIGSR TVLQVKSYAR QYFKNKVKCG LDKETPNQKT
GHNLQVKNED KGTKAWTPSC LRGRADPNLN AVKIEKLSDD EEVDITDEVD ELSSQTPQKN
SSSDLLLDFP NSKMHETNQG EFITSDSQEA LFSKSSRGCL QNEKQDETLS SSEITLWTEK
QSNGDKKSIE LNDQKFNELI KNCNKHDGRG IIVDARQLPS PEPCEIQKNL NDNEMLFHSC
QMVEESHEEE ELKPPEQEIE IDRNIIQEEE KQAIPEFFEG RQAKTPERYL KIRNYILDQW
EICKPKYLNK TSVRPGLKNC GDVNCIGRIH TYLELIGAIN FGCEQAVYNR PQTVDKVRIR
DRKDAVEAYQ LAQRLQSMRT RRRRVRDPWG NWCDAKDLEG QTFEHLSAEE LAKRREEEKG
RPVKSLKVPR PTKSSFDPFQ LIPCNFFSEE KQEPFQVKVA SEALLIMDLH AHVSMAEVIG
LLGGRYSEVD KVVEVCAAEP CNSLSTGLQC EMDPVSQTQA SETLAVRGFS VIGWYHSHPA
FDPNPSLRDI DTQAKYQSYF SRGGAKFIGM IVSPYNRNNP LPYSQITCLV ISEEISPDGS
YRLPYKFEVQ QMLEEPQWGL VFEKTRWIIE KYRLSHSSVP MDKIFRRDSD LTCLQKLLEC
MRKTLSKVTN CFMAEEFLTE IENLFLSNYK SNQENGVTEE NCTKELLM
