UBP36_DROME
ID UBP36_DROME Reviewed; 1038 AA.
AC Q9VRP5; M9NE30; Q7YTX7; Q86NM9; Q8IQ57; Q8IQ58; Q8IQ59; Q8IQ60; Q960Q4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 36;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 36;
DE AltName: Full=Protein scrawny;
DE AltName: Full=Ubiquitin thioesterase 36;
DE AltName: Full=Ubiquitin-specific-processing protease 36;
GN Name=scny; Synonyms=Usp36; ORFNames=CG5505;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C AND D).
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Booth B., Carlson J.W.,
RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA Celniker S.E.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-515; THR-658;
RP THR-662; SER-672; SER-674; SER-747; SER-779; THR-782; SER-785; SER-819;
RP THR-825; SER-843 AND THR-846, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [6]
RP FUNCTION, INTERACTION WITH IMD, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF CYS-181 AND HIS-439.
RX PubMed=19837371; DOI=10.1016/j.chom.2009.09.007;
RA Thevenon D., Engel E., Avet-Rochex A., Gottar M., Bergeret E., Tricoire H.,
RA Benaud C., Baudier J., Taillebourg E., Fauvarque M.O.;
RT "The Drosophila ubiquitin-specific protease dUSP36/Scny targets IMD to
RT prevent constitutive immune signaling.";
RL Cell Host Microbe 6:309-320(2009).
RN [7]
RP FUNCTION, INTERACTION WITH ATMS, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-181.
RX PubMed=19039105; DOI=10.1126/science.1165678;
RA Buszczak M., Paterno S., Spradling A.C.;
RT "Drosophila stem cells share a common requirement for the histone H2B
RT ubiquitin protease scrawny.";
RL Science 323:248-251(2009).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22622177; DOI=10.4161/auto.19381;
RA Taillebourg E., Gregoire I., Viargues P., Jacomin A.C., Thevenon D.,
RA Faure M., Fauvarque M.O.;
RT "The deubiquitinating enzyme USP36 controls selective autophagy activation
RT by ubiquitinated proteins.";
RL Autophagy 8:767-779(2012).
RN [9]
RP FUNCTION.
RX PubMed=25027767; DOI=10.1186/s12964-014-0041-2;
RA Engel E., Viargues P., Mortier M., Taillebourg E., Coute Y., Thevenon D.,
RA Fauvarque M.O.;
RT "Identifying USPs regulating immune signals in Drosophila: USP2
RT deubiquitinates Imd and promotes its degradation by interacting with the
RT proteasome.";
RL Cell Commun. Signal. 12:41-41(2014).
CC -!- FUNCTION: Hydrolase that deubiquitinates polyubiquitinated target
CC proteins including imd (PubMed:19837371, PubMed:19039105). Required for
CC preventing the constitutive activation of the imd/NF-kappa-B (Imd)
CC signaling cascade under unchalleneged conditions (PubMed:19837371,
CC PubMed:25027767). Deubiquitinates imd linked 'Lys-63' chains which
CC leads its proteasomal degradation and consequently down-regulation of
CC the Imd signaling cascade (PubMed:19837371). Removal of the activating
CC 'Lys-63'-linked chains is likely to enable their replacement with 'Lys-
CC 48'-linked chains which act as 'tags' the for proteosomal degradation
CC of imd (PubMed:19837371). Required for maintaining multiple types of
CC adult stem cells, including male and female germline, epithelial
CC follicle cell and intestinal stem cells (PubMed:19039105). May function
CC as a transcriptional repressor by continually deubiquiting histone H2B
CC at the promoters of genes critical for cellular differentiation,
CC thereby preventing histone H3 'Lys-4' trimethylation (H3K4me3)
CC (PubMed:19039105). Controls selective autophagy activation by
CC ubiquitinated proteins (PubMed:22622177). {ECO:0000269|PubMed:19039105,
CC ECO:0000269|PubMed:19837371, ECO:0000269|PubMed:22622177,
CC ECO:0000269|PubMed:25027767}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12;
CC -!- SUBUNIT: Interacts with atms/PAF1, but not with CycT (PubMed:19039105).
CC Interacts (via C-terminus) with imd (via N-terminus) (PubMed:19837371).
CC {ECO:0000269|PubMed:19039105, ECO:0000269|PubMed:19837371}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19039105}.
CC Cytoplasm {ECO:0000269|PubMed:19837371}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=D;
CC IsoId=Q9VRP5-3; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9VRP5-2; Sequence=VSP_037591, VSP_037592;
CC Name=C;
CC IsoId=Q9VRP5-6; Sequence=VSP_037590, VSP_037593;
CC Name=G; Synonyms=H;
CC IsoId=Q9VRP5-7; Sequence=VSP_054032;
CC Name=I;
CC IsoId=Q9VRP5-8; Sequence=VSP_037590, VSP_037593, VSP_054032;
CC Name=J;
CC IsoId=Q9VRP5-9; Sequence=VSP_037591, VSP_037592, VSP_054032;
CC -!- DISRUPTION PHENOTYPE: Mutants are lethal at larval stages
CC (PubMed:19837371, PubMed:22622177). They are significantly smaller
CC without gross morphological defects and die 5 days after egg laying
CC (PubMed:22622177). Cells show accumulation of ubiquitinated proteins in
CC both the nucleus and the cytoplasm, forming dense dots
CC (PubMed:22622177). Double mutants for ref(2)P and scny die 96 hours
CC after egg laying (PubMed:22622177). RNAi-mediated knockdown is also
CC larval lethal (PubMed:19837371). RNAi-mediated knockdown in the fat
CC body or gut of uninfected adults, results in a significant increase in
CC the expression of the antimicrobial peptide genes Dpt, AttA and puc
CC (PubMed:19837371). Adults raised under axenic conditions do not display
CC any increase in Dpt, AttA and puc expression (PubMed:19837371). No
CC significant increase in the expression of the antifungal peptide gene
CC Drs (PubMed:19837371). Double knockdown with imd in the adult fat body,
CC prevents the enhanced expression of Dpt in uninfected flies
CC (PubMed:19837371). {ECO:0000269|PubMed:19837371,
CC ECO:0000269|PubMed:22622177}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AE014296; AAN12107.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN12108.2; -; Genomic_DNA.
DR EMBL; AE014296; AAN12109.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN12110.2; -; Genomic_DNA.
DR EMBL; AE014296; AAN12111.1; -; Genomic_DNA.
DR EMBL; AE014296; AFH04310.1; -; Genomic_DNA.
DR EMBL; AE014296; AFH04311.1; -; Genomic_DNA.
DR EMBL; AY051916; AAK93340.1; -; mRNA.
DR EMBL; BT004507; AAO42671.1; -; mRNA.
DR EMBL; BT010120; AAQ22589.1; -; mRNA.
DR EMBL; BT046169; ACI47091.1; -; mRNA.
DR RefSeq; NP_001246639.1; NM_001259710.2. [Q9VRP5-7]
DR RefSeq; NP_001246640.1; NM_001259711.2. [Q9VRP5-7]
DR RefSeq; NP_647986.3; NM_139729.3. [Q9VRP5-9]
DR RefSeq; NP_729092.1; NM_168132.3. [Q9VRP5-3]
DR RefSeq; NP_729093.2; NM_168133.2. [Q9VRP5-8]
DR RefSeq; NP_729094.1; NM_168134.2. [Q9VRP5-6]
DR RefSeq; NP_729095.1; NM_168135.2. [Q9VRP5-2]
DR AlphaFoldDB; Q9VRP5; -.
DR SMR; Q9VRP5; -.
DR BioGRID; 64109; 11.
DR IntAct; Q9VRP5; 99.
DR STRING; 7227.FBpp0076806; -.
DR MEROPS; C19.097; -.
DR iPTMnet; Q9VRP5; -.
DR PaxDb; Q9VRP5; -.
DR PRIDE; Q9VRP5; -.
DR DNASU; 38648; -.
DR EnsemblMetazoa; FBtr0077100; FBpp0076806; FBgn0260936. [Q9VRP5-3]
DR EnsemblMetazoa; FBtr0077101; FBpp0076807; FBgn0260936. [Q9VRP5-2]
DR EnsemblMetazoa; FBtr0077103; FBpp0076809; FBgn0260936. [Q9VRP5-6]
DR EnsemblMetazoa; FBtr0307975; FBpp0300344; FBgn0260936. [Q9VRP5-7]
DR EnsemblMetazoa; FBtr0307976; FBpp0300345; FBgn0260936. [Q9VRP5-7]
DR EnsemblMetazoa; FBtr0330127; FBpp0303160; FBgn0260936. [Q9VRP5-8]
DR EnsemblMetazoa; FBtr0330128; FBpp0303161; FBgn0260936. [Q9VRP5-9]
DR GeneID; 38648; -.
DR KEGG; dme:Dmel_CG5505; -.
DR CTD; 38648; -.
DR FlyBase; FBgn0260936; scny.
DR VEuPathDB; VectorBase:FBgn0260936; -.
DR eggNOG; KOG1865; Eukaryota.
DR GeneTree; ENSGT00940000170426; -.
DR HOGENOM; CLU_006208_0_0_1; -.
DR InParanoid; Q9VRP5; -.
DR OMA; KRFSMMG; -.
DR PhylomeDB; Q9VRP5; -.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR Reactome; R-DME-9648002; RAS processing.
DR SignaLink; Q9VRP5; -.
DR BioGRID-ORCS; 38648; 2 hits in 3 CRISPR screens.
DR ChiTaRS; scny; fly.
DR GenomeRNAi; 38648; -.
DR PRO; PR:Q9VRP5; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0260936; Expressed in saliva-secreting gland and 24 other tissues.
DR Genevisible; Q9VRP5; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:FlyBase.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IDA:FlyBase.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0035616; P:histone H2B conserved C-terminal lysine deubiquitination; IDA:FlyBase.
DR GO; GO:0002785; P:negative regulation of antimicrobial peptide production; IMP:FlyBase.
DR GO; GO:0045824; P:negative regulation of innate immune response; IMP:FlyBase.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IMP:UniProtKB.
DR GO; GO:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IMP:FlyBase.
DR GO; GO:0016579; P:protein deubiquitination; IMP:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:FlyBase.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1038
FT /note="Ubiquitin carboxyl-terminal hydrolase 36"
FT /id="PRO_0000378498"
FT DOMAIN 172..480
FT /note="USP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT REGION 22..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035,
FT ECO:0000305|PubMed:19039105, ECO:0000305|PubMed:19837371"
FT ACT_SITE 439
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093,
FT ECO:0000305|PubMed:19837371"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 658
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 662
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 779
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 782
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 825
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 843
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 846
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..90
FT /note="Missing (in isoform C and isoform I)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_037590"
FT VAR_SEQ 1..70
FT /note="Missing (in isoform B and isoform J)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_037591"
FT VAR_SEQ 71..110
FT /note="ESVLENLKSKYIVIKPGNPGAINGFSGKNNTGKLVGANGH -> MTVIMVDG
FT FALWLLYKLFLSPCCLLLWHVLKLSTVLFTFA (in isoform B and isoform
FT J)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_037592"
FT VAR_SEQ 91..110
FT /note="AINGFSGKNNTGKLVGANGH -> MLHSPVPRYNKCVPFPTLRT (in
FT isoform C and isoform I)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_037593"
FT VAR_SEQ 911..1038
FT /note="ELLVDAREQRQRDIDDDEENEMDRGRQRKVKSGSAKGNNASNSTPGYNPFQE
FT YEGQKRWNKNGGGGGFPRFYNQNYRQNFQQRNKFKFNRFGGPGSAKFQQQRALQRHLSA
FT GGGFSRRQPSAQQQQQT -> ETFELVCAKRIAGHGSVEGSDIVEGSVAVDAAVTSGSD
FT SKDVVVIAVAVTDTTADAPDPDRLTDGR (in isoform G, isoform I and
FT isoform J)"
FT /evidence="ECO:0000305"
FT /id="VSP_054032"
FT MUTAGEN 181
FT /note="C->S: Loss of H2B deubiquitination. Loss of 'K-
FT 48'- and 'K-63'-linked polyubiquitin chain hydrolysis; when
FT associated with N-369."
FT /evidence="ECO:0000269|PubMed:19039105,
FT ECO:0000269|PubMed:19837371"
FT MUTAGEN 439
FT /note="H->N: Loss of 'K-48'- and 'K-63'-linked
FT polyubiquitin chain hydrolysis; when associated with S-
FT 181."
FT /evidence="ECO:0000269|PubMed:19837371"
FT CONFLICT 115
FT /note="A -> T (in Ref. 4; AAQ22589)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="N -> D (in Ref. 4; AAQ22589/AAO42671)"
FT /evidence="ECO:0000305"
FT CONFLICT 766
FT /note="P -> T (in Ref. 4; AAQ22589)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1038 AA; 114088 MW; 98CECD6993333E22 CRC64;
MPVSMAVCET ANVVNAALRE SLGGNSSAGS STDQAKSGED TNGSLQNHIV ANAKRILMAK
IEYEEVPNYH ESVLENLKSK YIVIKPGNPG AINGFSGKNN TGKLVGANGH DNNGARKQAE
HPNNQSHHIN HHNHQHPTSN PNELPKPKRV LYPRENIRIG WKQSERKWQV GTGMINVGNT
CYLNSTLQAL LHIPALANWL VSEQAHLADC NVAEPGSGCI ICAMTKTLLA TQSNQSAVRP
FLIYSKLKQI CKHMVVGRQE DAHEFLRFLV EAMERAYLMR FRNYKELDQL VKETTPLGQI
FGGYLRSEVR CLSCNHVSIT FQHFQDLLLD IRKADSLEDA FEGHFSRERL EDMGYKCEGC
KKKVSATKQF SLERAPITLC IQLKRFSMIG NKLTKQISFK SRIDLSKYAA RSQAAQAQPL
TYRLVSMVTH LGASQHCGHY TAIGSTDTGS FYNFDDSYVR PIAMHSVCNT NAYIMFFELD
LSQAASPAAN RPNGVRLTNG HSTTPVPAAT VSSPSPTRFI GPQLPAGGAN GYTNGNAQKT
AIQFKQQNQQ SPQNGLQLGT GKFQDTAKPP LVGAHAKGEA TSAPTANGNK SSSPSSNSSS
NHKSINQQQY LPISSDDEDI EDEMKPRPTT AQLPSMPNMT ENHTEPKAKS PVKIQVKTPV
KTPLKSLVPY ESASEEEEAP LPNPRKRPSG EDSSESDQES GQTNGHSKTN GSHTNGSASS
SVHVNNSKQK TDAIDEIFKS LKKSADSDED DDEEEPSIQL TNGWHPQKQS QSQSKAPPSP
KTPPSPAVIK SKTGIWKVTR NDEVDAIEDD VDVVVVEGSP VKIPTPNKNH RNPFSSSKPS
TDSPATPGAK RQKLLNGSAL KSHQQPRVGN GYQSNATSNG STINELLKQS YRGYGSPVLS
WNGKPAELEK ELLVDAREQR QRDIDDDEEN EMDRGRQRKV KSGSAKGNNA SNSTPGYNPF
QEYEGQKRWN KNGGGGGFPR FYNQNYRQNF QQRNKFKFNR FGGPGSAKFQ QQRALQRHLS
AGGGFSRRQP SAQQQQQT
