TRI33_MOUSE
ID TRI33_MOUSE Reviewed; 1142 AA.
AC Q99PP7; Q6SI71; Q6ZPX5;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM33;
DE EC=2.3.2.27;
DE AltName: Full=Ectodermin homolog;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM33 {ECO:0000305};
DE AltName: Full=Transcription intermediary factor 1-gamma;
DE Short=TIF1-gamma;
DE AltName: Full=Tripartite motif-containing protein 33;
GN Name=Trim33; Synonyms=Kiaa1113;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RX PubMed=15256250; DOI=10.1016/j.gene.2004.02.056;
RA Yan K.P., Dolle P., Mark M., Lerouge T., Wendling O., Chambon P.,
RA Losson R.;
RT "Molecular cloning, genomic structure, and expression analysis of the mouse
RT transcriptional intermediary factor 1 gamma gene.";
RL Gene 334:3-13(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-1142 (ISOFORM BETA).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 949-1142 (ISOFORM ALPHA).
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [4]
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=15314655; DOI=10.1371/journal.pbio.0020237;
RA Ransom D.G., Bahary N., Niss K., Traver D., Burns C., Trede N.S.,
RA Paffett-Lugassy N., Saganic W.J., Lim C.A., Hersey C., Zhou Y., Barut B.A.,
RA Lin S., Kingsley P.D., Palis J., Orkin S.H., Zon L.I.;
RT "The zebrafish moonshine gene encodes transcriptional intermediary factor 1
RT gamma, an essential regulator of hematopoiesis.";
RL PLoS Biol. 2:1188-1196(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=16751102; DOI=10.1016/j.cell.2006.03.045;
RA He W., Dorn D.C., Erdjument-Bromage H., Tempst P., Moore M.A., Massague J.;
RT "Hematopoiesis controlled by distinct TIF1gamma and Smad4 branches of the
RT TGFbeta pathway.";
RL Cell 125:929-941(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-818 AND THR-830, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP SUMOYLATION WITH SUMO1.
RX PubMed=23213215; DOI=10.1073/pnas.1215366110;
RA Tirard M., Hsiao H.H., Nikolov M., Urlaub H., Melchior F., Brose N.;
RT "In vivo localization and identification of SUMOylated proteins in the
RT brain of His6-HA-SUMO1 knock-in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:21122-21127(2012).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-778; LYS-784; LYS-808; LYS-966
RP AND LYS-968, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-531; ARG-593; ARG-607; ARG-614
RP AND ARG-620, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4
CC ubiquitination, nuclear exclusion and degradation via the ubiquitin
CC proteasome pathway (By similarity). May act as a transcriptional
CC repressor (By similarity). Inhibits the transcriptional response to
CC TGF-beta/BMP signaling cascade (By similarity). Plays a role in the
CC control of cell proliferation (By similarity). Its association with
CC SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic
CC stem/progenitor. Monoubiquitinates SMAD4 and acts as an inhibitor of
CC SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of
CC SMAD4 hampers its ability to form a stable complex with activated
CC SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade) (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:16751102}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homooligomer and heterooligomer with TRIM24 and TRIM28 family
CC members (By similarity). Interacts with SMAD4 in unstimulated cells (By
CC similarity). Found in a complex with SMAD2 and SMAD3 upon addition of
CC TGF-beta (By similarity). Interacts with SMAD2 and SMAD3 (By
CC similarity). Interacts with SMAD4 under basal and induced conditions
CC and, upon TGF-beta signaling, with activated SMAD2. Forms a ternary
CC complex with SMAD4 and SMAD2 upon TGF-beta signaling (By similarity).
CC {ECO:0000250|UniProtKB:Q9UPN9}.
CC -!- INTERACTION:
CC Q99PP7; Q64127: Trim24; NbExp=2; IntAct=EBI-3043980, EBI-307947;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15314655,
CC ECO:0000269|PubMed:16751102}. Note=In discrete nuclear dots resembling
CC nuclear bodies.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha;
CC IsoId=Q99PP7-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q99PP7-2; Sequence=VSP_012068;
CC -!- TISSUE SPECIFICITY: Ubiquitous with high level in testis.
CC -!- DEVELOPMENTAL STAGE: Expressed in round hematopoietic cells in yolk sac
CC blood islands at 8.5 dpc. Expressed uniformly at 10.5 dpc. Expressed in
CC the brain, spinal cord, neuroepithelium and in spinal ganglia at 12.5
CC dpc. Expressed in brain, spinal cord, developing epithelia of the lung,
CC stomach, intestine, outer region of the developing kidney, liver, brown
CC fat tissue, skeletal muscle, developing craniofacial region, thymus,
CC cochlear and pharyngeal epithelia and olfactory and respiratory
CC epithelia at 16.5 dpc. {ECO:0000269|PubMed:15314655,
CC ECO:0000269|PubMed:16751102}.
CC -!- PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:23213215}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AY458590; AAS10352.1; -; mRNA.
DR EMBL; AK129293; BAC98103.1; -; mRNA.
DR EMBL; AF220138; AAG53511.1; -; mRNA.
DR RefSeq; NP_001073299.1; NM_001079830.2.
DR RefSeq; NP_444400.2; NM_053170.3.
DR AlphaFoldDB; Q99PP7; -.
DR SMR; Q99PP7; -.
DR BioGRID; 220448; 6.
DR CORUM; Q99PP7; -.
DR DIP; DIP-59674N; -.
DR IntAct; Q99PP7; 5.
DR STRING; 10090.ENSMUSP00000029444; -.
DR iPTMnet; Q99PP7; -.
DR PhosphoSitePlus; Q99PP7; -.
DR EPD; Q99PP7; -.
DR jPOST; Q99PP7; -.
DR MaxQB; Q99PP7; -.
DR PaxDb; Q99PP7; -.
DR PRIDE; Q99PP7; -.
DR ProteomicsDB; 259318; -. [Q99PP7-1]
DR ProteomicsDB; 259319; -. [Q99PP7-2]
DR DNASU; 94093; -.
DR GeneID; 94093; -.
DR KEGG; mmu:94093; -.
DR CTD; 51592; -.
DR MGI; MGI:2137357; Trim33.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q99PP7; -.
DR OrthoDB; 756911at2759; -.
DR PhylomeDB; Q99PP7; -.
DR Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 94093; 13 hits in 78 CRISPR screens.
DR ChiTaRS; Trim33; mouse.
DR PRO; PR:Q99PP7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99PP7; protein.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0070410; F:co-SMAD binding; ISS:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
DR GO; GO:0070412; F:R-SMAD binding; ISS:BHF-UCL.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Bromodomain; Coiled coil; DNA-binding;
KW Isopeptide bond; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1142
FT /note="E3 ubiquitin-protein ligase TRIM33"
FT /id="PRO_0000056396"
FT DOMAIN 989..1061
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT ZN_FING 141..201
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 228..275
FT /note="B box-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 287..328
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 902..949
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..163
FT /note="Necessary for E3 ubiquitin-protein ligase activity
FT and repression of SMAD4 signaling and transcriptional
FT repression"
FT /evidence="ECO:0000250"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..417
FT /note="Necessary for oligomerization"
FT /evidence="ECO:0000250"
FT REGION 657..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 315..417
FT /evidence="ECO:0000255"
FT COMPBIAS 100..130
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 531
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 531
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 551
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT MOD_RES 593
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 607
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 607
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT MOD_RES 614
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 620
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 778
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 784
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 808
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 818
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 830
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 877
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT MOD_RES 966
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 968
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1066
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT MOD_RES 1117
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT MOD_RES 1120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT MOD_RES 1134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 345
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 497
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 520
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 543
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 778
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 784
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 789
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 791
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 791
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 808
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 808
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 811
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 876
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 968
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 1022
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 1058
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 1072
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT CROSSLNK 1133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN9"
FT VAR_SEQ 1056..1072
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_012068"
FT CONFLICT 949..952
FT /note="IGKP -> HASA (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1142 AA; 123843 MW; D43699AE75F0893F CRC64;
MAENKGGGEA ESGGGGSGSA PVTAGAAGPT AQEAEPPLAA VLVEEEEEEG GRAGAEGGAA
GPDDGGVAAA SSSSAPAASV PAASVGSAVP GGAASTPAPA AAPAPAPAPA PAPAPAPAPA
PAPGSSSGPP LGPPASLLDT CAVCQQSLQS RREAEPKLLP CLHSFCLRCL PEPERQLSVP
IPGGSNGDVQ QVGVIRCPVC RQECRQIDLV DNYFVKDTSE APSSSDEKSE QVCTSCEDNA
SAVGFCVECG EWLCKTCIEA HQRVKFTKDH LIRKKEDVSE SVGTSGQRPV FCPVHKQEQL
KLFCETCDRL TCRDCQLLEH KEHRYQFLEE AFQNQKGAIE NLLAKLLEKK NYVHFAATQV
QNRIKEVNET NKRVEQEIKV AIFTLINEIN KKGKSLLQQL ENVTKERQMK LLQQQNDITG
LSRQVKHVMN FTNWAIASGS STALLYSKRL ITFQLRHILK ARCDPVPAAN GAIRFHCDPT
FWAKNVVNLG NLVIESKPAP GYTPNVVVGQ VPPGTNHISK TPGQINLAQL RLQHMQQQVY
AQKHQQLQQM RLQQPPAPIP TTTATTQQHP RQAAPQMLQQ QPPRLISVQT MQRGNMNCGA
FQAHQMRLAQ NAARIPGIPR HSAPQYSMMQ PHLQRQHSNP GHAGPFPVVS AHNPINPTSP
TTATMANANR GPTSPSVTAI ELIPSVTNPE NLPSLPDIPP IQLEDAGSSS LDNLLSRYIS
GSHLPPQPTS TMNPSPGPSA LSPGSSGLSN SHTPVRPPST SSTGSRGSCG SSGRTAEKSA
HSFKSDQVKV KQEPGTEEEI CSFSGAVKQE KTEDGRRSAC MLSSPESSLT PPLSTNLHLE
SELDTLTGLE NHVKTEPTDI SESCKQSGLS NLVNGKSPIR NLMHRSARIG GDGNSKDDDP
NEDWCAVCQN GGDLLCCEKC PKVFHLTCHV PTLLSFPSGD WICTFCRDIG KPEVEYDCDN
MQHSKKGKTA QGLSPVDQRK CERLLLYLYC HELSIEFQEP VPVSIPNYYK IIKKPMDLST
VKKKLQKKHS QHYQIPDDFV ADVRLIFKNC ERFNEMMKVV QVYADTQEIN LKGDSEVAKA
GKAVALYFED KLSEIYSDRT FTPLPEFEQD EDDGEVTEDS DEDFIQPRRK RLKSDERPVH
IK
