RBM33_HUMAN
ID RBM33_HUMAN Reviewed; 1170 AA.
AC Q96EV2; A4D244; B5MC24; Q52LF5; Q75LN9; Q75ML5; Q9NSV0;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=RNA-binding protein 33;
DE AltName: Full=Proline-rich protein 8;
DE AltName: Full=RNA-binding motif protein 33;
GN Name=RBM33; Synonyms=PRR8;
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1043-1170 (ISOFORM 1).
RC TISSUE=Brain, and Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-993 (ISOFORM 1).
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-205, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-205, AND
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-205, 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-41; SER-205 AND SER-765, AND
RP 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-41; SER-205 AND SER-765, 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-205; SER-233;
RP SER-741; SER-765; SER-951 AND SER-991, AND IDENTIFICATION BY MASS
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-765, 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 [16]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-470 AND ARG-1028, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-960, 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).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96EV2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96EV2-2; Sequence=VSP_030143, VSP_030144;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH93947.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH93949.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS01989.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAS02026.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAS07551.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB70894.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=EAL23911.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAL23912.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAX04539.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009403; AAS02026.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC078834; AAS01989.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC092460; AAS07551.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH236954; EAL23911.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH236954; EAL23912.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471149; EAX04539.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC011923; AAH11923.1; -; mRNA.
DR EMBL; BC093947; AAH93947.1; ALT_INIT; mRNA.
DR EMBL; BC093949; AAH93949.1; ALT_INIT; mRNA.
DR EMBL; AL137724; CAB70894.1; ALT_SEQ; mRNA.
DR CCDS; CCDS5941.2; -. [Q96EV2-1]
DR PIR; T46375; T46375.
DR RefSeq; NP_444271.2; NM_053043.2. [Q96EV2-1]
DR AlphaFoldDB; Q96EV2; -.
DR SMR; Q96EV2; -.
DR BioGRID; 127585; 78.
DR IntAct; Q96EV2; 31.
DR MINT; Q96EV2; -.
DR STRING; 9606.ENSP00000384160; -.
DR GlyGen; Q96EV2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96EV2; -.
DR PhosphoSitePlus; Q96EV2; -.
DR BioMuta; RBM33; -.
DR DMDM; 215274198; -.
DR EPD; Q96EV2; -.
DR jPOST; Q96EV2; -.
DR MassIVE; Q96EV2; -.
DR MaxQB; Q96EV2; -.
DR PaxDb; Q96EV2; -.
DR PeptideAtlas; Q96EV2; -.
DR PRIDE; Q96EV2; -.
DR ProteomicsDB; 76453; -. [Q96EV2-1]
DR ProteomicsDB; 76454; -. [Q96EV2-2]
DR Antibodypedia; 18863; 51 antibodies from 11 providers.
DR DNASU; 155435; -.
DR Ensembl; ENST00000287912.7; ENSP00000287912.3; ENSG00000184863.11. [Q96EV2-2]
DR Ensembl; ENST00000401878.8; ENSP00000384160.3; ENSG00000184863.11. [Q96EV2-1]
DR GeneID; 155435; -.
DR KEGG; hsa:155435; -.
DR MANE-Select; ENST00000401878.8; ENSP00000384160.3; NM_053043.3; NP_444271.2.
DR UCSC; uc003wme.4; human. [Q96EV2-1]
DR CTD; 155435; -.
DR DisGeNET; 155435; -.
DR GeneCards; RBM33; -.
DR HGNC; HGNC:27223; RBM33.
DR HPA; ENSG00000184863; Low tissue specificity.
DR neXtProt; NX_Q96EV2; -.
DR OpenTargets; ENSG00000184863; -.
DR PharmGKB; PA142671093; -.
DR VEuPathDB; HostDB:ENSG00000184863; -.
DR eggNOG; ENOG502QR1Z; Eukaryota.
DR GeneTree; ENSGT00530000063891; -.
DR HOGENOM; CLU_093358_0_0_1; -.
DR InParanoid; Q96EV2; -.
DR OMA; ETHFMPA; -.
DR OrthoDB; 287384at2759; -.
DR PhylomeDB; Q96EV2; -.
DR TreeFam; TF332363; -.
DR PathwayCommons; Q96EV2; -.
DR SignaLink; Q96EV2; -.
DR BioGRID-ORCS; 155435; 201 hits in 1079 CRISPR screens.
DR ChiTaRS; RBM33; human.
DR GeneWiki; RBM33; -.
DR GenomeRNAi; 155435; -.
DR Pharos; Q96EV2; Tdark.
DR PRO; PR:Q96EV2; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96EV2; protein.
DR Bgee; ENSG00000184863; Expressed in calcaneal tendon and 177 other tissues.
DR ExpressionAtlas; Q96EV2; baseline and differential.
DR Genevisible; Q96EV2; HS.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR039878; RBM33.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR22014; PTHR22014; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Isopeptide bond;
KW Methylation; Phosphoprotein; Reference proteome; RNA-binding;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1170
FT /note="RNA-binding protein 33"
FT /id="PRO_0000292982"
FT DOMAIN 1098..1170
FT /note="RRM"
FT REGION 1..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 789..835
FT /evidence="ECO:0000255"
FT COMPBIAS 16..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..333
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..382
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..439
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..494
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..570
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..629
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, 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 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 470
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 951
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CXK9"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1028
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1028
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 960
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 247..268
FT /note="ELSAEAKAALLEFEERERQHKQ -> GNFFACLPSSFTLISTSSIVLL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030143"
FT VAR_SEQ 269..1170
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030144"
FT VARIANT 574
FT /note="T -> A (in dbSNP:rs3735576)"
FT /id="VAR_052223"
SQ SEQUENCE 1170 AA; 129986 MW; 08039CCFCACDBBDE CRC64;
MAAALGASGG AGAGDDDFDQ FDKPGAERSW RRRAADEDWD SELEDDLLGE DLLSGKKNQS
DLSDEELNDD LLQSDNEDEE NFSSQGVTIS LNATSGMVTS FELSDNTNDQ SGEQESEYEQ
EQGEDELVYH KSDGSELYTQ EYPEEGQYEG HEAELTEDQI EYVEEPEEEQ LYTDEVLDIE
INEPLDEFTG GMETLELQKD IKEESDEEEE DDEESGRLRF KTERKEGTII RLSDVTRERR
NIPETLELSA EAKAALLEFE ERERQHKQGR YSSRRGGRRG GPLMCRGVGD QRRESTERGR
MKDHRPALLP TQPPVVPQAP PPPPPPPQQQ PIRSLFQPQP LQPLLPVQHP HHPSPPQGMH
MPPQLETPRM MMTPPPVTPQ QPKNIHINPH FKGTVVTPVQ VPLLPVPSQP RPAVGPQRFP
GPPEFPQHTP GPVPNSFSQP PRLPLQDQWR APPPPQDRDP FFLGVSGEPR FPSHLFLEQR
SPPPPPPPPT LLNSSHPVPT QSPLPFTQPG PAFNQQGQQP VFPRERPVRP ALQPPGPVGI
LHFSQPGSAT TRPFIPPRQP FLPGPGQPFL PTHTQPNLQG PLHPPLPPPH QPQPQQPQQQ
PPPQHQPPHQ PPHQPPPQHQ PPPQHPPQHP PQHQHHHHHH HLSVPPPPLM PMSQPQFRPH
VQTAQPQASS SRMQCPQRQG LRHNTTSQNV SKRPMQQMQP TAPRNSNLRE LPIAPSHVIE
MSSSRCSATP SAQVKPIVSA SPPSRAVAGS RSSQGKTEVK VKPASPVAQP KEEAKTETEF
PDEDEETRLY RLKIEEQKRL REEILKQKEL RRQQQAGARK KELLERLAQQ QQQLYAPPPP
AEQEEQALSP SPTNGNPLLP FPGAQVRQNV KNRLLVKNQD VSISNVQPKT SNFVPSSANM
QYQGQQMKAL KHLRQTRTVP QSQTQPLHKV LPIKPADVEE PAVPQTPRVA SIQGRPQDTK
PGVKRTVTHR TNSGGGDGPH ISSKVRVIKL SGGGGESDGF FHPEGQPQRL PQPPEVGPQP
ARKVTLTRGG LQQPPHLPAG PHAHSPVPPG IKSIQGIHPA KKAIMHGRGR GVAGPMGRGR
LMPNKQNLRV VECKPQPCVV SVEGLSSSTT DAQLKSLLMS VGPIQSLQML PQQRKAIAKF
KEPAHALAFQ QKFHRHMIDL SHINVALIVE
