TRA2A_HUMAN
ID TRA2A_HUMAN Reviewed; 282 AA.
AC Q13595; B4DQI6; B4DUA9; E9PD75;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Transformer-2 protein homolog alpha {ECO:0000305};
DE Short=TRA-2 alpha;
DE Short=TRA2-alpha;
DE AltName: Full=Transformer-2 protein homolog A;
GN Name=TRA2A {ECO:0000312|HGNC:HGNC:16645};
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 [MRNA] (ISOFORMS LONG AND SHORT).
RX PubMed=8799144; DOI=10.1073/pnas.93.17.9004;
RA Dauwalder B., Amaya-Manzanares F., Mattox W.;
RT "A human homologue of the Drosophila sex determination factor transformer-2
RT has conserved splicing regulatory functions.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:9004-9009(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Prostate;
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=9546399; DOI=10.1016/s0092-8674(00)81153-8;
RA Tacke R., Tohyama M., Ogawa S., Manley J.L.;
RT "Human Tra2 proteins are sequence-specific activators of pre-mRNA
RT splicing.";
RL Cell 93:139-148(1998).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP 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-84; SER-86; THR-88; THR-202
RP AND THR-204, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2; SER-14; THR-202 AND THR-204, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2; SER-14; THR-24; SER-84; SER-86; THR-88; SER-96; SER-98
RP AND THR-204, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], 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 SER-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-2; SER-14; SER-82; SER-84;
RP SER-86; THR-88; THR-202 AND SER-236, 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-198, 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 -!- FUNCTION: Sequence-specific RNA-binding protein which participates in
CC the control of pre-mRNA splicing. {ECO:0000269|PubMed:9546399}.
CC -!- SUBUNIT: Binds to A3 enhancer proteins SRp75, SRp55, SRp40 and SRp30
CC (Probable). Interacts with ILDR1 (via C-terminus) and ILDR2 (By
CC similarity). {ECO:0000250|UniProtKB:Q6PFR5, ECO:0000305}.
CC -!- INTERACTION:
CC Q13595; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-2685506, EBI-746778;
CC Q13595; Q15287: RNPS1; NbExp=3; IntAct=EBI-2685506, EBI-395959;
CC Q13595; P78362: SRPK2; NbExp=2; IntAct=EBI-2685506, EBI-593303;
CC Q13595; O43592: XPOT; NbExp=3; IntAct=EBI-2685506, EBI-286683;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9546399}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Long;
CC IsoId=Q13595-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q13595-2; Sequence=VSP_005893, VSP_005894, VSP_005895;
CC Name=3;
CC IsoId=Q13595-3; Sequence=VSP_005893;
CC Name=4;
CC IsoId=Q13595-4; Sequence=VSP_005893, VSP_057405;
CC -!- PTM: Phosphorylated in the RS domains. {ECO:0000269|PubMed:9546399}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; U53209; AAC50658.1; -; mRNA.
DR EMBL; AK298815; BAG60948.1; -; mRNA.
DR EMBL; AK300565; BAG62271.1; -; mRNA.
DR EMBL; AK300741; BAG62410.1; -; mRNA.
DR EMBL; AC023105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017094; AAH17094.1; -; mRNA.
DR CCDS; CCDS5383.1; -. [Q13595-1]
DR CCDS; CCDS64609.1; -. [Q13595-3]
DR CCDS; CCDS75569.1; -. [Q13595-4]
DR RefSeq; NP_001269686.1; NM_001282757.1. [Q13595-3]
DR RefSeq; NP_001269687.1; NM_001282758.1. [Q13595-3]
DR RefSeq; NP_001269688.1; NM_001282759.1. [Q13595-4]
DR RefSeq; NP_037425.1; NM_013293.4. [Q13595-1]
DR RefSeq; XP_005249782.1; XM_005249725.1.
DR RefSeq; XP_016867578.1; XM_017012089.1.
DR RefSeq; XP_016867579.1; XM_017012090.1. [Q13595-3]
DR AlphaFoldDB; Q13595; -.
DR SMR; Q13595; -.
DR BioGRID; 118948; 308.
DR IntAct; Q13595; 120.
DR MINT; Q13595; -.
DR STRING; 9606.ENSP00000297071; -.
DR GlyGen; Q13595; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13595; -.
DR PhosphoSitePlus; Q13595; -.
DR SwissPalm; Q13595; -.
DR BioMuta; TRA2A; -.
DR DMDM; 4033480; -.
DR CPTAC; CPTAC-1647; -.
DR EPD; Q13595; -.
DR jPOST; Q13595; -.
DR MassIVE; Q13595; -.
DR MaxQB; Q13595; -.
DR PaxDb; Q13595; -.
DR PeptideAtlas; Q13595; -.
DR PRIDE; Q13595; -.
DR ProteomicsDB; 4878; -.
DR ProteomicsDB; 5170; -.
DR ProteomicsDB; 59587; -. [Q13595-1]
DR ProteomicsDB; 59588; -. [Q13595-2]
DR Antibodypedia; 25690; 180 antibodies from 29 providers.
DR DNASU; 29896; -.
DR Ensembl; ENST00000297071.9; ENSP00000297071.4; ENSG00000164548.12. [Q13595-1]
DR Ensembl; ENST00000392502.8; ENSP00000376290.4; ENSG00000164548.12. [Q13595-4]
DR Ensembl; ENST00000621813.4; ENSP00000480822.1; ENSG00000164548.12. [Q13595-3]
DR GeneID; 29896; -.
DR KEGG; hsa:29896; -.
DR MANE-Select; ENST00000297071.9; ENSP00000297071.4; NM_013293.5; NP_037425.1.
DR UCSC; uc011jzb.4; human.
DR UCSC; uc011jzc.5; human. [Q13595-1]
DR CTD; 29896; -.
DR DisGeNET; 29896; -.
DR GeneCards; TRA2A; -.
DR HGNC; HGNC:16645; TRA2A.
DR HPA; ENSG00000164548; Low tissue specificity.
DR MIM; 602718; gene.
DR neXtProt; NX_Q13595; -.
DR OpenTargets; ENSG00000164548; -.
DR PharmGKB; PA164726707; -.
DR VEuPathDB; HostDB:ENSG00000164548; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000157167; -.
DR HOGENOM; CLU_050438_3_0_1; -.
DR InParanoid; Q13595; -.
DR OMA; GRYSPEY; -.
DR PhylomeDB; Q13595; -.
DR TreeFam; TF106265; -.
DR PathwayCommons; Q13595; -.
DR SignaLink; Q13595; -.
DR BioGRID-ORCS; 29896; 23 hits in 1084 CRISPR screens.
DR ChiTaRS; TRA2A; human.
DR GeneWiki; TRA2A; -.
DR GenomeRNAi; 29896; -.
DR Pharos; Q13595; Tbio.
DR PRO; PR:Q13595; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q13595; protein.
DR Bgee; ENSG00000164548; Expressed in right uterine tube and 205 other tissues.
DR ExpressionAtlas; Q13595; baseline and differential.
DR Genevisible; Q13595; HS.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
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:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378"
FT CHAIN 2..282
FT /note="Transformer-2 protein homolog alpha"
FT /id="PRO_0000081981"
FT DOMAIN 119..197
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..225
FT /note="Linker"
FT REGION 201..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..88
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 88
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 202
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 204
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 232
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFR5"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 198
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..101
FT /note="Missing (in isoform Short, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:8799144"
FT /id="VSP_005893"
FT VAR_SEQ 214
FT /note="H -> Q (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8799144"
FT /id="VSP_005894"
FT VAR_SEQ 215..282
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8799144"
FT /id="VSP_005895"
FT VAR_SEQ 257
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057405"
SQ SEQUENCE 282 AA; 32689 MW; EDB5ABE7BEA023FD CRC64;
MSDVEENNFE GRESRSQSKS PTGTPARVKS ESRSGSRSPS RVSKHSESHS RSRSKSRSRS
RRHSHRRYTR SRSHSHSHRR RSRSRSYTPE YRRRRSRSHS PMSNRRRHTG SRANPDPNTC
LGVFGLSLYT TERDLREVFS RYGPLSGVNV VYDQRTGRSR GFAFVYFERI DDSKEAMERA
NGMELDGRRI RVDYSITKRA HTPTPGIYMG RPTHSGGGGG GGGGGGGGGG GRRRDSYYDR
GYDRGYDRYE DYDYRYRRRS PSPYYSRYRS RSRSRSYSPR RY
