SFR19_HUMAN
ID SFR19_HUMAN Reviewed; 1312 AA.
AC Q9H7N4; Q7Z5V7; Q8WVA1; Q9NR59;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Splicing factor, arginine/serine-rich 19;
DE AltName: Full=SR-related C-terminal domain-associated factor 1;
DE Short=SR-related and CTD-associated factor 1;
DE AltName: Full=SR-related-CTD-associated factor;
DE Short=SCAF;
DE AltName: Full=Serine arginine-rich pre-mRNA splicing factor SR-A1;
DE Short=SR-A1;
GN Name=SCAF1; Synonyms=SFRS19, SRA1;
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 [GENOMIC DNA], INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=11461075; DOI=10.1054/bjoc.2001.1885;
RA Scorilas A., Kyriakopoulou L., Katsaros D., Diamandis E.P.;
RT "Cloning of a gene (SR-A1), encoding for a new member of the human Ser/Arg-
RT rich family of pre-mRNA splicing factors: overexpression in aggressive
RT ovarian cancer.";
RL Br. J. Cancer 85:190-198(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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].
RC TISSUE=Eye, and Lung;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=15493872; DOI=10.1515/bc.2004.102;
RA Mathioudaki K., Leotsakou T., Papadokostopoulou A., Paraskevas E.,
RA Ardavanis A., Talieri M., Scorilas A.;
RT "SR-A1, a member of the human pre-mRNA splicing factor family, and its
RT expression in colon cancer progression.";
RL Biol. Chem. 385:785-790(2004).
RN [5]
RP INTERACTION WITH POLR2A.
RX PubMed=15992770; DOI=10.1016/j.bbrc.2005.06.053;
RA Katsarou M.E., Papakyriakou A., Katsaros N., Scorilas A.;
RT "Expression of the C-terminal domain of novel human SR-A1 protein:
RT interaction with the CTD domain of RNA polymerase II.";
RL Biochem. Biophys. Res. Commun. 334:61-68(2005).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=16631123; DOI=10.1016/j.bbrc.2006.03.184;
RA Leoutsakou T., Talieri M., Scorilas A.;
RT "Expression analysis and prognostic significance of the SRA1 gene, in
RT ovarian cancer.";
RL Biochem. Biophys. Res. Commun. 344:667-674(2006).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=17132108; DOI=10.1515/bc.2006.201;
RA Leoutsakou T., Talieri M., Scorilas A.;
RT "Prognostic significance of the expression of SR-A1, encoding a novel SR-
RT related CTD-associated factor, in breast cancer.";
RL Biol. Chem. 387:1613-1618(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526; SER-738 AND SER-874, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498; SER-500; SER-734 AND
RP SER-738, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-498; SER-500;
RP SER-734; SER-738; SER-965 AND THR-989, AND IDENTIFICATION BY MASS
RP 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-448; SER-453;
RP SER-498; SER-500; SER-548; SER-734; SER-738 AND SER-965, AND IDENTIFICATION
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-498; SER-500;
RP SER-548; SER-734; SER-738; SER-874; SER-965; THR-976 AND THR-1001, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-498; SER-500;
RP SER-612; SER-614; SER-734; SER-738; SER-874; SER-929; SER-936; SER-965 AND
RP THR-1001, AND 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-498; SER-500;
RP SER-548; THR-706; SER-719; SER-725; SER-734; SER-738; SER-872; SER-874;
RP SER-965; THR-976 AND THR-989, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; THR-335; SER-498;
RP SER-500; TYR-732; SER-734; SER-738; SER-874 AND THR-989, AND IDENTIFICATION
RP BY 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-865, 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: May function in pre-mRNA splicing. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with POLR2A. {ECO:0000269|PubMed:15992770}.
CC -!- INTERACTION:
CC Q9H7N4; Q99828: CIB1; NbExp=5; IntAct=EBI-1222181, EBI-372594;
CC Q9H7N4; O15499: GSC2; NbExp=3; IntAct=EBI-1222181, EBI-19954058;
CC Q9H7N4; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1222181, EBI-16439278;
CC Q9H7N4; Q765P7: MTSS2; NbExp=3; IntAct=EBI-1222181, EBI-2815102;
CC Q9H7N4; Q8WWV3: RTN4IP1; NbExp=3; IntAct=EBI-1222181, EBI-743502;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in fetal brain and
CC liver, poorly expressed in salivary gland, heart, skin and ovary.
CC Expressed in colorectal carcinomas and ovarian cancers. Overexpressed
CC in colorectal carcinomas as compared to normal colonic mucosa.
CC {ECO:0000269|PubMed:11461075, ECO:0000269|PubMed:15493872,
CC ECO:0000269|PubMed:16631123, ECO:0000269|PubMed:17132108}.
CC -!- INDUCTION: Up-regulated by estrogens, androgens and glucocorticoids.
CC {ECO:0000269|PubMed:11461075}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15734.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SCAF1ID46074ch19q13.html";
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DR EMBL; AF254411; AAF87552.1; -; Genomic_DNA.
DR EMBL; AK024444; BAB15734.1; ALT_INIT; mRNA.
DR EMBL; BC018398; AAH18398.1; -; mRNA.
DR EMBL; BC053992; AAH53992.1; -; mRNA.
DR CCDS; CCDS33074.1; -.
DR RefSeq; NP_067051.2; NM_021228.2.
DR RefSeq; XP_005259179.1; XM_005259122.4.
DR AlphaFoldDB; Q9H7N4; -.
DR SMR; Q9H7N4; -.
DR BioGRID; 121834; 110.
DR IntAct; Q9H7N4; 44.
DR MINT; Q9H7N4; -.
DR STRING; 9606.ENSP00000353769; -.
DR GlyGen; Q9H7N4; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9H7N4; -.
DR PhosphoSitePlus; Q9H7N4; -.
DR SwissPalm; Q9H7N4; -.
DR BioMuta; SCAF1; -.
DR DMDM; 296452955; -.
DR EPD; Q9H7N4; -.
DR jPOST; Q9H7N4; -.
DR MassIVE; Q9H7N4; -.
DR MaxQB; Q9H7N4; -.
DR PaxDb; Q9H7N4; -.
DR PeptideAtlas; Q9H7N4; -.
DR PRIDE; Q9H7N4; -.
DR ProteomicsDB; 81132; -.
DR ABCD; Q9H7N4; 7 sequenced antibodies.
DR Antibodypedia; 32077; 82 antibodies from 18 providers.
DR Ensembl; ENST00000360565.8; ENSP00000353769.2; ENSG00000126461.15.
DR GeneID; 58506; -.
DR KEGG; hsa:58506; -.
DR MANE-Select; ENST00000360565.8; ENSP00000353769.2; NM_021228.3; NP_067051.2.
DR UCSC; uc002poq.4; human.
DR CTD; 58506; -.
DR DisGeNET; 58506; -.
DR GeneCards; SCAF1; -.
DR HGNC; HGNC:30403; SCAF1.
DR HPA; ENSG00000126461; Low tissue specificity.
DR MIM; 617264; gene.
DR neXtProt; NX_Q9H7N4; -.
DR OpenTargets; ENSG00000126461; -.
DR PharmGKB; PA162402459; -.
DR VEuPathDB; HostDB:ENSG00000126461; -.
DR eggNOG; KOG0825; Eukaryota.
DR GeneTree; ENSGT00950000183205; -.
DR HOGENOM; CLU_006936_0_0_1; -.
DR InParanoid; Q9H7N4; -.
DR OMA; PDERAPT; -.
DR OrthoDB; 332377at2759; -.
DR PhylomeDB; Q9H7N4; -.
DR TreeFam; TF332183; -.
DR PathwayCommons; Q9H7N4; -.
DR SignaLink; Q9H7N4; -.
DR BioGRID-ORCS; 58506; 186 hits in 1082 CRISPR screens.
DR ChiTaRS; SCAF1; human.
DR GenomeRNAi; 58506; -.
DR Pharos; Q9H7N4; Tbio.
DR PRO; PR:Q9H7N4; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9H7N4; protein.
DR Bgee; ENSG00000126461; Expressed in sural nerve and 118 other tissues.
DR ExpressionAtlas; Q9H7N4; baseline and differential.
DR Genevisible; Q9H7N4; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; IPI:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR InterPro; IPR042841; SCAF1.
DR PANTHER; PTHR47013; PTHR47013; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT CHAIN 1..1312
FT /note="Splicing factor, arginine/serine-rich 19"
FT /id="PRO_0000299406"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1312
FT /note="Necessary for interaction with the CTD domain of
FT POLR2A"
FT REGION 1277..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..227
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..289
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..440
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..613
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..650
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..926
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..959
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..990
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1041
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1312
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 706
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 725
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 732
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 734
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 872
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 963
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U4C3"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="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 976
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 989
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 992
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U4C3"
FT MOD_RES 1001
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 865
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 895
FT /note="T -> A (in dbSNP:rs3745470)"
FT /id="VAR_052235"
FT VARIANT 1146
FT /note="M -> T (in dbSNP:rs2304208)"
FT /id="VAR_052236"
FT CONFLICT 420
FT /note="T -> P (in Ref. 2; BAB15734 and 3; AAH53992)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1312 AA; 139270 MW; 0CB1C87C963C52BD CRC64;
MEEEDESRGK TEESGEDRGD GPPDRDPTLS PSAFILRAIQ QAVGSSLQGD LPNDKDGSRC
HGLRWRRCRS PRSEPRSQES GGTDTATVLD MATDSFLAGL VSVLDPPDTW VPSRLDLRPG
ESEDMLELVA EVRIGDRDPI PLPVPSLLPR LRAWRTGKTV SPQSNSSRPT CARHLTLGTG
DGGPAPPPAP SSASSSPSPS PSSSSPSPPP PPPPPAPPAP PAPRFDIYDP FHPTDEAYSP
PPAPEQKYDP FEPTGSNPSS SAGTPSPEEE EEEEEEEEEE EEDEEEEEGL SQSISRISET
LAGIYDDNSL SQDFPGDESP RPDAQPTQPT PAPGTPPQVD STRADGAMRR RVFVVGTEAE
ACREGKVSVE VVTAGGAALP PPLLPPGDSE IEEGEIVQPE EEPRLALSLF RPGGRAARPT
PAASATPTAQ PLPQPPAPRA PEGDDFLSLH AESDGEGALQ VDLGEPAPAP PAADSRWGGL
DLRRKILTQR RERYRQRSPS PAPAPAPAAA AGPPTRKKSR RERKRSGEAK EAASSSSGTQ
PAPPAPASPW DSKKHRSRDR KPGSHASSSA RRRSRSRSRS RSTRRRSRST DRRRGGSRRS
RSREKRRRRR RSASPPPATS SSSSSRRERH RGKHRDGGGS KKKKKRSRSR GEKRSGDGSE
KAPAPAPPPS GSTSCGDRDS RRRGAVPPSI QDLTDHDLFA IKRTITVGRL DKSDPRGPSP
APASSPKREV LYDSEGLSGE ERGGKSSQKD RRRSGAASSS SSSREKGSRR KALDGGDRDR
DRDRDRDRDR SSKKARPPKE SAPSSGPPPK PPVSSGSGSS SSSSSCSSRK VKLQSKVAVL
IREGVSSTTP AKDAASAGLG SIGVKFSRDR ESRSPFLKPD ERAPTEMAKA APGSTKPKKT
KVKAKAGAKK TKGTKGKTKP SKTRKKVRSG GGSGGSGGQV SLKKSKADSC SQAAGTKGAE
ETSWSGEERA AKVPSTPPPK AAPPPPALTP DSQTVDSSCK TPEVSFLPEE ATEEAGVRGG
AEEEEEEEEE EEEEEEEEEQ QPATTTATST AAAAPSTAPS AGSTAGDSGA EDGPASRVSQ
LPTLPPPMPW NLPAGVDCTT SGVLALTALL FKMEEANLAS RAKAQELIQA TNQILSHRKP
PSSLGMTPAP VPTSLGLPPG PSSYLLPGSL PLGGCGSTPP TPTGLAATSD KREGSSSSEG
RGDTDKYLKK LHTQERAVEE VKLAIKPYYQ KKDITKEEYK DILRKAVHKI CHSKSGEINP
VKVSNLVRAY VQRYRYFRKH GRKPGDPPGP PRPPKEPGPP DKGGPGLPLP PL
