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Luc7-like protein 3 (Cisplatin resistance-associated-overexpressed protein) (Luc7A) (Okadaic acid-inducible phosphoprotein OA48-18) (cAMP regulatory element-associated protein 1) (CRE-associated protein 1) (CREAP-1)

 LC7L3_HUMAN             Reviewed;         432 AA.
O95232; B3KN54; D3DTY1; Q6PHR9; Q9NUY0; Q9P2S7;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
02-MAY-2006, sequence version 2.
22-NOV-2017, entry version 133.
RecName: Full=Luc7-like protein 3;
AltName: Full=Cisplatin resistance-associated-overexpressed protein;
AltName: Full=Luc7A;
AltName: Full=Okadaic acid-inducible phosphoprotein OA48-18;
AltName: Full=cAMP regulatory element-associated protein 1;
Short=CRE-associated protein 1;
Short=CREAP-1;
Name=LUC7L3; Synonyms=CREAP1, CROP, O48;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=10631324; DOI=10.1016/S0014-5793(99)01744-5;
Nishii Y., Morishima M., Kakehi Y., Umehara K., Kioka N., Terano Y.,
Amachi T., Ueda K.;
"CROP/Luc7A, a novel serine/arginine-rich nuclear protein, isolated
from cisplatin-resistant cell line.";
FEBS Lett. 465:153-156(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Placenta;
PubMed=16462885; DOI=10.1139/o05-139;
Shipman K.L., Robinson P.J., King B.R., Smith R., Nicholson R.C.;
"Identification of a family of DNA-binding proteins with homology to
RNA splicing factors.";
Biochem. Cell Biol. 84:9-19(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=PNS;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 378-432.
TISSUE=Fetal brain;
PubMed=10754390; DOI=10.1007/BF02256622;
Chin L.S., Singh S.K., Wang Q., Murray S.F.;
"Identification of okadaic-acid-induced genes by mRNA differential
display in glioma cells.";
J. Biomed. Sci. 7:152-159(2000).
[7]
INTERACTION WITH SFRS1, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=12565863; DOI=10.1016/S0006-291X(02)03017-6;
Umehara H., Nishii Y., Morishima M., Kakehi Y., Kioka N., Amachi T.,
Koizumi J., Hagiwara M., Ueda K.;
"Effect of cisplatin treatment on speckled distribution of a
serine/arginine-rich nuclear protein CROP/Luc7A.";
Biochem. Biophys. Res. Commun. 301:324-329(2003).
[8]
INTERACTION WITH RSRC1.
PubMed=15798186; DOI=10.1128/MCB.25.8.2969-2980.2005;
Cazalla D., Newton K., Caceres J.F.;
"A novel SR-related protein is required for the second step of pre-
mRNA splicing.";
Mol. Cell. Biol. 25:2969-2980(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[10]
INTERACTION WITH RBM25.
PubMed=18663000; DOI=10.1128/MCB.00560-08;
Zhou A., Ou A.C., Cho A., Benz E.J. Jr., Huang S.C.;
"Novel splicing factor RBM25 modulates Bcl-x pre-mRNA 5' splice site
selection.";
Mol. Cell. Biol. 28:5924-5936(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425 AND SER-431, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-231, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
INTERACTION WITH JMJD6.
PubMed=19574390; DOI=10.1126/science.1175865;
Webby C.J., Wolf A., Gromak N., Dreger M., Kramer H., Kessler B.,
Nielsen M.L., Schmitz C., Butler D.S., Yates J.R. III, Delahunty C.M.,
Hahn P., Lengeling A., Mann M., Proudfoot N.J., Schofield C.J.,
Boettger A.;
"Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated
with RNA splicing.";
Science 325:90-93(2009).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-3; SER-425 AND SER-431, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420 AND SER-425, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-115; SER-425
AND SER-431, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
INTERACTION WITH RRP1B.
PubMed=23604122; DOI=10.1038/onc.2013.133;
NISC Comparative Sequencing Program;
Lee M., Dworkin A.M., Gildea D., Trivedi N.S., Moorhead G.B.,
Crawford N.P.;
"RRP1B is a metastasis modifier that regulates the expression of
alternative mRNA isoforms through interactions with SRSF1.";
Oncogene 33:1818-1827(2014).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-424, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-424, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Binds cAMP regulatory element DNA sequence. May play a
role in RNA splicing. {ECO:0000269|PubMed:16462885}.
-!- SUBUNIT: May interact with SFRS1 and form homodimers
(PubMed:12565863). Interacts with JMJD6 (PubMed:19574390).
Interacts with RBM25 (PubMed:18663000). Interacts with RSRC1 (via
Arg/Ser-rich domain) (PubMed:15798186). Interacts with RRP1B
(PubMed:23604122). {ECO:0000269|PubMed:12565863,
ECO:0000269|PubMed:15798186, ECO:0000269|PubMed:18663000,
ECO:0000269|PubMed:19574390, ECO:0000269|PubMed:23604122}.
-!- SUBCELLULAR LOCATION: Nucleus speckle
{ECO:0000269|PubMed:10631324, ECO:0000269|PubMed:12565863}.
Note=The subnuclear localization is affected by cisplatin.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O95232-1; Sequence=Displayed;
Name=2;
IsoId=O95232-2; Sequence=VSP_018136, VSP_018137;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay. No
experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Highest levels in heart,
brain, pancreas, thymus, ovary, small intestine and peripheral
blood leukocytes, as well as cerebellum, putamen and pituitary
gland. Lowest levels in lung, liver and kidney. Also expressed in
fetal tissues, including brain, heart, kidney, thymus and lung.
{ECO:0000269|PubMed:10631324, ECO:0000269|PubMed:16462885}.
-!- PTM: Phosphorylated in vitro by SRPK1, SRPK2 and CLK1.
{ECO:0000269|PubMed:12565863}.
-!- SIMILARITY: Belongs to the Luc7 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC79807.1; Type=Erroneous translation; Note=Erroneous CDS prediction.; Evidence={ECO:0000305};
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EMBL; AB034205; BAA90542.1; -; mRNA.
EMBL; DQ013876; AAY26238.1; -; mRNA.
EMBL; AK001925; BAA91981.1; -; mRNA.
EMBL; AK023672; BAG51216.1; -; mRNA.
EMBL; CH471109; EAW94583.1; -; Genomic_DNA.
EMBL; CH471109; EAW94585.1; -; Genomic_DNA.
EMBL; CH471109; EAW94587.1; -; Genomic_DNA.
EMBL; BC056409; AAH56409.1; -; mRNA.
EMBL; AF069250; AAC79807.1; ALT_SEQ; mRNA.
CCDS; CCDS11573.1; -. [O95232-1]
RefSeq; NP_006098.2; NM_006107.3. [O95232-1]
RefSeq; NP_057508.2; NM_016424.4. [O95232-1]
UniGene; Hs.130293; -.
ProteinModelPortal; O95232; -.
SMR; O95232; -.
BioGrid; 119710; 56.
CORUM; O95232; -.
IntAct; O95232; 17.
MINT; MINT-1683180; -.
STRING; 9606.ENSP00000240304; -.
iPTMnet; O95232; -.
PhosphoSitePlus; O95232; -.
SwissPalm; O95232; -.
BioMuta; LUC7L3; -.
EPD; O95232; -.
MaxQB; O95232; -.
PaxDb; O95232; -.
PeptideAtlas; O95232; -.
PRIDE; O95232; -.
DNASU; 51747; -.
Ensembl; ENST00000240304; ENSP00000240304; ENSG00000108848. [O95232-1]
Ensembl; ENST00000505658; ENSP00000425092; ENSG00000108848. [O95232-1]
GeneID; 51747; -.
KEGG; hsa:51747; -.
UCSC; uc002isr.4; human. [O95232-1]
CTD; 51747; -.
DisGeNET; 51747; -.
EuPathDB; HostDB:ENSG00000108848.15; -.
GeneCards; LUC7L3; -.
HGNC; HGNC:24309; LUC7L3.
HPA; HPA018475; -.
HPA; HPA018484; -.
HPA; HPA020017; -.
MIM; 609434; gene.
neXtProt; NX_O95232; -.
OpenTargets; ENSG00000108848; -.
PharmGKB; PA165432062; -.
eggNOG; KOG0796; Eukaryota.
eggNOG; COG5200; LUCA.
GeneTree; ENSGT00730000110670; -.
HOGENOM; HOG000215956; -.
HOVERGEN; HBG062167; -.
InParanoid; O95232; -.
PhylomeDB; O95232; -.
TreeFam; TF354312; -.
ChiTaRS; LUC7L3; human.
GeneWiki; CROP_(gene); -.
GenomeRNAi; 51747; -.
PRO; PR:O95232; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108848; -.
ExpressionAtlas; O95232; baseline and differential.
Genevisible; O95232; HS.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003729; F:mRNA binding; IMP:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0006376; P:mRNA splice site selection; IBA:GO_Central.
GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
InterPro; IPR004882; Luc7-rel.
PANTHER; PTHR12375; PTHR12375; 2.
Pfam; PF03194; LUC7; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Coiled coil; Complete proteome;
DNA-binding; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 432 Luc7-like protein 3.
/FTId=PRO_0000058013.
COILED 124 181 {ECO:0000255}.
COMPBIAS 228 282 Glu-rich.
COMPBIAS 235 395 Arg/Ser-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:23186163}.
MOD_RES 115 115 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 231 231 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 425 425 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 431 431 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CROSSLNK 424 424 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 424 424 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 56 79 GPCEKIHDENLRKQYEKSSRFMKV -> DVFGRGDNISDVS
KFLEDDKWMEE (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_018136.
VAR_SEQ 80 432 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_018137.
CONFLICT 217 217 H -> Y (in Ref. 3; BAA91981).
{ECO:0000305}.
CONFLICT 378 379 EK -> HE (in Ref. 6; AAC79807).
{ECO:0000305}.
SEQUENCE 432 AA; 51466 MW; E75F55EC0137310C CRC64;
MISAAQLLDE LMGRDRNLAP DEKRSNVRWD HESVCKYYLC GFCPAELFTN TRSDLGPCEK
IHDENLRKQY EKSSRFMKVG YERDFLRYLQ SLLAEVERRI RRGHARLALS QNQQSSGAAG
PTGKNEEKIQ VLTDKIDVLL QQIEELGSEG KVEEAQGMMK LVEQLKEERE LLRSTTSTIE
SFAAQEKQME VCEVCGAFLI VGDAQSRVDD HLMGKQHMGY AKIKATVEEL KEKLRKRTEE
PDRDERLKKE KQEREEREKE REREREERER KRRREEEERE KERARDRERR KRSRSRSRHS
SRTSDRRCSR SRDHKRSRSR ERRRSRSRDR RRSRSHDRSE RKHRSRSRDR RRSKSRDRKS
YKHRSKSRDR EQDRKSKEKE KRGSDDKKSS VKSGSREKQS EDTNTESKES DTKNEVNGTS
EDIKSEGDTQ SN


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