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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.
13-FEB-2019, entry version 144.
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; -.
UniGene; Hs.655691; -.
ProteinModelPortal; O95232; -.
SMR; O95232; -.
BioGrid; 119710; 76.
CORUM; O95232; -.
IntAct; O95232; 21.
MINT; O95232; -.
STRING; 9606.ENSP00000240304; -.
CarbonylDB; O95232; -.
iPTMnet; O95232; -.
PhosphoSitePlus; O95232; -.
SwissPalm; O95232; -.
BioMuta; LUC7L3; -.
EPD; O95232; -.
jPOST; O95232; -.
MaxQB; O95232; -.
PaxDb; O95232; -.
PeptideAtlas; O95232; -.
PRIDE; O95232; -.
ProteomicsDB; 50730; -.
ProteomicsDB; 50731; -. [O95232-2]
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; ENSGT00940000154855; -.
HOGENOM; HOG000215956; -.
HOVERGEN; HBG062167; -.
InParanoid; O95232; -.
OrthoDB; 1499212at2759; -.
PhylomeDB; O95232; -.
TreeFam; TF354312; -.
ChiTaRS; LUC7L3; human.
GeneWiki; CROP_(gene); -.
GenomeRNAi; 51747; -.
PRO; PR:O95232; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108848; Expressed in 242 organ(s), highest expression level in testis.
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; HDA: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; 1.
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);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 424 424 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {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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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP2199: Seed Development
WP731: Sterol regulatory element binding protein related
WP1493: Carbon assimilation C4 pathway
WP1654: gamma-Hexachlorocyclohexane degradation
WP1700: Selenoamino acid metabolism
WP1909: Signal regulatory protein (SIRP) family interactions
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair

Related Genes :
[ATF2 CREB2 CREBP1] Cyclic AMP-dependent transcription factor ATF-2 (cAMP-dependent transcription factor ATF-2) (EC 2.3.1.48) (Activating transcription factor 2) (Cyclic AMP-responsive element-binding protein 2) (CREB-2) (cAMP-responsive element-binding protein 2) (HB16) (Histone acetyltransferase ATF2) (cAMP response element-binding protein CRE-BP1)
[AHK4 CRE1 RAW1 WOL At2g01830 T23K3.2] Histidine kinase 4 (EC 2.7.13.3) (Arabidopsis histidine kinase 4) (AtHK4) (Cytokinin receptor CYTOKININ RESPONSE 1) (AtCRE1) (Cytokinin receptor CRE1) (Phosphoprotein phosphatase AHK4) (EC 3.1.3.16) (Protein AUTHENTIC HIS-KINASE 4) (Protein ROOT AS IN WOL 1) (Protein WOODEN LEG)
[Creb3l4 Atce1 Jal Tisp40] Cyclic AMP-responsive element-binding protein 3-like protein 4 (cAMP-responsive element-binding protein 3-like protein 4) (Attaching to CRE-like 1) (ATCE1) (Acre1) (Transcript induced in spermiogenesis protein 40) (Tisp40) (mJAL) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 4]
[Atf2] Cyclic AMP-dependent transcription factor ATF-2 (cAMP-dependent transcription factor ATF-2) (EC 2.3.1.48) (Activating transcription factor 2) (MXBP protein) (cAMP response element-binding protein CRE-BP1)
[CREB1] Cyclic AMP-responsive element-binding protein 1 (CREB-1) (cAMP-responsive element-binding protein 1)
[Atf2] Cyclic AMP-dependent transcription factor ATF-2 (cAMP-dependent transcription factor ATF-2) (EC 2.3.1.48) (Activating transcription factor 2) (cAMP response element-binding protein CRE-BP1)
[Creb3l1 Oasis] Cyclic AMP-responsive element-binding protein 3-like protein 1 (cAMP-responsive element-binding protein 3-like protein 1) (Old astrocyte specifically-induced substance) (OASIS) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 1 (Oasis N-terminal fragment) (OA-N)]
[Srebf1 Srebp1] Sterol regulatory element-binding protein 1 (SREBP-1) (Sterol regulatory element-binding transcription factor 1) [Cleaved into: Processed sterol regulatory element-binding protein 1]
[SRPK1] SRSF protein kinase 1 (EC 2.7.11.1) (SFRS protein kinase 1) (Serine/arginine-rich protein-specific kinase 1) (SR-protein-specific kinase 1)
[CREB3 LZIP] Cyclic AMP-responsive element-binding protein 3 (CREB-3) (cAMP-responsive element-binding protein 3) (Leucine zipper protein) (Luman) (Transcription factor LZIP-alpha) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3 (N-terminal Luman) (Transcriptionally active form)]
[Creb1 Creb-1] Cyclic AMP-responsive element-binding protein 1 (CREB-1) (cAMP-responsive element-binding protein 1)
[Creb1 Creb-1] Cyclic AMP-responsive element-binding protein 1 (CREB-1) (cAMP-responsive element-binding protein 1)
[Crem] cAMP-responsive element modulator (Inducible cAMP early repressor) (ICER)
[XBP1 TREB5 XBP2] X-box-binding protein 1 (XBP-1) (Tax-responsive element-binding protein 5) (TREB-5) [Cleaved into: X-box-binding protein 1, cytoplasmic form; X-box-binding protein 1, luminal form]
[PRKAR1A PKR1 PRKAR1 TSE1] cAMP-dependent protein kinase type I-alpha regulatory subunit (Tissue-specific extinguisher 1) (TSE1)
[JMJD6 KIAA0585 PSR PTDSR] Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC 1.14.11.-) (Histone arginine demethylase JMJD6) (JmjC domain-containing protein 6) (Jumonji domain-containing protein 6) (Lysyl-hydroxylase JMJD6) (Peptide-lysine 5-dioxygenase JMJD6) (Phosphatidylserine receptor) (Protein PTDSR)
[Atf5 Atfx Nap1] Cyclic AMP-dependent transcription factor ATF-5 (cAMP-dependent transcription factor ATF-5) (Activating transcription factor 5-alpha/beta) (BZIP protein ATF7) (NAP1) (NRIF3-associated protein) (Transcription factor ATFx) (Transcription factor-like protein ODA-10)
[Xbp1 Treb5] X-box-binding protein 1 (XBP-1) (Tax-responsive element-binding protein 5) (TREB-5) [Cleaved into: X-box-binding protein 1, cytoplasmic form; X-box-binding protein 1, luminal form]
[SLC9A3R1 NHERF NHERF1] Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (NHERF-1) (Ezrin-radixin-moesin-binding phosphoprotein 50) (EBP50) (Regulatory cofactor of Na(+)/H(+) exchanger) (Sodium-hydrogen exchanger regulatory factor 1) (Solute carrier family 9 isoform A3 regulatory factor 1)
[RBM25 RNPC7] RNA-binding protein 25 (Arg/Glu/Asp-rich protein of 120 kDa) (RED120) (Protein S164) (RNA-binding motif protein 25) (RNA-binding region-containing protein 7)
[ERECTA ER QRP1 QRS1 TE1 At2g26330 T1D16.3] LRR receptor-like serine/threonine-protein kinase ERECTA (EC 2.7.11.1) (Protein QUANTITATIVE RESISTANCE TO PLECTOSPHAERELLA 1) (Protein QUANTITATIVE RESISTANCE TO RALSTONIA SOLANACEARUM 1) (Protein TRANSPIRATION EFFICIENCY 1)
[CREB3L3 CREBH HYST1481] Cyclic AMP-responsive element-binding protein 3-like protein 3 (cAMP-responsive element-binding protein 3-like protein 3) (Transcription factor CREB-H) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 3]
[Crtc1 Kiaa0616 Mect1 Torc1] CREB-regulated transcription coactivator 1 (Mucoepidermoid carcinoma translocated protein 1 homolog) (Transducer of regulated cAMP response element-binding protein 1) (TORC-1) (Transducer of CREB protein 1)
[NPR1 NIM1 SAI1 At1g64280 F15H21.6] Regulatory protein NPR1 (BTB/POZ domain-containing protein NPR1) (Non-inducible immunity protein 1) (Nim1) (Nonexpresser of PR genes 1) (Salicylic acid insensitive 1) (Sai1)
[CREM] cAMP-responsive element modulator (Inducible cAMP early repressor) (ICER)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[HIF1A BHLHE78 MOP1 PASD8] Hypoxia-inducible factor 1-alpha (HIF-1-alpha) (HIF1-alpha) (ARNT-interacting protein) (Basic-helix-loop-helix-PAS protein MOP1) (Class E basic helix-loop-helix protein 78) (bHLHe78) (Member of PAS protein 1) (PAS domain-containing protein 8)
[Scnm1 Scnm1-ps] Sodium channel modifier 1
[DDX58] Probable ATP-dependent RNA helicase DDX58 (EC 3.6.4.13) (DEAD box protein 58) (RIG-I-like receptor 1) (RLR-1) (Retinoic acid-inducible gene 1 protein) (RIG-1) (Retinoic acid-inducible gene I protein) (RIG-I)

Bibliography :