PAIRB_MOUSE
ID PAIRB_MOUSE Reviewed; 407 AA.
AC Q9CY58; Q8BHS2; Q8BHU0; Q91WP3; Q9CSN0; Q9DBY6;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Plasminogen activator inhibitor 1 RNA-binding protein;
DE AltName: Full=PAI1 RNA-binding protein 1;
DE Short=PAI-RBP1;
DE AltName: Full=SERPINE1 mRNA-binding protein 1;
GN Name=Serbp1; Synonyms=Pairbp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Embryonic liver, Lung, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Eye, and Salivary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-234; SER-329 AND
RP SER-391, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND THR-240
RP (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND THR-234
RP (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52; LYS-122 AND LYS-328, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP INTERACTION WITH SPIN1.
RX PubMed=23894536; DOI=10.1371/journal.pone.0069764;
RA Chew T.G., Peaston A., Lim A.K., Lorthongpanich C., Knowles B.B.,
RA Solter D.;
RT "A tudor domain protein SPINDLIN1 interacts with the mRNA-binding protein
RT SERBP1 and is involved in mouse oocyte meiotic resumption.";
RL PLoS ONE 8:E69764-E69764(2013).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-165; ARG-188; ARG-216; ARG-363;
RP ARG-366 AND ARG-369, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, and Embryo;
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).
CC -!- FUNCTION: May play a role in the regulation of mRNA stability. Binds to
CC the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers
CC cyclic nucleotide regulation of message decay. Seems to play a role in
CC PML-nuclear bodies formation. {ECO:0000250|UniProtKB:Q8NC51}.
CC -!- SUBUNIT: Interacts with SPIN1 (PubMed:23894536). Interacts with CHD3
CC and TDRD3. Interacts with ZDHHC17 (via ANK repeats) (By similarity).
CC {ECO:0000250|UniProtKB:Q8NC51, ECO:0000269|PubMed:23894536}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NC51}. Nucleus
CC {ECO:0000250|UniProtKB:Q8NC51}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q8NC51}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9CY58-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CY58-2; Sequence=VSP_011633;
CC Name=3;
CC IsoId=Q9CY58-3; Sequence=VSP_011632, VSP_011633;
CC Name=4;
CC IsoId=Q9CY58-4; Sequence=VSP_011634, VSP_011635;
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to intron retention.
CC {ECO:0000305}.
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DR EMBL; AK004678; BAB23466.1; -; mRNA.
DR EMBL; AK010860; BAB27229.1; -; mRNA.
DR EMBL; AK012390; BAB28207.1; -; mRNA.
DR EMBL; AK045190; BAC32255.1; -; mRNA.
DR EMBL; AK088278; BAC40253.1; -; mRNA.
DR EMBL; BC013665; AAH13665.1; -; mRNA.
DR EMBL; BC030502; AAH30502.1; -; mRNA.
DR CCDS; CCDS20219.1; -. [Q9CY58-1]
DR CCDS; CCDS85060.1; -. [Q9CY58-2]
DR CCDS; CCDS85062.1; -. [Q9CY58-3]
DR RefSeq; NP_001107037.1; NM_001113565.1. [Q9CY58-2]
DR RefSeq; NP_001107038.1; NM_001113566.1. [Q9CY58-3]
DR RefSeq; NP_080090.2; NM_025814.2. [Q9CY58-1]
DR PDB; 7LS1; EM; 3.30 A; A=1-407.
DR PDB; 7LS2; EM; 3.10 A; A=1-407.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; Q9CY58; -.
DR BioGRID; 211777; 33.
DR IntAct; Q9CY58; 5.
DR MINT; Q9CY58; -.
DR STRING; 10090.ENSMUSP00000039110; -.
DR iPTMnet; Q9CY58; -.
DR PhosphoSitePlus; Q9CY58; -.
DR SwissPalm; Q9CY58; -.
DR EPD; Q9CY58; -.
DR jPOST; Q9CY58; -.
DR MaxQB; Q9CY58; -.
DR PaxDb; Q9CY58; -.
DR PeptideAtlas; Q9CY58; -.
DR PRIDE; Q9CY58; -.
DR ProteomicsDB; 287768; -. [Q9CY58-1]
DR ProteomicsDB; 287769; -. [Q9CY58-2]
DR ProteomicsDB; 287770; -. [Q9CY58-3]
DR ProteomicsDB; 287771; -. [Q9CY58-4]
DR TopDownProteomics; Q9CY58-1; -. [Q9CY58-1]
DR TopDownProteomics; Q9CY58-3; -. [Q9CY58-3]
DR Antibodypedia; 19619; 389 antibodies from 28 providers.
DR DNASU; 66870; -.
DR Ensembl; ENSMUST00000042990; ENSMUSP00000039110; ENSMUSG00000036371. [Q9CY58-1]
DR Ensembl; ENSMUST00000203077; ENSMUSP00000144913; ENSMUSG00000036371. [Q9CY58-2]
DR Ensembl; ENSMUST00000204293; ENSMUSP00000145472; ENSMUSG00000036371. [Q9CY58-3]
DR GeneID; 66870; -.
DR KEGG; mmu:66870; -.
DR UCSC; uc009cfh.1; mouse. [Q9CY58-2]
DR UCSC; uc009cfi.1; mouse. [Q9CY58-4]
DR UCSC; uc009cfj.2; mouse. [Q9CY58-1]
DR CTD; 26135; -.
DR MGI; MGI:1914120; Serbp1.
DR VEuPathDB; HostDB:ENSMUSG00000036371; -.
DR eggNOG; KOG2945; Eukaryota.
DR GeneTree; ENSGT00520000055591; -.
DR HOGENOM; CLU_037366_2_1_1; -.
DR InParanoid; Q9CY58; -.
DR OMA; NEGADWK; -.
DR OrthoDB; 1183388at2759; -.
DR PhylomeDB; Q9CY58; -.
DR TreeFam; TF318374; -.
DR BioGRID-ORCS; 66870; 16 hits in 75 CRISPR screens.
DR ChiTaRS; Serbp1; mouse.
DR PRO; PR:Q9CY58; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9CY58; protein.
DR Bgee; ENSMUSG00000036371; Expressed in primitive streak and 248 other tissues.
DR ExpressionAtlas; Q9CY58; baseline and differential.
DR Genevisible; Q9CY58; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:HGNC-UCL.
DR GO; GO:0043022; F:ribosome binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0032183; F:SUMO binding; ISS:UniProtKB.
DR GO; GO:0030578; P:PML body organization; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR InterPro; IPR039764; HABP4/SERBP1.
DR InterPro; IPR006861; HABP4_PAIRBP1-bd.
DR InterPro; IPR032381; IHABP4_N.
DR InterPro; IPR027205; SERBP1.
DR PANTHER; PTHR12299; PTHR12299; 1.
DR PANTHER; PTHR12299:SF29; PTHR12299:SF29; 1.
DR Pfam; PF04774; HABP4_PAI-RBP1; 1.
DR Pfam; PF16174; IHABP4_N; 1.
DR SMART; SM01233; HABP4_PAI-RBP1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..407
FT /note="Plasminogen activator inhibitor 1 RNA-binding
FT protein"
FT /id="PRO_0000058183"
FT REGION 33..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 52
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 68
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT MOD_RES 122
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 140
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT MOD_RES 165
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 188
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AXS5"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT MOD_RES 211
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT MOD_RES 216
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 328
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 363
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 366
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 369
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT CROSSLNK 52
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT CROSSLNK 211
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT CROSSLNK 228
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT CROSSLNK 228
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT CROSSLNK 280
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NC51"
FT VAR_SEQ 203..208
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_011632"
FT VAR_SEQ 233..247
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_011633"
FT VAR_SEQ 233..235
FT /note="ESP -> LVF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011634"
FT VAR_SEQ 236..407
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011635"
FT CONFLICT 5
FT /note="L -> P (in Ref. 1; BAC40253)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="F -> S (in Ref. 1; BAB23466)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9CY58-2:237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9CY58-2:240
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9CY58-3:231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9CY58-3:234
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 407 AA; 44714 MW; AC4F61EF7F38A8E5 CRC64;
MPGHLQEGFG CVVTNRFDQL FDDESDPFEV LKAAENKKKE AGGGGVGGPG AKSAAQAAAQ
TNSNAAGKQL RKESQKDRKN PLPPSVGVAD KKEETQPPVA LKKEGIRRVG RRPDQQLQGD
GKLIDRRAER RPPRERRFEK PLEEKGEGGE FSVDRPIIER PIRGRGGLGR GRGGRGRGMG
RGDGFDSRGK REFDRHSGSD RSSFSHYSGL KHEDKRGGSG SHNWGTVKDE LTESPKYIQK
QISYNCSDLD QSNVTEETPE GEEHPVADTE NKENEVEEVK EEGPKEMTLD EWKAIQNKDR
AKVEFNIRKP NEGADGQWKK GFVLHKSKSE EAHAEDSVMD HHFRKPANDI TSQLEINFGD
LGRPGRGGRG GRGGRGRGGR PNRGSRTDKS SASAPDVDDP EAFPALA
