ID   UBE2O_MOUSE             Reviewed;        1288 AA.
AC   Q6ZPJ3; A2A7X3; Q60800; Q6PCR9; Q7TPN2; Q8BLE8;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme UBE2O;
DE            EC=2.3.2.24;
DE   AltName: Full=E2/E3 hybrid ubiquitin-protein ligase UBE2O;
DE   AltName: Full=Ubiquitin carrier protein O;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2 O;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2 of 230 kDa;
DE            Short=Ubiquitin-conjugating enzyme E2-230K;
DE   AltName: Full=Ubiquitin-protein ligase O;
GN   Name=Ube2o; Synonyms=Kiaa1734;
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].
RC   TISSUE=Embryonic tail;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 103-628, TISSUE SPECIFICITY, AND INDUCTION.
RC   TISSUE=Reticulocyte;
RX   PubMed=7761435; DOI=10.1073/pnas.92.11.4982;
RA   Wefes I., Mastrandrea L.D., Haldeman M., Koury S.T., Tamburlin J.,
RA   Pickart C.M., Finley D.;
RT   "Induction of ubiquitin-conjugating enzymes during terminal erythroid
RT   differentiation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:4982-4986(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-1288.
RC   STRAIN=FVB/N; TISSUE=Liver;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 867-1288.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
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   [6]
RP   ACTIVITY REGULATION.
RX   PubMed=8634298; DOI=10.1021/bi952105y;
RA   Berleth E.S., Pickart C.M.;
RT   "Mechanism of ubiquitin conjugating enzyme E2-230K: catalysis involving a
RT   thiol relay?";
RL   Biochemistry 35:1664-1671(1996).
RN   [7]
RP   INTERACTION WITH CPNE1 AND CPNE4.
RX   PubMed=12522145; DOI=10.1074/jbc.m212632200;
RA   Tomsig J.L., Snyder S.L., Creutz C.E.;
RT   "Identification of targets for calcium signaling through the copine family
RT   of proteins. Characterization of a coiled-coil copine-binding motif.";
RL   J. Biol. Chem. 278:10048-10054(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-84; SER-833 AND
RP   SER-836, AND 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   [9]
RP   IDENTIFICATION BY 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-84; SER-394; SER-436;
RP   SER-833; THR-835 AND SER-836, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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   [11]
RP   INTERACTION WITH UBR2.
RX   PubMed=31268597; DOI=10.15252/embj.2019101996;
RA   Xu H., Shi J., Gao H., Liu Y., Yang Z., Shao F., Dong N.;
RT   "The N-end rule ubiquitin ligase UBR2 mediates NLRP1B inflammasome
RT   activation by anthrax lethal toxin.";
RL   EMBO J. 38:e101996-e101996(2019).
CC   -!- FUNCTION: E2/E3 hybrid ubiquitin-protein ligase that displays both E2
CC       and E3 ligase activities and mediates monoubiquitination of target
CC       proteins. Negatively regulates TRAF6-mediated NF-kappa-B activation
CC       independently of its E2 activity. Acts as a positive regulator of BMP7
CC       signaling by mediating monoubiquitination of SMAD6, thereby regulating
CC       adipogenesis. Mediates monoubiquitination at different sites of the
CC       nuclear localization signal (NLS) of BAP1, leading to cytoplasmic
CC       retention of BAP1. Also able to monoubiquitinate the NLS of other
CC       chromatin-associated proteins, such as INO80 and CXXC1, affecting their
CC       subcellular location. Acts as a regulator of retrograde transport by
CC       assisting the TRIM27:MAGEL2 E3 ubiquitin ligase complex to mediate
CC       'Lys-63'-linked ubiquitination of WASHC1, leading to promote endosomal
CC       F-actin assembly. {ECO:0000250|UniProtKB:Q9C0C9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-
CC         cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.24; Evidence={ECO:0000250|UniProtKB:Q9C0C9,
CC         ECO:0000255|PROSITE-ProRule:PRU00388};
CC   -!- ACTIVITY REGULATION: Inhibited by inorganic arsenite such as
CC       phenylarsenoxides. {ECO:0000269|PubMed:8634298}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBUNIT: Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA
CC       domain) (PubMed:12522145). Interacts with UBR2 (PubMed:31268597).
CC       {ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:31268597}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9C0C9}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9C0C9}. Note=Mainly localizes to the cytoplasm.
CC       {ECO:0000250|UniProtKB:Q9C0C9}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in reticulocytes.
CC       {ECO:0000269|PubMed:7761435}.
CC   -!- INDUCTION: By EPO/Erythropoietin which induces erythroid
CC       differentiation. {ECO:0000269|PubMed:7761435}.
CC   -!- PTM: Phosphorylated. Phosphorylation affects subcellular location.
CC       {ECO:0000250|UniProtKB:Q9C0C9}.
CC   -!- PTM: Ubiquitinated: autoubiquitinates, possibly affecting its
CC       subcellular location. {ECO:0000250|UniProtKB:Q9C0C9}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA69916.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAH59193.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC32345.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC98241.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK129431; BAC98241.1; ALT_INIT; mRNA.
DR   EMBL; AL607039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL645851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U20780; AAA69916.1; ALT_FRAME; mRNA.
DR   EMBL; BC059193; AAH59193.1; ALT_INIT; mRNA.
DR   EMBL; AK045398; BAC32345.1; ALT_INIT; mRNA.
DR   CCDS; CCDS25670.1; -.
DR   PIR; I49264; I49264.
DR   RefSeq; NP_776116.2; NM_173755.3.
DR   AlphaFoldDB; Q6ZPJ3; -.
DR   SMR; Q6ZPJ3; -.
DR   BioGRID; 229895; 17.
DR   IntAct; Q6ZPJ3; 5.
DR   MINT; Q6ZPJ3; -.
DR   STRING; 10090.ENSMUSP00000080791; -.
DR   GlyGen; Q6ZPJ3; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6ZPJ3; -.
DR   MetOSite; Q6ZPJ3; -.
DR   PhosphoSitePlus; Q6ZPJ3; -.
DR   SwissPalm; Q6ZPJ3; -.
DR   EPD; Q6ZPJ3; -.
DR   jPOST; Q6ZPJ3; -.
DR   MaxQB; Q6ZPJ3; -.
DR   PaxDb; 10090-ENSMUSP00000080791; -.
DR   PeptideAtlas; Q6ZPJ3; -.
DR   ProteomicsDB; 298182; -.
DR   Pumba; Q6ZPJ3; -.
DR   Antibodypedia; 32408; 202 antibodies from 36 providers.
DR   DNASU; 217342; -.
DR   Ensembl; ENSMUST00000082152.5; ENSMUSP00000080791.5; ENSMUSG00000020802.9.
DR   GeneID; 217342; -.
DR   KEGG; mmu:217342; -.
DR   UCSC; uc007mlm.1; mouse.
DR   AGR; MGI:2444266; -.
DR   CTD; 63893; -.
DR   MGI; MGI:2444266; Ube2o.
DR   VEuPathDB; HostDB:ENSMUSG00000020802; -.
DR   eggNOG; KOG0895; Eukaryota.
DR   GeneTree; ENSGT00940000160755; -.
DR   HOGENOM; CLU_002088_1_0_1; -.
DR   InParanoid; Q6ZPJ3; -.
DR   OMA; ENQYFYE; -.
DR   OrthoDB; 5311053at2759; -.
DR   PhylomeDB; Q6ZPJ3; -.
DR   TreeFam; TF325556; -.
DR   BRENDA; 2.3.2.25; 3474.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 217342; 5 hits in 76 CRISPR screens.
DR   ChiTaRS; Ube2o; mouse.
DR   PRO; PR:Q6ZPJ3; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q6ZPJ3; Protein.
DR   Bgee; ENSMUSG00000020802; Expressed in blood and 231 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:MGI.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR46116; (E3-INDEPENDENT) E2 UBIQUITIN-CONJUGATING ENZYME; 1.
DR   PANTHER; PTHR46116:SF12; (E3-INDEPENDENT) E2 UBIQUITIN-CONJUGATING ENZYME; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50127; UBC_2; 1.
DR   Genevisible; Q6ZPJ3; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Cytoplasm; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN           1..1288
FT                   /note="(E3-independent) E2 ubiquitin-conjugating enzyme
FT                   UBE2O"
FT                   /id="PRO_0000280638"
FT   DOMAIN          950..1110
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          80..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          396..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          711..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          872..899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1158..1247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          809..879
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        402..418
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..510
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..529
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..739
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        872..893
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1196..1222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1037
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C0C9"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         84
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         394
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         436
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         483
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C0C9"
FT   MOD_RES         486
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C0C9"
FT   MOD_RES         510
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C0C9"
FT   MOD_RES         833
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         835
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         836
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         893
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C0C9"
FT   CONFLICT        309
FT                   /note="C -> S (in Ref. 3; AAA69916)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        317..319
FT                   /note="SPP -> CPR (in Ref. 3; AAA69916)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        343
FT                   /note="Q -> H (in Ref. 3; AAA69916)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        871
FT                   /note="A -> G (in Ref. 4; BAC32345)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1160
FT                   /note="L -> P (in Ref. 1; BAC98241 and 4; AAH59193)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1288 AA;  140834 MW;  D2BCE5F36A687CE1 CRC64;
     MADPAAPAPA QAQAAAAPTP AAAPAAAAPP PAPATDSASG PSSDSGPEAG SQRLLFSHDL
     VSGRYRGSVH FGLVRLIHGE DSDSEGDDDG RGSSGCSEAG GAGHEEGRAS PLRRGYVRVQ
     WYPEGVKQHV KETKLKLEDR SVVPRDVVRH MRSTDSQCGT VIDVNIDCAV KLIGTNCIIY
     PVNSKDLQHI WPFMYGDYIA YDCWLGKVYD LKNQIILKLS NGARCSMNTE DGAKLYDVCP
     HVSDSGLFFD DSYGFYPGQV LIGPAKIFSS VQWLSGVKPV LSTKSKFRVV VEEVQVVELK
     VTWITKSFCP GGTDSVSPPP SIITQENLGR VKRLGCFDHA QRQLGERCLY VFPAKVEPAK
     IAWECPEKNC AQGEGSMAKK VKRLLKKQVV RIMSCTPDTQ CPRDHSMEDP DKKGEARAGS
     EIGSASPEEQ PDGSASPVEM QDEGSEELQE TCEPLPPFLL KEGGDDGLHS AEQDADDEAA
     DDTDDTSSVT SSASSTTSSQ SGSGTGRKKS IPLSIKNLKR KHKRKKNKVT RDFKPGDRVA
     VEVVTTMTSA DVMWQDGSVE CNIRSNDLFP VHHLDNNEFC PGDFVVDKRV QSCPDPAVYG
     VVQSGDHVGR TCMVKWFKLR PSGDDVELIG EEEDVSVYDI ADHPDFRFRT TDIVIRIGNT
     EDGALPKEDE PSVGQVARVD VSSKVEVVWA DNSKTIILPQ HLYNIESEIE ESDYDSVEGS
     SSGASSDEWE DDSDSWETDN GLVDDEHPKI EELAAILPAE QPTAPEEDKG VVISEEAATA
     AIQGAVAMAA PVAGLMEKAG KDGPPKSFRE LKEAIKILES LKNMTVEQLL TGSPTSPTVE
     PEKPTREKKF LDDIKKLQEN LKKTLDNVAI AEEEKMEAVP DTERKEEKPE VQSPVKAEWP
     SETPVLCQQC GGRPGVTFTS AKGEVFSVLE FAPSNHSFKK IEFQPPEAKK FFSTVRKEMA
     LLATSLPDGI MVKTFEDRMD LFSALIKGPT RTPYEDGLYL FDIQLPNIYP AVPPHFCYLS
     QCSGRLNPNL YDNGKVCVSL LGTWIGKGTE RWTSKSSLLQ VLISIQGLIL VNEPYYNEAG
     FDSDRGLQEG YENSRCYNEM ALIRVVQSMT QLVRRPPEVF EQEIRQHFSV GGWRLVNRIE
     SWLETHAMQE RAQVMPNGAL KDSSSLEPMA AAELSDSGRE EPEDVGMAPG EASQGSDSEG
     GAQGPASASR DHTEQTETAP DASAPPSVRP KRRRKSYRSF LPEKSGYPDI GFPLFPLSKG
     FIKSIRGVLT QFRAALLEAG MPESTEDK
//