UBR5_MOUSE
ID UBR5_MOUSE Reviewed; 2792 AA.
AC Q80TP3; Q698K9; Q6PEQ8; Q6PFQ9; Q80VL4; Q810V6; Q9CXE9;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=E3 ubiquitin-protein ligase UBR5;
DE EC=2.3.2.26;
DE AltName: Full=E3 ubiquitin-protein ligase, HECT domain-containing 1;
DE AltName: Full=HECT-type E3 ubiquitin transferase UBR5;
DE AltName: Full=Hyperplastic discs protein homolog;
GN Name=Ubr5; Synonyms=Edd, Edd1, Kiaa0896;
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 [MRNA], AND FUNCTION.
RC STRAIN=C57BL/6J;
RX PubMed=15282321; DOI=10.1128/mcb.24.16.7225-7234.2004;
RA Saunders D.N., Hird S.L., Withington S.L., Dunwoodie S.L., Henderson M.J.,
RA Biben C., Sutherland R.L., Ormandy C.J., Watts C.K.W.;
RT "Edd, the murine hyperplastic disc gene, is essential for yolk sac
RT vascularization and chorioallantoic fusion.";
RL Mol. Cell. Biol. 24:7225-7234(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1028-2792.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1292-2792.
RC STRAIN=FVB/N-3; TISSUE=Eye, Liver, and Mammary 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2483-2792.
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16055722; DOI=10.1128/mcb.25.16.7120-7136.2005;
RA Tasaki T., Mulder L.C.F., Iwamatsu A., Lee M.J., Davydov I.V.,
RA Varshavsky A., Muesing M., Kwon Y.T.;
RT "A family of mammalian E3 ubiquitin ligases that contain the UBR box motif
RT and recognize N-degrons.";
RL Mol. Cell. Biol. 25:7120-7136(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen,
RC 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: E3 ubiquitin-protein ligase which is a component of the N-end
CC rule pathway. Ubiquitinates acetylated PCK1. Also acts as a regulator
CC of DNA damage response by acting as a suppressor of RNF168, an E3
CC ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked
CC histone H2A and H2AX at DNA damage sites, thereby acting as a guard
CC against excessive spreading of ubiquitinated chromatin at damaged
CC chromosomes (By similarity). Recognizes and binds to proteins bearing
CC specific N-terminal residues that are destabilizing according to the N-
CC end rule, leading to their ubiquitination and subsequent degradation.
CC Involved in maturation and/or transcriptional regulation of mRNA by
CC activating CDK9 by polyubiquitination. May play a role in control of
CC cell cycle progression. May have tumor suppressor function. Plays an
CC essential role in extraembryonic development. Regulates DNA
CC topoisomerase II binding protein (TopBP1) for the DNA damage response.
CC {ECO:0000250, ECO:0000269|PubMed:15282321,
CC ECO:0000269|PubMed:16055722}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Binds TOPBP1. Associates with CDK9 and TFIIS/TCEA1 and forms a
CC transcription regulatory complex made of CDK9, RNAP II, UBR5 and
CC TFIIS/TCEA1 that can stimulate target gene transcription by recruiting
CC their promoters. Associates with the E3 ligase complex containing
CC DYRK2, EDD/UBR5, DDB1 and DCAF1 proteins (EDVP complex). Interacts
CC directly with DYRK2. Interacts with PIH1D1.
CC {ECO:0000250|UniProtKB:O95071}.
CC -!- INTERACTION:
CC Q80TP3; Q3U2S4-1: Otud5; NbExp=2; IntAct=EBI-2553642, EBI-16131219;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-thioester
CC formation.
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DR EMBL; AY550908; AAT28194.1; -; mRNA.
DR EMBL; AK122398; BAC65680.1; -; mRNA.
DR EMBL; BC049162; AAH49162.1; -; mRNA.
DR EMBL; BC049224; AAH49224.1; -; mRNA.
DR EMBL; BC057458; AAH57458.1; -; mRNA.
DR EMBL; BC057923; AAH57923.1; -; mRNA.
DR EMBL; AK014485; BAB29387.1; -; mRNA.
DR CCDS; CCDS88751.1; -.
DR RefSeq; NP_001074828.2; NM_001081359.3.
DR RefSeq; NP_001106192.1; NM_001112721.2.
DR SMR; Q80TP3; -.
DR BioGRID; 214255; 37.
DR DIP; DIP-56890N; -.
DR IntAct; Q80TP3; 13.
DR MINT; Q80TP3; -.
DR STRING; 10090.ENSMUSP00000105965; -.
DR iPTMnet; Q80TP3; -.
DR PhosphoSitePlus; Q80TP3; -.
DR SwissPalm; Q80TP3; -.
DR EPD; Q80TP3; -.
DR jPOST; Q80TP3; -.
DR MaxQB; Q80TP3; -.
DR PaxDb; Q80TP3; -.
DR PeptideAtlas; Q80TP3; -.
DR PRIDE; Q80TP3; -.
DR ProteomicsDB; 300078; -.
DR GeneID; 70790; -.
DR KEGG; mmu:70790; -.
DR CTD; 51366; -.
DR MGI; MGI:1918040; Ubr5.
DR eggNOG; KOG0943; Eukaryota.
DR InParanoid; Q80TP3; -.
DR OrthoDB; 717at2759; -.
DR PhylomeDB; Q80TP3; -.
DR BRENDA; 2.3.2.26; 3474.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 70790; 27 hits in 112 CRISPR screens.
DR ChiTaRS; Ubr5; mouse.
DR PRO; PR:Q80TP3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80TP3; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:2000780; P:negative regulation of double-strand break repair; ISS:UniProtKB.
DR GO; GO:1901315; P:negative regulation of histone H2A K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0032700; P:negative regulation of interleukin-17 production; IGI:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
DR GO; GO:0050847; P:progesterone receptor signaling pathway; ISS:HGNC-UCL.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:2000779; P:regulation of double-strand break repair; IBA:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
DR CDD; cd14423; CUE_UBR5; 1.
DR Gene3D; 2.130.10.30; -; 1.
DR InterPro; IPR024725; E3_UbLigase_EDD_UBA.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR003126; Znf_UBR.
DR Pfam; PF11547; E3_UbLigase_EDD; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00658; PABP; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF50985; SSF50985; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR SUPFAM; SSF63570; SSF63570; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA damage; DNA repair; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT CHAIN 2..2792
FT /note="E3 ubiquitin-protein ligase UBR5"
FT /id="PRO_0000086932"
FT DOMAIN 2371..2448
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT DOMAIN 2455..2792
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT ZN_FING 1171..1239
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT REGION 77..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1509..1734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1853..1884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1978..2015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2111..2137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2317..2387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2467..2494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1025
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1571
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1572..1602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1616..1645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1654..1679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1870..1884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1990..2008
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2323..2364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2467..2484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2761
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 631
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 922
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 1012
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 1109
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 1129
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 1302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 1349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 1369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 1475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 1543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 1730
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 1735
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 1740
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 1774
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 1963
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 1984
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 2020
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 2022
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 2024
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 2070
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 2207
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 2235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 2283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 2463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 2477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT MOD_RES 2479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95071"
FT CONFLICT 1121
FT /note="S -> P (in Ref. 1; AAT28194)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2792 AA; 308352 MW; 19E5E56E5094F5B6 CRC64;
MTSIHFVVHP LPGTEDQLND RLREVSEKLN KYNLNSHPPL NVLEQATIKQ CVVGPNHAAF
LLEDGRICRI GFSVQPDRLE LGKPDNNDGS KLNSSSGTGR TSRPGRTSDS PWFLSGSETL
GRLAGNTLGS RWSSGVGGSG GGSSGRSSAG ARDSRRQTRV IRTGRDRGSG LLGSQPQPVI
PASVIPEELI SQAQVVLQGK SRSVIIRELQ RTNLDVNLAV NNLLSRDDED GDDGDDTASE
SYLPGEDLMS LLDADIHSAH PSVIIDADAM FSEDISYFGY PSFRRSSLSR LGSSRERDSE
LLRERESVLR LRERRWLDGA SFDNERGSTS KEGESNPDKK NTPVQSPVSL GEDLQWWPDK
DGTKFTCIGA LYSELLAVSS KGELYQWKWS ESEPYRNAQN PSLHHPRATF LGLTNEKIVL
LSANSIRATV ATENNKVATW VDETLSSVAS KLEHTAQTYS ELQGERIVSL HCCALYTCAQ
LENNLYWWGV VPFSQRKKML EKARAKNKKP KSSAGISSMP NITVGTQVCL RNNPLYHAGA
VAFSISAGIP KVGVLMESVW NMNDSCRFQL RSPESLKSME KASKTLETKP ESKQEPVKTE
MGPPPSPAST CSDASSIASS ASMPYKRRRS TPAPREEEKV NEEQWPLREV VFVEDVKNVP
VGKVLKVDGA YVAVKFPGTS TNTTCQNSSG PDADPSSLLQ DCRLLRIDEL QVVKTGGTPK
VPDCFQRTPK KLCIPEKTEI LAVNVDSKGV HAVLKTGSWV RYCVFDLATG KAEQENNFPT
SSVAFLGQDE RSVAIFTAGQ ESPIVLRDGN GTIYPMAKDC MGGIRDPDWL DLPPISSLGM
GVHSLINLPA NSTIKKKAAI IIMAVEKQTL MQHILRCDYE ACRQYLVNLE QAVVLEQNRQ
MLQTFISHRC DGNRNILHAC VSVCFPTSNK ETKEEEEAER SERNTFAERL SAVEAIANAI
SVVSSNGPGN RAGSSNSRSL RLREMMRRSL RAAGLGRHEA GASSSDHQDP VSPPIAPPSW
VPDPPSMDPD GDIDFILAPA VGSLTTAATG SGQGPSTSTI PGPSTEPSVV ESKDRKANAH
FILKLLCDSA VLQPYLRELL SAKDARGMTP FMSAVSGRAY SAAITILETA QKIAKAEVSA
SEKEEDVFMG MVCPSGTNPD DSPLYVLCCN DTCSFTWTGA EHINQDIFEC RTCGLLESLC
CCTECARVCH KGHDCKLKRT SPTAYCDCWE KCKCKTLIAG QKSARLDLLY RLLTATNLVT
LPNSRGEHLL LFLVQTVARQ TVEHCQYRPP RIREDRNRKT ASPEDSDMPD HDLEPPRFAQ
LALERVLQDW NALRSMIMFG SQENKDPLSA SSRIGHLLPE EQVYLNQQSG TIRLDCFTHC
LIVKCTADIL LLDTLLGTLV KELQNKYTPG RREEAIAVTM RFLRSVARVF VILSVEMASS
KKKNNFIPQP IGKCKRVFQA LLPYAVEELC NVAESLIVPV RMGIARPTAP FTLASTSIDA
MQGSEELFSV EPLPPRPSSD QASSSSQSQS SYIIRNPQQR RISQSQPVRG RDEEQDDIVS
ADVEEVEVVE GVAGEEDHHD EQEEHGEENA EAEGHHDEHD EDGSDMELDL LAAAETESDS
ESNHSNQDNA SGRRSVVTAA TAGSEAGASS VPAFFSEDDS QSNDSSDSDS SSSQSDDIEQ
ETFMLDEPLE RTTNSSHANG AAQAPRSMQW AVRNPQHQRA ASTAPSSTST PAASSAGLIY
IDPSNLRRSG TISTSAAAAA AALEASNASS YLTSASSLAR AYSIVIRQIS DLMGLIPKYN
HLVYSQIPAA VKLTYQDAVN LQNYVEEKLI PTWNWMVSVM DSTEAQLRYG SALASAGDPG
HPNHPLHASQ NSARRERMTA REEASLRTLE GRRRATLLSA RQGMMSARGD FLNYALSLMR
SHNDEHSDVL PVLDVCSLKH VAYVFQALIY WIKAMNQQTT LDTPQLERKR TRELLELGID
NEDSEHENDD DTSQSATLND KDDDSLPAET GQNHPFFRRS DSMTFLGCIP PNPFEVPLAE
AIPLADQPHL LQPNARKEDL FGRPSQGLYS SSAGSGKCIV EVTMDRNCLE VLPTKMSYAA
NLKNVMNMQN RQKKEGEEQS LLAEEADSSK PGPSAPDVAA QLKSSLLAEI GLTESEGPPL
TSFRPQCSFM GMVISHDMLL GRWRLSLELF GRVFMEDVGA EPGSILTELG GFEVKESKFR
REMEKLRNQQ SRDLSLEVDR DRDLLIQQTM RQLNNHFGRR CATTPMAVHR VKVTFKDEPG
EGSGVARSFY TAIAQAFLSN EKLPNLDCIQ NANKGTHTSL MQRLRNRGER DREREREREM
RRSSGLRAGS RRDRDRDFRR QLSIDTRPFR PASEGNPSDD PDPLPAHRQA LGERLYPRVQ
AMQPAFASKI TGMLLELSPA QLLLLLASED SLRARVDEAM ELIIAHGREN GADSILDLGL
LDSSEKVQEN RKRHGSSRSV VDMDLEDTDD GDDNAPLFYQ PGKRGFYTPR PGKNTEARLN
CFRNIGRILG LCLLQNELCP ITLNRHVIKV LLGRKVNWHD FAFFDPVMYE SLRQLILASQ
SSDADAVFSA MDLAFAIDLC KEEGGGQVEL IPNGVNIPVT PQNVYEYVRK YAEHRMLVVA
EQPLHAMRKG LLDVLPKNSL EDLTAEDFRL LVNGCGEVNV QMLISFTSFN DESGENAEKL
LQFKRWFWSI VEKMSMTERQ DLVYFWTSSP SLPASEEGFQ PMPSITIRPP DDQHLPTANT
CISRLYVPLY SSKQILKQKL LLAIKTKNFG FV
