CE350_MOUSE
ID CE350_MOUSE Reviewed; 3095 AA.
AC E9Q309; A0A1D5RMJ4; D3YTP2; Q6A062; Q8BXM7;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Centrosome-associated protein 350;
DE Short=Cep350;
GN Name=Cep350 {ECO:0000312|MGI:MGI:1921331};
GN Synonyms=Kiaa0480 {ECO:0000303|PubMed:15368895};
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-382.
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1159-3095.
RC TISSUE=Intestine;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
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. 11:205-218(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1812, AND IDENTIFICATION BY
RP 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 IDENTIFICATION BY 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-874; SER-935; SER-1200;
RP SER-1606; SER-1930; SER-2421 AND SER-2809, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, 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 [7]
RP INTERACTION WITH CFAP157.
RX PubMed=27965440; DOI=10.1242/dev.139626;
RA Weidemann M., Schuster-Gossler K., Stauber M., Wrede C., Hegermann J.,
RA Ott T., Boldt K., Beyer T., Serth K., Kremmer E., Blum M., Ueffing M.,
RA Gossler A.;
RT "CFAP157 is a murine downstream effector of FOXJ1 that is specifically
RT required for flagellum morphogenesis and sperm motility.";
RL Development 143:4736-4748(2016).
CC -!- FUNCTION: Plays an essential role in centriole growth by stabilizing a
CC procentriolar seed composed of at least, SASS6 and CENPJ. Required for
CC anchoring microtubules to the centrosomes and for the integrity of the
CC microtubule network. Recruits PPARA to discrete subcellular
CC compartments and thereby modulates PPARA activity. Required for
CC ciliation. {ECO:0000250|UniProtKB:Q5VT06}.
CC -!- SUBUNIT: Part of a ternary complex that contains CEP350, CEP43 and
CC MAPRE1. Interacts (via C-terminus) directly with CEP43 (via N-
CC terminus). Interacts with NR1H3, PPARA, PPARD and PPARG. Interacts
CC directly with microtubules. Interacts with the fusion protein CEP43-
CC FGFR1, and by doing so recruits and activates PI3K and PLC-gamma.
CC Interacts with CYLD (By similarity). Interacts with CFAP157
CC (PubMed:27965440). Interacts with CEP19 (via C-terminus) (By
CC similarity). {ECO:0000250|UniProtKB:Q5VT06,
CC ECO:0000269|PubMed:27965440}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q5VT06}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:Q5VT06}. Nucleus
CC {ECO:0000250|UniProtKB:Q5VT06}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q5VT06}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q5VT06}. Note=Associated with mitotic
CC spindles. Nuclear, in discrete foci. Associated with intermediate
CC filaments. Also present in the pericentrosomal area. Localizes on both
CC mother and daughter centrioles. Localizes to an axial position on the
CC mother centriole. Localizes to the distal end of the centriole on the
CC subdistal appendage region. {ECO:0000250|UniProtKB:Q5VT06}.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000250|UniProtKB:Q5VT06}.
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DR EMBL; AC120391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK044664; BAC32024.1; -; mRNA.
DR EMBL; AK172956; BAD32234.1; -; mRNA.
DR CCDS; CCDS48400.1; -.
DR RefSeq; NP_001034273.1; NM_001039184.1.
DR SMR; E9Q309; -.
DR IntAct; E9Q309; 12.
DR MINT; E9Q309; -.
DR STRING; 10090.ENSMUSP00000120085; -.
DR iPTMnet; E9Q309; -.
DR PhosphoSitePlus; E9Q309; -.
DR EPD; E9Q309; -.
DR jPOST; E9Q309; -.
DR MaxQB; E9Q309; -.
DR PaxDb; E9Q309; -.
DR PeptideAtlas; E9Q309; -.
DR PRIDE; E9Q309; -.
DR ProteomicsDB; 281368; -.
DR Antibodypedia; 34424; 79 antibodies from 21 providers.
DR Ensembl; ENSMUST00000138762; ENSMUSP00000120085; ENSMUSG00000033671.
DR GeneID; 74081; -.
DR KEGG; mmu:74081; -.
DR UCSC; uc007dbs.2; mouse.
DR CTD; 9857; -.
DR MGI; MGI:1921331; Cep350.
DR VEuPathDB; HostDB:ENSMUSG00000033671; -.
DR eggNOG; KOG4568; Eukaryota.
DR GeneTree; ENSGT00940000155130; -.
DR HOGENOM; CLU_000421_0_0_1; -.
DR InParanoid; E9Q309; -.
DR OMA; DCYSDEQ; -.
DR OrthoDB; 145016at2759; -.
DR PhylomeDB; E9Q309; -.
DR TreeFam; TF329845; -.
DR BioGRID-ORCS; 74081; 10 hits in 72 CRISPR screens.
DR ChiTaRS; Cep350; mouse.
DR PRO; PR:E9Q309; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; E9Q309; protein.
DR Bgee; ENSMUSG00000033671; Expressed in metanephric cortical collecting duct and 249 other tissues.
DR ExpressionAtlas; E9Q309; baseline and differential.
DR Genevisible; E9Q309; MM.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0034453; P:microtubule anchoring; IEA:InterPro.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:MGI.
DR Gene3D; 2.30.30.190; -; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR028750; CEP350.
DR InterPro; IPR025486; DUF4378.
DR PANTHER; PTHR13958; PTHR13958; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF14309; DUF4378; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..3095
FT /note="Centrosome-associated protein 350"
FT /id="PRO_0000440628"
FT DOMAIN 2504..2546
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1490..1668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1787..1864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1893..2017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2116..2155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2191..2265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2286..2427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2440..2471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2767..2793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 596..641
FT /evidence="ECO:0000255"
FT COILED 1363..1402
FT /evidence="ECO:0000255"
FT COILED 1700..1793
FT /evidence="ECO:0000255"
FT COILED 1850..1893
FT /evidence="ECO:0000255"
FT COILED 2043..2092
FT /evidence="ECO:0000255"
FT COILED 2700..2731
FT /evidence="ECO:0000255"
FT COMPBIAS 68..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1490..1537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1587..1601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1603..1650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1651..1668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1787..1809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1822..1841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1842..1864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1893..1916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1926..1940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1959..2000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2126..2146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2230..2263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2286..2304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2305..2327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2346..2366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2378..2410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2442..2466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT06"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT06"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT06"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT06"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT06"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 935
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1057
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT06"
FT MOD_RES 1200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1253
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT06"
FT MOD_RES 1256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT06"
FT MOD_RES 1259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT06"
FT MOD_RES 1606
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT06"
FT MOD_RES 1646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT06"
FT MOD_RES 1812
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 1930
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT06"
FT MOD_RES 2198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT06"
FT MOD_RES 2421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT06"
FT MOD_RES 2671
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT06"
FT MOD_RES 2809
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2818
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT06"
FT CONFLICT 2050
FT /note="L -> P (in Ref. 3; BAD32234)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3095 AA; 346456 MW; DE26691E49024B63 CRC64;
MRSSKSKEVP LPNPRNSQSK ETIQDVTTSW DALSQTKAAL RHIENKLEVT PTSTAVIDSV
MDTKKSASAT RKISRKDGRC LDDSWASAPT SKFSKPRKEK SRSPLRATTL ESNVKKNNRV
EFREPLVSYR ETHGTPFSLS PSHLESKHVY CIHEEKPESG KQMVVSREDR NIQCCDFESA
QPSVISDTVV RFLNDGPAID ALHSSECLMK MGVHVRTEDE MPNRTKGSEN NSKPSLNNME
HDVDPKVMLL SDSSPSSSAC NSQRSDISKR QQHDIKLEKL KERIRKQWEH SEEINGQAQT
LGHIDHPVMV VNVDNSVTTK VRKVATAPPA PAYKGFNPSE TKIRTPDGKV WQEAEFQSMS
RELYRDLALQ FTDDTSVKEK PVEKSKEKKV VKPVRKIQKV TQLSNPECKT GSSRLISTSS
WRDGQKLVKK ILGPAPKMEQ KERRPTSNDR SGRERVAKFG GHIGRAESDP KLDVSHKQLP
RSSARSRSSR AWSETNIVKS ALSLPDNKQE ESAALNKDFL PVEIRGILDD LQLDSSAQAV
RQEAGEGQNQ KSSAPEQVPR SHSPVKRKPD KITANEDPPV ISKKRHYDTD EVRQYIVRQQ
EERRRRQHEE KKAQKEATEQ KNKRLQELYR RQREAFSKAK TVPPSDPLVS RRLQETYSKL
LLEKTLLEEP ARQHVTQDIQ ARPGYQPSGE SDKENKIQER PPSASSSSDL SLSEPPQPLA
RRDLMEPTWM QPDRLSPRVH SSQAQPLAGT TENLLSHLLH LEHVGILHKD YESVLPAKKS
HNTASGPLTF TPQPYLTSQA PHPDALLKPS TSQYKTKLDR IEALKATAAS LSSRIESEAK
KLAGASINYG SVWNTECDVK LAPQENGPWT KAISPPVKED IEDAFSARIQ KMLGTCVSHA
AFDDELPGVG SLSEYKKLPE MIRPQSAISS LRMKSPSPKP GGLLAQLCRR QTDSSSSDIQ
ACSQERAKRS LCSSIDSVSE GPLLSEGSLS EEEERRDARP LLKVAEILKE KEFCAGERNS
YEPIKEFQKE AEKFLPLFGH IGGTQSKGPW EELAKGSPHS VINIFTKSYQ LYGKGFEDRG
TLVSRPLNAT ATPLSSVSYE DDFVSSPGSG TLTERKSTLE SQVDGSSLGV QEEHLSRQFA
CDLASVDATS QHSSGARSAG STRSSSASKG KKGKKDKMDW LDSLTGSAQN PLIDEEKVQS
DSERGSHPSR KLGTGSKLAV GDSEQTLDAE STLEDLSGHS VSGSSDKGRS QKTPTSPLSP
SSQKLLQFDL PGTSLERSKS SVIVPPTTTG FKPTAAFTDV NKTEMASAPG PQRFSPAGLQ
HRMAAELSYL SALEESVRQL SDVERVRGIA LAQQESVSLA QIIKAQQQRH ERDLALLKLK
AEQEALECQR QLEETRNKTA QVHAESLQQV VKSQREVTEV LQEATCKIAA QQSETARLTT
DAARQICEMA ELTRTHLADA ITTSGVPLAT LYDHQRQHFP DFMRKLRTKA ETDRISHSAS
HSQSKEGAVD SKRQKFSPSR DSYSESSRYK SHDYRSSGSS RQDSPSVPPS KENEKPFHGE
KMESSVDEQL QTAADDSLRS DSIPSLPDEK DSTSIATEYS LKFDESMTED EIEEKSFRSL
LPSESHRRFN MEKKRGHHDD SDEDASPDKT ALSSTKELSM PFSGGQDSFS KFTMEMVRQY
MKEEEVRAAH QSSLLRLREK ALKEKTKAEL AWLEHQKKHL RDKGEDDKMP PLRKKQRGLL
LRLQQEKAEI KRLQEANKAA RKERQLILKQ QEEIERIRQT TIKLQEKLKS AGEKKLGSLA
DDDEAEDNKA ASPGPPGLET RSPSPISISS SETSSIMQKL KSMRSRMDEK FLTKREQKLM
QRRQHAEELL EWKRRLDAEE AEIQQMEKQA LAAWDKELVK PRTPKKEQES QRTEQKGIAS
EEGSPMPSYS PRNSESCIPE DLGSPSDLCV PSEARVQAQP GSPEHSTLTE EMVFSQELES
TSPSKHSPPK SCLSMSKQES SKASHRTEGH CHLPVKSHQP CYSWSDESLS MTQSETTSDQ
SDIEGRIRAL KDELRKRKSV VEQLKREQRK RQKERLKAQE ASLLRQLETY DEFIKKTEGE
LSQDLDISPT SKFQMKTLSS VSEKPKIKPH PLHRSETAKT WKSVTESERS RGSLASIAEH
VDSSLSCSER AISERSLSAY AKRGVELDSR IEHLQASSPD LSSRKAQTES RDSLESAPSL
SPVKELNAPD RIYDVSEAKA EDTSQKSEIQ EIESMKLESS EVEDACCKQS GGSEVLLKLD
LASETLSSKE LPSDSANVQQ DLDKPATETS HEKEEALKED QSNHSTDDRS PDIQSAGGIP
EQGCRESGDS TCSGQLSVPK ESSYSEDFEV SSFRKGISAD EISKDDSEGS SPSSLRKDSQ
SHRDRSQLTR SSRSRATGSG SDEEISECLG EKSLSVHSGV HSERLLELRS PTELMKSKER
SDVGHEQGGT EPLPLAATEE LLDFHIGDRV LIGSVQPGTL RFKGETDFAK GFWAGVELDK
PEGNNNGTYD GIVYFVCKDK HGIFAPPQKI SHLLENFDDT DINEDEESYS DEQYQPYNQE
QKDIKCLKDR ENNIAEYFCE KSLPSMHNTD ASVDKDRSLN IETDTSEVLE VHGHQQPSVD
PLISYKENKV LVSDATESVP AAAGAATSDN TFSGESKQQQ LAEKEENFYS QVLEKPSTPL
LDLLTREKNQ LEAQLKSSIS EEKKSKQQLE TVSLLTDSLL QVFVKDTVSQ LQQVKKARNE
KIQLSNQEFL DQKKVPPQDL PQNTEEQSPS VPSCFLRSEL EDEKEEISSP DMCPRPESPV
FGASGQEELA KRLAELEISR EFLSALDDQD WFDEDFGLSS SHKIQKNKAE ETIVPLMAEP
KRAPQKPCET LLAVPHTAEE VESLVHNAAE ELWKWKELGQ DLHGLSLPTT FLGGASKGLD
IGSTSRRVYK QAVFDLTKEI FEEIFAEDPN VNQPVWMKPC RINSSYFRRV KNPNNLDEIK
HFITTEVLKL LSLKKEPNHK TDWQKMMKFG RKKRDRVDHI LVQELHEEEA QWVNYDEDEL
CVKMQLADGI FETLIKDTID VLNQISEKQG RMLLV
