TICRR_HUMAN
ID TICRR_HUMAN Reviewed; 1910 AA.
AC Q7Z2Z1; B2RE07; B3KVV9; D3IUT4; Q8N4X8; Q8NCH6; Q9BU55;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Treslin;
DE AltName: Full=TopBP1-interacting checkpoint and replication regulator;
DE AltName: Full=TopBP1-interacting, replication-stimulating protein;
GN Name=TICRR; Synonyms=C15orf42;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RX PubMed=20116089; DOI=10.1016/j.cell.2009.12.049;
RA Kumagai A., Shevchenko A., Shevchenko A., Dunphy W.G.;
RT "Treslin collaborates with TopBP1 in triggering the initiation of DNA
RT replication.";
RL Cell 140:349-359(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 134-367 (ISOFORM 1), AND VARIANT
RP CYS-287.
RA Stevens M., Wei C., Gross S.S., McPherson J., Brent M.R.;
RT "Exhaustive RT-PCR and sequencing of all novel TWINSCAN predictions in
RT human.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 635-1910, AND VARIANTS CYS-1523;
RP THR-1718 AND CYS-1885.
RC TISSUE=Teratocarcinoma, Tongue, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 901-1910.
RC TISSUE=Rectum tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1321-1910, AND VARIANT CYS-1523.
RC TISSUE=Lung, and Muscle;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1307 AND SER-1413, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1026; THR-1307 AND SER-1484,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TOPBP1.
RX PubMed=20080954; DOI=10.1101/gad.1860310;
RA Sansam C.L., Cruz N.M., Danielian P.S., Amsterdam A., Lau M.L., Hopkins N.,
RA Lees J.A.;
RT "A vertebrate gene, ticrr, is an essential checkpoint and replication
RT regulator.";
RL Genes Dev. 24:183-194(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441; SER-599; SER-820;
RP SER-838; SER-923; SER-1001 AND SER-1078, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292; SER-441; SER-599;
RP SER-838; SER-865; SER-923; SER-938; SER-1001; SER-1026; SER-1057; SER-1078;
RP SER-1125; THR-1134 AND SER-1484, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP INTERACTION WITH DONSON.
RX PubMed=28191891; DOI=10.1038/ng.3790;
RA Reynolds J.J., Bicknell L.S., Carroll P., Higgs M.R., Shaheen R.,
RA Murray J.E., Papadopoulos D.K., Leitch A., Murina O., Tarnauskaite Z.,
RA Wessel S.R., Zlatanou A., Vernet A., von Kriegsheim A., Mottram R.M.,
RA Logan C.V., Bye H., Li Y., Brean A., Maddirevula S., Challis R.C.,
RA Skouloudaki K., Almoisheer A., Alsaif H.S., Amar A., Prescott N.J.,
RA Bober M.B., Duker A., Faqeih E., Seidahmed M.Z., Al Tala S., Alswaid A.,
RA Ahmed S., Al-Aama J.Y., Altmueller J., Al Balwi M., Brady A.F., Chessa L.,
RA Cox H., Fischetto R., Heller R., Henderson B.D., Hobson E., Nuernberg P.,
RA Percin E.F., Peron A., Spaccini L., Quigley A.J., Thakur S., Wise C.A.,
RA Yoon G., Alnemer M., Tomancak P., Yigit G., Taylor A.M., Reijns M.A.,
RA Simpson M.A., Cortez D., Alkuraya F.S., Mathew C.G., Jackson A.P.,
RA Stewart G.S.;
RT "Mutations in DONSON disrupt replication fork stability and cause
RT microcephalic dwarfism.";
RL Nat. Genet. 49:537-549(2017).
CC -!- FUNCTION: Regulator of DNA replication and S/M and G2/M checkpoints.
CC Regulates the triggering of DNA replication initiation via its
CC interaction with TOPBP1 by participating in CDK2-mediated loading of
CC CDC45L onto replication origins. Required for the transition from pre-
CC replication complex (pre-RC) to pre-initiation complex (pre-IC).
CC Required to prevent mitotic entry after treatment with ionizing
CC radiation. {ECO:0000269|PubMed:20116089}.
CC -!- SUBUNIT: Interacts with TOPBP1 (via BRCT domains); interaction takes
CC place in a CDK2-dependent manner (PubMed:20080954). Component of the
CC replisome complex composed of at least DONSON, MCM2, MCM7, PCNA and
CC TICRR (PubMed:28191891). {ECO:0000269|PubMed:20080954,
CC ECO:0000269|PubMed:28191891}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20080954}.
CC Note=Associates with chromatin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z2Z1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z2Z1-2; Sequence=VSP_039218;
CC -!- SIMILARITY: Belongs to the treslin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11165.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG38104.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG53921.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; GQ227787; ADC30133.1; -; mRNA.
DR EMBL; AC013391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC013787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DR731357; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK074727; BAC11165.1; ALT_INIT; mRNA.
DR EMBL; AK123612; BAG53921.1; ALT_INIT; mRNA.
DR EMBL; AK315750; BAG38104.1; ALT_INIT; mRNA.
DR EMBL; BX538335; CAD98102.1; -; mRNA.
DR EMBL; BC002881; AAH02881.2; -; mRNA.
DR EMBL; BC033209; AAH33209.2; -; mRNA.
DR CCDS; CCDS10352.2; -. [Q7Z2Z1-1]
DR CCDS; CCDS76791.1; -. [Q7Z2Z1-2]
DR RefSeq; NP_001294954.1; NM_001308025.1. [Q7Z2Z1-2]
DR RefSeq; NP_689472.3; NM_152259.3. [Q7Z2Z1-1]
DR AlphaFoldDB; Q7Z2Z1; -.
DR BioGRID; 124706; 15.
DR IntAct; Q7Z2Z1; 5.
DR STRING; 9606.ENSP00000268138; -.
DR iPTMnet; Q7Z2Z1; -.
DR PhosphoSitePlus; Q7Z2Z1; -.
DR BioMuta; TICRR; -.
DR DMDM; 156631024; -.
DR EPD; Q7Z2Z1; -.
DR jPOST; Q7Z2Z1; -.
DR MassIVE; Q7Z2Z1; -.
DR MaxQB; Q7Z2Z1; -.
DR PaxDb; Q7Z2Z1; -.
DR PeptideAtlas; Q7Z2Z1; -.
DR PRIDE; Q7Z2Z1; -.
DR ProteomicsDB; 68989; -. [Q7Z2Z1-1]
DR ProteomicsDB; 68990; -. [Q7Z2Z1-2]
DR Antibodypedia; 64736; 44 antibodies from 18 providers.
DR DNASU; 90381; -.
DR Ensembl; ENST00000268138.12; ENSP00000268138.7; ENSG00000140534.14. [Q7Z2Z1-1]
DR Ensembl; ENST00000560985.5; ENSP00000453306.1; ENSG00000140534.14. [Q7Z2Z1-2]
DR GeneID; 90381; -.
DR KEGG; hsa:90381; -.
DR MANE-Select; ENST00000268138.12; ENSP00000268138.7; NM_152259.4; NP_689472.3.
DR UCSC; uc002boe.4; human. [Q7Z2Z1-1]
DR CTD; 90381; -.
DR DisGeNET; 90381; -.
DR GeneCards; TICRR; -.
DR HGNC; HGNC:28704; TICRR.
DR HPA; ENSG00000140534; Tissue enhanced (bone marrow, esophagus, lymphoid tissue).
DR MIM; 613298; gene.
DR neXtProt; NX_Q7Z2Z1; -.
DR OpenTargets; ENSG00000140534; -.
DR PharmGKB; PA142672278; -.
DR VEuPathDB; HostDB:ENSG00000140534; -.
DR eggNOG; ENOG502QW0J; Eukaryota.
DR GeneTree; ENSGT00390000005222; -.
DR HOGENOM; CLU_241727_0_0_1; -.
DR InParanoid; Q7Z2Z1; -.
DR OMA; DWKEPQM; -.
DR OrthoDB; 150355at2759; -.
DR PhylomeDB; Q7Z2Z1; -.
DR TreeFam; TF332114; -.
DR PathwayCommons; Q7Z2Z1; -.
DR SignaLink; Q7Z2Z1; -.
DR BioGRID-ORCS; 90381; 803 hits in 1086 CRISPR screens.
DR ChiTaRS; TICRR; human.
DR GenomeRNAi; 90381; -.
DR Pharos; Q7Z2Z1; Tbio.
DR PRO; PR:Q7Z2Z1; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q7Z2Z1; protein.
DR Bgee; ENSG00000140534; Expressed in secondary oocyte and 105 other tissues.
DR ExpressionAtlas; Q7Z2Z1; baseline and differential.
DR Genevisible; Q7Z2Z1; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IMP:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR InterPro; IPR026153; Treslin.
DR InterPro; IPR032746; Treslin_N.
DR PANTHER; PTHR21556; PTHR21556; 2.
DR Pfam; PF15292; Treslin_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; DNA damage; DNA repair; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1910
FT /note="Treslin"
FT /id="PRO_0000296623"
FT REGION 545..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1580..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1687..1709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1746..1766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1796..1830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1850..1877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1012
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1748..1766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1803..1823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 865
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1001
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1026
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1057
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1078
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1134
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BQ33"
FT MOD_RES 1307
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 1413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 312
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:20116089"
FT /id="VSP_039218"
FT VARIANT 287
FT /note="R -> C (in dbSNP:rs10775247)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_050886"
FT VARIANT 402
FT /note="R -> W (in dbSNP:rs11629584)"
FT /id="VAR_050887"
FT VARIANT 628
FT /note="R -> C (in dbSNP:rs3743372)"
FT /id="VAR_034631"
FT VARIANT 747
FT /note="V -> A (in dbSNP:rs12905387)"
FT /id="VAR_050888"
FT VARIANT 923
FT /note="S -> C (in dbSNP:rs16943377)"
FT /id="VAR_050889"
FT VARIANT 1523
FT /note="R -> C (in dbSNP:rs894157)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_050890"
FT VARIANT 1718
FT /note="S -> T (in dbSNP:rs1866928)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_050891"
FT VARIANT 1885
FT /note="R -> C (in dbSNP:rs3743372)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_050892"
FT CONFLICT 152
FT /note="N -> Y (in Ref. 3; DR731357)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="K -> T (in Ref. 3; DR731357)"
FT /evidence="ECO:0000305"
FT CONFLICT 1009
FT /note="S -> G (in Ref. 1; ADC30133 and 4; BAG53921)"
FT /evidence="ECO:0000305"
FT CONFLICT 1344
FT /note="Q -> L (in Ref. 4; BAG38104)"
FT /evidence="ECO:0000305"
FT CONFLICT 1373
FT /note="V -> I (in Ref. 4; BAG53921)"
FT /evidence="ECO:0000305"
FT CONFLICT 1427
FT /note="L -> P (in Ref. 4; BAC11165)"
FT /evidence="ECO:0000305"
FT CONFLICT 1667
FT /note="W -> R (in Ref. 4; BAC11165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1910 AA; 210857 MW; 3E726E5091B9FA5B CRC64;
MACCHKVMLL LDTAGGAARH SRVRRAALRL LTYLSCRFGL ARVHWAFKFF DSQGARSRPS
RVSDFRELGS RSWEDFEEEL EARLEDRAHL PGPAPRATHT HGALMETLLD YQWDRPEITS
PTKPILRSSG RRLLDVESEA KEAEAALGGL VNAVFLLAPC PHSQRELLQF VSGCEAQAQR
LPPTPKQVME KLLPKRVREV MVARKITFYW VDTTEWSKLW ESPDHLGYWT VCELLHHGGG
TVLPSESFSW DFAQAGEMLL RSGIKLSSEP HLSPWISMLP TDATLNRLLY NSPEYEASFP
RMEGMLFLPV EAGKEIQETW TVTLEPLAMH QRHFQKPVRI FLKGSVAQWS LPTSSTLGTD
SWMLGSPEES TATQRLLFQQ LVSRLTAEEL HLVADVDPGE GRPPITGVIS PLSASAMILT
VCRTKEAEFQ RHVLQTAVAD SPRDTASLFS DVVDSILNQT HDSLADTASA ASPVPEWAQQ
ELGHTTPWSP AVVEKWFPFC NISGASSDLM ESFGLLQAAS ANKEESSKTE GELIHCLAEL
YQRKSREEST IAHQEDSKKK RGVPRTPVRQ KMNTMCRSLK MLNVARLNVK AQKLHPDGSP
DVAGEKGIQK IPSGRTVDKL EDRGRTLRSS KPKDFKTEEE LLSYIRENYQ KTVATGEIML
YACARNMIST VKMFLKSKGT KELEVNCLNQ VKSSLLKTSK SLRQNLGKKL DKEDKVRECQ
LQVFLRLEMC LQCPSINEST DDMEQVVEEV TDLLRMVCLT EDSAYLAEFL EEILRLYIDS
IPKTLGNLYN SLGFVIPQKL AGVLPTDFFS DDSMTQENKS PLLSVPFLSS ARRSVSGSPE
SDELQELRTR SAKKRRKNAL IRHKSIAEVS QNLRQIEIPK VSKRATKKEN SHPAPQQPSQ
PVKDTVQEVT KVRRNLFNQE LLSPSKRSLK RGLPRSHSVS AVDGLEDKLD NFKKNKGYHK
LLTKSVAETP VHKQISKRLL HRQIKGRSSD PGPDIGVVEE SPEKGDEISL RRSPRIKQLS
FSRTHSASFY SVSQPKSRSV QRVHSFQQDK SDQRENSPVQ SIRSPKSLLF GAMSEMISPS
EKGSARMKKR SRNTLDSEVP AAYQTPKKSH QKSLSFSKTT PRRISHTPQT PLYTPERLQK
SPAKMTPTKQ AAFKESLKDS SSPGHDSPLD SKITPQKRHT QAGEGTSLET KTPRTPKRQG
TQPPGFLPNC TWPHSVNSSP ESPSCPAPPT SSTAQPRREC LTPIRDPLRT PPRAAAFMGT
PQNQTHQQPH VLRAARAEEP AQKLKDKAIK TPKRPGNSTV TSSPPVTPKK LFTSPLCDVS
KKSPFRKSKI ECPSPGELDQ KEPQMSPSVA ASLSCPVPST PPELSQRATL DTVPPPPPSK
VGKRCRKTSD PRRSIVECQP DASATPGVGT ADSPAAPTDS RDDQKGLSLS PQSPPERRGY
PGPGLRSDWH ASSPLLITSD TEHVTLLSEA EHHGIGDLKS NVLSVEEGEG LRTADAEKSS
LSHPGIPPSP PSCGPGSPLM PSRDVHCTTD GRQCQASAQL DNLPASAWHS TDSASPQTYE
VELEMQASGL PKLRIKKIDP SSSLEAEPLS KEESSLGEES FLPALSMPRA SRSLSKPEPT
YVSPPCPRLS HSTPGKSRGQ TYICQACTPT HGPSSTPSPF QTDGVPWTPS PKHSGKTTPD
IIKDWPRRKR AVGCGAGSSS GRGEVGADLP GSLSLLESEG KDHGLELSIH RTPILEDFEL
EGVCQLPDQS PPRNSMPKAE EASSWGQFGL SSRKRVLLAK EEADRGAKRI CDLREDSEVS
KSKEGSPSWS AWQLPSTGDE EVFVSGSTPP PSCAVRSCLS ASALQALTQS PLLFQGKTPS
SQSKDPRDED VDVLPSTVED SPFSRAFSRR RPISRTYTRK KLMGTWLEDL
