RIF1_MOUSE
ID RIF1_MOUSE Reviewed; 2419 AA.
AC Q6PR54; Q6T8D9; Q7TPD8; Q8BTU2; Q8C408; Q9CS77;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Telomere-associated protein RIF1 {ECO:0000305};
DE AltName: Full=Rap1-interacting factor 1 homolog {ECO:0000305|PubMed:15042697};
DE Short=mRif1 {ECO:0000303|PubMed:15042697};
GN Name=Rif1 {ECO:0000312|MGI:MGI:1098622};
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] (ISOFORM 1), INTERACTION WITH TRF2, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=129/Sv;
RX PubMed=15042697; DOI=10.1002/dvdy.10471;
RA Adams I.R., McLaren A.;
RT "Identification and characterisation of mRif1: a mouse telomere-associated
RT protein highly expressed in germ cells and embryo-derived pluripotent stem
RT cells.";
RL Dev. Dyn. 229:733-744(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Silvermann J., Takai H., Buonomo S.B.C., Eisenhaber F., de Lange T.;
RT "ATM-mediated S-phase checkpoint function for hRif1.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 416-1011; 1061-1556 AND
RP 1859-2419.
RC STRAIN=C57BL/6J; TISSUE=Liver, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1860-2419.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385; SER-391; SER-1407;
RP SER-1457; SER-1528; SER-1538; SER-1540; SER-1550; SER-1565; SER-1683 AND
RP SER-2144, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, 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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP TP53BP1.
RX PubMed=23333305; DOI=10.1016/j.molcel.2013.01.002;
RA Chapman J.R., Barral P., Vannier J.B., Borel V., Steger M., Tomas-Loba A.,
RA Sartori A.A., Adams I.R., Batista F.D., Boulton S.J.;
RT "RIF1 is essential for 53BP1-dependent nonhomologous end joining and
RT suppression of DNA double-strand break resection.";
RL Mol. Cell 49:858-871(2013).
RN [7]
RP FUNCTION.
RX PubMed=23333306; DOI=10.1016/j.molcel.2013.01.001;
RA Escribano-Diaz C., Orthwein A., Fradet-Turcotte A., Xing M., Young J.T.,
RA Tkac J., Cook M.A., Rosebrock A.P., Munro M., Canny M.D., Xu D.,
RA Durocher D.;
RT "A cell cycle-dependent regulatory circuit composed of 53BP1-RIF1 and
RT BRCA1-CtIP controls DNA repair pathway choice.";
RL Mol. Cell 49:872-883(2013).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TP53BP1.
RX PubMed=23306437; DOI=10.1126/science.1231573;
RA Zimmermann M., Lottersberger F., Buonomo S.B., Sfeir A., de Lange T.;
RT "53BP1 regulates DSB repair using Rif1 to control 5' end resection.";
RL Science 339:700-704(2013).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TP53BP1.
RX PubMed=23306439; DOI=10.1126/science.1230624;
RA Di Virgilio M., Callen E., Yamane A., Zhang W., Jankovic M., Gitlin A.D.,
RA Feldhahn N., Resch W., Oliveira T.Y., Chait B.T., Nussenzweig A.,
RA Casellas R., Robbiani D.F., Nussenzweig M.C.;
RT "Rif1 prevents resection of DNA breaks and promotes immunoglobulin class
RT switching.";
RL Science 339:711-715(2013).
CC -!- FUNCTION: Key regulator of TP53BP1 that plays a key role in the repair
CC of double-strand DNA breaks (DSBs) in response to DNA damage: acts by
CC promoting non-homologous end joining (NHEJ)-mediated repair of DSBs
CC (PubMed:23333305, PubMed:23306437, PubMed:23306439). In response to DNA
CC damage, interacts with ATM-phosphorylated TP53BP1 (PubMed:23333305,
CC PubMed:23306437, PubMed:23306439). Interaction with TP53BP1 leads to
CC dissociate the interaction between NUDT16L1/TIRR and TP53BP1, thereby
CC unmasking the tandem Tudor-like domain of TP53BP1 and allowing
CC recruitment to DNA DSBs (By similarity). Once recruited to DSBs, RIF1
CC and TP53BP1 act by promoting NHEJ-mediated repair of DSBs
CC (PubMed:23333305, PubMed:23306437). In the same time, RIF1 and TP53BP1
CC specifically counteract the function of BRCA1 by blocking DSBs
CC resection via homologous recombination (HR) during G1 phase
CC (PubMed:23333305, PubMed:23306437). Also required for immunoglobulin
CC class-switch recombination (CSR) during antibody genesis, a process
CC that involves the generation of DNA DSBs (PubMed:23333305,
CC PubMed:23333306, PubMed:23306439). Promotes NHEJ of dysfunctional
CC telomeres (PubMed:23333305). {ECO:0000250|UniProtKB:Q5UIP0,
CC ECO:0000269|PubMed:23306437, ECO:0000269|PubMed:23306439,
CC ECO:0000269|PubMed:23333305, ECO:0000269|PubMed:23333306}.
CC -!- SUBUNIT: Interacts with TP53BP1 (when phosphorylated by ATM)
CC (PubMed:23333305, PubMed:23306437, PubMed:23306439). May interact with
CC TRF2 (PubMed:15042697). Interacts with SHLD2 (By similarity). Interacts
CC with ERCC6 (via WHD region) (By similarity).
CC {ECO:0000250|UniProtKB:Q5UIP0, ECO:0000269|PubMed:23306437,
CC ECO:0000269|PubMed:23306439, ECO:0000269|PubMed:23333305,
CC ECO:0000305|PubMed:15042697}.
CC -!- INTERACTION:
CC Q6PR54; Q80Z64: Nanog; NbExp=5; IntAct=EBI-2312621, EBI-2312517;
CC Q6PR54; Q61066: Nr0b1; NbExp=2; IntAct=EBI-2312621, EBI-2312665;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15042697}. Chromosome
CC {ECO:0000269|PubMed:23306437, ECO:0000269|PubMed:23306439,
CC ECO:0000269|PubMed:23333305}. Chromosome, telomere
CC {ECO:0000269|PubMed:15042697}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q5UIP0}. Note=Exhibits ATM- and TP53BP1-
CC dependent localization to uncapped or aberrant telomeres and to DNA
CC double strand breaks (DSBs). Following interaction with TP53BP1,
CC recruited to sites of DNA damage, such as DSBs (PubMed:23333305,
CC PubMed:23306437, PubMed:23306439). Localizes to microtubules of the
CC midzone of the mitotic spindle during anaphase, and to condensed
CC chromosomes in telophase (By similarity). While the majority of the
CC protein appears nuclear and distinct from normal telomere structures, a
CC small fraction may bind to telomeres in embryonic stem cells
CC (PubMed:15042697). {ECO:0000250|UniProtKB:Q5UIP0,
CC ECO:0000269|PubMed:15042697, ECO:0000269|PubMed:23306437,
CC ECO:0000269|PubMed:23306439, ECO:0000269|PubMed:23333305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6PR54-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PR54-2; Sequence=VSP_014433;
CC Name=3;
CC IsoId=Q6PR54-3; Sequence=VSP_014432;
CC -!- TISSUE SPECIFICITY: Expressed in Sertoli cells, prospermatagonia, early
CC primary spermatocytes, and in oocytes at all stages of their growth.
CC Expressed in embryonic stem (ES) and embryonic germ (EG) cells:
CC expression is lost upon differentiation. {ECO:0000269|PubMed:15042697}.
CC -!- DEVELOPMENTAL STAGE: Found in the nucleus of germinal-vesicle (GV)
CC stage oocytes prior to fertilization. Accumulates in the male and
CC female pronucleus after fertilization. Expressed in the nuclei of all
CC blastomeres from the two cell stage to the compacted morula stage,
CC although absent from the polar body and inner cell mass (ICM). Found in
CC the nuclei of polar and mural trophectoderm cells from 3.5 dpc, and at
CC high levels in the epiblast from 5.5 dpc to 7.5 dpc. Expressed by
CC primitive germ cells (PGCs) in both male and female from 9.5 dpc to
CC 13.5 dpc, at which point expression declines. A low level is observed
CC in Sertoli cells of the testis at 17.5 dpc.
CC {ECO:0000269|PubMed:15042697}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality in inbred 129/Ola and outbred
CC MF1 mouse strains: 7.5 dpc embryos display significant developmental
CC retardation (PubMed:23333305). Female-specific lethality in a CD1
CC strain background, while males survive (PubMed:23333305). Surviving
CC males grow normally, are fertile, but are subject to infections due to
CC defects in the immune response (PubMed:23333305). Surviving males are
CC severely compromised for TP53BP1-dependent class-switch recombination
CC (CSR) and fusion of dysfunctional telomeres (PubMed:23333305).
CC {ECO:0000269|PubMed:23333305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RIF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB30843.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC38846.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
CC Sequence=BAC40506.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AY428571; AAR87833.2; -; mRNA.
DR EMBL; AY585206; AAS94124.1; -; mRNA.
DR EMBL; AK017618; BAB30843.1; ALT_INIT; mRNA.
DR EMBL; AK083291; BAC38846.1; ALT_SEQ; mRNA.
DR EMBL; AK088688; BAC40506.1; ALT_SEQ; mRNA.
DR EMBL; BC055320; AAH55320.1; -; mRNA.
DR CCDS; CCDS50583.1; -. [Q6PR54-3]
DR RefSeq; NP_780447.4; NM_175238.5. [Q6PR54-3]
DR RefSeq; XP_006498240.1; XM_006498177.2.
DR RefSeq; XP_011237438.1; XM_011239136.1. [Q6PR54-2]
DR AlphaFoldDB; Q6PR54; -.
DR BioGRID; 206234; 15.
DR DIP; DIP-54907N; -.
DR IntAct; Q6PR54; 6.
DR MINT; Q6PR54; -.
DR STRING; 10090.ENSMUSP00000108313; -.
DR iPTMnet; Q6PR54; -.
DR PhosphoSitePlus; Q6PR54; -.
DR SwissPalm; Q6PR54; -.
DR EPD; Q6PR54; -.
DR jPOST; Q6PR54; -.
DR MaxQB; Q6PR54; -.
DR PaxDb; Q6PR54; -.
DR PeptideAtlas; Q6PR54; -.
DR PRIDE; Q6PR54; -.
DR ProteomicsDB; 253284; -. [Q6PR54-1]
DR ProteomicsDB; 253285; -. [Q6PR54-2]
DR ProteomicsDB; 253286; -. [Q6PR54-3]
DR Antibodypedia; 33653; 140 antibodies from 29 providers.
DR DNASU; 51869; -.
DR Ensembl; ENSMUST00000112693; ENSMUSP00000108313; ENSMUSG00000036202. [Q6PR54-3]
DR GeneID; 51869; -.
DR KEGG; mmu:51869; -.
DR UCSC; uc008jqq.1; mouse. [Q6PR54-3]
DR UCSC; uc008jqr.1; mouse. [Q6PR54-1]
DR UCSC; uc008jqt.1; mouse. [Q6PR54-2]
DR CTD; 55183; -.
DR MGI; MGI:1098622; Rif1.
DR VEuPathDB; HostDB:ENSMUSG00000036202; -.
DR eggNOG; ENOG502QV6C; Eukaryota.
DR GeneTree; ENSGT00390000012204; -.
DR HOGENOM; CLU_000989_0_0_1; -.
DR InParanoid; Q6PR54; -.
DR OMA; NKNETYV; -.
DR OrthoDB; 10400at2759; -.
DR TreeFam; TF323789; -.
DR Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR BioGRID-ORCS; 51869; 18 hits in 110 CRISPR screens.
DR ChiTaRS; Rif1; mouse.
DR PRO; PR:Q6PR54; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q6PR54; protein.
DR Bgee; ENSMUSG00000036202; Expressed in spermatocyte and 259 other tissues.
DR ExpressionAtlas; Q6PR54; baseline and differential.
DR Genevisible; Q6PR54; MM.
DR GO; GO:0000785; C:chromatin; IMP:BHF-UCL.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:MGI.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:BHF-UCL.
DR GO; GO:0000793; C:condensed chromosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0001939; C:female pronucleus; IDA:MGI.
DR GO; GO:0001940; C:male pronucleus; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
DR GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; IMP:BHF-UCL.
DR GO; GO:0045830; P:positive regulation of isotype switching; IMP:UniProtKB.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:BHF-UCL.
DR GO; GO:0000723; P:telomere maintenance; IMP:BHF-UCL.
DR GO; GO:0043247; P:telomere maintenance in response to DNA damage; ISO:MGI.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR028566; Rif1.
DR InterPro; IPR022031; Rif1_N.
DR PANTHER; PTHR22928; PTHR22928; 2.
DR Pfam; PF12231; Rif1_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Chromosome; Cytoplasm; Cytoskeleton;
KW DNA damage; DNA repair; Nucleus; Phosphoprotein; Reference proteome;
KW Telomere.
FT CHAIN 1..2419
FT /note="Telomere-associated protein RIF1"
FT /id="PRO_0000097334"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1613..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1812..1836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1882..2419
FT /note="Interaction with condensed chromosomes in telophase"
FT /evidence="ECO:0000250"
FT REGION 1890..1914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1929..1983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2119..2394
FT /note="Interaction with ERCC6"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT REGION 2182..2212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1401..1452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1522..1539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 779
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 976
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 1005
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 1044
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 1215
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 1231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 1233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 1407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 1457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 1504
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 1528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1542
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 1550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 1565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1680
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 1683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1780
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 1784
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 1842
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 1931
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 2094
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 2109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 2121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 2125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 2144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 2208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 2287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 2341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 2413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT MOD_RES 2419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5UIP0"
FT VAR_SEQ 167
FT /note="I -> ISHWFLHC (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_014432"
FT VAR_SEQ 2198..2223
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_014433"
FT CONFLICT 211
FT /note="M -> V (in Ref. 1; AAR87833)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="M -> V (in Ref. 1; AAR87833)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="F -> L (in Ref. 1; AAR87833 and 3; BAC40506)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="E -> G (in Ref. 1; AAR87833 and 3; BAC40506)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="E -> G (in Ref. 1; AAR87833 and 3; BAC40506)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="S -> A (in Ref. 1; AAR87833 and 3; BAC40506)"
FT /evidence="ECO:0000305"
FT CONFLICT 743
FT /note="V -> A (in Ref. 1; AAR87833 and 3; BAC40506)"
FT /evidence="ECO:0000305"
FT CONFLICT 802
FT /note="K -> E (in Ref. 3; BAC40506)"
FT /evidence="ECO:0000305"
FT CONFLICT 959
FT /note="I -> S (in Ref. 1; AAR87833 and 3; BAC40506)"
FT /evidence="ECO:0000305"
FT CONFLICT 1066
FT /note="K -> R (in Ref. 3; BAB30843)"
FT /evidence="ECO:0000305"
FT CONFLICT 1122
FT /note="M -> T (in Ref. 1; AAR87833)"
FT /evidence="ECO:0000305"
FT CONFLICT 1179
FT /note="L -> M (in Ref. 1; AAR87833)"
FT /evidence="ECO:0000305"
FT CONFLICT 1238
FT /note="I -> M (in Ref. 1; AAR87833)"
FT /evidence="ECO:0000305"
FT CONFLICT 1527
FT /note="A -> R (in Ref. 3; BAB30843)"
FT /evidence="ECO:0000305"
FT CONFLICT 1584
FT /note="A -> S (in Ref. 1; AAR87833)"
FT /evidence="ECO:0000305"
FT CONFLICT 1671
FT /note="N -> T (in Ref. 1; AAR87833)"
FT /evidence="ECO:0000305"
FT CONFLICT 1772
FT /note="V -> L (in Ref. 1; AAR87833)"
FT /evidence="ECO:0000305"
FT CONFLICT 1798
FT /note="P -> S (in Ref. 1; AAR87833)"
FT /evidence="ECO:0000305"
FT CONFLICT 1897
FT /note="V -> I (in Ref. 1; AAR87833)"
FT /evidence="ECO:0000305"
FT CONFLICT 1918
FT /note="E -> D (in Ref. 1; AAR87833)"
FT /evidence="ECO:0000305"
FT CONFLICT 1997
FT /note="L -> F (in Ref. 1; AAR87833)"
FT /evidence="ECO:0000305"
FT CONFLICT 2018
FT /note="F -> L (in Ref. 1; AAR87833)"
FT /evidence="ECO:0000305"
FT CONFLICT 2024
FT /note="M -> T (in Ref. 1; AAR87833)"
FT /evidence="ECO:0000305"
FT CONFLICT 2052
FT /note="N -> K (in Ref. 1; AAR87833)"
FT /evidence="ECO:0000305"
FT CONFLICT 2114
FT /note="Missing (in Ref. 1; AAR87833)"
FT /evidence="ECO:0000305"
FT CONFLICT 2394
FT /note="E -> G (in Ref. 1; AAR87833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2419 AA; 266228 MW; 016A1A4CEF25B8F9 CRC64;
MTAPGRSPLE PLLETWEDPS VPPGEQTDAY LTLTSRMTGE EGKEVIAEIE KNLSRLYTVL
KAHISSQNSE LSSAALQALG FCLYNPRITS GLSEANIQEL LLTLNGIIKS SDKNVCTRAL
WVISKQTFPA ELVSKMVSSI IDSLEVILSK GEIHSAVVDF EALNVIIRLI EQAPVQMGEE
SVRWAKLVIP LVVHSAQKVH LRGATALEMG MPLLLQKQQE IALITEHLMT TKLISELQKL
FKNKNETYVL KLWPLFVKLL GKTLHRSGSF INSLLQLEEL GFRSGTPMIK KIAFIAWKSL
IDNFALNPDI LCSAKRLKLL MQPLSSIHVR TETLALTKLE VWWYLLMRLG PQLPANFEQV
CVPLIQSTIS VDSIPSPQGN SSRGSASPGL SPLTPGHKGA SPYGSPRGNL SSNTGGMAAI
PSIQLLGLEM MLHFLLGPEV LSFAKQHKIV LSLEPLEHPL ISSPSFFSKY AHTLITAVHD
SFVSVGKDAS DAVVSAIWKE LISLVKSVTE AGNRKEKSGS EVLTLLLKSL ENIVKSEVFP
VSKTLVLMEI TVKGLPPKVL GSPAYQVANM DILNGTPALF LIQLIFNNNL LECGVEDEKF
FLNLETLVGC VLSGPTSPLA FSDSVLTVIN QNAKQLVNKE HLWRMWSMIV SPLTDVIHQT
NEVNQGDALE HNFSAIYGAL TLPINHIFSA QTFPTGTMKA LLKTWSELYR AFTRCASLVA
TAEENLCCEE LSSKIMCSLE DEVLSDLLFL DRISHIIIVM VDCIDFSPYN KKYQPKIKSP
QRSSDWSRKK KEPLGKLASL FKLIVKVIDT FHTLSLKETF SDTLLAIGNS IISMLSNVFG
HISLPSMIRE IFATFTRPLA LLYENSKLDE APKVYTSLNN KLEKLLGEIV ACLQFSYLGA
YDSELLEHLS PLLCVIFLHK NKQIRKQSAL LWNATFAKAT ALVYPEELKP ILRQAKQKIL
LLLPGLENVE MMDESSEPYS ESTENSQLNV KISGMERKSS GKRDSILAHT KDKKKKVKLS
AKLKLESSSP KIKSGKLLEE EKSTDFVFIP PEGKETKARV LTEHQKEVLK TKRCDIPALY
NNLDASQDTL FSAQFSQEES MESLTLTEKP KEDAKIIKEE QMESTIFIHQ DAPENCGIDE
HSENASLPNC GGSVAETNPE TLITGFDARK EVLISSKILS AESSSSTETS VVSSSSVSNA
TFSGTPPQPT SRRQTFITLE KFDGSETRPF SPSPLNNISS TVTVRNNQDN TTNTDMPPKA
RKREVTNSKS DSENLANAGK KSSRRWSKAE QSVTKKSKPS LTSEQEEHSS ENNSPDLLSP
TEHVSENDDH PSEATLEHKD GDPKPAVENA SLEDLTTEEK NVGINMESKE STASVVARTE
QIVNEDSQAA ALAPNPKTLR RSSRRRSEAV DSCSDSQERE SGQQKKERRK EEEKIISKSP
LRIKDDKLPT QKLTDESPIQ ENLTEKGNTL PERTSGEPSV NAEIDQNRRK PDLENVSSEG
GGGTLDNLDK SSEKPLRGRT RYQTRRASQG LISAVENSES DSSEAKEEVS RKKRSGKWKN
RSSDSVDIEE QEEKKAEEEV MKTANQTLDG QAVPDVDVNA AAQVCEKSTN NNRVILQDSA
GPADSLQAPP KGEEKSKINK CVDSSFVSLP VPESNLRTRN ASKRLLYKQD NDSNVRVSDS
SLSPEKFTQV ECQHKRSRRV RRSKSCDCCG EKSQSQEKSF IGLKNTESYA IKSVEKKKTD
LQVPETAPET REARDHAETK LAGEEPLVNF HVGLKEENCT TGDSVKSEAE LQEASLPPEI
VTVKEKTYDT DASEAVSEIQ GPCSENHSPA EDPGLSECKD ISQKQLSENG ELDISDVGKA
CKVIAGSSPE GVETMELNVR NDAFVAADSE KSTQMDVSVD VATEEDNKKD ECEAVTTEVN
VEGVATEDFN SGMDLSDTPI PVSKDVETEH AASGEIEGES NESDSGSCEE MNKEMGSHKA
QMSTEIDSAR VKETDILASA SKSEEALIGR LDVNTQSFVS DIEMSSGERT VNCKTETSIE
LNKLDEAKLS GNEATVGNDT LQEVCFTSEK VEKLPQCLLV QVASELGAES NTTSPEKLEL
DSFGSVNESP SGMQQARCVW SPLASPSTSI LKRGLKRSQE DEISPVNKIR RVSFADPIYQ
AGLADDIDRR CSVVRSHSSN SSPIIKSVKT SPTSHSKHNT TSAKGFLSPG SQSSKFKSPK
KCLITEMAQE SMLSPTESVY PALVNCAASV DIILPQITSN MWARGLGQLI RAKNIKTIGD
LSTLTASEIK TLPIRSPKVF NVKKALRVYH EQQMKSRGLE EIPIFDISEK AVNGVESRTV
STDEERFASD LIEPVTLDTP LSKNLVAQIS ALALQLDSED LYSYTGSQLF EMHEKLGTMA
NSIIRNLQSR WRSPAHENS
