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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
 
 
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