ANR17_MOUSE
ID ANR17_MOUSE Reviewed; 2603 AA.
AC Q99NH0; Q3TV99; Q5F4T7; Q6PG69; Q6ZQ66; Q8CHT4;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Ankyrin repeat domain-containing protein 17;
DE AltName: Full=Ankyrin repeat domain-containing protein FOE;
DE AltName: Full=Gene trap ankyrin repeat protein;
GN Name=Ankrd17; Synonyms=Foe, Gtar, Kiaa0697;
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 2).
RA Chen X., Shen J.C.-K.;
RT "A novel ankyrin repeat domain-containing protein.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, DEVELOPMENTAL
RP STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv;
RX PubMed=11165478; DOI=10.1016/s0925-4773(00)00530-x;
RA Watt A.J., Jones E.A., Ure J.M., Peddie D., Wilson D.I., Forrester L.M.;
RT "A gene trap integration provides an early in situ marker for hepatic
RT specification of the foregut endoderm.";
RL Mech. Dev. 100:205-215(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1034-1482 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1482-2603 (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
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. 10:167-180(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1902-2603 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=11740861; DOI=10.1006/excr.2001.5396;
RA Jones E.A., Tosh D., Wilson D.I., Lindsay S., Forrester L.M.;
RT "Hepatic differentiation of murine embryonic stem cells.";
RL Exp. Cell Res. 272:15-22(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2043, 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 [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19619540; DOI=10.1016/j.febslet.2009.07.025;
RA Hou S.C., Chan L.W., Chou Y.C., Su C.Y., Chen X., Shih Y.L., Tsai P.C.,
RA Shen C.K., Yan Y.T.;
RT "Ankrd17, an ubiquitously expressed ankyrin factor, is essential for the
RT vascular integrity during embryogenesis.";
RL FEBS Lett. 583:2765-2771(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-42; SER-1692;
RP SER-1696; SER-1705; SER-2040; SER-2041; SER-2043; SER-2055 AND SER-2401,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1870, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Could play pivotal roles in cell cycle and DNA regulation.
CC Involved in innate immune defense against viruse by positively
CC regulating the viral dsRNA receptors DDX58 and IFIH1 signaling
CC pathways. Involves in NOD2- and NOD1-mediated responses to bacteria
CC suggesting a role in innate antibacterial immune pathways too. Could
CC play a central role for the formation and/or maintenance of the blood
CC vessels of the circulation system (PubMed:19619540).
CC {ECO:0000250|UniProtKB:O75179, ECO:0000269|PubMed:19619540}.
CC -!- SUBUNIT: Interacts (via N-terminus) with NOD2. Interacts with CDK2,
CC MCM3, MCM5, MCM7, CDC6 and PCNA. Interacts with MAVS and IFIH1.
CC Interacts (via the second ankyrin repeat cluster) with DDX58.
CC {ECO:0000250|UniProtKB:O75179}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75179}. Nucleus
CC {ECO:0000250|UniProtKB:O75179}. Note=Detected around the nucleolus.
CC {ECO:0000250|UniProtKB:O75179}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=The N-terminus of another isoform lacking the first 141 amino
CC acids is described in. {ECO:0000269|PubMed:11165478};
CC Name=1;
CC IsoId=Q99NH0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99NH0-2; Sequence=VSP_028866, VSP_028867, VSP_028871;
CC Name=3;
CC IsoId=Q99NH0-3; Sequence=VSP_028868, VSP_028869, VSP_028870;
CC -!- TISSUE SPECIFICITY: Highly expressed in fetal liver. Detected in adult
CC liver cells, ovarian oocytes, seminiferous tubules of the testes and
CC pelvic region of the kidney. It was not detected in heart, gut, lung,
CC spleen and skeletal muscle. Earliest specific in situ marker of hepatic
CC differentiation during embryogenesis, useful for characterization of
CC inductive events involved in hepatic specification.
CC {ECO:0000269|PubMed:11165478, ECO:0000269|PubMed:11740861,
CC ECO:0000269|PubMed:19619540}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 8.0-8.5 dpc in the foregut endoderm
CC and at 9.5 dpc in cells migrating into the septum transversum. At 10.5
CC dpc, highly expressed exclusively in the fetal liver. From 10.5 dpc,
CC expressed in the developing liver throughout gestation and in neonates.
CC At 17.5 dpc, detected in the dorsal root ganglia of the peripheral
CC nervous system. {ECO:0000269|PubMed:11165478}.
CC -!- PTM: Phosphorylated by CDK2. {ECO:0000250|UniProtKB:O75179}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice display embryonic lethality during
CC organogenesis with hemorrhages, impaired vascular smooth muscle cell
CC development, impaired vascular integrity and growth retardation.
CC {ECO:0000269|PubMed:19619540}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39213.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC98003.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA.; Evidence={ECO:0000305};
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DR EMBL; AF130371; AAQ13559.1; -; mRNA.
DR EMBL; AC117578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC162171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY026253; AAK07672.1; -; mRNA.
DR EMBL; AK160263; BAE35720.1; -; mRNA.
DR EMBL; AK129193; BAC98003.1; ALT_SEQ; Transcribed_RNA.
DR EMBL; BC039213; AAH39213.1; ALT_INIT; mRNA.
DR EMBL; BC057195; AAH57195.1; -; mRNA.
DR CCDS; CCDS57354.1; -. [Q99NH0-1]
DR RefSeq; NP_112148.2; NM_030886.2. [Q99NH0-1]
DR AlphaFoldDB; Q99NH0; -.
DR SMR; Q99NH0; -.
DR BioGRID; 219887; 12.
DR IntAct; Q99NH0; 4.
DR STRING; 10090.ENSMUSP00000014421; -.
DR iPTMnet; Q99NH0; -.
DR PhosphoSitePlus; Q99NH0; -.
DR SwissPalm; Q99NH0; -.
DR EPD; Q99NH0; -.
DR jPOST; Q99NH0; -.
DR MaxQB; Q99NH0; -.
DR PaxDb; Q99NH0; -.
DR PeptideAtlas; Q99NH0; -.
DR PRIDE; Q99NH0; -.
DR ProteomicsDB; 281872; -. [Q99NH0-1]
DR ProteomicsDB; 281873; -. [Q99NH0-2]
DR ProteomicsDB; 281874; -. [Q99NH0-3]
DR Antibodypedia; 24452; 147 antibodies from 18 providers.
DR DNASU; 81702; -.
DR Ensembl; ENSMUST00000014421; ENSMUSP00000014421; ENSMUSG00000055204. [Q99NH0-1]
DR GeneID; 81702; -.
DR KEGG; mmu:81702; -.
DR UCSC; uc008yav.1; mouse. [Q99NH0-2]
DR UCSC; uc008yay.1; mouse. [Q99NH0-3]
DR UCSC; uc029vje.1; mouse. [Q99NH0-1]
DR CTD; 26057; -.
DR MGI; MGI:1932101; Ankrd17.
DR VEuPathDB; HostDB:ENSMUSG00000055204; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4369; Eukaryota.
DR GeneTree; ENSGT00940000153768; -.
DR InParanoid; Q99NH0; -.
DR OMA; GWLEMER; -.
DR OrthoDB; 1115202at2759; -.
DR PhylomeDB; Q99NH0; -.
DR TreeFam; TF328552; -.
DR BioGRID-ORCS; 81702; 15 hits in 73 CRISPR screens.
DR ChiTaRS; Ankrd17; mouse.
DR PRO; PR:Q99NH0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q99NH0; protein.
DR Bgee; ENSMUSG00000055204; Expressed in animal zygote and 261 other tissues.
DR ExpressionAtlas; Q99NH0; baseline and differential.
DR Genevisible; Q99NH0; MM.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001955; P:blood vessel maturation; IMP:MGI.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0007492; P:endoderm development; TAS:MGI.
DR GO; GO:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0051151; P:negative regulation of smooth muscle cell differentiation; IMP:MGI.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:1900245; P:positive regulation of MDA-5 signaling pathway; ISS:UniProtKB.
DR GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; ISS:UniProtKB.
DR GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
DR Gene3D; 1.25.40.20; -; 7.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 9.
DR Pfam; PF00013; KH_1; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 25.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF48403; SSF48403; 3.
DR SUPFAM; SSF54791; SSF54791; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 20.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ANK repeat; Coiled coil; Cytoplasm;
KW Immunity; Innate immunity; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT CHAIN 1..2603
FT /note="Ankyrin repeat domain-containing protein 17"
FT /id="PRO_0000307918"
FT REPEAT 229..258
FT /note="ANK 1"
FT REPEAT 262..291
FT /note="ANK 2"
FT REPEAT 296..325
FT /note="ANK 3"
FT REPEAT 329..358
FT /note="ANK 4"
FT REPEAT 362..391
FT /note="ANK 5"
FT REPEAT 396..425
FT /note="ANK 6"
FT REPEAT 429..458
FT /note="ANK 7"
FT REPEAT 462..491
FT /note="ANK 8"
FT REPEAT 495..524
FT /note="ANK 9"
FT REPEAT 529..558
FT /note="ANK 10"
FT REPEAT 559..588
FT /note="ANK 11"
FT REPEAT 592..621
FT /note="ANK 12"
FT REPEAT 625..654
FT /note="ANK 13"
FT REPEAT 659..688
FT /note="ANK 14"
FT REPEAT 692..721
FT /note="ANK 15"
FT REPEAT 1078..1107
FT /note="ANK 16"
FT REPEAT 1111..1140
FT /note="ANK 17"
FT REPEAT 1145..1174
FT /note="ANK 18"
FT REPEAT 1178..1207
FT /note="ANK 19"
FT REPEAT 1213..1242
FT /note="ANK 20"
FT REPEAT 1247..1276
FT /note="ANK 21"
FT REPEAT 1280..1309
FT /note="ANK 22"
FT REPEAT 1315..1344
FT /note="ANK 23"
FT REPEAT 1348..1377
FT /note="ANK 24"
FT REPEAT 1381..1410
FT /note="ANK 25"
FT DOMAIN 1721..1785
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1475..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1513..1713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1902..1991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2007..2195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2269..2327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2378..2447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1438..1522
FT /evidence="ECO:0000255"
FT COMPBIAS 79..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..127
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1528..1563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1592..1649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1667..1702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1940..1991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2007..2025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2047..2109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2123..2164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2269..2296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2378..2401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2433..2447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O75179"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75179"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75179"
FT MOD_RES 1453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75179"
FT MOD_RES 1631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75179"
FT MOD_RES 1692
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1705
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1870
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2038
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75179"
FT MOD_RES 2040
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2041
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2043
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2055
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2063
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75179"
FT MOD_RES 2373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75179"
FT MOD_RES 2401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 314
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75179"
FT VAR_SEQ 1..141
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_028866"
FT VAR_SEQ 774..1024
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_028867"
FT VAR_SEQ 1024
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11165478"
FT /id="VSP_028868"
FT VAR_SEQ 1597..1600
FT /note="GESK -> VSFL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11165478"
FT /id="VSP_028869"
FT VAR_SEQ 1601..2603
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11165478"
FT /id="VSP_028870"
FT VAR_SEQ 1723..2603
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_028871"
FT CONFLICT 347
FT /note="K -> E (in Ref. 3; AAK07672)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="E -> G (in Ref. 3; AAK07672)"
FT /evidence="ECO:0000305"
FT CONFLICT 908
FT /note="F -> L (in Ref. 3; AAK07672)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2603 AA; 274213 MW; 246DAA0E473C3D55 CRC64;
MEKATVPAAA EGEGSPPAAA AVAAPPAAAA AEVGGGARPA SSPRGMVRVC DLLLKKKPPQ
QQQQQQPPHH KAKRNRTCRP PSSSESSSDS DNSGGGGGGG GGGGGGTSSN NSEEEEDDDD
EEEEVSEVES FILDQDDLEN PMLETASKLL LSGTADGADL RTVDPETQAR LEALLEAAGI
GKLSTADGKA FADPEVLRRL TSSVSCALDE AAAALTRMRA ESTANAGQSD NRSLAEACSE
GDVNAVRKLL IEGRSVNEHT EEGESLLCLA CSAGYYELAQ VLLAMHANVE DRGIKGDITP
LMAAANGGHV KIVKLLLAHK ADVNAQSSTG NTALTYACAG GYVDVVKVLL ESGASIEDHN
ENGHTPLMEA GSAGHVEVAR LLLENGAGIN THSNEFKESA LTLACYKGHL EMVRFLLEAG
ADQEHKTDEM HTALMEACMD GHVEVARLLL DSGAQVNMPA DSFESPLTLA ACGGHVELAA
LLIERGASLE EVNDEGYTPL MEAAREGHEE MVALLLGQGA NINAQTEETQ ETALTLACCG
GFLEVADFLI KAGADIELGC STPLMEAAQE GHLELVKYLL AAGANVHATT ATGDTALTYA
CENGHTDVAD VLLQAGADLE HESEGGRTPL MKAARAGHVC TVQFLISKGA NVNRTTANND
HTVLSLACAG GHLAVVELLL AHGADPTHRL KDGSTMLIEA AKGGHTSVVC YLLDYPNNLL
AAPPPDVTQL TPPSHDLNRA PRVPVQALPM VVPPQEPDKP PANLAATLPV RSKAASKQKS
NSHLPANSQD VQGYITNQSP ESIVEEAQGK LTELEQRIKE AIEKNAQLQS LELAHADQLT
KEKIEELNKT REEQIQKKQK ILEELQKVER ELQLKTQQQL KKQYLEVKAQ RIQLQQQQQQ
SCQHLGLFTS VGVGEQLSEG DYARLQQVDP VLLKDEPQQT AAQMGFAPIQ PLAMPQALPL
ATGPLPPGSI ANLTELQGVI VGQPVLGQAQ LAGLGQGILT ETQQGLMVAS PAQTLNDTLD
DIMAAVSGRA SAMSNTPTHS IAASVSQPQT PTPSPIISPS AMLPIYPAID IDAQTESNHD
TALTLACAGG HEELVQTLLE RGASIEHRDK KGFTPLILAA TAGHVGVVEI LLDNGADIEA
QSERTKDTPL SLACSGGRQE VVELLLARGA NKEHRNVSDY TPLSLAASGG YVNIIKILLN
AGAEINSRTG SKLGISPLML AAMNGHTAAV KLLLDMGSDI NAQIETNRNT ALTLACFQGR
TEVVSLLLDR KANVEHRAKT GLTPLMEAAS GGYAEVGRVL LDKGADVNAP PVPSSRDTAL
TIAADKGHYK FCELLIGKGA HIDVRNKKGN TPLWLAANGG HLDVVQLLVQ ATADVDAADN
RKITPLMAAF RKGHVKVVRY LVKEVNQFPS DSECMRYIAT ITDKEMLKKC HLCMESIVQA
KDRQAAEANK NASILLEELD LEKLREESRR LALAAKREKR KEKRRKKKEE QRRKLEEIEA
KNKENFELQA AQEKEKLKVE EEPEVLTEPP SATTTTTIGI SATWTTLAGS HGKRNNTITT
TSSKRKNRKN KITPENVQII FDDPLPISYS QPEKVNGESK SSSTSESGDS DNMRISSCSD
ESSNSNSSRK SNNHASAVVT TTMASKKQPS VLVTFPKEER KSVSGKASIK LSETVNEGTS
NSLSTCTKSG PSPLSSPNGK LTVASPKRGP KREEGWKEVV RRSKKVSVPS TVISRVIGRG
GCNINAIREC TGAHIDIDKQ KDKTGDRIIT IRGGTESTRQ ATQLINALIK DPDKEIDELI
PKNRLKSSTA NSKIGSSAPT TTAANSSLMG IKMTTVALSS TSQTATALTV PAISSASTHK
TIKNPVNNVR PGFPVSLPLA YPPPQFAHAL LAAQTFQQIR PPRLPMTHFG GTFPPAQSTW
GPFPVRPLSP ARATNSPKPH MVPRHSNQNS SGSQVNSAGS LTSSPTTTAS SSASAVPGTT
SNGSPSSPSV RRQLFVTVVK TSNATTTTVT TTASNNSTAP TNATYPMPTA KEHYPVSSPS
SPSPPAQPGG VSRNSPLDCG SASPNKGASA SEQEASSPPV VEPANSRPPH SSSSSGSSSG
HSTQQQPPGS VPQEPRPPLQ QSQVPSPDVR MTVPPTATSS APVAVPSTAP VTYPMPQTQM
GCSQPPKMEA PAIRPPSHAT AAPHKTPAPV QSSSASVLNV NHIKRPHSVP SSVQLPSTLS
TQSACQNSVH PANKPVAPNF SAPLPFGPFS TLFENNPTNA HAFWGGPVVS SQSTPESMLS
GKSSYLPNSD PLHQSDTSKA PGFRPPLQRP APSPSGIVNM DTPYGSVTPS STHLGNFASS
LSGGQMYGPG APLGGAPLGG APTAANFNRQ HFSPLSLLTP CSSASNESPA QSVSSGVRAP
SPAPSSVPLG SEKPSSVSQD RKVPVPIGTE RSARIRQTGT SAPSVIGSNL STSVGHSGIW
SFEGIGGNQD KVDWCNPGMG NPMIHRPMSD PGVFSQHQAM ERDSTGIVTP SGTFHQHVPA
GYMDFPKVGS MPFSVYGNAM LPPVAPIADG AGGPIFNGPH SAEPSWNSLI KMVSSSTENN
GPQTVWTGPW APHMNSVHMN QLG
