ZN106_MOUSE
ID ZN106_MOUSE Reviewed; 1888 AA.
AC O88466; A2AKH3; O55185; O88465; O88467; Q792M1; Q792P4; Q8CDZ8; Q8R3I4;
AC Q9ESU3;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Zinc finger protein 106;
DE Short=Zfp-106;
DE AltName: Full=H3a minor histocompatibility antigen;
DE AltName: Full=Son of insulin receptor mutant;
DE AltName: Full=Zinc finger protein 474;
GN Name=Znf106; Synonyms=H3a, Sh3bp3, Sirm, Zfp106, Znf474;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANTS.
RC STRAIN=129/J, BALB/cJ, C57BL/10, C57BL/6 X DBA/2, and C57BL/6J;
RC TISSUE=Embryo {ECO:0000312|EMBL:AAD04328.1},
RC Lymphoblast {ECO:0000312|EMBL:AAD04330.1},
RC T-cell {ECO:0000312|EMBL:AAD04327.1}, and
RC Thymic lymphoma {ECO:0000312|EMBL:AAD04329.1};
RX PubMed=9846490; DOI=10.1016/s1074-7613(00)80666-4;
RA Zuberi A.R., Christianson G.J., Mendoza L.M., Shastri N., Roopenian D.C.;
RT "Positional cloning and molecular characterization of an immunodominant
RT cytotoxic determinant of the mouse H3 minor histocompatibility complex.";
RL Immunity 9:687-698(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-1188.
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary 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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 186-1888 (ISOFORM 3), INTERACTION WITH FYN
RP AND GRB2, TISSUE SPECIFICITY, INDUCTION, PHOSPHORYLATION, AND VARIANTS.
RC STRAIN=Swiss Webster;
RX PubMed=9507006; DOI=10.1074/jbc.273.12.6989;
RA Salvatore P., Hanash C.R., Kido Y., Imai Y., Accili D.;
RT "Identification of sirm, a novel insulin-regulated SH3 binding protein that
RT associates with Grb-2 and FYN.";
RL J. Biol. Chem. 273:6989-6997(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1567-1888 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [6]
RP INTERACTION WITH KNOP1, AND SUBCELLULAR LOCATION.
RX PubMed=15833274; DOI=10.1016/j.biocel.2005.01.013;
RA Grasberger H., Bell G.I.;
RT "Subcellular recruitment by TSG118 and TSPYL implicates a role for zinc
RT finger protein 106 in a novel developmental pathway.";
RL Int. J. Biochem. Cell Biol. 37:1421-1437(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1293, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-876; SER-878; SER-953;
RP SER-1040; SER-1041; SER-1291; SER-1296; SER-1339; SER-1381 AND THR-1383,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen, and
RC 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 [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=26604141; DOI=10.1093/hmg/ddv471;
RA Joyce P.I., Fratta P., Landman A.S., Mcgoldrick P., Wackerhage H.,
RA Groves M., Busam B.S., Galino J., Corrochano S., Beskina O.A., Esapa C.,
RA Ryder E., Carter S., Stewart M., Codner G., Hilton H., Teboul L.,
RA Tucker J., Lionikas A., Estabel J., Ramirez-Solis R., White J.K.,
RA Brandner S., Plagnol V., Bennet D.L., Abramov A.Y., Greensmith L.,
RA Fisher E.M., Acevedo-Arozena A.;
RT "Deficiency of the zinc finger protein ZFP106 causes motor and sensory
RT neurodegeneration.";
RL Hum. Mol. Genet. 25:291-307(2016).
RN [10]
RP FUNCTION, INTERACTION WITH RBM39, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=27418600; DOI=10.1073/pnas.1608423113;
RA Anderson D.M., Cannavino J., Li H., Anderson K.M., Nelson B.R.,
RA McAnally J., Bezprozvannaya S., Liu Y., Lin W., Liu N., Bassel-Duby R.,
RA Olson E.N.;
RT "Severe muscle wasting and denervation in mice lacking the RNA-binding
RT protein ZFP106.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E4494-E4503(2016).
RN [11]
RP FUNCTION, INTERACTION WITH TARDBP AND NUP107, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=28072389; DOI=10.7554/elife.19032;
RA Celona B., Dollen J.V., Vatsavayai S.C., Kashima R., Johnson J.R.,
RA Tang A.A., Hata A., Miller B.L., Huang E.J., Krogan N.J., Seeley W.W.,
RA Black B.L.;
RT "Suppression of C9orf72 RNA repeat-induced neurotoxicity by the ALS-
RT associated RNA-binding protein Zfp106.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: RNA-binding protein (PubMed:27418600, PubMed:28072389).
CC Specifically binds to 5'-GGGGCC-3' sequence repeats in RNA
CC (PubMed:28072389). Essential for maintenance of peripheral motor neuron
CC and skeletal muscle function (PubMed:26604141, PubMed:27418600,
CC PubMed:28072389). Required for normal expression and/or alternative
CC splicing of a number of genes in spinal cord and skeletal muscle,
CC including the neurite outgrowth inhibitor RTN4 (PubMed:26604141,
CC PubMed:27418600). Also contributes to normal mitochondrial respiratory
CC function in motor neurons, via an unknown mechanism (PubMed:26604141).
CC {ECO:0000269|PubMed:26604141, ECO:0000269|PubMed:27418600,
CC ECO:0000269|PubMed:28072389}.
CC -!- SUBUNIT: Interacts with KNOP1 (PubMed:15833274). Interacts with TARDBP
CC and NUP107 (PubMed:28072389). Interacts (via N-terminus) with RBM39
CC (PubMed:27418600). Interacts with the SH3 domains of FYN and GRB2
CC (PubMed:9507006). {ECO:0000269|PubMed:15833274,
CC ECO:0000269|PubMed:27418600, ECO:0000269|PubMed:28072389,
CC ECO:0000269|PubMed:9507006}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15833274,
CC ECO:0000269|PubMed:27418600, ECO:0000269|PubMed:28072389,
CC ECO:0000269|PubMed:9507006}. Nucleus speckle
CC {ECO:0000269|PubMed:27418600, ECO:0000269|PubMed:28072389}.
CC Note=Colocalizes with RBM39 in nuclear speckles. Inhibition of RNA
CC synthesis, or overexpression of KNOP1, induces translocation from
CC nuclear speckles to the nucleolus. {ECO:0000269|PubMed:27418600}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O88466-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88466-2; Sequence=VSP_011440, VSP_011441;
CC Name=3;
CC IsoId=O88466-3; Sequence=VSP_011438, VSP_011439;
CC -!- TISSUE SPECIFICITY: Widely expressed, with strongest expression in
CC skeletal muscle, heart and brain (at protein level) (PubMed:9507006,
CC PubMed:26604141, PubMed:27418600, PubMed:28072389). Detected in spinal
CC cord motor neurons (PubMed:28072389). {ECO:0000269|PubMed:26604141,
CC ECO:0000269|PubMed:27418600, ECO:0000269|PubMed:28072389,
CC ECO:0000269|PubMed:9507006}.
CC -!- DEVELOPMENTAL STAGE: During embryonic stages 12.5 dpc and 15.5 dpc,
CC highly expressed in skeletal muscle and cardiac tissue.
CC {ECO:0000269|PubMed:27418600}.
CC -!- INDUCTION: [Isoform 3]: Down-regulated in response to insulin.
CC {ECO:0000269|PubMed:9507006}.
CC -!- PTM: Phosphorylated by FYN in vitro. {ECO:0000269|PubMed:9507006}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB96870.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC26389.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF067397; AAD04340.1; -; Genomic_DNA.
DR EMBL; AF067398; AAD04341.1; -; Genomic_DNA.
DR EMBL; AF067399; AAD04342.1; -; Genomic_DNA.
DR EMBL; AL772299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL935121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF060243; AAG27479.1; -; Genomic_DNA.
DR EMBL; AF060242; AAG27479.1; JOINED; Genomic_DNA.
DR EMBL; AF060244; AAD04327.1; -; mRNA.
DR EMBL; AF060245; AAD04328.1; -; mRNA.
DR EMBL; AF060246; AAD04329.1; -; mRNA.
DR EMBL; AF060247; AAD04330.1; -; mRNA.
DR EMBL; BC025424; AAH25424.1; -; mRNA.
DR EMBL; U59739; AAB96870.1; ALT_FRAME; mRNA.
DR EMBL; AK029313; BAC26389.1; ALT_INIT; mRNA.
DR CCDS; CCDS16621.1; -. [O88466-1]
DR PIR; T14273; T14273.
DR AlphaFoldDB; O88466; -.
DR SMR; O88466; -.
DR BioGRID; 203204; 6.
DR STRING; 10090.ENSMUSP00000055602; -.
DR iPTMnet; O88466; -.
DR PhosphoSitePlus; O88466; -.
DR EPD; O88466; -.
DR jPOST; O88466; -.
DR MaxQB; O88466; -.
DR PaxDb; O88466; -.
DR PeptideAtlas; O88466; -.
DR PRIDE; O88466; -.
DR ProteomicsDB; 275274; -. [O88466-1]
DR ProteomicsDB; 275275; -. [O88466-2]
DR ProteomicsDB; 275276; -. [O88466-3]
DR MGI; MGI:1270153; Zfp106.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; O88466; -.
DR TreeFam; TF105569; -.
DR ChiTaRS; Zfp106; mouse.
DR PRO; PR:O88466; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O88466; protein.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001515; F:opioid peptide activity; IPI:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017124; F:SH3 domain binding; IDA:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR042622; Znf106.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR14435; PTHR14435; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00564; PQQ; 4.
DR SMART; SM00320; WD40; 6.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Ubl conjugation;
KW WD repeat; Zinc; Zinc-finger.
FT CHAIN 1..1888
FT /note="Zinc finger protein 106"
FT /id="PRO_0000051468"
FT REPEAT 1534..1573
FT /note="WD 1"
FT REPEAT 1575..1618
FT /note="WD 2"
FT REPEAT 1659..1700
FT /note="WD 3"
FT REPEAT 1703..1742
FT /note="WD 4"
FT REPEAT 1743..1780
FT /note="WD 5"
FT REPEAT 1783..1820
FT /note="WD 6"
FT ZN_FING 5..29
FT /note="C2H2-type 1; atypical"
FT ZN_FING 43..67
FT /note="C2H2-type 2; atypical"
FT ZN_FING 1818..1843
FT /note="C2H2-type 3; atypical"
FT REGION 68..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1468..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1509..1531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1404..1418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT MOD_RES 909
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT MOD_RES 953
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1036
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT MOD_RES 1040
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1046
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 1296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT MOD_RES 1339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1383
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 155
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 265
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 309
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 375
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 384
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 390
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 435
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 469
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 479
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 524
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 534
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 544
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 577
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 620
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 687
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 700
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 721
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 738
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 758
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 792
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 824
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 921
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 1310
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 1335
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 1391
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 1403
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 1406
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 1460
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 1492
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 1509
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 1590
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 1742
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT CROSSLNK 1869
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2Y7"
FT VAR_SEQ 829..839
FT /note="FGIEMVPLVQN -> CVPLIPVLGFF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9507006"
FT /id="VSP_011438"
FT VAR_SEQ 840..1888
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9507006"
FT /id="VSP_011439"
FT VAR_SEQ 1245..1246
FT /note="RV -> SK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011440"
FT VAR_SEQ 1247..1888
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011441"
FT VARIANT 253
FT /note="G -> S (in strain: C57BL/6 and Swiss Webster)"
FT VARIANT 262
FT /note="L -> P (in strain: C57BL/6 and Swiss Webster)"
FT VARIANT 269
FT /note="G -> D (in strain: Swiss Webster)"
FT VARIANT 293
FT /note="S -> T (in strain: Swiss Webster)"
FT VARIANT 447
FT /note="A -> P (in strain: C57BL/6 and Swiss Webster)"
FT VARIANT 451
FT /note="S -> P (in strain: C57BL/6 and Swiss Webster)"
FT VARIANT 526
FT /note="L -> R (in strain: C57BL/6 and Swiss Webster)"
FT VARIANT 552
FT /note="N -> S (in strain: C57BL/6)"
FT VARIANT 579
FT /note="M -> T (in strain: C57BL/6)"
FT VARIANT 656
FT /note="T -> A (in strain: C57BL/10)"
FT VARIANT 659
FT /note="R -> C (in strain: C57BL/10)"
FT VARIANT 685
FT /note="D -> N (in strain: C57BL/10)"
FT VARIANT 706
FT /note="E -> G (in strain: Swiss Webster)"
FT VARIANT 711
FT /note="E -> G (in strain: Swiss Webster)"
FT VARIANT 717
FT /note="T -> A (in strain: C57BL/10)"
FT VARIANT 778
FT /note="S -> C (in strain: 129/J)"
FT VARIANT 996
FT /note="S -> T (in strain: C57BL/6)"
FT VARIANT 1188
FT /note="P -> S (in strain: C57BL/6)"
FT /evidence="ECO:0000269|PubMed:19468303"
FT VARIANT 1196..1199
FT /note="MSTF -> TCTL (in strain: C57BL/6)"
FT CONFLICT 19
FT /note="Missing (in Ref. 3; AAH25424)"
FT /evidence="ECO:0000305"
FT CONFLICT 1263
FT /note="S -> P (in Ref. 1; AAD04329)"
FT /evidence="ECO:0000305"
FT CONFLICT 1608
FT /note="I -> V (in Ref. 1; AAD04327)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1888 AA; 208964 MW; 73C37BF7A188A061 CRC64;
MVRERKCILC HIVYGSKKEM DEHMRSMLHH RELENLKGRD ISHECRVCRV TEVGLSAYAK
HISGQLHKDN VDAQEREDDG KEEEEEEYFD KELVQLIQER KEQSRQDEPP SNSQEVNSDD
RQPQWRREDR IPYQDRESYS QPPRHHRGPP QRDWKWEKDG FNSTRKNSFP HSLRNSGGPR
GSSVWHKGAT RGSSTWFLNH SNSGGGWHSN NGMVDWNYNG TGRNSSWHSE GTGGFPSWHM
NNSNGNWKSS VRGTNSWNYN GLGDKFQQGR NRNPNYQMED MTKMWNKKSN KPSKYSQERC
KWQRQDRDKA AKYRSPPEGY ASDTFPSEGL LEFNFEQRES QTTKQTDTAA SKINGKNGTK
ARDKFRRWTP YPSQKTLDLQ SALKEVIGSK SDTLEKPLFN FSLITAGLRK PVDKTSNPPV
IKTQKAGPPG SPSHKAISDG TAFCEVARAC SITEQSEPHQ KSNKIPLLKS PLLPLPTPKS
GPHKQNLKNR SKNKETKSFP SGDHSHLLNT STLEGSHGSS YTSKSLGLCP RVLKENKTVS
GTQKEPDEKL NNTSQKAQDT VLQCPKTLQN PLPTTPKRME NDAKESSVEE SAKDSLSIES
QPHSAGNSAM TSDAENHGIK SEGVASLTTE VVSCSTHTVD KEQGSQIPGT PENLSTSPRN
STVLQKEAEV QVSAATSPHS GLLLDLKTSL EDAQDNNLVK SDGPFETESF EDTSLDTELQ
KPDLNNQPPG TLLPELSKLG FPASLQRDLS RHISLKSKTG THLPEPNLNS ARRIRNVSGH
RKNETEKESG LKPTLRQILN ASRRNVNWEQ VIQQVTKKKQ ELGKGLPRFG IEMVPLVQNE
QEVLDLDEEP DLSSLEGFQW EGVSIPSSSG LARKRSLSES SVVMDRAPVY SFFTGEGTGK
ENEAQQSPSP NTALSAAQSQ KTAMYLEQEV APLTPSVGTG ERVGNIPTQR RHSAQLPSGH
IMPVMHSARD LHSQERSTPL SERHAQESTG EGNSLSSNAS SGHAVSSLAD AATDSSCTSG
AEQTDGHSIR KKRRATGDGS SPELPSLERK NKRRKIKGKK ERSQVDQLLT ISLREEELSK
SLQCMDNKLL QARAALQTAY VEVQRLLVLK QQITVEMSAL RTHRIQILQG LQETYEPPEH
PDQAPCSLIS REQRNSRSQT SFETALLPAP FFPGFLDPPP SHASLPSPGN PLQITMSTFQ
AHGTAPDSSV QIKQEPMSPE QEGNMNALPQ GCASNVSKEL LQTNRVVDDG SSVYPAIPAV
IASESTENCQ EVSKDLNFSV EQGNSRSKGN SPSCQSPDLP GINRGEETAK GSSGSEACSS
SFLRLSFTPE TPAEKETQSP ADQPEQQAES TLASAETRGS KKKKKLRKKK TLRATHVPEN
SDTEQDVFTA KPARKVKTAK AAKGAKVTTS QTGQEQGTAR DEPDSDSSLE VLEVTNPQLE
VVAIDTSESG DEKPDSPSKK DAWIAAEQNP IETSRSGCDE VSSTSELGTR YKDGVPVSVA
ETQTVISIKA SKHSSEISSE PGDDEEPTEG SFEGHQAAVN AIQIFGNFLY TCSADTTVRV
YNLVSRKCVG VFEGHTSKVN CLLVTHTSGK SSVLYTGSSD HTIRCYNIKT RECMEQLQLE
DRVLCLHNRW RTLYAGLANG TVVTFDIKNN KRQEIFECHG PRAVSCLATA QEGARKLLVV
GSYDCTISVR DARNGLLLRT LEGHSKTVLC MKVVNDLVFS GSSDQSVHAH NIHTGELVRI
YKGHNHAVTV VNILGKVMVT ACLDKFVRVY ELQSHDRLQV YGGHKDMIMC MTIHKSVIYT
GCYDGSIQAV RLNLMQNYRC WWYGCTLIFG VVDHLKQHLL TDHTNPNFQT LKCRWRNCDA
FFTARKGSKQ DVAGHIERHA EDDSKIDS
