MINT_MOUSE
ID MINT_MOUSE Reviewed; 3644 AA.
AC Q62504; Q80TN9; Q99PS4; Q9QZW2;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Msx2-interacting protein;
DE AltName: Full=SMART/HDAC1-associated repressor protein;
DE AltName: Full=SPEN homolog;
GN Name=Spen; Synonyms=Kiaa0929, Mint, Sharp;
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 [LARGE SCALE MRNA] OF 1-112.
RC STRAIN=C57BL/6J; TISSUE=Egg;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-3644 (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DNA-BINDING, AND INTERACTION WITH MSX2.
RC TISSUE=Testis;
RX PubMed=10451362; DOI=10.1021/bi990967j;
RA Newberry E.P., Latifi T., Towler D.A.;
RT "The RRM domain of MINT, a novel msx2 binding protein, recognizes and
RT regulates the rat osteocalcin promoter.";
RL Biochemistry 38:10678-10690(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-3644 (ISOFORM 2), AND VARIANTS THR-348;
RP PHE-762; PHE-773 AND LEU-933.
RC STRAIN=ICR; TISSUE=Brain;
RA Sakamoto T., Gotou T., Isagawa Y., Mimura H., Kimura K., Kawaichi M.;
RT "MINT/spen negatively regulates Notch signaling by inhibiting RBP-J/Su(H)
RT activity.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 318-578, AND VARIANT THR-348.
RC TISSUE=Cochlea;
RX PubMed=9119401; DOI=10.1006/geno.1996.4526;
RA Crozet F., El-Amraoui A., Blanchard S., Lenoir M., Ripoll C., Vago P.,
RA Hamel C., Fizames C., Levi-Acobas F., Depetris D., Mattei M.-G., Weil D.,
RA Pujol R., Petit C.;
RT "Cloning of the genes encoding two murine and human cochlear unconventional
RT type I myosins.";
RL Genomics 40:332-341(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2600-3644 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [6]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=12374742; DOI=10.1093/emboj/cdf549;
RA Oswald F., Kostezka U., Astrahantseff K., Bourteele S., Dillinger K.,
RA Zechner U., Ludwig L., Wilda M., Hameister H., Knoechel W., Liptay S.,
RA Schmid R.M.;
RT "SHARP is a novel component of the Notch/RBP-Jkappa signalling pathway.";
RL EMBO J. 21:5417-5426(2002).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12594956; DOI=10.1016/s1074-7613(03)00029-3;
RA Kuroda K., Han H., Tani S., Tanigaki K., Tun T., Furukawa T., Taniguchi Y.,
RA Kurooka H., Hamada Y., Toyokuni S., Honjo T.;
RT "Regulation of marginal zone B cell development by MINT, a suppressor of
RT Notch/RBP-J signaling pathway.";
RL Immunity 18:301-312(2003).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15131132; DOI=10.1074/jbc.m314098200;
RA Sierra O.L., Cheng S.L., Loewy A.P., Charlton-Kachigian N., Towler D.A.;
RT "MINT, the Msx2 interacting nuclear matrix target, enhances Runx2-dependent
RT activation of the osteocalcin fibroblast growth factor response element.";
RL J. Biol. Chem. 279:32913-32923(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1395, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852; SER-855; SER-869 AND
RP SER-1395, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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 [12]
RP FUNCTION, AND INTERACTION WITH HIPK3.
RX PubMed=20484411; DOI=10.1210/me.2010-0029;
RA Sierra O.L., Towler D.A.;
RT "Runx2 trans-activation mediated by the MSX2-interacting nuclear target
RT requires homeodomain interacting protein kinase-3.";
RL Mol. Endocrinol. 24:1478-1497(2010).
CC -!- FUNCTION: May serve as a nuclear matrix platform that organizes and
CC integrates transcriptional responses. In osteoblasts, supports
CC transcription activation: synergizes with RUNX2 to enhance FGFR2-
CC mediated activation of the osteocalcin FGF-responsive element (OCFRE).
CC Has also been shown to be an essential corepressor protein, which
CC probably regulates different key pathways, such as the Notch pathway.
CC Negative regulator of the Notch pathway via its interaction with
CC RBPSUH, which prevents the association between NOTCH1 and RBPSUH, and
CC therefore suppresses the transactivation activity of Notch signaling.
CC Blocks the differentiation of precursor B-cells into marginal zone B-
CC cells. Probably represses transcription via the recruitment of large
CC complexes containing histone deacetylase proteins. May bind both to DNA
CC and RNA. {ECO:0000269|PubMed:10451362, ECO:0000269|PubMed:12594956,
CC ECO:0000269|PubMed:15131132, ECO:0000269|PubMed:20484411}.
CC -!- SUBUNIT: Interacts with NCOR2, HDAC1, HDAC2, RBBP4, MBD3 and MTA1L1.
CC Interacts with the nuclear receptors RAR and PPARD. Interacts with RAR
CC in absence of ligand. Binds to the steroid receptor RNA coactivator SRA
CC (By similarity). Interacts with MSX2. Interacts with RBPSUH; this
CC interaction may prevent the interaction between RBPSUH and NOTCH1.
CC Binds to HIPK3. {ECO:0000250, ECO:0000269|PubMed:10451362,
CC ECO:0000269|PubMed:20484411}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10451362,
CC ECO:0000269|PubMed:15131132}. Note=Associates with chromatin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q62504-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62504-2; Sequence=VSP_008564;
CC Name=3;
CC IsoId=Q62504-3; Sequence=VSP_013802, VSP_013803, VSP_013804;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Expressed at lower
CC level in brain, lung, spleen, liver and kidney. Weakly expressed in
CC cardiac and skeletal muscles and ovary. In spleen, it is expressed in
CC follicular B-cells, while it is weakly expressed in marginal zone B-
CC cells. {ECO:0000269|PubMed:10451362, ECO:0000269|PubMed:12374742,
CC ECO:0000269|PubMed:12594956}.
CC -!- DOMAIN: The RID domain mediates the interaction with nuclear receptors.
CC -!- DOMAIN: The SPOC domain, which mediates the interaction with NCOR2, is
CC essential for the repressive activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM Spen family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD55931.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB01562.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB01562.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BY726481; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF156529; AAD55931.1; ALT_INIT; mRNA.
DR EMBL; AB055980; BAB32786.1; -; mRNA.
DR EMBL; Z78160; CAB01562.1; ALT_SEQ; mRNA.
DR EMBL; AK122402; BAC65684.3; -; Transcribed_RNA.
DR RefSeq; NP_062737.2; NM_019763.2.
DR BMRB; Q62504; -.
DR SMR; Q62504; -.
DR BioGRID; 207942; 34.
DR CORUM; Q62504; -.
DR IntAct; Q62504; 3.
DR STRING; 10090.ENSMUSP00000101412; -.
DR iPTMnet; Q62504; -.
DR PhosphoSitePlus; Q62504; -.
DR EPD; Q62504; -.
DR jPOST; Q62504; -.
DR MaxQB; Q62504; -.
DR PaxDb; Q62504; -.
DR PeptideAtlas; Q62504; -.
DR PRIDE; Q62504; -.
DR ProteomicsDB; 295607; -. [Q62504-1]
DR ProteomicsDB; 295608; -. [Q62504-2]
DR ProteomicsDB; 295609; -. [Q62504-3]
DR DNASU; 56381; -.
DR GeneID; 56381; -.
DR KEGG; mmu:56381; -.
DR CTD; 23013; -.
DR MGI; MGI:1891706; Spen.
DR eggNOG; KOG0112; Eukaryota.
DR InParanoid; Q62504; -.
DR OrthoDB; 367857at2759; -.
DR PhylomeDB; Q62504; -.
DR Reactome; R-MMU-9013422; RHOBTB1 GTPase cycle.
DR BioGRID-ORCS; 56381; 10 hits in 75 CRISPR screens.
DR ChiTaRS; Spen; mouse.
DR PRO; PR:Q62504; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q62504; protein.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0017053; C:transcription repressor complex; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd12348; RRM1_SHARP; 1.
DR CDD; cd12349; RRM2_SHARP; 1.
DR CDD; cd12350; RRM3_SHARP; 1.
DR CDD; cd12351; RRM4_SHARP; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034172; SHARP_RRM1.
DR InterPro; IPR034173; SHARP_RRM2.
DR InterPro; IPR034174; SHARP_RRM3.
DR InterPro; IPR034175; SHARP_RRM4.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR012921; SPOC_C.
DR InterPro; IPR010912; SPOC_met.
DR Pfam; PF00076; RRM_1; 3.
DR Pfam; PF07744; SPOC; 1.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF100939; SSF100939; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 4.
DR PROSITE; PS50917; SPOC; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; DNA-binding; Methylation;
KW Notch signaling pathway; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..3644
FT /note="Msx2-interacting protein"
FT /id="PRO_0000081628"
FT DOMAIN 6..81
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 336..416
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 439..514
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 518..590
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 2216..2704
FT /note="RID"
FT DOMAIN 3478..3644
FT /note="SPOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00249"
FT DNA_BIND 1..574
FT REGION 103..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..1413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1494..1538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1557..2447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2138..2462
FT /note="Interaction with MSX2"
FT /evidence="ECO:0000269|PubMed:10451362"
FT REGION 2453..2472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2481..2528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2706..2845
FT /note="Interaction with RBPSUH"
FT REGION 2745..2781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2829..2849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2974..3023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3310..3473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 559..575
FT /evidence="ECO:0000255"
FT COILED 822..850
FT /evidence="ECO:0000255"
FT COILED 1185..1206
FT /evidence="ECO:0000255"
FT COILED 1509..1544
FT /evidence="ECO:0000255"
FT COILED 1607..1627
FT /evidence="ECO:0000255"
FT COMPBIAS 191..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..849
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..1073
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1580..1594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1754..1781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1782..1798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1799..1814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1857..1894
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1917..1931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1933..1957
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1973..1994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2040..2106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2129..2148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2279..2293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2355..2370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2403..2417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2503..2528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2748..2762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2999..3013
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3310..3336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3337..3354
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3355..3396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3422..3436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 108
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 792
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1077
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1454
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1456
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1634
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1844
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1915
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1936
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 1965
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 2128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 2134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 2171
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 2366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 2419
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 2450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 2454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 2458
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 2491
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 2913
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 2925
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 3088
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 3096
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT MOD_RES 3413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T58"
FT VAR_SEQ 618..640
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_008564"
FT VAR_SEQ 3318..3322
FT /note="PPEGE -> RKPAFF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_013802"
FT VAR_SEQ 3550..3552
FT /note="ETD -> RLE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_013803"
FT VAR_SEQ 3553..3644
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_013804"
FT VARIANT 348
FT /note="I -> T"
FT /evidence="ECO:0000269|PubMed:9119401, ECO:0000269|Ref.3"
FT VARIANT 762
FT /note="S -> F"
FT /evidence="ECO:0000269|Ref.3"
FT VARIANT 773
FT /note="S -> F"
FT /evidence="ECO:0000269|Ref.3"
FT VARIANT 933
FT /note="S -> L"
FT /evidence="ECO:0000269|Ref.3"
FT CONFLICT 366
FT /note="V -> E (in Ref. 4; CAB01562)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="L -> B (in Ref. 4; CAB01562)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="V -> E (in Ref. 4; CAB01562)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="V -> E (in Ref. 4; CAB01562)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="I -> K (in Ref. 4; CAB01562)"
FT /evidence="ECO:0000305"
FT CONFLICT 454..462
FT /note="DLRNIFQRF -> EPSETSFSAL (in Ref. 4; CAB01562)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="F -> L (in Ref. 4; CAB01562)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="S -> P (in Ref. 4; CAB01562)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="H -> N (in Ref. 4; CAB01562)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="A -> V (in Ref. 4; CAB01562)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="A -> V (in Ref. 4; CAB01562)"
FT /evidence="ECO:0000305"
FT CONFLICT 573..577
FT /note="TKGRK -> DQGQE (in Ref. 4; CAB01562)"
FT /evidence="ECO:0000305"
FT CONFLICT 754
FT /note="R -> G (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 1524
FT /note="D -> A (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 1560
FT /note="H -> Y (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 1570
FT /note="F -> L (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 1574
FT /note="R -> G (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 1609
FT /note="Q -> R (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 1659
FT /note="I -> V (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 1669
FT /note="S -> F (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 1705
FT /note="V -> A (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 1815
FT /note="A -> V (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 2097
FT /note="G -> A (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 2201..2202
FT /note="Missing (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 2322
FT /note="A -> V (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 2385
FT /note="P -> Q (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 2502
FT /note="R -> K (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 2505
FT /note="E -> K (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 2519
FT /note="D -> N (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 2554
FT /note="T -> S (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 2679..2688
FT /note="LVSTPAGPVN -> VGEHPWWARD (in Ref. 3; BAB32786)"
FT /evidence="ECO:0000305"
FT CONFLICT 3010
FT /note="L -> P (in Ref. 3; BAB32786 and 5; BAC65684)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3644 AA; 398754 MW; 9C7EC49A81A7DA4A CRC64;
MVRETRHLWV GNLPENVREE KIIEHFKRYG RVESVKILPK RGSEGGVAAF VDFVDIKSAQ
KAHNSVNKMG DRDLRTDYNE PGTIPSAARG LDETVSIASR SREVSGFRGS AGGPAYGPPP
SLHAREGRYE RRLDGASDNR ERAYEHSAYG HHERGTGAFD RTRHYDQDYY RDPRERTLQH
GLYYTSRSRS PNRFDAHDPR YEPRAREQFT LPSVVHRDIY RDDITREVRG RRPERSYQHS
RSRSPHSSQS RNQSPQRLAS QASRPTRSPS GSGSRSRSSS SDSISSSSSS SNTDSSDSSS
TASDDSPARS VQSAAVPAPT SQLLSSLEKD EPRKSFGIKV QNLPVRSIDT SLKDGLFHEF
KKFGKVTSVQ IHGASEERYG LVFFRQQEDQ EKALTASKGK LFFGMQIEVT AWVGPETESE
NEFRPLDERI DEFHPKATRT LFIGNLEKTT TYHDLRNIFQ RFGEIVDIDI KKVNGVPQYA
FLQYCDIASV CKAIKKMDGE YLGNNRLKLG FGKSMPTNCV WLDGLSSNVS DQYLTRHFCR
YGPVVKVVFD RLKGMALVLY SEIEDAQAAV KETKGRKIGG NKIKVDFANR ESQLAFYHCM
EKSGQDMRDF YEMLTERRAG QMAQSKHEDW SADAQSPHKC REERRGSYEY SQERTYYENV
RTPGTYPEDS RRDYPARGRE FYSEWETYQG EYYDSRYYDE PREYREYRSD PYEQDIREYS
YRQRERERER ERFESDRDHE RRPIERSQSP VHLRRPQSPG VSPAHSERLP SDSERRLYRR
SSERSGSCSS VSPPRYDKLE KARLERYTKN EKADKERTFD PERVERERRI VRKEKGEKDK
AERQKRKGKA HSPSSQPSET EQENDREQSP EKPRGSTKLS RDRADKEGPA KNRLELVPCV
VLTRVKEKEG KVIEHPPPEK LKARLGRDTT KASALDQKPQ AAQGEPAKSD PARGKALREK
VLPSHAEVGE KEGRTKLRKH LKAEQTPELS ALDLEKLEAR KRRFADSGLK IEKQKPEIKK
TSPETEDTRI LLKKQPDTSR DGVLLREGES ERKPVRKEIL KRESKKTKLE RLNSALSPKD
CQDPAAVSAG SGSRPSSDVH AGLGELTHGS VETQETQPKK AIPSKPQPKQ LQLLENQGPE
KEEVRKNYCR PREEPAEHRA GQEKPHGGNA EEKLGIDIDH TQSYRKQMEQ SRRKQRMEME
IAKAEKFGSP KKDVDDYERR SLVHEVGKPP QDVTDDSPPS KKRRTDHVDF DICTKRERNY
RSSRQISEDS ERTSCSPSVR HGSFHDDDDP RGSPRLVSVK GSPKGDEKGL PYPNAAVRDD
PLKCNPYDSG KREQTADTAK IKLSVLNSEG EPSRWDPPMK QDPSRFDVSF PNSVIKRDSL
RKRSVRDLEP GEVPSDSDED AEHRSQSPRA SSFYDSPRLS FLLRDRDQKL RERDERLASS
LERNKFYSFA LDKTITPDTK ALLERAKSLS SSREENWSFL DWDSRFANFR NNKDKEKVDS
APRPIPSWYM KKKKIRTDSE GKLDDKKDER REEEQERQEL FASRFLHSSI FEQDSKRLQH
LERKSEESDF PPGRLYGRQA SEGANSTSDS VQEPVVLFHS RFMELTRMQQ KEKEKDQKPK
EAEKQEEPET HPKTPEPAAE TKEPEPKAPV SAGLPAVTIT VVTPEPASSA PEKAEEAAEA
PSPAGEKPAE PAPVSEETKL VSEPVSVPVE QPRQSDVPPG EDSRDSQDSA ALAPSAPQES
AATDAVPCVN AEPLTPGTTV SQVESSVDPK PSSPQPLSKL TQRSEEAEEG KVEKPDTTPS
TEPDATQNAG VASEAQPPAS EDVEANPPVA AKDRKTNKSK RSKTSVQAAA ASVVEKPVTR
KSERIDREKL KRSSSPRGEA QKLLELKMEA EKITRTASKS SGGDTEHPEP SLPLSRSRRR
NVRSVYATMT DHESRSPAKE PVEQPRVTRK RLERELQEAV VPPTTPRRGR PPKTRRRAEE
DGEHERKEPA ETPRPAEGWR SPRSQKSAAA AGPQGKRGRN EQKVEAAAEA GAQASTREGN
PKSRGEREAA SEPKRDRRDP STDKSGPDTF PVEVLERKPP EKTYKSKRGR ARSTRSGMDR
AAHQRSLEMA ARAAGQAADK EAGPAAASPQ ESESPQKGSG SSPQLANNPA DPDREAEEES
ASASTAPPEG TQLARQIELE QAVQNIAKLP EPSAAAASKG TATATATAAS EEPAPEHGHK
PAHQASETEL AAAIGSIISD ASGEPENFSA PPSVPPGSQT HPREGMEPGL HEAESGILET
GTATESSAPQ VSALDPPEGS ADTKETRGNS GDSVQEAKGS KAEVTPPRKD KGRQKTTRRR
KRNANKKVVA ITETRASEAE QTQSESPAAE EATAATPEAP QEEKPSEKPP SPPAECTFDP
SKTPPAESLS QENSAAEKTP CKAPVLPALP PLSQPALMDD GPQARFKVHS IIESDPVTPP
SDSGIPPPTI PLVTIAKLPP PVIPGGVPHQ SPPPKVTEWI TRQEEPRAQS TPSPALPPDT
KASDMDTSSS TLRKILMDPK YVSATGVTST SVTTAIAEPV SAPCLQEAPA PPCDPKHPPL
EGVSAAAVPN ADTQASEVPV AADKEKVAPV IAPKITSVIS RMPVSIDLEN SQKITLAKPA
PQTLTGLVSA LTGLVNVSLV PVNALKGPVK GSVATLKGLV STPAGPVNLL KGPVNVLTGP
VNVLTTPVSA TVGTVNAAPG PVTAACGVTA TTGTAAVTGA VTAPAAKGKQ RASSNENSRF
HPGSMSVIDD RPADTGSGAG LRVNTSEGVV LLSYSGQKTE GPQRISAKIS QIPPASAMDI
EFQQSVSKSQ VKADSITPTQ SAPKGPQTPS AFANVAAHST LVLTAQTYNA SPVISSVKTD
RPSLEKPEPI HLSVSTPVTQ GGTVKVLTQG INTPPVLVHN QLVLTPSIVT TNKKLADPVT
LKIETKVLQP ANLGPTLTPH HPPALPSKLP AEVNHVPSGP STPADRTIAH LATPKPDTHS
PRPTGPTPGL FPRPCHPSST TSTALSTNAT VMLAAGIPVP QFISSIHPEQ SVIMPPHSIT
QTVSLGHLSQ GEVRMSTPTL PSITYSIRPE TLHSPRAPLQ PQQIEARAPQ RVGTPQPATT
GVPALATQHP PEEEVHYHLP VARAAAPVQS EVLVMQSEYR LHPYTVPRDV RIMVHPHVTA
VSEQPRATEG VVKVPPANKA PQQLVKEAVK TSDAKAVPAP APVPVPVPVP TPAPPPHGEA
RILTVTPSSQ LQGLPLTPPV VVTHGVQIVH SSGELFQEYR YGDVRTYHAP AQQLTHTQFP
VASSISLASR TKTSAQVPPE GEPLQSTQSA QPAPSTQATQ PIPPAPPCQP SQLSQPAQPP
SGKIPQVSQE AKGTQTGGVE QTRLPAIPTN RPSEPHAQLQ RAPVETAQPA HPSPVSVSMK
PDLPSPLSSQ AAPKQPLFVP ANSGPSTPPG LALPHAEVQP APKQESSPHG TPQRPVDMVQ
LLKKYPIVWQ GLLALKNDTA AVQLHFVSGN NVLAHRSLPL SEGGPPLRIA QRMRLEASQL
EGVARRMTVE TDYCLLLALP CGRDQEDVVS QTESLKAAFI TYLQAKQAAG IINVPNPGSN
QPAYVLQIFP PCEFSESHLS RLAPDLLASI SNISPHLMIV IASV
