RBM15_MOUSE
ID RBM15_MOUSE Reviewed; 962 AA.
AC Q0VBL3; A0PJG5; Q3THK4; Q3TLX0; Q571M7; Q66JP8; Q6PGG1; Q7TT82;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=RNA-binding protein 15 {ECO:0000303|PubMed:17376872};
DE AltName: Full=One-twenty two protein 1 {ECO:0000303|PubMed:17376872};
DE AltName: Full=RNA-binding motif protein 15 {ECO:0000303|PubMed:17376872};
GN Name=Rbm15 {ECO:0000303|PubMed:17376872, ECO:0000312|MGI:MGI:2443205};
GN Synonyms=Kiaa4257 {ECO:0000303|Ref.1}, Ott1 {ECO:0000303|PubMed:17376872};
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 (ISOFORM 2).
RC TISSUE=Embryonic tail;
RA Okazaki N., Kikuno R.F., 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. The
RT Complete Nucleotide Sequences of Mouse KIAA-homologous cDNAs Identified by
RT Screening of Terminal sequences of cDNA Clones Randomly Sampled from Size-
RT Fractionated Libraries.";
RL Submitted (FEB-2005) 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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Eye, and Thymus;
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 [LARGE SCALE MRNA] OF 11-958 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-962 (ISOFORM 1).
RC TISSUE=Mammary gland {ECO:0000312|EMBL:BAE38672.1};
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RBPJ.
RX PubMed=17283045; DOI=10.1128/mcb.01339-06;
RA Ma X., Renda M.J., Wang L., Cheng E.C., Niu C., Morris S.W., Chi A.S.,
RA Krause D.S.;
RT "Rbm15 modulates Notch-induced transcriptional activation and affects
RT myeloid differentiation.";
RL Mol. Cell. Biol. 27:3056-3064(2007).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17376872; DOI=10.1073/pnas.0609041104;
RA Raffel G.D., Mercher T., Shigematsu H., Williams I.R., Cullen D.E.,
RA Akashi K., Bernard O.A., Gilliland D.G.;
RT "Ott1(Rbm15) has pleiotropic roles in hematopoietic development.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:6001-6006(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18981216; DOI=10.1128/mcb.00370-08;
RA Raffel G.D., Chu G.C., Jesneck J.L., Cullen D.E., Bronson R.T.,
RA Bernard O.A., Gilliland D.G.;
RT "Ott1 (Rbm15) is essential for placental vascular branching morphogenesis
RT and embryonic development of the heart and spleen.";
RL Mol. Cell. Biol. 29:333-341(2009).
RN [8]
RP FUNCTION, AND RNA BINDING.
RX PubMed=25468569; DOI=10.1182/blood-2014-08-593392;
RA Xiao N., Laha S., Das S.P., Morlock K., Jesneck J.L., Raffel G.D.;
RT "Ott1 (Rbm15) regulates thrombopoietin response in hematopoietic stem cells
RT through alternative splicing of c-Mpl.";
RL Blood 125:941-948(2015).
RN [9]
RP IDENTIFICATION IN THE WMM COMPLEX, AND FUNCTION.
RX PubMed=29535189; DOI=10.1101/gad.309146.117;
RA Knuckles P., Lence T., Haussmann I.U., Jacob D., Kreim N., Carl S.H.,
RA Masiello I., Hares T., Villasenor R., Hess D., Andrade-Navarro M.A.,
RA Biggiogera M., Helm M., Soller M., Buehler M., Roignant J.Y.;
RT "Zc3h13/Flacc is required for adenosine methylation by bridging the mRNA-
RT binding factor Rbm15/Spenito to the m6A machinery component Wtap/Fl(2)d.";
RL Genes Dev. 32:415-429(2018).
CC -!- FUNCTION: RNA-binding protein that acts as a key regulator of N6-
CC methyladenosine (m6A) methylation of RNAs, thereby regulating different
CC processes, such as hematopoietic cell homeostasis, alternative splicing
CC of mRNAs and X chromosome inactivation mediated by Xist RNA
CC (PubMed:29535189). Associated component of the WMM complex, a complex
CC that mediates N6-methyladenosine (m6A) methylation of RNAs, a
CC modification that plays a role in the efficiency of mRNA splicing and
CC RNA processing (PubMed:29535189). Plays a key role in m6A methylation,
CC possibly by binding target RNAs and recruiting the WMM complex
CC (PubMed:29535189). Involved in random X inactivation mediated by Xist
CC RNA: acts by binding Xist RNA and recruiting the WMM complex, which
CC mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA
CC and promoting transcription repression activity of Xist (By
CC similarity). Required for the development of multiple tissues, such as
CC the maintenance of the homeostasis of long-term hematopoietic stem
CC cells and for megakaryocyte (MK) and B-cell differentiation
CC (PubMed:17283045, PubMed:17376872, PubMed:18981216, PubMed:25468569).
CC Regulates megakaryocyte differentiation by regulating alternative
CC splicing of genes important for megakaryocyte differentiation; probably
CC regulates alternative splicing via m6A regulation (By similarity).
CC Required for placental vascular branching morphogenesis and embryonic
CC development of the heart and spleen (PubMed:18981216). Acts as a
CC regulator of thrombopoietin response in hematopoietic stem cells by
CC regulating alternative splicing of MPL (PubMed:25468569). May also
CC function as an mRNA export factor, stimulating export and expression of
CC RTE-containing mRNAs which are present in many retrotransposons that
CC require to be exported prior to splicing (By similarity). High affinity
CC binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the
CC export helicase DBP5 in a manner that is independent of splicing-
CC mediated NXF1 deposition, resulting in export prior to splicing (By
CC similarity). May be implicated in HOX gene regulation (By similarity).
CC {ECO:0000250|UniProtKB:Q96T37, ECO:0000269|PubMed:17283045,
CC ECO:0000269|PubMed:17376872, ECO:0000269|PubMed:18981216,
CC ECO:0000269|PubMed:25468569, ECO:0000269|PubMed:29535189}.
CC -!- SUBUNIT: Component of the WMM complex, a N6-methyltransferase complex
CC composed of a catalytic subcomplex, named MAC, and of an associated
CC subcomplex, named MACOM (PubMed:29535189). The MAC subcomplex is
CC composed of METTL3 and METTL14 (PubMed:29535189). The MACOM subcomplex
CC is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of
CC RBM15 (RBM15 or RBM15B) (PubMed:29535189). Also a component of a MACOM-
CC like complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1,
CC VIRMA, RBM15, BCLAF1 and THRAP3 (By similarity). Interacts with RBPJ
CC (PubMed:17283045). Interacts (via SPOC domain) with SETD1B (By
CC similarity). Interacts with NXF1, the interaction is required to
CC promote mRNA export (By similarity). Interacts with SF3B1 (By
CC similarity). {ECO:0000250|UniProtKB:Q96T37,
CC ECO:0000269|PubMed:17283045, ECO:0000269|PubMed:29535189}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q96T37}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:17283045}. Nucleus envelope
CC {ECO:0000250|UniProtKB:Q96T37}. Nucleus membrane
CC {ECO:0000250|UniProtKB:Q96T37}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96T37}. Note=Colocalizes at the nuclear pore
CC with DBP5 and NXF1. {ECO:0000250|UniProtKB:Q96T37}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0VBL3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0VBL3-2; Sequence=VSP_059625;
CC -!- PTM: Methylated at Arg-577 by PRMT1, leading to promote ubiquitination
CC by CNOT4 and subsequent degradation by the proteasome.
CC {ECO:0000250|UniProtKB:Q96T37}.
CC -!- PTM: Ubiquitinated by CNOT4 following methylation at Arg-577 by PRMT1.
CC {ECO:0000250|UniProtKB:Q96T37}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality around E9.5 (PubMed:17376872,
CC PubMed:18981216). Early embryos show growth retardation and incomplete
CC closure of the notochord, as well as placental defects in the
CC spongiotrophoblast and syncytiotrophoblast layers, resulting in an
CC arrest of vascular branching morphogenesis (PubMed:18981216).
CC Conditional knockout mice lacking Rbm15 within the hematopoietic
CC compartment display a loss of peripheral B-cells due to a block in
CC pro/pre-B differentiation, as well as a myeloid and megakaryocytic
CC expansion in spleen and bone marrow (PubMed:17376872).
CC {ECO:0000269|PubMed:17376872, ECO:0000269|PubMed:18981216}.
CC -!- SIMILARITY: Belongs to the RRM Spen family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH80828.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
CC Sequence=BAD90348.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK220162; BAD90348.1; ALT_INIT; mRNA.
DR EMBL; AC132405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028452; AAH28452.1; -; mRNA.
DR EMBL; BC051409; AAH51409.1; -; mRNA.
DR EMBL; BC057038; AAH57038.1; -; mRNA.
DR EMBL; BC080828; AAH80828.1; ALT_SEQ; mRNA.
DR EMBL; BC120590; AAI20591.1; -; mRNA.
DR EMBL; BC137741; AAI37742.1; -; mRNA.
DR EMBL; AK166271; BAE38672.1; -; mRNA.
DR EMBL; AK168242; BAE40192.1; -; mRNA.
DR CCDS; CCDS38590.1; -. [Q0VBL3-1]
DR RefSeq; NP_001039272.1; NM_001045807.1. [Q0VBL3-1]
DR AlphaFoldDB; Q0VBL3; -.
DR SMR; Q0VBL3; -.
DR IntAct; Q0VBL3; 4.
DR MINT; Q0VBL3; -.
DR STRING; 10090.ENSMUSP00000054424; -.
DR iPTMnet; Q0VBL3; -.
DR PhosphoSitePlus; Q0VBL3; -.
DR jPOST; Q0VBL3; -.
DR MaxQB; Q0VBL3; -.
DR PaxDb; Q0VBL3; -.
DR PeptideAtlas; Q0VBL3; -.
DR PRIDE; Q0VBL3; -.
DR ProteomicsDB; 338722; -. [Q0VBL3-1]
DR Antibodypedia; 4448; 136 antibodies from 26 providers.
DR Ensembl; ENSMUST00000061772; ENSMUSP00000054424; ENSMUSG00000048109. [Q0VBL3-1]
DR GeneID; 229700; -.
DR KEGG; mmu:229700; -.
DR UCSC; uc008qwz.1; mouse. [Q0VBL3-1]
DR CTD; 64783; -.
DR MGI; MGI:2443205; Rbm15.
DR VEuPathDB; HostDB:ENSMUSG00000048109; -.
DR eggNOG; KOG0112; Eukaryota.
DR GeneTree; ENSGT00940000158161; -.
DR HOGENOM; CLU_012724_1_0_1; -.
DR InParanoid; Q0VBL3; -.
DR OMA; YVCFRTP; -.
DR OrthoDB; 367857at2759; -.
DR PhylomeDB; Q0VBL3; -.
DR TreeFam; TF315637; -.
DR BioGRID-ORCS; 229700; 27 hits in 77 CRISPR screens.
DR ChiTaRS; Rbm15; mouse.
DR PRO; PR:Q0VBL3; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q0VBL3; protein.
DR Bgee; ENSMUSG00000048109; Expressed in indifferent gonad and 225 other tissues.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:MGI.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; ISS:UniProtKB.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0060674; P:placenta blood vessel development; IMP:MGI.
DR GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; IDA:MGI.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0045652; P:regulation of megakaryocyte differentiation; ISO:MGI.
DR GO; GO:0001510; P:RNA methylation; ISS:UniProtKB.
DR GO; GO:0048536; P:spleen development; IMP:MGI.
DR GO; GO:0038163; P:thrombopoietin-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:MGI.
DR CDD; cd12553; RRM1_RBM15; 1.
DR CDD; cd12555; RRM2_RBM15; 1.
DR CDD; cd12557; RRM3_RBM15; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034470; RBM15_RRM1.
DR InterPro; IPR034472; RBM15_RRM2.
DR InterPro; IPR034473; RBM15_RRM3.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR012921; SPOC_C.
DR InterPro; IPR010912; SPOC_met.
DR Pfam; PF00076; RRM_1; 2.
DR Pfam; PF07744; SPOC; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF100939; SSF100939; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
DR PROSITE; PS50917; SPOC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Isopeptide bond; Membrane; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..962
FT /note="RNA-binding protein 15"
FT /id="PRO_0000444611"
FT DOMAIN 169..251
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 373..450
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 454..528
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 778..957
FT /note="SPOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00249"
FT REGION 1..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 265
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 449
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 567
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 577
FT /note="Asymmetric dimethylarginine; alternate; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 577
FT /note="Omega-N-methylarginine; alternate; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT CROSSLNK 405
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT CROSSLNK 419
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT CROSSLNK 745
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96T37"
FT VAR_SEQ 956..962
FT /note="AKLVNSG -> GAS (in isoform 2)"
FT /id="VSP_059625"
FT CONFLICT 41
FT /note="R -> P (in Ref. 1; BAD90348)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="G -> S (in Ref. 4; BAE40192)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="S -> A (in Ref. 4; BAE38672)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="G -> S (in Ref. 4; BAE40192)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 962 AA; 105722 MW; D740EDBF23279C5D CRC64;
MRSAGREPLP RRSPRWRRAS PLCETSAGWR VSQLRRDDLR RPSTMKGKER SPVKPKRSRG
GEDSSSRGER SKKLGGSGGS NGSSSGKTDS GGSRRSLHLD KSSSRGGSRE YETGGGSSSS
RLHSYSSPST KNSSGGGESR SSSRGGGGES RSSGAASSAP GGGDGVEYKT LKISELGSQL
SDEAVEDGLF HEFKRFGDVS VKISHLSGSG SGDERVAFVN FRRPEDARAA KHARGRLVLY
DRPLKIEAVY VSRRRSRSPL DKDAYAPSSS VVGTSVGSHR HAPGGGGGQR SLSPGGAALG
YRDYRLQQLA LGRLPPPPPP PLPRELERER DYPFYDRVRP AYSLEPRVGA GAGAAPFREV
DEISPEDDQR ANRTLFLGNL DITVTENDLR RAFDRFGVIT EVDIKRPSRG QTSTYGFLKF
ENLDMSHRAK LAMSGKIIIR NPIKIGYGKA TPTTRLWVGG LGPWVPLAAL AREFDRFGTI
RTIDYRKGDS WAYIQYESLD AAHAAWTHMR GFPLGGPDRR LRVDFADTEH RYQQQYLQPL
PLTHYELVTD TFGHRAPDPL RSARDRTPPL LYRDRDRDLY TDSDWVPPPP PVRERSARAA
TSAVTAYEPL DSLDRRRDGW SLDRDRGDRD LPSSRDQPRK RRLPEESGGR HLDRSPESER
PRKQRHCTPS PDRSPELSSN RDRYNSDNDR SSRLLLLERS SPVRDRRGSL EKSQSDKRDR
KNSASAERDR KHRTAAPTEG KNPLKKEDRS DGNAPSASTS SSKQKPPSQK QDGGTAPVAA
SSPKLCLAWQ GMLLLKNSNF PSNMHLLQGD LQVASSLLVE GSTGGKVAQL KITQRLRLDQ
PKLDEVTRRI KVAGPNGYAI LLAVPGSSDS RSSSSSATSD TAASTQRPLR NLVSYLKQKQ
AAGVISLPVG GNKDKENTGV LHAFPPCEFS QQFLDSPAKA LAKSEEDYLV MIIVRAKLVN
SG
