SAFB1_MOUSE
ID SAFB1_MOUSE Reviewed; 937 AA.
AC D3YXK2;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Scaffold attachment factor B1;
DE Short=SAF-B1;
GN Name=Safb; Synonyms=Safb1;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-203.
RC TISSUE=Mammary tumor;
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 405-937.
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 INTERACTION WITH CLK2.
RX PubMed=11118435; DOI=10.1074/jbc.m006851200;
RA Stoss O., Olbrich M., Hartmann A.M., Koenig H., Memmott J., Andreadis A.,
RA Stamm S.;
RT "The STAR/GSG family protein rSLM-2 regulates the selection of alternative
RT splice sites.";
RL J. Biol. Chem. 276:8665-8673(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [7]
RP FUNCTION, INTERACTION WITH RBMX, AND ASSOCIATION WITH CHROMATIN.
RX PubMed=19403048; DOI=10.5483/bmbrep.2009.42.4.232;
RA Omura Y., Nishio Y., Takemoto T., Ikeuchi C., Sekine O., Morino K.,
RA Maeno Y., Obata T., Ugi S., Maegawa H., Kimura H., Kashiwagi A.;
RT "SAFB1, an RBMX-binding protein, is a newly identified regulator of hepatic
RT SREBP-1c gene.";
RL BMB Rep. 42:232-237(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, 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-832; ARG-890; ARG-896; ARG-906
RP AND ARG-912, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, and 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: Binds to scaffold/matrix attachment region (S/MAR) DNA and
CC forms a molecular assembly point to allow the formation of a
CC 'transcriptosomal' complex (consisting of SR proteins and RNA
CC polymerase II) coupling transcription and RNA processing (By
CC similarity). Functions as an estrogen receptor corepressor and can also
CC bind to the HSP27 promoter and decrease its transcription (By
CC similarity). Thereby acts as a negative regulator of cell proliferation
CC (By similarity). When associated with RBMX, binds to and stimulates
CC transcription from the SREBF1 promoter (PubMed:19403048).
CC {ECO:0000250|UniProtKB:Q15424, ECO:0000269|PubMed:19403048}.
CC -!- SUBUNIT: Monomer and homodimer (By similarity). Forms heterodimers with
CC SAFB2 (By similarity). Interacts with KHDRBS3 (By similarity).
CC Interacts with CLK2 (PubMed:11118435). Interacts with POLR2A,
CC ASF/SRSF1, SRp30c/SRFS9 and TRA2B/SFRS10 (By similarity). Interacts
CC with SRPK1 and inhibits its activity (By similarity). Interacts with
CC RBMX (PubMed:19403048). Interacts with FUS (By similarity). Interacts
CC with ZBED4 (By similarity). {ECO:0000250|UniProtKB:O88453,
CC ECO:0000250|UniProtKB:Q15424, ECO:0000269|PubMed:11118435,
CC ECO:0000269|PubMed:19403048}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15424}.
CC -!- PTM: Sumoylated by PIAS1 with SUMO1 and SUMO2/3, desumoylated by SENP1.
CC Sumoylation is required for transcriptional repressor activity.
CC {ECO:0000250|UniProtKB:Q15424}.
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; CT485788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466537; EDL38175.1; -; Genomic_DNA.
DR EMBL; BC018200; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK087504; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS50152.1; -.
DR RefSeq; NP_001156772.1; NM_001163300.1.
DR AlphaFoldDB; D3YXK2; -.
DR SMR; D3YXK2; -.
DR BioGRID; 230338; 11.
DR IntAct; D3YXK2; 9.
DR MINT; D3YXK2; -.
DR STRING; 10090.ENSMUSP00000092849; -.
DR iPTMnet; D3YXK2; -.
DR PhosphoSitePlus; D3YXK2; -.
DR SwissPalm; D3YXK2; -.
DR EPD; D3YXK2; -.
DR jPOST; D3YXK2; -.
DR MaxQB; D3YXK2; -.
DR PaxDb; D3YXK2; -.
DR PeptideAtlas; D3YXK2; -.
DR PRIDE; D3YXK2; -.
DR ProteomicsDB; 260821; -.
DR Antibodypedia; 4536; 308 antibodies from 32 providers.
DR Ensembl; ENSMUST00000095224; ENSMUSP00000092849; ENSMUSG00000071054.
DR GeneID; 224903; -.
DR KEGG; mmu:224903; -.
DR UCSC; uc012avv.1; mouse.
DR CTD; 6294; -.
DR MGI; MGI:2146974; Safb.
DR VEuPathDB; HostDB:ENSMUSG00000071054; -.
DR eggNOG; KOG4661; Eukaryota.
DR GeneTree; ENSGT00940000155916; -.
DR InParanoid; D3YXK2; -.
DR PhylomeDB; D3YXK2; -.
DR TreeFam; TF325240; -.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR BioGRID-ORCS; 224903; 8 hits in 76 CRISPR screens.
DR ChiTaRS; Safb; mouse.
DR PRO; PR:D3YXK2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; D3YXK2; protein.
DR Bgee; ENSMUSG00000071054; Expressed in retinal neural layer and 261 other tissues.
DR ExpressionAtlas; D3YXK2; baseline and differential.
DR Genevisible; D3YXK2; MM.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0042445; P:hormone metabolic process; IMP:MGI.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IMP:MGI.
DR GO; GO:0050684; P:regulation of mRNA processing; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034781; SAFB1.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR PANTHER; PTHR15683:SF6; PTHR15683:SF6; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; DNA-binding; Isopeptide bond; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; RNA-binding;
KW Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CHAIN 2..937
FT /note="Scaffold attachment factor B1"
FT /id="PRO_0000413022"
FT DOMAIN 31..65
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 428..506
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..814
FT /note="Interaction with POLR2A; SFRS1; SFRS9 and SFRS10"
FT /evidence="ECO:0000250|UniProtKB:O88453"
FT REGION 621..937
FT /note="Interaction with SAFB2"
FT /evidence="ECO:0000250"
FT REGION 684..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 652..726
FT /evidence="ECO:0000255"
FT MOTIF 621..638
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 77..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..117
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..287
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..855
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88453"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 188
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88453"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 629
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 832
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 890
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 896
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 906
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 912
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 172
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 231
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 316
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 403
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 414
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 505
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 536
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 565
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 592
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 600
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 600
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 869
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
SQ SEQUENCE 937 AA; 105104 MW; D246A419FA465C3D CRC64;
MAETLSGLGD ASAAGAAAVS SAASETGTRR LSDLRVIDLR AELKKRNLDS SGNKSVLMER
LKKAIEDEGG NPDEIEVTSE CNKKMPKRPS KGRKPEDEGV EDNGLEENSG DGQEDVETSL
ENLQDMDMMD ISVLDEADID NGSVADCVEE EEEATLPEGL ADSTELVEGD LKGLPEQLQE
HAIDDKDTVN NVDTSSSDFT MLQEMEEASL EPENEKILDI LGETCKSEPV KEEGSELEQP
FAQATSSVGP DRKLAEEEDL FESCGHPEEE EEEEEEDQEE EQEEEGDLAL ASSSKSESPS
TRCQWSEADA PLAVVKREPA DAPGGGTGMD REPVGLEEPV EQSSTAAQLP EATSQELVRA
PTAALSPEPQ DSKEDVKKFA FDACNDVPAP PKESSASEGA DQKMSSVEED SDTKRLSREE
KGRSSCGRNF WVSGLSSTTR ATDLKNLFSR YGKVVGAKVV TNARSPGARC YGFVTMSTAE
EATKCISHLH KTELHGKMIS VEKAKSEPTG KRVPDRRDGD SKKEKASTSD RSANLKREEK
GERKDDAKKT DDGSTEKSKD ADDQKPGPSE RSRTTKSGSR GTERTVVMDK SKGVPVISVK
TSGSKERASK SQDRKSASRE KRSVVSFDKV KESRKSRDSE SRRERERSER EQRLQAQWER
EERERLEIAR ERLAFHRHRL ERERMERERL ERERMHVEQE RRREQERIHR EREELRRQQE
LRYEQERRPA VRRPYEVDGR RDDAYWPEAK RAALDDRYHS DFSRQDRFHD FDHRDRGRYP
NHSVDRREGS RSMMGDREGQ HYPERHGGPE RHGRDSRDGW GYGSNKRLSE GRGLPPPPRR
DWGEHGRRLE DDRAWQGTAD GGMMERDHKR WQGGERSMSG HSGPGHMMNR GGMSGRGSFA
PGGASRGHVI PRGGMQAGFG GQSRGSRPSD ARFTRRY
