ZN609_MOUSE
ID ZN609_MOUSE Reviewed; 1413 AA.
AC Q8BZ47; Q05DD7; Q6PD47; Q6ZQE3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Zinc finger protein 609;
GN Name=Znf609; Synonyms=Kiaa0295, Zfp609;
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 MRNA] OF 1-1136.
RC TISSUE=Brain, and Eye;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-1413.
RC STRAIN=C57BL/6J; TISSUE=Bone;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 610-1413.
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575 AND SER-577, AND
RP IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-361; SER-467;
RP SER-533; SER-575; SER-577; SER-845; SER-848 AND SER-1057, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY ZNF608.
RX PubMed=23076336; DOI=10.1038/gene.2012.47;
RA Reed N.P., Henderson M.A., Oltz E.M., Aune T.M.;
RT "Reciprocal regulation of Rag expression in thymocytes by the zinc-finger
RT proteins, Zfp608 and Zfp609.";
RL Genes Immun. 14:7-12(2013).
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=25921068; DOI=10.1016/j.molcel.2015.03.027;
RA Rybak-Wolf A., Stottmeister C., Glazar P., Jens M., Pino N., Giusti S.,
RA Hanan M., Behm M., Bartok O., Ashwal-Fluss R., Herzog M., Schreyer L.,
RA Papavasileiou P., Ivanov A., Oehman M., Refojo D., Kadener S., Rajewsky N.;
RT "Circular RNAs in the mammalian brain are highly abundant, conserved, and
RT dynamically expressed.";
RL Mol. Cell 58:870-885(2015).
RN [9]
RP FUNCTION (ISOFORM 2), TISSUE SPECIFICITY, AND IDENTIFICATION (ISOFORM 2).
RX PubMed=28344082; DOI=10.1016/j.molcel.2017.02.017;
RA Legnini I., Di Timoteo G., Rossi F., Morlando M., Briganti F.,
RA Sthandier O., Fatica A., Santini T., Andronache A., Wade M., Laneve P.,
RA Rajewsky N., Bozzoni I.;
RT "Circ-ZNF609 is a circular RNA that can be translated and functions in
RT myogenesis.";
RL Mol. Cell 0:0-0(2017).
RN [10]
RP FUNCTION, INTERACTION WITH THE INTEGRATOR COMPLEX AND NIPBL, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=28041881; DOI=10.1016/j.neuron.2016.11.047;
RA van den Berg D.L., Azzarelli R., Oishi K., Martynoga B., Urban N.,
RA Dekkers D.H., Demmers J.A., Guillemot F.;
RT "Nipbl interacts with Zfp609 and the Integrator complex to regulate
RT cortical neuron migration.";
RL Neuron 93:348-361(2017).
CC -!- FUNCTION: Transcription factor, which activates RAG1, and possibly
CC RAG2, transcription. Through the regulation of RAG1/2 expression, may
CC regulate thymocyte maturation (PubMed:28344082). Along with NIPBL and
CC the multiprotein complex Integrator, promotes cortical neuron migration
CC during brain development by regulating the transcription of crucial
CC genes in this process. Preferentially binds promoters containing paused
CC RNA polymerase II. Up-regulates the expression of SEMA3A, NRP1, PLXND1
CC and GABBR2 genes, among others (PubMed:28041881).
CC {ECO:0000269|PubMed:28041881, ECO:0000269|PubMed:28344082}.
CC -!- FUNCTION: [Isoform 2]: Involved in regulation of myoblast proliferation
CC during myogenesis. {ECO:0000269|PubMed:28344082}.
CC -!- SUBUNIT: Interacts (via N-terminus) with NIPBL (PubMed:28041881).
CC Interacts with the multiprotein complex Integrator (PubMed:28041881).
CC {ECO:0000269|PubMed:28041881}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28041881}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BZ47-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BZ47-2; Sequence=VSP_059084, VSP_059085;
CC -!- TISSUE SPECIFICITY: Expressed in myoblasts (PubMed:28344082). Expressed
CC in neurons in various brain regions, including striatum, prefrontal
CC cortex, olfactory bulb, midbrain, cerebellum and hippocampus
CC (PubMed:25921068). Expressed in neural stem cells (at protein level)
CC (PubMed:28041881). Expressed in thymocytes (PubMed:23076336).
CC {ECO:0000269|PubMed:23076336, ECO:0000269|PubMed:25921068,
CC ECO:0000269|PubMed:28041881, ECO:0000269|PubMed:28344082}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing brain at 12.5 dpc. At
CC 14.5 dpc, becomes enriched in the ventricular zone and later,
CC restricted to the progenitor population as cortical neurogenesis peaks.
CC At this stage, not detected in the subventricular zone/intermediate
CC zone (SVZ/IZ). At later stages, detected in the neurons of the cortical
CC plate and in stem cells near the ventricular surface.
CC {ECO:0000269|PubMed:28041881}.
CC -!- INDUCTION: Down-regulated by ZNF608 (PubMed:23076336). Isoform 2 is up-
CC regulated during neuronal differentiation (PubMed:25921068).
CC {ECO:0000269|PubMed:23076336, ECO:0000269|PubMed:25921068}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by a back-splicing reaction which
CC joins the 5'-splice site of the first coding exon with the 3'-splice
CC site of the upstream intron resulting in a circular RNA, called circ-
CC ZNF609. The translation starts with the same initiator methionine as
CC that of the linear transcript encoding isoform 1. The stop codon is
CC created upon circularization. {ECO:0000269|PubMed:28344082}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29549.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC151906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016271; AAH16271.1; -; mRNA.
DR EMBL; BC058943; AAH58943.1; ALT_SEQ; mRNA.
DR EMBL; AK036715; BAC29549.1; ALT_INIT; mRNA.
DR EMBL; AK129111; BAC97921.1; -; mRNA.
DR CCDS; CCDS23297.2; -. [Q8BZ47-1]
DR RefSeq; NP_766124.2; NM_172536.3. [Q8BZ47-1]
DR AlphaFoldDB; Q8BZ47; -.
DR BioGRID; 229567; 7.
DR IntAct; Q8BZ47; 2.
DR MINT; Q8BZ47; -.
DR STRING; 10090.ENSMUSP00000124089; -.
DR iPTMnet; Q8BZ47; -.
DR PhosphoSitePlus; Q8BZ47; -.
DR EPD; Q8BZ47; -.
DR jPOST; Q8BZ47; -.
DR MaxQB; Q8BZ47; -.
DR PaxDb; Q8BZ47; -.
DR PRIDE; Q8BZ47; -.
DR ProteomicsDB; 275089; -. [Q8BZ47-1]
DR ProteomicsDB; 275090; -. [Q8BZ47-2]
DR Antibodypedia; 25830; 36 antibodies from 13 providers.
DR Ensembl; ENSMUST00000159109; ENSMUSP00000124089; ENSMUSG00000040524. [Q8BZ47-1]
DR GeneID; 214812; -.
DR KEGG; mmu:214812; -.
DR UCSC; uc009qdw.2; mouse. [Q8BZ47-1]
DR CTD; 214812; -.
DR MGI; MGI:2674092; Zfp609.
DR VEuPathDB; HostDB:ENSMUSG00000040524; -.
DR eggNOG; ENOG502RCUP; Eukaryota.
DR GeneTree; ENSGT00390000008748; -.
DR HOGENOM; CLU_004142_0_0_1; -.
DR InParanoid; Q8BZ47; -.
DR OMA; VDRNCPS; -.
DR OrthoDB; 60503at2759; -.
DR PhylomeDB; Q8BZ47; -.
DR TreeFam; TF329775; -.
DR BioGRID-ORCS; 214812; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Zfp609; mouse.
DR PRO; PR:Q8BZ47; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BZ47; protein.
DR Bgee; ENSMUSG00000040524; Expressed in trigeminal ganglion and 69 other tissues.
DR ExpressionAtlas; Q8BZ47; baseline and differential.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:ARUK-UCL.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:2001224; P:positive regulation of neuron migration; IMP:UniProtKB.
DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; TAS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:2000291; P:regulation of myoblast proliferation; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR InterPro; IPR040010; ZN608/ZN609.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR21564; PTHR21564; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Developmental protein; Isopeptide bond;
KW Metal-binding; Myogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1413
FT /note="Zinc finger protein 609"
FT /id="PRO_0000280423"
FT ZN_FING 495..520
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..948
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1042
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT MOD_RES 381
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT MOD_RES 745
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT MOD_RES 803
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT MOD_RES 822
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT MOD_RES 841
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 848
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1057
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 479
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT CROSSLNK 788
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT CROSSLNK 1063
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT CROSSLNK 1155
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT CROSSLNK 1299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15014"
FT VAR_SEQ 250
FT /note="M -> Q (in isoform 2)"
FT /id="VSP_059084"
FT VAR_SEQ 251..1413
FT /note="Missing (in isoform 2)"
FT /id="VSP_059085"
FT CONFLICT 697
FT /note="S -> G (in Ref. 3; BAC29549)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="D -> K (in Ref. 2; AAH16271)"
FT /evidence="ECO:0000305"
FT CONFLICT 914
FT /note="S -> N (in Ref. 4; BAC97921)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1413 AA; 151117 MW; 6BC74B23591605FF CRC64;
MSLSSGACGG KGVDANPVET YDSGDEWDIG VGNLIIDLDA DLEKDQQKLE MSGSKEVGIP
APNAVATLPD NIKFVTPVPG PQGKEGKSKS KRSKSGKDAS KPTPGTSLFS PSEGAASKKE
VQGRAGDGAS AGGLVAAVAP KGSEKAAKAS RSVAGSKKEK ENSSSKGKKE RSEGVGTCSE
KDPGVLQPVP LGGRGSQYDG SAGMDTGTVE PLGSIAIEPG AALNPLGTKP EPEEGENECR
PLKKVKSEKM ESPVSTPAVL PLHLLVPVVN NDISSPCEQI MVRTRSVGVN TCDVALATEP
ECLGPCEPGT SVNLEGIVWQ ETEDGMLVVN VTWRNKTYVG TLLDCTRHDW APPRFCDSPT
SDLEMRNGRG RGKRMRPSSN TPVSEAAAAS DSKGTSSSSK TRAGANSKGR RGSQNSSEHR
PPASSTSEDV KASPSSANKR KSKPLSDMEL NSSSEDSKGS KRVRTNSMGS ATGPLPGTKV
EPTLVDRNCP SPVLIDCPHP NCNKKYKHIN GLKYHQAHAH TDDDSKPEAD GDSEYGEEPA
LHADLSCNGA PVPQKGSLSP ARSATPKVRL VEPHSPSPSS KFSTKGLCKK KLSGEGDTDP
GALSNDGSDD GPSVMDETSN DAFDSLERKC MEKEKCKKPS SLKSEKIPSK SLKSARPIAP
AIPPQQIYTF QTATFTAASP GSSSGLTTTV VQAMPNSPQL KPIQPKPTVM GEPFTVNPAL
TPAKDKKKKD KKKKDSSKEL ESPLTPGKVC RAEEGKSPFR DAAGDGIKVE SLLNGSSESH
QSRLASIKAE ADKIYSFTDN APSPSIGGSS RLDSTTPTQP LTPLHVVTQN GAEASSVKTN
SPAYSDISDA GEDGEGKVDS AKSKDPEQLV KEGAKKTLFP PQPQSKDSPY YQGFESYYSP
GYAQSSPGTL TSSSQAGMEG QPLKTKKDEE PESVEGKVKN DVCEEKKPEL SNSSQQPSVI
QQRPNMYMQS LYYNQYAYVP PYGYSDQSYH SHLLSTNTAY RQQYEEQQKR QSLEQQQQQQ
RGLDKKTEMG LKEREASLKE EWKQKPSIPP TLTKAPSLTD LVKSGPGKAK EPGTDPAKSV
IIPKLDDSSK LPSQPPEGLK GKLGEASHLG KEASEAKTGT ECGRQAEVDP ILWYRQETES
RMWTYVYPAK YSDIKSEDDR WKEERDRKLK EDRSRSKDSV PKEDGKESTS SDCKLPPSEE
SRLGSKEPRP SVHVPVSSPL TQHQSYIPYM HGYSYSQSYD PNHPSYRGMP AVMMQNYPGS
YLPSSYSFSP YGSKVSGGED ADKARASPSV SCKASSESKA LDILQQHASH YKSKSPTISD
KNSQERDRGG CGVVGGGGSC GSVAGAGGTD RSADRPRTSP SQRLMSTHHH HHHLGYSLLP
AQYNLPYAAG LSSTAIVASQ QGSTPSLYPP PRR
