SMRCD_MOUSE
ID SMRCD_MOUSE Reviewed; 1021 AA.
AC Q04692; Q3UGK6; Q3UYR6;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase SMARCAD1;
DE AltName: Full=Enhancer trap locus homolog 1;
DE Short=Etl-1;
GN Name=Smarcad1; Synonyms=Etl1, Kiaa1122;
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 [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=1489724; DOI=10.1016/0925-4773(92)90030-n;
RA Soininen R., Schoor M., Henseling U., Tepe C., Kisters-Woike B.,
RA Rossant J., Gossler A.;
RT "The mouse Enhancer trap locus 1 (Etl-1): a novel mammalian gene related to
RT Drosophila and yeast transcriptional regulator genes.";
RL Mech. Dev. 39:111-123(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N;
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 1-760.
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=8219362; DOI=10.1002/aja.1001970307;
RA Schoor M., Schuster-Gossler K., Gossler A.;
RT "The Etl-1 gene encodes a nuclear protein differentially expressed during
RT early mouse development.";
RL Dev. Dyn. 197:227-237(1993).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=10415348; DOI=10.1016/s0925-4773(99)00090-8;
RA Schoor M., Schuster-Gossler K., Roopenian D., Gossler A.;
RT "Skeletal dysplasias, growth retardation, reduced postnatal survival, and
RT impaired fertility in mice lacking the SNF2/SWI2 family member ETL1.";
RL Mech. Dev. 85:73-83(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Teratocarcinoma;
RX PubMed=17622165; DOI=10.1021/pr070122r;
RA Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT cells.";
RL J. Proteome Res. 6:3174-3186(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144 AND SER-145, 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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=18675275; DOI=10.1016/j.jmb.2008.07.031;
RA Okazaki N., Ikeda S., Ohara R., Shimada K., Yanagawa T., Nagase T.,
RA Ohara O., Koga H.;
RT "The novel protein complex with SMARCAD1/KIAA1122 binds to the vicinity of
RT TSS.";
RL J. Mol. Biol. 382:257-265(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-127; SER-144;
RP SER-145 AND SER-151, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 SUBCELLULAR LOCATION.
RX PubMed=21549307; DOI=10.1016/j.molcel.2011.02.036;
RA Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N.,
RA Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P.,
RA Mermoud J.E.;
RT "Maintenance of silent chromatin through replication requires SWI/SNF-like
RT chromatin remodeler SMARCAD1.";
RL Mol. Cell 42:285-296(2011).
CC -!- FUNCTION: DNA helicase that possesses intrinsic ATP-dependent
CC nucleosome-remodeling activity and is both required for DNA repair and
CC heterochromatin organization. Promotes DNA end resection of double-
CC strand breaks (DSBs) following DNA damage: probably acts by weakening
CC histone DNA interactions in nucleosomes flanking DSBs. Required for the
CC restoration of heterochromatin organization after replication. Acts at
CC replication sites to facilitate the maintenance of heterochromatin by
CC directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation
CC (H3K9me3) and restoration of silencing (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Binds to DNA preferentially in the vicinity of transcriptional
CC start sites. Interacts with MSH2 and TRIM28. Part of a complex composed
CC of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with PCNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18675275,
CC ECO:0000269|PubMed:21549307, ECO:0000269|PubMed:8219362}. Chromosome
CC {ECO:0000250}. Note=Colocalizes with PCNA at replication forks during S
CC phase. Recruited to double-strand breaks (DSBs) sites of DNA damage (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q04692-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q04692-2; Sequence=VSP_007080;
CC -!- DEVELOPMENTAL STAGE: Detected at low levels in fertilized and
CC unfertilized eggs. Levels increased in two-cell embryos, decreased up
CC to morula stage and were highest in blastocysts. Highly expressed in
CC the inner cell mass of 3.5 day old blastocysts. Highly expressed in
CC ectoderm and visceral endoderm at day 5.5. Detected throughout the
CC brain and spinal cord at day 10 to 15. Detected in the basal layer of
CC the epidermis after day 12.5, in particular on snout and distal on
CC fore- and hindlimbs. {ECO:0000269|PubMed:8219362}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice have reduced viability and show
CC growth retardation, skeletal dysplasia and impaired fertility.
CC {ECO:0000269|PubMed:10415348}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65736.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA49560.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X69942; CAA49560.1; ALT_INIT; mRNA.
DR EMBL; AK122454; BAC65736.1; ALT_INIT; mRNA.
DR EMBL; BC042442; AAH42442.1; -; mRNA.
DR EMBL; AK134442; BAE22146.1; -; mRNA.
DR EMBL; AK147884; BAE28202.1; -; mRNA.
DR CCDS; CCDS20204.1; -. [Q04692-1]
DR PIR; A56559; A56559.
DR RefSeq; NP_001240321.1; NM_001253392.1. [Q04692-2]
DR RefSeq; NP_031984.1; NM_007958.1. [Q04692-1]
DR RefSeq; XP_006505572.1; XM_006505509.3.
DR RefSeq; XP_006505573.1; XM_006505510.2. [Q04692-1]
DR RefSeq; XP_006505575.1; XM_006505512.3. [Q04692-2]
DR RefSeq; XP_011239507.1; XM_011241205.2. [Q04692-2]
DR AlphaFoldDB; Q04692; -.
DR SMR; Q04692; -.
DR BioGRID; 199524; 8.
DR STRING; 10090.ENSMUSP00000031984; -.
DR iPTMnet; Q04692; -.
DR PhosphoSitePlus; Q04692; -.
DR EPD; Q04692; -.
DR jPOST; Q04692; -.
DR MaxQB; Q04692; -.
DR PaxDb; Q04692; -.
DR PeptideAtlas; Q04692; -.
DR PRIDE; Q04692; -.
DR ProteomicsDB; 261280; -. [Q04692-1]
DR ProteomicsDB; 261281; -. [Q04692-2]
DR Antibodypedia; 14709; 141 antibodies from 26 providers.
DR DNASU; 13990; -.
DR Ensembl; ENSMUST00000031984; ENSMUSP00000031984; ENSMUSG00000029920. [Q04692-1]
DR GeneID; 13990; -.
DR KEGG; mmu:13990; -.
DR UCSC; uc009ced.1; mouse. [Q04692-1]
DR CTD; 56916; -.
DR MGI; MGI:95453; Smarcad1.
DR VEuPathDB; HostDB:ENSMUSG00000029920; -.
DR eggNOG; KOG0389; Eukaryota.
DR GeneTree; ENSGT00910000144252; -.
DR HOGENOM; CLU_000315_16_3_1; -.
DR InParanoid; Q04692; -.
DR OMA; HNKYEDY; -.
DR OrthoDB; 61251at2759; -.
DR PhylomeDB; Q04692; -.
DR TreeFam; TF105768; -.
DR BioGRID-ORCS; 13990; 7 hits in 115 CRISPR screens.
DR ChiTaRS; Smarcad1; mouse.
DR PRO; PR:Q04692; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q04692; protein.
DR Bgee; ENSMUSG00000029920; Expressed in undifferentiated genital tubercle and 282 other tissues.
DR ExpressionAtlas; Q04692; baseline and differential.
DR Genevisible; Q04692; MM.
DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR GO; GO:0043596; C:nuclear replication fork; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0051304; P:chromosome separation; ISS:UniProtKB.
DR GO; GO:0000729; P:DNA double-strand break processing; ISS:UniProtKB.
DR GO; GO:0070932; P:histone H3 deacetylation; ISS:UniProtKB.
DR GO; GO:0070933; P:histone H4 deacetylation; ISS:UniProtKB.
DR GO; GO:0000018; P:regulation of DNA recombination; ISS:UniProtKB.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51140; CUE; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Chromatin regulator;
KW Chromosome; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..1021
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily A containing DEAD/H box 1"
FT /id="PRO_0000074357"
FT DOMAIN 156..198
FT /note="CUE 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT DOMAIN 247..290
FT /note="CUE 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT DOMAIN 504..672
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 853..1005
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 623..626
FT /note="DEGH box"
FT MOTIF 716..733
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 1000..1003
FT /note="DEAD box"
FT COMPBIAS 44..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 516..524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 892..899
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT CROSSLNK 77
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT CROSSLNK 330
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT CROSSLNK 466
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT CROSSLNK 719
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT CROSSLNK 991
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT VAR_SEQ 1..185
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007080"
FT CONFLICT 857
FT /note="I -> S (in Ref. 1; CAA49560)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1021 AA; 116451 MW; E3237AA2B135538A CRC64;
MNLFNLDRFR FEKRSKIEEA PEAAPQPSQA RPSSPISLSA EEENAEGEGS RANTPDSDVT
EKTEDSSVPE PPDNERKASL SCFQNQRAIQ EYIDLSSDTE DVSPNCSSTV QEKKFSKDTV
IIVSEPSEDE ESHDLPSVTR RNDSSELEDL SELEDLKDAK LQTLKELFPQ RSDSDLLKLI
ESTSTMDGAI AAALLMFGDA GGGPRKRKLS SSSEEDDVND DQSVKQPRGD RGEESNESAE
ASSNWEKQES IVLKLQKEFP NFDKQELREV LKEHEWMYTE ALESLKVFAE DQDVQCASQS
EVTNGKEVAR NQNYSKNATK IKMKQKISVK PQNGFNKKRK KNVFNPKKAV EDSEYDSGSD
AGSSLDEDYS SCEEVMEDGY KGKILHFLQV SSIAELTLIP KCSQKKAQKI TELRPFNNWE
ALFTKMSKIN GLSEDLIWNC KTVIQERDVV IRLMNKCEDI SNKLTKQVTM LTGNGGGWNR
EQPSLLNQSL SLKPYQKVGL NWLALVHKHG LNGILADEMG LGKTIQAIAF LAYLFQEGNK
GPHLIVVPAS TIDNWLREVN LWCPSLNVLC YYGSQEERKQ IRFNIHNKYE DYNVIVTTYN
CAISSSDDRS LFRRLKLNYA IFDEGHMLKN MGSIRYQHLM TINARNRLLL TGTPVQNNLL
ELMSLLNFVM PHMFSSSTSE IRRMFSSKTK PADEQSIYEK ERIAHAKQII KPFILRRVKE
EVLKLLPPKK DRIELCAMSE KQEQLYSGLF NRLKKSINNL EKNTEMCNVM MQLRKMANHP
LLHRQYYTPE KLKEMSQLML KEPTHCEANP DLIFEDMEVM TDFELHVLCK QYQHINSYQL
DMDLILDSGK FRALGCILSE LKQKGDRVVL FSQFTMMLDI LEVLLKHHQH RYLRLDGKTQ
ISERIHLIDE FNTDMDIFVF LLSTKAGGLG INLTSANVVI LHDIDCNPYN DKQAEDRCHR
VGQTKEVLVI KLISQGTIEE SMLKINQQKL KLEQDMTTVD EADEGSMPAD IATLLKTSMG
L
