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   27-MAR-2024, entry version 188.
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,
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   [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.
DR   AlphaFoldDB; Q04692; -.
DR   SMR; Q04692; -.
DR   BioGRID; 199524; 8.
DR   STRING; 10090.ENSMUSP00000031984; -.
DR   ChEMBL; CHEMBL4879452; -.
DR   iPTMnet; Q04692; -.
DR   PhosphoSitePlus; Q04692; -.
DR   EPD; Q04692; -.
DR   jPOST; Q04692; -.
DR   MaxQB; Q04692; -.
DR   PaxDb; 10090-ENSMUSP00000031984; -.
DR   PeptideAtlas; Q04692; -.
DR   ProteomicsDB; 261280; -. [Q04692-1]
DR   ProteomicsDB; 261281; -. [Q04692-2]
DR   Pumba; Q04692; -.
DR   Antibodypedia; 14709; 159 antibodies from 26 providers.
DR   DNASU; 13990; -.
DR   Ensembl; ENSMUST00000031984.9; ENSMUSP00000031984.7; ENSMUSG00000029920.10. [Q04692-1]
DR   GeneID; 13990; -.
DR   KEGG; mmu:13990; -.
DR   UCSC; uc009ced.1; mouse. [Q04692-1]
DR   AGR; MGI:95453; -.
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; MEMRRMA; -.
DR   OrthoDB; 5482994at2759; -.
DR   PhylomeDB; Q04692; -.
DR   TreeFam; TF105768; -.
DR   BioGRID-ORCS; 13990; 7 hits in 121 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 285 other cell types or tissues.
DR   ExpressionAtlas; Q04692; baseline and differential.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
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:0000018; P:regulation of DNA recombination; ISS:UniProtKB.
DR   CDD; cd17998; DEXHc_SMARCAD1; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 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; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   PANTHER; PTHR10799:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51140; CUE; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   Genevisible; Q04692; MM.
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
//