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SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5 (EC 3.6.4.-) (Sucrose nonfermenting protein 2 homolog) (mSnf2h)

 SMCA5_MOUSE             Reviewed;        1051 AA.
Q91ZW3; Q8C791; Q8CA22; Q8VDG1; Q925M9;
25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
12-SEP-2018, entry version 166.
RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;
EC=3.6.4.-;
AltName: Full=Sucrose nonfermenting protein 2 homolog;
Short=mSnf2h;
Name=Smarca5; Synonyms=Snf2h;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
TISSUE=Erythroleukemia;
PubMed=10914549; DOI=10.1038/sj.leu.2401807;
Stopka T., Zakova D., Fuchs O., Kubrova O., Blafkova J., Jelinek J.,
Necas E., Zivny J.;
"Chromatin remodeling gene SMARCA5 is dysregulated in primitive
hematopoietic cells of acute leukemia.";
Leukemia 14:1247-1252(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11359880; DOI=10.1046/j.1471-4159.2001.00324.x;
Lazzaro M.A., Picketts D.J.;
"Cloning and characterization of the murine Imitation Switch (ISWI)
genes: differential expression patterns suggest distinct developmental
roles for Snf2h and Snf2l.";
J. Neurochem. 77:1145-1156(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 440-1007.
STRAIN=C57BL/6J; TISSUE=Heart, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE NORC COMPLEX,
AND INTERACTION WITH BAZ2A.
PubMed=11532953; DOI=10.1093/emboj/20.17.4892;
Strohner R., Nemeth A., Jansa P., Hofmann-Rohrer U., Santoro R.,
Laengst G., Grummt I.;
"NoRC -- a novel member of mammalian ISWI-containing chromatin
remodeling machines.";
EMBO J. 20:4892-4900(2001).
[6]
FUNCTION, IDENTIFICATION IN THE WICH COMPLEX, AND INTERACTION WITH
BAZ1B.
PubMed=11980720; DOI=10.1093/emboj/21.9.2231;
Bozhenok L., Wade P.A., Varga-Weisz P.;
"WSTF-ISWI chromatin remodeling complex targets heterochromatic
replication foci.";
EMBO J. 21:2231-2241(2002).
[7]
FUNCTION, IDENTIFICATION IN THE NORC COMPLEX, AND INTERACTION WITH
BAZ2A AND HDAC1.
PubMed=12198165; DOI=10.1093/emboj/cdf460;
Zhou Y., Santoro R., Grummt I.;
"The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal
gene promoter and represses RNA polymerase I transcription.";
EMBO J. 21:4632-4640(2002).
[8]
FUNCTION, AND INTERACTION WITH BAZ2A; DNMT1; DNMT3B AND HDAC1.
PubMed=12368916; DOI=10.1038/ng1010;
Santoro R., Li J., Grummt I.;
"The nucleolar remodeling complex NoRC mediates heterochromatin
formation and silencing of ribosomal gene transcription.";
Nat. Genet. 32:393-396(2002).
[9]
FUNCTION.
PubMed=14617767; DOI=10.1073/pnas.2336105100;
Stopka T., Skoultchi A.I.;
"The ISWI ATPase Snf2h is required for early mouse development.";
Proc. Natl. Acad. Sci. U.S.A. 100:14097-14102(2003).
[10]
REVIEW, AND CHARACTERIZATION OF ISWI COMPLEXES.
PubMed=15284901; DOI=10.1139/o04-044;
Dirscherl S.S., Krebs J.E.;
"Functional diversity of ISWI complexes.";
Biochem. Cell Biol. 82:482-489(2004).
[11]
INTERACTION WITH MYO1C.
PubMed=16514417; DOI=10.1038/sj.embor.7400657;
Percipalle P., Fomproix N., Cavellan E., Voit R., Reimer G.,
Krueger T., Thyberg J., Scheer U., Grummt I.,
Oestlund Farrants A.-K.O.;
"The chromatin remodelling complex WSTF-SNF2h interacts with nuclear
myosin 1 and has a role in RNA polymerase I transcription.";
EMBO Rep. 7:525-530(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[14]
FUNCTION, AND INTERACTION WITH BAZ1B.
PubMed=19092802; DOI=10.1038/nature07668;
Xiao A., Li H., Shechter D., Ahn S.H., Fabrizio L.A.,
Erdjument-Bromage H., Ishibe-Murakami S., Wang B., Tempst P.,
Hofmann K., Patel D.J., Elledge S.J., Allis C.D.;
"WSTF regulates the H2A.X DNA damage response via a novel tyrosine
kinase activity.";
Nature 457:57-62(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55; SER-65 AND THR-112,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-439, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Helicase that possesses intrinsic ATP-dependent
nucleosome-remodeling activity. Complexes containing SMARCA5 are
capable of forming ordered nucleosome arrays on chromatin; this
may require intact histone H4 tails. Also required for replication
of pericentric heterochromatin in S-phase specifically in
conjunction with BAZ1A. Probably plays a role in repression of
polI dependent transcription of the rDNA locus, through the
recruitment of the SIN3/HDAC1 corepressor complex to the rDNA
promoter. Essential component of the WICH complex, a chromatin
remodeling complex that mobilizes nucleosomes and reconfigures
irregular chromatin to a regular nucleosomal array structure. The
WICH complex regulates the transcription of various genes, has a
role in RNA polymerase I and RNA polymerase III transcription,
mediates the histone H2AX phosphorylation at 'Tyr-142', and is
involved in the maintenance of chromatin structures during DNA
replication processes. Essential component of the NoRC (nucleolar
remodeling complex) complex, a complex that mediates silencing of
a fraction of rDNA by recruiting histone-modifying enzymes and DNA
methyltransferases, leading to heterochromatin formation and
transcriptional silencing. {ECO:0000269|PubMed:11532953,
ECO:0000269|PubMed:11980720, ECO:0000269|PubMed:12198165,
ECO:0000269|PubMed:12368916, ECO:0000269|PubMed:14617767,
ECO:0000269|PubMed:19092802}.
-!- SUBUNIT: Catalytic subunit of the four known chromatin-remodeling
complexes: CHRAC, RSF, ACF/WCRF, and WICH. Each complex contains
subunits which may regulate the specificity or catalytic activity
of SMARCA5. ACF/WCRF contains BAZ1A; CHRAC contains BAZ1A, CHRAC1,
and POLE3; RSF contains HBXAP; WICH contains BAZ1B/WSTF. SMARCA5
is the catalytic subunit of the NoRC chromatin-remodeling complex,
which also contains BAZ2A/TIP5. The BAZ2A/TIP5 subunit of NoRC
also interacts with DNMT1, DNMT3B and HDAC1, which allows NoRC to
actively suppress rDNA transcription by a combination of
nucleosome remodeling, histone deacetylation, and DNA methylation.
Catalytic subunit of SMARCA5/cohesin/NuRD complexes. Component of
the B-WICH complex, at least composed of SMARCA5/SNF2H,
BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts
with MYO1C. Interacts with BEND3 (By similarity).
{ECO:0000250|UniProtKB:O60264, ECO:0000269|PubMed:11532953,
ECO:0000269|PubMed:11980720, ECO:0000269|PubMed:12198165,
ECO:0000269|PubMed:12368916, ECO:0000269|PubMed:16514417,
ECO:0000269|PubMed:19092802}.
-!- INTERACTION:
Q9Z277:Baz1b; NbExp=2; IntAct=EBI-927547, EBI-927576;
P54843:Maf; NbExp=2; IntAct=EBI-927547, EBI-3842521;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00624, ECO:0000269|PubMed:11532953}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
-!- DEVELOPMENTAL STAGE: Expressed in CD34-positive erythrocyte
progenitor cells. Down-regulated upon differentiation.
{ECO:0000269|PubMed:10914549}.
-!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH21922.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF375046; AAL25793.1; -; mRNA.
EMBL; AF325921; AAK52454.1; -; mRNA.
EMBL; BC021922; AAH21922.1; ALT_INIT; mRNA.
EMBL; BC053069; AAH53069.1; -; mRNA.
EMBL; AK039811; BAC30458.1; -; mRNA.
EMBL; AK052320; BAC34934.2; -; mRNA.
CCDS; CCDS22442.1; -.
RefSeq; NP_444354.2; NM_053124.2.
UniGene; Mm.246803; -.
UniGene; Mm.474173; -.
ProteinModelPortal; Q91ZW3; -.
SMR; Q91ZW3; -.
BioGrid; 220300; 17.
ComplexPortal; CPX-1133; B-WICH chromatin remodelling complex.
ComplexPortal; CPX-424; NoRC complex.
ComplexPortal; CPX-444; ACF complex.
ComplexPortal; CPX-463; RSF complex.
ComplexPortal; CPX-841; WICH chromatin remodelling complex.
ComplexPortal; CPX-858; CHRAC chromatin remodeling complex.
CORUM; Q91ZW3; -.
DIP; DIP-36073N; -.
IntAct; Q91ZW3; 18.
MINT; Q91ZW3; -.
STRING; 10090.ENSMUSP00000044361; -.
iPTMnet; Q91ZW3; -.
PhosphoSitePlus; Q91ZW3; -.
EPD; Q91ZW3; -.
MaxQB; Q91ZW3; -.
PaxDb; Q91ZW3; -.
PeptideAtlas; Q91ZW3; -.
PRIDE; Q91ZW3; -.
Ensembl; ENSMUST00000043359; ENSMUSP00000044361; ENSMUSG00000031715.
GeneID; 93762; -.
KEGG; mmu:93762; -.
UCSC; uc009mja.2; mouse.
CTD; 8467; -.
MGI; MGI:1935129; Smarca5.
eggNOG; KOG0385; Eukaryota.
eggNOG; COG0553; LUCA.
GeneTree; ENSGT00900000140963; -.
HOGENOM; HOG000192862; -.
HOVERGEN; HBG056329; -.
InParanoid; Q91ZW3; -.
KO; K11654; -.
OMA; MAFTEWI; -.
OrthoDB; EOG091G01GJ; -.
PhylomeDB; Q91ZW3; -.
TreeFam; TF300674; -.
Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
PRO; PR:Q91ZW3; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031715; Expressed in 312 organ(s), highest expression level in cumulus cell.
Genevisible; Q91ZW3; MM.
GO; GO:0005677; C:chromatin silencing complex; IDA:UniProtKB.
GO; GO:0000793; C:condensed chromosome; ISO:MGI.
GO; GO:0001650; C:fibrillar center; ISO:MGI.
GO; GO:0031010; C:ISWI-type complex; IPI:MGI.
GO; GO:0043596; C:nuclear replication fork; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0016589; C:NURF complex; ISO:MGI.
GO; GO:0031213; C:RSF complex; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0016887; F:ATPase activity; ISO:MGI.
GO; GO:0003677; F:DNA binding; ISO:MGI.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0042393; F:histone binding; IEA:Ensembl.
GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; ISO:MGI.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:0006333; P:chromatin assembly or disassembly; IDA:MGI.
GO; GO:0006338; P:chromatin remodeling; IDA:MGI.
GO; GO:0000183; P:chromatin silencing at rDNA; IDA:UniProtKB.
GO; GO:0006352; P:DNA-templated transcription, initiation; ISO:MGI.
GO; GO:0006334; P:nucleosome assembly; ISO:MGI.
GO; GO:0016584; P:nucleosome positioning; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:MGI.
CDD; cd00079; HELICc; 1.
CDD; cd00167; SANT; 2.
Gene3D; 1.10.1040.30; -; 1.
Gene3D; 3.40.50.10810; -; 1.
InterPro; IPR020838; DBINO.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR029915; ISWI.
InterPro; IPR015194; ISWI_HAND-dom.
InterPro; IPR036306; ISWI_HAND-dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR017884; SANT_dom.
InterPro; IPR015195; SLIDE.
InterPro; IPR038718; SNF2-like_sf.
InterPro; IPR000330; SNF2_N.
PANTHER; PTHR10799:SF887; PTHR10799:SF887; 1.
Pfam; PF13892; DBINO; 1.
Pfam; PF09110; HAND; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF09111; SLIDE; 1.
Pfam; PF00176; SNF2_N; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00717; SANT; 2.
SUPFAM; SSF101224; SSF101224; 1.
SUPFAM; SSF46689; SSF46689; 2.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51293; SANT; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Chromatin regulator; Complete proteome;
Helicase; Hydrolase; Isopeptide bond; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O60264}.
CHAIN 2 1051 SWI/SNF-related matrix-associated actin-
dependent regulator of chromatin
subfamily A member 5.
/FTId=PRO_0000074355.
DOMAIN 191 356 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 486 637 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 839 891 SANT 1. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
DOMAIN 942 1006 SANT 2. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
NP_BIND 204 211 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 307 310 DEAH box.
COMPBIAS 7 13 Poly-Pro.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:O60264}.
MOD_RES 55 55 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 65 65 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 112 112 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 115 115 Phosphoserine.
{ECO:0000250|UniProtKB:O60264}.
MOD_RES 136 136 Phosphoserine.
{ECO:0000250|UniProtKB:O60264}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000250|UniProtKB:O60264}.
MOD_RES 439 439 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 754 754 Phosphoserine.
{ECO:0000250|UniProtKB:O60264}.
CROSSLNK 82 82 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O60264}.
CROSSLNK 643 643 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O60264}.
CROSSLNK 646 646 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O60264}.
CROSSLNK 693 693 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O60264}.
CROSSLNK 721 721 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O60264}.
CROSSLNK 734 734 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O60264}.
CROSSLNK 965 965 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O60264}.
CONFLICT 44 45 AP -> GS (in Ref. 2; AAK52454).
{ECO:0000305}.
CONFLICT 143 143 R -> C (in Ref. 2; AAK52454).
{ECO:0000305}.
CONFLICT 157 157 S -> R (in Ref. 2; AAK52454).
{ECO:0000305}.
CONFLICT 249 249 K -> R (in Ref. 2; AAK52454).
{ECO:0000305}.
CONFLICT 318 318 K -> N (in Ref. 2; AAK52454).
{ECO:0000305}.
CONFLICT 373 373 C -> S (in Ref. 2; AAK52454).
{ECO:0000305}.
CONFLICT 498 498 G -> S (in Ref. 2; AAK52454).
{ECO:0000305}.
SEQUENCE 1051 AA; 121627 MW; C6CB69E7FADE73FC CRC64;
MSSAVEPPPP PPPESAPSKP SAAGAGGSSS GNKGGPEGGA APAAPCAAGS GPADTEMEEV
FDHGSPGKQK EIQEPDPTYE EKMQTDRANR FEYLLKQTEL FAHFIQPAAQ KTPTSPLKMK
PGRPRVKKDE KQNLLSVGDY RHRRTEQEED EELLTESSKA TNVCTRFEDS PSYVKWGKLR
DYQVRGLNWL ISLYENGING ILADEMGLGK TLQTISLLGY MKHYRNIPGP HMVLVPKSTL
HNWMSEFKKW VPTLRSVCLI GDKEQRAAFV RDVLLPGEWD VCVTSYEMLI KEKSVFKKFN
WRYLVIDEAH RIKNEKSKLS EIVREFKTTN RLLLTGTPLQ NNLHELWSLL NFLLPDVFNS
ADDFDSWFDT NNCLGDQKLV ERLHMVLRPF LLRRIKADVE KSLPPKKEVK IYVGLSKMQR
EWYTRILMKD IDILNSAGKM DKMRLLNILM QLRKCCNHPY LFDGAEPGPP YTTDMHLVTN
SGKMVVLDKL LPKLKEQGSR VLIFSQMTRV LDILEDYCMW RNYEYCRLDG QTPHDERQDS
INAYNEPNST KFVFMLSTRA GGLGINLATA DVVILYDSDW NPQVDLQAMD RAHRIGQTKT
VRVFRFITDN TVEERIVERA EMKLRLDSIV IQQGRLVDQN LNKIGKDEML QMIRHGATHV
FASKESEITD EDIDGILERG AKKTAEMNEK LSKMGESSLR NFTMDTESSV YNFEGEDYRE
KQKIAFTEWI EPPKRERKAN YAVDAYFREA LRVSEPKAPK APRPPKQPNV QDFQFFPPRL
FELLEKEILY YRKTIGYKVP RSPDLPNAAQ AQKEEQLKID EAEPLNDEEL EEKEKLLTQG
FTNWNKRDFN QFIKANEKWG RDDIENIARE VEGKTPEEVI EYSAVFWERC NELQDIEKIM
AQIERGEARI QRRISIKKAL DTKIGRYKAP FHQLRISYGT NKGKNYTEEE DRFLICMLHK
LGFDKENVYD ELRQCIRNSP QFRFDWFLKS RTAMELQRRC NTLITLIERE NMELEEKEKA
EKKKRGPKPS TQKRKMDGAP DGRGRKKKLK L


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