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Poly [ADP-ribose] polymerase 1 (PARP-1) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 1) (ARTD1) (NAD( ) ADP-ribosyltransferase 1) (ADPRT 1) (Poly[ADP-ribose] synthase 1) (msPARP)

 PARP1_MOUSE             Reviewed;        1013 AA.
P11103; Q9JLX4; Q9QVQ3;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 190.
RecName: Full=Poly [ADP-ribose] polymerase 1;
Short=PARP-1;
EC=2.4.2.30;
AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 1;
Short=ARTD1;
AltName: Full=NAD(+) ADP-ribosyltransferase 1;
Short=ADPRT 1;
AltName: Full=Poly[ADP-ribose] synthase 1;
Short=msPARP;
Name=Parp1; Synonyms=Adprp, Adprt, Adprt1;
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] (ISOFORM 1).
STRAIN=BXSB;
PubMed=2498841; DOI=10.1093/nar/17.9.3387;
Huppi K., Bhatia K., Siwarski D., Klinman D., Cherney B., Smulson M.;
"Sequence and organization of the mouse poly (ADP-ribose) polymerase
gene.";
Nucleic Acids Res. 17:3387-3401(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND CHARACTERIZATION.
STRAIN=C57BL/6 X 129/Sv; TISSUE=Fibroblast;
PubMed=10809783; DOI=10.1074/jbc.275.20.15504;
Sallmann F.R., Vodenicharov M.D., Wang Z.-Q., Poirier G.G.;
"Characterization of sPARP-1. An alternative product of PARP-1 gene
with poly(ADP-ribose) polymerase activity independent of DNA strand
breaks.";
J. Biol. Chem. 275:15504-15511(2000).
[3]
PROTEIN SEQUENCE OF 109-119 AND 865-875, SUBUNIT, AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Spleen;
PubMed=9642267; DOI=10.1074/jbc.273.27.17025;
Borggrefe T., Wabl M., Akhmedov A.T., Jessberger R.;
"A B-cell-specific DNA recombination complex.";
J. Biol. Chem. 273:17025-17035(1998).
[4]
DISRUPTION PHENOTYPE.
PubMed=7578427; DOI=10.1016/0300-9084(96)88158-2;
Auer B., Flick K., Wang Z.Q., Haidacher D., Jaeger S., Berghammer H.,
Kofler B., Schweiger M., Wagner E.F.;
"On the biological role of the nuclear polymerizing NAD+: protein(ADP-
ribosyl) transferase (ADPRT): ADPRT from Dictyostelium discoideum and
inactivation of the ADPRT gene in the mouse.";
Biochimie 77:444-449(1995).
[5]
DEVELOPMENTAL STAGE.
PubMed=11948190; DOI=10.1074/jbc.M202390200;
Schreiber V., Ame J.-C., Dolle P., Schultz I., Rinaldi B., Fraulob V.,
Menissier-de Murcia J., de Murcia G.M.;
"Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base
excision DNA repair in association with PARP-1 and XRCC1.";
J. Biol. Chem. 277:23028-23036(2002).
[6]
INTERACTION WITH ZNF423.
PubMed=14623329; DOI=10.1016/j.bbrc.2003.10.053;
Ku M.-C., Stewart S., Hata A.;
"Poly(ADP-ribose) polymerase 1 interacts with OAZ and regulates BMP-
target genes.";
Biochem. Biophys. Res. Commun. 311:702-707(2003).
[7]
S-NITROSYLATION.
PubMed=16464859; DOI=10.1074/jbc.M511049200;
Yu Z., Kuncewicz T., Dubinsky W.P., Kone B.C.;
"Nitric oxide-dependent negative feedback of PARP-1 trans-activation
of the inducible nitric-oxide synthase gene.";
J. Biol. Chem. 281:9101-9109(2006).
[8]
INTERACTION WITH TIAM2.
PubMed=17320046; DOI=10.1016/j.bbrc.2007.02.028;
Takefuji M., Mori K., Morita Y., Arimura N., Nishimura T.,
Nakayama M., Hoshino M., Iwamatsu A., Murohara T., Kaibuchi K.,
Amano M.;
"Rho-kinase modulates the function of STEF, a Rac GEF, through its
phosphorylation.";
Biochem. Biophys. Res. Commun. 355:788-794(2007).
[9]
INTERACTION WITH RNF4.
PubMed=19779455; DOI=10.1038/emboj.2009.279;
Martin N., Schwamborn K., Schreiber V., Werner A., Guillier C.,
Zhang X.D., Bischof O., Seeler J.S., Dejean A.;
"PARP-1 transcriptional activity is regulated by sumoylation upon heat
shock.";
EMBO J. 28:3534-3548(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Liver, Pancreas, 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).
[11]
INTERACTION WITH SNAI1.
PubMed=21577210; DOI=10.1038/onc.2011.153;
Rodriguez M.I., Gonzalez-Flores A., Dantzer F., Collard J.,
de Herreros A.G., Oliver F.J.;
"Poly(ADP-ribose)-dependent regulation of Snail1 protein stability.";
Oncogene 30:4365-4372(2011).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-97, 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: Involved in the base excision repair (BER) pathway, by
catalyzing the poly(ADP-ribosyl)ation of a limited number of
acceptor proteins involved in chromatin architecture and in DNA
metabolism. This modification follows DNA damages and appears as
an obligatory step in a detection/signaling pathway leading to the
reparation of DNA strand breaks. Mediates the poly(ADP-
ribosyl)ation of APLF and CHFR. Positively regulates the
transcription of MTUS1 and negatively regulates the transcription
of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as
a T-helper 1 (Th1) cell-specific transcription factor and binds
the promoter of IFN-gamma to directly regulate its transcription,
and is thus involved importantly in Th1 cytokine production.
Required for PARP9 and DTX3L recruitment to DNA damage sites.
PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the
rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and
BRCA1 to DNA damage sites. Mediates serine ADP-ribosylation of
target proteins following interaction with HPF1; HPF1 conferring
serine specificity. Mediates the poly(ADP-ribosyl)ation of
histones in a HPF1-dependent manner. Involved in the synthesis of
ATP in the nucleus, together with NMNAT1, PARG and NUDT5. Nuclear
ATP generation is required for extensive chromatin remodeling
events that are energy-consuming. {ECO:0000250|UniProtKB:P09874}.
-!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
{ECO:0000250|UniProtKB:P09874, ECO:0000255|PROSITE-
ProRule:PRU00397}.
-!- SUBUNIT: Component of a base excision repair (BER) complex,
containing at least XRCC1, PARP2, POLB and LRIG3. Homo- and
heterodimer with PARP2. Interacts with PARP3, APTX and SRY
Interacts (when poly-ADP-ribosylated) with CHD1L. Interacts with
the DNA polymerase alpha catalytic subunit POLA1; this interaction
functions as part of the control of replication fork progression
(By similarity). The SWAP complex consists of NPM1, NCL, PARP1 and
SWAP70. Interacts with TIAM2 (PubMed:17320046). Interacts with
ZNF423 (PubMed:14623329). Interacts with RNF4 (PubMed:19779455).
Interacts with EEF1A1 and TXK (By similarity). Interacts with
RNF146 (By similarity). Interacts with SNAI1 (via zinc fingers);
the interaction requires SNAI1 to be poly-ADP-ribosylated and non-
phosphorylated (active) by GSK3B (PubMed:21577210). Interacts
(when poly-ADP-ribosylated) with PARP9 (By similarity). Interacts
with NR4A3; activates PARP1 by improving acetylation of PARP1 and
suppressing the interaction between PARP1 and SIRT1 (By
similarity). Interacts (via catalytic domain) with PUM3; the
interaction inhibits the poly(ADP-ribosyl)ation activity of PARP1
and the degradation of PARP1 by CASP3 following genotoxic stress.
Interacts (via the PARP catalytic domain) with HPF1 (By
similarity). Interacts with RRP1B (By similarity).
{ECO:0000250|UniProtKB:P09874, ECO:0000250|UniProtKB:P27008,
ECO:0000269|PubMed:14623329, ECO:0000269|PubMed:17320046,
ECO:0000269|PubMed:19779455, ECO:0000269|PubMed:21577210}.
-!- INTERACTION:
P03087:- (xeno); NbExp=2; IntAct=EBI-642213, EBI-1555770;
Q9WTL8:Arntl; NbExp=7; IntAct=EBI-642213, EBI-644534;
P70677:Casp3; NbExp=3; IntAct=EBI-642213, EBI-1790419;
P97864:Casp7; NbExp=3; IntAct=EBI-642213, EBI-5307197;
P70288:Hdac2; NbExp=3; IntAct=EBI-642213, EBI-302251;
P20263:Pou5f1; NbExp=2; IntAct=EBI-642213, EBI-1606219;
Q3TKT4:Smarca4; NbExp=2; IntAct=EBI-642213, EBI-1210244;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09874}.
Nucleus, nucleolus {ECO:0000250|UniProtKB:P09874}. Note=Localizes
at sites of DNA damage. {ECO:0000250|UniProtKB:P09874}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=1; Synonyms=Long;
IsoId=P11103-1; Sequence=Displayed;
Name=2; Synonyms=Short {ECO:0000303|PubMed:10809783}, sPARP-1
{ECO:0000303|PubMed:10809783};
IsoId=P11103-2; Sequence=VSP_018970;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Expression is correlated
with proliferation, with higher levels occurring during early
fetal development and organogenesis and in the highly
proliferative cell compartments of adult. Expressed in B-cells
that have been induced to switch to various Ig isotypes.
{ECO:0000269|PubMed:9642267}.
-!- DEVELOPMENTAL STAGE: At stage E12.5, expressed at high level in
the developing liver and kidneys. Expressed at higher level in the
genital ridge and the spinal ganglia. At E18.5, preferentially
expressed in the thymus and in regions of the nervous system.
Within the developing trunk, preferential expression persisted in
the liver and became restricted to the cortical region of the
kidney, spleen, adrenal gland, and to stomach and intestinal
epithelia. From E14.5 to E18.5, as well as in the adult, expressed
at the highest level in thymus. Expression is particularly high in
the subcapsular zone of the thymus where immature lymphocytes
proliferate. Expressed at high level in the seminiferous tubules
of the developing testis. {ECO:0000269|PubMed:11948190}.
-!- PTM: Phosphorylated by PRKDC and TXK.
{ECO:0000250|UniProtKB:P09874}.
-!- PTM: Poly-ADP-ribosylated by PARP2; poly-ADP-ribosylation mediates
the recruitment of CHD1L to DNA damage sites. ADP-ribosylated on
serine by autocatalysis; serine ADP-ribosylation takes place
following interaction with HPF1. {ECO:0000250|UniProtKB:P09874}.
-!- PTM: S-nitrosylated, leading to inhibit transcription regulation
activity. {ECO:0000269|PubMed:16464859}.
-!- DISRUPTION PHENOTYPE: Mice show a complete lack of nuclear
poly(ADP-ribosyl)ation. Mice are however viable and fertile.
Moreover, repair of UV and MNNG induced DNA damage are not
affected. However, about 30% of the mutant mice developed
pathological skin aberrations on a mixed 129/Sv x C57B1/6 genetic
background. {ECO:0000269|PubMed:7578427}.
-!- MISCELLANEOUS: The ADP-D-ribosyl group of NAD(+) is transferred to
an acceptor carboxyl group on a histone or the enzyme itself, and
further ADP-ribosyl groups are transferred to the 2'-position of
the terminal adenosine moiety, building up a polymer with an
average chain length of 20-30 units.
-!- SEQUENCE CAUTION:
Sequence=AAF61293.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X14206; CAA32421.1; -; mRNA.
EMBL; AF126717; AAF61293.1; ALT_INIT; mRNA.
PIR; S04200; S04200.
UniGene; Mm.277779; -.
ProteinModelPortal; P11103; -.
SMR; P11103; -.
CORUM; P11103; -.
DIP; DIP-39371N; -.
IntAct; P11103; 18.
MINT; MINT-237428; -.
STRING; 10090.ENSMUSP00000027777; -.
BindingDB; P11103; -.
ChEMBL; CHEMBL3740; -.
iPTMnet; P11103; -.
PhosphoSitePlus; P11103; -.
EPD; P11103; -.
MaxQB; P11103; -.
PaxDb; P11103; -.
PeptideAtlas; P11103; -.
PRIDE; P11103; -.
MGI; MGI:1340806; Parp1.
eggNOG; KOG1037; Eukaryota.
eggNOG; ENOG410XP18; LUCA.
HOVERGEN; HBG053513; -.
InParanoid; P11103; -.
PhylomeDB; P11103; -.
PRO; PR:P11103; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_PARP1; -.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0000784; C:nuclear chromosome, telomeric region; ISO:MGI.
GO; GO:0005635; C:nuclear envelope; ISO:MGI.
GO; GO:0005730; C:nucleolus; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003910; F:DNA ligase (ATP) activity; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:MGI.
GO; GO:1990404; F:protein ADP-ribosylase activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; ISO:MGI.
GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; ISS:UniProtKB.
GO; GO:0006284; P:base-excision repair; IMP:MGI.
GO; GO:0048148; P:behavioral response to cocaine; IMP:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
GO; GO:0071451; P:cellular response to superoxide; IDA:MGI.
GO; GO:0051103; P:DNA ligation involved in DNA repair; IBA:GO_Central.
GO; GO:0006259; P:DNA metabolic process; IMP:MGI.
GO; GO:0006281; P:DNA repair; TAS:MGI.
GO; GO:0006302; P:double-strand break repair; IGI:MGI.
GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
GO; GO:0032042; P:mitochondrial DNA metabolic process; ISO:MGI.
GO; GO:0043504; P:mitochondrial DNA repair; ISO:MGI.
GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
GO; GO:2001170; P:negative regulation of ATP biosynthetic process; ISO:MGI.
GO; GO:1905077; P:negative regulation of interleukin-17 secretion; IMP:MGI.
GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; IMP:BHF-UCL.
GO; GO:0018312; P:peptidyl-serine ADP-ribosylation; ISS:UniProtKB.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0006471; P:protein ADP-ribosylation; ISO:MGI.
GO; GO:0036211; P:protein modification process; ISO:MGI.
GO; GO:0070212; P:protein poly-ADP-ribosylation; IDA:MGI.
GO; GO:0050790; P:regulation of catalytic activity; ISO:MGI.
GO; GO:1903827; P:regulation of cellular protein localization; ISO:MGI.
GO; GO:0040009; P:regulation of growth rate; IMP:MGI.
GO; GO:1903516; P:regulation of single strand break repair; IMP:MGI.
GO; GO:0000723; P:telomere maintenance; IMP:MGI.
CDD; cd00027; BRCT; 1.
Gene3D; 1.20.142.10; -; 1.
Gene3D; 2.20.140.10; -; 1.
Gene3D; 3.30.1740.10; -; 2.
Gene3D; 3.40.50.10190; -; 1.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR036420; BRCT_dom_sf.
InterPro; IPR012982; PADR1.
InterPro; IPR008288; PARP.
InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
InterPro; IPR036930; WGR_dom_sf.
InterPro; IPR008893; WGR_domain.
InterPro; IPR001510; Znf_PARP.
InterPro; IPR036957; Znf_PARP_sf.
Pfam; PF00533; BRCT; 1.
Pfam; PF08063; PADR1; 1.
Pfam; PF00644; PARP; 1.
Pfam; PF02877; PARP_reg; 1.
Pfam; PF05406; WGR; 1.
Pfam; PF00645; zf-PARP; 2.
PIRSF; PIRSF000489; NAD_ADPRT; 1.
SMART; SM00292; BRCT; 1.
SMART; SM01335; PADR1; 1.
SMART; SM00773; WGR; 1.
SMART; SM01336; zf-PARP; 2.
SUPFAM; SSF142921; SSF142921; 1.
SUPFAM; SSF47587; SSF47587; 1.
SUPFAM; SSF52113; SSF52113; 1.
PROSITE; PS50172; BRCT; 1.
PROSITE; PS51060; PARP_ALPHA_HD; 1.
PROSITE; PS51059; PARP_CATALYTIC; 1.
PROSITE; PS00347; PARP_ZN_FINGER_1; 2.
PROSITE; PS50064; PARP_ZN_FINGER_2; 2.
1: Evidence at protein level;
Acetylation; ADP-ribosylation; Alternative initiation;
Complete proteome; Direct protein sequencing; DNA damage; DNA repair;
DNA-binding; Glycosyltransferase; Isopeptide bond; Metal-binding; NAD;
Nucleus; Phosphoprotein; Reference proteome; Repeat; S-nitrosylation;
Transcription; Transcription regulation; Transferase; Ubl conjugation;
Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P09874}.
CHAIN 2 1013 Poly [ADP-ribose] polymerase 1.
/FTId=PRO_0000023259.
DOMAIN 385 476 BRCT. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 661 778 PARP alpha-helical. {ECO:0000255|PROSITE-
ProRule:PRU00398}.
DOMAIN 787 1013 PARP catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00397}.
DNA_BIND 2 372
ZN_FING 9 93 PARP-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00264}.
ZN_FING 113 203 PARP-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00264}.
REGION 373 523 Automodification domain.
MOTIF 207 209 Nuclear localization signal.
MOTIF 221 226 Nuclear localization signal.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 97 97 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 105 105 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 131 131 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 179 179 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 185 185 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 274 274 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 277 277 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 407 407 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 413 413 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 435 435 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 437 437 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 444 444 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 445 445 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 448 448 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 456 456 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 484 484 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 488 488 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 491 491 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 499 499 ADP-ribosylserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 506 506 ADP-ribosylserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 512 512 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 513 513 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 518 518 ADP-ribosylserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 519 519 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 599 599 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 620 620 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 781 781 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 785 785 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 192 192 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 203 203 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 203 203 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 249 249 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 467 467 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 486 486 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 486 486 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 511 511 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 527 527 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 747 747 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 747 747 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P09874}.
VAR_SEQ 1 521 Missing (in isoform 2).
{ECO:0000303|PubMed:10809783}.
/FTId=VSP_018970.
CONFLICT 114 114 A -> L (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 591 591 L -> V (in Ref. 2; AAF61293).
{ECO:0000305}.
CONFLICT 608 608 E -> D (in Ref. 2; AAF61293).
{ECO:0000305}.
CONFLICT 612 612 Q -> H (in Ref. 2; AAF61293).
{ECO:0000305}.
CONFLICT 629 629 N -> D (in Ref. 2; AAF61293).
{ECO:0000305}.
CONFLICT 679 679 D -> E (in Ref. 2; AAF61293).
{ECO:0000305}.
CONFLICT 717 717 Q -> E (in Ref. 2; AAF61293).
{ECO:0000305}.
CONFLICT 758 758 Q -> L (in Ref. 2; AAF61293).
{ECO:0000305}.
CONFLICT 982 982 A -> C (in Ref. 2; AAF61293).
{ECO:0000305}.
SEQUENCE 1013 AA; 113100 MW; 5E54C3E5F60BB922 CRC64;
MAEASERLYR VQYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH WYHFSCFWKV
GQSIRHPDVE VDGFSELRWD DQQKVKKTAE AGGVAGKGQD GSGGKAEKTL GDFAAEYAKS
NRSMCKGCLE KIEKGQMRLS KKMVDPEKPQ LGMIDRWYHP TCFVKKRDEL GFRPEYSASQ
LKGFSLLSAE DKEALKKQLP AIKNEGKRKG DEVDGTDEVA KKKSRKETDK YSKLEKALKA
QNELIWNIKD ELKKACSTND LKELLIFNQQ QVPSGESAIL DRVADGMAFG ALLPCKECSG
QLVFKSDAYY CTGDVTAWTK CMVKTQNPSR KEWVTPKEFR EISYLKKLKV KKQDRIFPPE
SSAPITVHWP LSVTSAPTAV NSSAPADKPL SNMKILTLGK LSQNKDEAKA VIEKLGGKLT
GSANKASLCI SIKKEVEKMN KKMEEVKEAN IRVVSEDFLQ DVSASTKSLQ DLLSAHSLSP
WGAEVKAEPG EVVAPRGKSA APSKKSKGCF KEEGVNKSEK RMKLTLKGGA AVDPDSGLEH
SAHVLEKGGK VFSATLGLVD IVKGTNSYYK LQLLEDDKES RYWIFRSWGR LGTVIGSNKL
EQMPSKEEAV EQFMKLYEEK TGNAWHSKNF TKYPKKFYPL EIDYGQDEEA VKKLTVKPGT
KSKLPKPVQE LVGMIFDVDS MKKALVEYEI DLQKMPLGKL SRRQIQAAYS ILSEVQQPVS
QGSSESQILD LSNRFYTLIP HDFGMKKPPL LNNADSVQAK VEMLDNLLDI EVAYSLLRGG
SDDSSKDPID VNYEKLKTDI KVVDRDSEEA EVIRKYVKNT HATTHNAYDL EVIDIFKIER
EGESQRYKPF RQLHNRRLLW HGSRTTNFAG ILSQGLRIAP PEAPVTGYMF GKGIYFADMV
SKSANYCHTS QGDPIGLIML GEVALGNMYE LKHASHISKL PKGKHSVKGL GKTTPDPSAS
ITLEGVEVPL GTGIPSGVND TALLYNEYIV YDIAQVNLKY LLKLKFNFKT SLW


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