ID   XPC_MOUSE               Reviewed;         930 AA.
AC   P51612; P54732; Q3TKI2; Q920M1; Q9DBW7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   24-JAN-2024, entry version 173.
DE   RecName: Full=DNA repair protein complementing XP-C cells homolog;
DE   AltName: Full=Xeroderma pigmentosum group C-complementing protein homolog;
DE   AltName: Full=p125;
GN   Name=Xpc;
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] OF 3-930.
RX   PubMed=8604333; DOI=10.1093/nar/24.6.1026;
RA   Li L., Peterson C., Legerski R.;
RT   "Sequence of the mouse XPC cDNA and genomic structure of the human XPC
RT   gene.";
RL   Nucleic Acids Res. 24:1026-1028(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yokoi M., Hanaoka F.;
RT   "Molecular cloning of mouse XPC.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Skin;
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 [MRNA] OF 59-617.
RC   STRAIN=129/Sv;
RX   PubMed=7675084; DOI=10.1038/377162a0;
RA   Sands A.T., Abuin A., Sanchez A., Conti C.J., Bradley A.;
RT   "High susceptibility to ultraviolet-induced carcinogenesis in mice lacking
RT   XPC.";
RL   Nature 377:162-165(1995).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-875 AND SER-876, 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-875 AND SER-876, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-875 AND SER-876, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
CC   -!- FUNCTION: Involved in global genome nucleotide excision repair (GG-NER)
CC       by acting as damage sensing and DNA-binding factor component of the XPC
CC       complex. Has only a low DNA repair activity by itself which is
CC       stimulated by RAD23B and RAD23A. Has a preference to bind DNA
CC       containing a short single-stranded segment but not to damaged
CC       oligonucleotides. This feature is proposed to be related to a dynamic
CC       sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-
CC       bonded bases by forming a transient nucleoprotein intermediate complex
CC       which matures into a stable recognition complex through an intrinsic
CC       single-stranded DNA-binding activity. The XPC complex is proposed to
CC       represent the first factor bound at the sites of DNA damage and
CC       together with other core recognition factors, XPA, RPA and the TFIIH
CC       complex, is part of the pre-incision (or initial recognition) complex.
CC       The XPC complex recognizes a wide spectrum of damaged DNA characterized
CC       by distortions of the DNA helix such as single-stranded loops,
CC       mismatched bubbles or single-stranded overhangs. The orientation of XPC
CC       complex binding appears to be crucial for inducing a productive NER.
CC       XPC complex is proposed to recognize and to interact with unpaired
CC       bases on the undamaged DNA strand which is followed by recruitment of
CC       the TFIIH complex and subsequent scanning for lesions in the opposite
CC       strand in a 5'-to-3' direction by the NER machinery. Cyclobutane
CC       pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage
CC       esacpe detection by the XPC complex due to a low degree of structural
CC       perurbation. Instead they are detected by the UV-DDB complex which in
CC       turn recruits and cooperates with the XPC complex in the respective DNA
CC       repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER;
CC       it preferentially binds to cisplatin and UV-damaged double-stranded DNA
CC       and also binds to a variety of chemically and structurally diverse DNA
CC       adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion
CC       with a preference for the 5' side. XPC:RAD23B induces a bend in DNA
CC       upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases
CC       TDG and SMUG1. {ECO:0000250|UniProtKB:Q01831}.
CC   -!- FUNCTION: In absence of DNA repair, the XPC complex also acts as a
CC       transcription coactivator: XPC interacts with the DNA-binding
CC       transcription factor E2F1 at a subset of promoters to recruit KAT2A and
CC       histone acetyltransferase complexes (HAT). KAT2A recruitment
CC       specifically promotes acetylation of histone variant H2A.Z.1/H2A.Z, but
CC       not H2A.Z.2/H2A.V, thereby promoting expression of target genes.
CC       {ECO:0000250|UniProtKB:Q01831}.
CC   -!- SUBUNIT: Component of the XPC complex composed of XPC, RAD23B and
CC       CETN2. Interacts with RAD23A; the interaction is suggesting the
CC       existence of a functional equivalent variant XPC complex. Interacts
CC       with TDG; the interaction is demonstrated using the XPC:RAD23B dimer.
CC       Interacts with SMUG1; the interaction is demonstrated using the
CC       XPC:RAD23B dimer. Interacts with DDB2. Interacts with CCNH, GTF2H1 and
CC       ERCC3. Interacts with E2F1 and KAT2A; leading to KAT2A recruitment to
CC       promoters and subsequent acetylation of histones.
CC       {ECO:0000250|UniProtKB:Q01831}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q01831}.
CC       Chromosome {ECO:0000250|UniProtKB:Q01831}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q01831}. Note=Omnipresent in the nucleus and
CC       consistently associates with and dissociates from DNA in the absence of
CC       DNA damage. Continuously shuttles between the cytoplasm and the
CC       nucleus, which is impeded by the presence of NER lesions.
CC       {ECO:0000250|UniProtKB:Q01831}.
CC   -!- PTM: Ubiquitinated upon UV irradiation; the ubiquitination requires the
CC       UV-DDB complex, appears to be reversible and does not serve as a signal
CC       for degradation. Ubiquitinated by RNF11 via 'Lys-63'-linked
CC       ubiquitination. Ubiquitination by RNF111 is polysumoylation-dependent
CC       and promotes nucleotide excision repair.
CC       {ECO:0000250|UniProtKB:Q01831}.
CC   -!- PTM: Sumoylated; sumoylation promotes ubiquitination by RNF111.
CC       {ECO:0000250|UniProtKB:Q01831}.
CC   -!- SIMILARITY: Belongs to the XPC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC52500.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U27398; AAC52500.1; ALT_FRAME; mRNA.
DR   EMBL; AB071144; BAB64540.1; -; mRNA.
DR   EMBL; AK004713; BAB23497.1; -; mRNA.
DR   EMBL; AK028595; BAC26023.1; -; mRNA.
DR   EMBL; AK166981; BAE39163.1; -; mRNA.
DR   EMBL; U40005; AAA82720.1; -; mRNA.
DR   CCDS; CCDS39569.1; -.
DR   PIR; S70630; S70630.
DR   RefSeq; NP_033557.2; NM_009531.2.
DR   AlphaFoldDB; P51612; -.
DR   SMR; P51612; -.
DR   BioGRID; 204605; 3.
DR   IntAct; P51612; 2.
DR   STRING; 10090.ENSMUSP00000032182; -.
DR   iPTMnet; P51612; -.
DR   PhosphoSitePlus; P51612; -.
DR   EPD; P51612; -.
DR   jPOST; P51612; -.
DR   MaxQB; P51612; -.
DR   PaxDb; 10090-ENSMUSP00000032182; -.
DR   PeptideAtlas; P51612; -.
DR   ProteomicsDB; 297654; -.
DR   Pumba; P51612; -.
DR   Antibodypedia; 4092; 369 antibodies from 31 providers.
DR   Ensembl; ENSMUST00000032182.5; ENSMUSP00000032182.4; ENSMUSG00000030094.9.
DR   GeneID; 22591; -.
DR   KEGG; mmu:22591; -.
DR   UCSC; uc009cyd.2; mouse.
DR   AGR; MGI:103557; -.
DR   CTD; 7508; -.
DR   MGI; MGI:103557; Xpc.
DR   VEuPathDB; HostDB:ENSMUSG00000030094; -.
DR   eggNOG; KOG2179; Eukaryota.
DR   GeneTree; ENSGT00390000005194; -.
DR   HOGENOM; CLU_009925_1_1_1; -.
DR   InParanoid; P51612; -.
DR   OMA; FQAKHLG; -.
DR   OrthoDB; 181129at2759; -.
DR   PhylomeDB; P51612; -.
DR   TreeFam; TF101242; -.
DR   Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR   Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR   BioGRID-ORCS; 22591; 1 hit in 117 CRISPR screens.
DR   ChiTaRS; Xpc; mouse.
DR   PRO; PR:P51612; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P51612; Protein.
DR   Bgee; ENSMUSG00000030094; Expressed in granulocyte and 241 other cell types or tissues.
DR   ExpressionAtlas; P51612; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0000109; C:nucleotide-excision repair complex; ISS:UniProtKB.
DR   GO; GO:0000111; C:nucleotide-excision repair factor 2 complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0090734; C:site of DNA damage; IDA:MGI.
DR   GO; GO:0071942; C:XPC complex; ISS:UniProtKB.
DR   GO; GO:0003684; F:damaged DNA binding; IDA:MGI.
DR   GO; GO:0140612; F:DNA damage sensor activity; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:MGI.
DR   GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0006974; P:DNA damage response; IMP:MGI.
DR   GO; GO:0006281; P:DNA repair; IMP:MGI.
DR   GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR   GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IGI:MGI.
DR   GO; GO:0045721; P:negative regulation of gluconeogenesis; ISS:UniProtKB.
DR   GO; GO:0006289; P:nucleotide-excision repair; IDA:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0000720; P:pyrimidine dimer repair by nucleotide-excision repair; IMP:MGI.
DR   GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; ISO:MGI.
DR   GO; GO:0010996; P:response to auditory stimulus; IEA:Ensembl.
DR   GO; GO:0010224; P:response to UV-B; IMP:MGI.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0070914; P:UV-damage excision repair; IDA:MGI.
DR   Gene3D; 2.20.20.110; Rad4, beta-hairpin domain BHD1; 1.
DR   Gene3D; 3.30.70.2460; Rad4, beta-hairpin domain BHD3; 1.
DR   Gene3D; 3.90.260.10; Transglutaminase-like; 2.
DR   InterPro; IPR018327; BHD_2.
DR   InterPro; IPR004583; DNA_repair_Rad4.
DR   InterPro; IPR018026; DNA_repair_Rad4-like.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR018325; Rad4/PNGase_transGLS-fold.
DR   InterPro; IPR018326; Rad4_beta-hairpin_dom1.
DR   InterPro; IPR018328; Rad4_beta-hairpin_dom3.
DR   InterPro; IPR042488; Rad4_BHD3_sf.
DR   InterPro; IPR036985; Transglutaminase-like_sf.
DR   NCBIfam; TIGR00605; rad4; 1.
DR   PANTHER; PTHR12135:SF0; DNA REPAIR PROTEIN COMPLEMENTING XP-C CELLS; 1.
DR   PANTHER; PTHR12135; DNA REPAIR PROTEIN XP-C / RAD4; 1.
DR   Pfam; PF10403; BHD_1; 1.
DR   Pfam; PF10404; BHD_2; 1.
DR   Pfam; PF10405; BHD_3; 1.
DR   Pfam; PF03835; Rad4; 1.
DR   SMART; SM01030; BHD_1; 1.
DR   SMART; SM01031; BHD_2; 1.
DR   SMART; SM01032; BHD_3; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   Genevisible; P51612; MM.
PE   1: Evidence at protein level;
KW   Chromosome; Cytoplasm; DNA damage; DNA repair; DNA-binding;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..930
FT                   /note="DNA repair protein complementing XP-C cells homolog"
FT                   /id="PRO_0000218294"
FT   REGION          1..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          489..727
FT                   /note="Interaction with RAD23B"
FT                   /evidence="ECO:0000250"
FT   REGION          600..759
FT                   /note="Minimal sensor domain involved in damage
FT                   recognition"
FT                   /evidence="ECO:0000250"
FT   REGION          600..734
FT                   /note="DNA-binding; preference for heteroduplex DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          760..824
FT                   /note="DNA-binding; preference for single stranded DNA;
FT                   required for formation of stable nucleoprotein complex"
FT                   /evidence="ECO:0000250"
FT   REGION          809..930
FT                   /note="Interaction with ERCC2 and GTF2H1"
FT                   /evidence="ECO:0000250"
FT   REGION          840..859
FT                   /note="Interaction with CETN2"
FT                   /evidence="ECO:0000250"
FT   REGION          867..930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           388..393
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..408
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..461
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        901..930
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         126
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01831"
FT   MOD_RES         165
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01831"
FT   MOD_RES         395
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01831"
FT   MOD_RES         397
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01831"
FT   MOD_RES         875
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         876
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         883
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01831"
FT   MOD_RES         895
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01831"
FT   CROSSLNK        40
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q01831"
FT   CROSSLNK        80
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q01831"
FT   CROSSLNK        88
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q01831"
FT   CROSSLNK        157
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q01831"
FT   CONFLICT        13
FT                   /note="K -> N (in Ref. 2; BAB64540)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        84
FT                   /note="L -> S (in Ref. 1; AAC52500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="F -> L (in Ref. 1; AAC52500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        101
FT                   /note="S -> L (in Ref. 1; AAC52500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148..149
FT                   /note="AT -> CP (in Ref. 2; BAB64540)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165..166
FT                   /note="TP -> RG (in Ref. 1; AAC52500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196..201
FT                   /note="EVQENM -> GVHEDT (in Ref. 4; AAA82720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="S -> N (in Ref. 4; AAA82720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="S -> N (in Ref. 4; AAA82720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        221..223
FT                   /note="RQP -> SQL (in Ref. 4; AAA82720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        373..375
FT                   /note="GKA -> AKP (in Ref. 4; AAA82720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        373
FT                   /note="G -> GS (in Ref. 1; AAC52500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        397
FT                   /note="S -> R (in Ref. 1; AAC52500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        454
FT                   /note="E -> K (in Ref. 2; BAB64540)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        458
FT                   /note="R -> C (in Ref. 4; AAA82720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        497
FT                   /note="S -> C (in Ref. 1; AAC52500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        614
FT                   /note="E -> K (in Ref. 1; AAC52500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        621..622
FT                   /note="KH -> ND (in Ref. 1; AAC52500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        683
FT                   /note="W -> R (in Ref. 1; AAC52500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        712..715
FT                   /note="LSEP -> HLGA (in Ref. 1; AAC52500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        751
FT                   /note="N -> K (in Ref. 1; AAC52500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        777
FT                   /note="R -> H (in Ref. 1; AAC52500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        797
FT                   /note="C -> S (in Ref. 1; AAC52500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        921
FT                   /note="A -> P (in Ref. 1; AAC52500)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   930 AA;  104522 MW;  0C469AB21B4E4EE9 CRC64;
     MAPKRTADGR RRKRGQKTED NKVARHEESV ADDFEDEKQK PRRKSSFPKV SQGKRKRGCS
     DPGDPTNGAA KKKVAKATAK SKNLKVLKEE ALSDGDDFRD SPADCKKAKK HPKSKVVDQG
     TDEDDSEDDW EEVEELTEPV LDMGENSATS PSDMPVKAVE IEIETPQQAK ERERSEKIKM
     EFETYLRRMM KRFNKEVQEN MHKVHLLCLL ASGFYRNSIC RQPDLLAIGL SIIPIRFTKV
     PLQDRDAYYL SNLVKWFIGT FTVNADLSAS EQDDLQTTLE RRIAIYSARD NEELVHIFLL
     ILRALQLLTR LVLSLQPIPL KSAVTKGRKS SKETSVEGPG GSSELSSNSP ESHNKPTTSR
     RIKEEETLSE GRGKATARGK RGTGTAGSRQ RRKPSCSEGE EAEQKVQGRP HARKRRVAAK
     VSYKEESESD GAGSGSDFEP SSGEGQHSSD EDCEPGPRKQ KRASAPQRTK AGSKSASKTQ
     RGSQCEPSSF PEASSSSSGC KRGKKVSSGA EEMADRKPAG VDQWLEVYCE PQAKWVCVDC
     VHGVVGQPVA CYKYATKPMT YVVGIDSDGW VRDVTQRYDP AWMTATRKCR VDAEWWAETL
     RPYRSLLTER EKKEDQEFQA KHLDQPLPTS ISTYKNHPLY ALKRHLLKFQ AIYPETAAVL
     GYCRGEAVYS RDCVHTLHSR DTWLKQARVV RLGEVPYKMV KGFSNRARKA RLSEPQLHDH
     NDLGLYGHWQ TEEYQPPIAV DGKVPRNEFG NVYLFLPSMM PVGCVQMTLP NLNRVARKLG
     IDCVQAITGF DFHGGYCHPV TDGYIVCEEF RDVLLAAWEN EQAIIEKKEK EKKEKRALGN
     WKLLVRGLLI RERLKLRYGA KSEAAAPHAA GGGLSSDEEE GTSSQAEAAR VLAASWPQNR
     EDPEQKSEYT KMTRKRRAAE ASHLFPFEKL
//