SDE2_HUMAN
ID SDE2_HUMAN Reviewed; 451 AA.
AC Q6IQ49; A8K4P3; Q5TD36; Q6ZS26; Q8NAG7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Replication stress response regulator SDE2 {ECO:0000305};
DE Flags: Precursor;
GN Name=SDE2; Synonyms=C1orf55;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, and Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-319, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-274 AND SER-278, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE AT GLY-77, MUTAGENESIS
RP OF 47-PHE--PHE-48 AND 76-GLY--GLY-77, PIP-BOX DOMAIN, SAP DOMAIN, AND
RP UBIQUITINATION.
RX PubMed=27906959; DOI=10.1371/journal.pgen.1006465;
RA Jo U., Cai W., Wang J., Kwon Y., D'Andrea A.D., Kim H.;
RT "PCNA-dependent cleavage and degradation of SDE2 regulates response to
RT replication stress.";
RL PLoS Genet. 12:E1006465-E1006465(2016).
CC -!- FUNCTION: Involved in both DNA replication and cell cycle control
CC (PubMed:27906959). Unprocessed SDE2 interacts with PCNA via its PIP-
CC box. The interaction with PCNA prevents monoubiquitination of the
CC latter thereby inhibiting translesion DNA synthesis. The binding of
CC SDE2 to PCNA also leads to processing of SDE2 by an unidentified
CC deubiquitinating enzyme, cleaving off the N-terminal ubiquitin-like
CC domain. The resulting mature SDE2 is degraded by the DCX(DTL) complex
CC in a cell cycle- and DNA damage dependent manner (PubMed:27906959).
CC Binding of SDE2 to PCNA is necessary to counteract damage due to
CC ultraviolet light induced replication stress. The complete degradation
CC of SDE2 is necessary to allow S-phase progression (PubMed:27906959).
CC {ECO:0000269|PubMed:27906959}.
CC -!- INTERACTION:
CC Q6IQ49; Q96EW2: HSPBAP1; NbExp=2; IntAct=EBI-2362709, EBI-720457;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27906959}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6IQ49-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6IQ49-2; Sequence=VSP_024982;
CC Name=3;
CC IsoId=Q6IQ49-3; Sequence=VSP_024981;
CC -!- DOMAIN: The PIP-box (PCNA interacting peptide) motif mediates both the
CC interaction with PCNA and cleavage of the SDE2 precursor by a
CC deubiquitinating enzyme. {ECO:0000269|PubMed:27906959}.
CC -!- DOMAIN: The SAP domain is necessary for specific binding to DNA.
CC {ECO:0000305|PubMed:27906959}.
CC -!- DOMAIN: The propeptide displays a ubiquitin-like fold.
CC {ECO:0000305|PubMed:27906959}.
CC -!- PTM: The protein is cleaved at Gly-77 by a deubiquitinating enzyme to
CC form the active SDE2. {ECO:0000269|PubMed:27906959}.
CC -!- PTM: Both SDE2-UBL and the mature SDE2 are polyubiquitinated.
CC {ECO:0000269|PubMed:27906959}.
CC -!- SIMILARITY: Belongs to the SDE2 family. {ECO:0000305}.
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DR EMBL; AK092701; BAC03952.1; -; mRNA.
DR EMBL; AK127780; BAC87130.1; -; mRNA.
DR EMBL; AK291008; BAF83697.1; -; mRNA.
DR EMBL; AL133288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471098; EAW69769.1; -; Genomic_DNA.
DR EMBL; BC071563; AAH71563.1; -; mRNA.
DR CCDS; CCDS41473.1; -. [Q6IQ49-1]
DR RefSeq; NP_689821.3; NM_152608.3. [Q6IQ49-1]
DR PDB; 6QDV; EM; 3.30 A; z=93-126.
DR PDBsum; 6QDV; -.
DR AlphaFoldDB; Q6IQ49; -.
DR SMR; Q6IQ49; -.
DR BioGRID; 127881; 23.
DR IntAct; Q6IQ49; 10.
DR MINT; Q6IQ49; -.
DR STRING; 9606.ENSP00000272091; -.
DR GlyGen; Q6IQ49; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6IQ49; -.
DR MetOSite; Q6IQ49; -.
DR PhosphoSitePlus; Q6IQ49; -.
DR SwissPalm; Q6IQ49; -.
DR BioMuta; SDE2; -.
DR DMDM; 74748828; -.
DR EPD; Q6IQ49; -.
DR jPOST; Q6IQ49; -.
DR MassIVE; Q6IQ49; -.
DR MaxQB; Q6IQ49; -.
DR PaxDb; Q6IQ49; -.
DR PeptideAtlas; Q6IQ49; -.
DR PRIDE; Q6IQ49; -.
DR ProteomicsDB; 66484; -. [Q6IQ49-1]
DR ProteomicsDB; 66485; -. [Q6IQ49-2]
DR ProteomicsDB; 66486; -. [Q6IQ49-3]
DR Antibodypedia; 34648; 105 antibodies from 17 providers.
DR DNASU; 163859; -.
DR Ensembl; ENST00000272091.8; ENSP00000272091.7; ENSG00000143751.10. [Q6IQ49-1]
DR GeneID; 163859; -.
DR KEGG; hsa:163859; -.
DR MANE-Select; ENST00000272091.8; ENSP00000272091.7; NM_152608.4; NP_689821.3.
DR UCSC; uc001hpu.5; human. [Q6IQ49-1]
DR CTD; 163859; -.
DR GeneCards; SDE2; -.
DR HGNC; HGNC:26643; SDE2.
DR HPA; ENSG00000143751; Low tissue specificity.
DR neXtProt; NX_Q6IQ49; -.
DR OpenTargets; ENSG00000143751; -.
DR PharmGKB; PA142672506; -.
DR VEuPathDB; HostDB:ENSG00000143751; -.
DR eggNOG; KOG2827; Eukaryota.
DR GeneTree; ENSGT00530000063402; -.
DR HOGENOM; CLU_042333_0_0_1; -.
DR InParanoid; Q6IQ49; -.
DR OMA; QRQCHEM; -.
DR OrthoDB; 1446978at2759; -.
DR PhylomeDB; Q6IQ49; -.
DR TreeFam; TF314323; -.
DR PathwayCommons; Q6IQ49; -.
DR SignaLink; Q6IQ49; -.
DR BioGRID-ORCS; 163859; 766 hits in 1078 CRISPR screens.
DR ChiTaRS; SDE2; human.
DR GenomeRNAi; 163859; -.
DR Pharos; Q6IQ49; Tbio.
DR PRO; PR:Q6IQ49; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6IQ49; protein.
DR Bgee; ENSG00000143751; Expressed in secondary oocyte and 191 other tissues.
DR Genevisible; Q6IQ49; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IDA:UniProtKB.
DR GO; GO:0016485; P:protein processing; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR InterPro; IPR024974; Sde2_N.
DR Pfam; PF13019; Sde2_N_Ubi; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Coiled coil;
KW DNA replication; DNA-binding; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT PROPEP 1..77
FT /note="UBL"
FT /evidence="ECO:0000305|PubMed:27906959"
FT /id="PRO_0000442521"
FT CHAIN 78..451
FT /note="Replication stress response regulator SDE2"
FT /id="PRO_0000286084"
FT DOMAIN 396..430
FT /note="SAP"
FT /evidence="ECO:0000305|PubMed:27906959"
FT REGION 182..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 109..149
FT /evidence="ECO:0000255"
FT MOTIF 39..52
FT /note="PIP-box"
FT /evidence="ECO:0000305|PubMed:27906959"
FT COMPBIAS 267..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 77..78
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:27906959"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1J5"
FT MOD_RES 274
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 319
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BJN8"
FT VAR_SEQ 1..142
FT /note="MAEAAALVWIRGPGFGCKAVRCASGRCTVRDFIHRHCQDQNVPVENFFVKCN
FT GALINTSDTVQHGAVYSLEPRLCGGKGGFGSMLRALGAQIEKTTNREACRDLSGRRLRD
FT VNHEKAMAEWVKQQAEREAEKEQKRLERLQR -> MEHSLTPVTQCSMELFIVWNPDFA
FT VEKEVLDLCSEHLVLRLRRQPIE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024981"
FT VAR_SEQ 53..64
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024982"
FT VARIANT 312
FT /note="M -> I (in dbSNP:rs34348128)"
FT /id="VAR_032068"
FT MUTAGEN 47..48
FT /note="FF->AA: No binding to PCNA; no cleavage at Gly-77."
FT /evidence="ECO:0000269|PubMed:27906959"
FT MUTAGEN 76..77
FT /note="GG->AA: No cleavage at Gly-77."
FT /evidence="ECO:0000269|PubMed:27906959"
FT CONFLICT 162
FT /note="E -> G (in Ref. 1; BAC87130)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="E -> D (in Ref. 1; BAC03952)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 49742 MW; D7C19152E0051A21 CRC64;
MAEAAALVWI RGPGFGCKAV RCASGRCTVR DFIHRHCQDQ NVPVENFFVK CNGALINTSD
TVQHGAVYSL EPRLCGGKGG FGSMLRALGA QIEKTTNREA CRDLSGRRLR DVNHEKAMAE
WVKQQAEREA EKEQKRLERL QRKLVEPKHC FTSPDYQQQC HEMAERLEDS VLKGMQAASS
KMVSAEISEN RKRQWPTKSQ TDRGASAGKR RCFWLGMEGL ETAEGSNSES SDDDSEEAPS
TSGMGFHAPK IGSNGVEMAA KFPSGSQRAR VVNTDHGSPE QLQIPVTDSG RHILEDSCAE
LGESKEHMES RMVTETEETQ EKKAESKEPI EEEPTGAGLN KDKETEERTD GERVAEVAPE
ERENVAVAKL QESQPGNAVI DKETIDLLAF TSVAELELLG LEKLKCELMA LGLKCGGTLQ
ERAARLFSVR GLAKEQIDPA LFAKPLKGKK K
