SDE2_MOUSE
ID SDE2_MOUSE Reviewed; 448 AA.
AC Q8K1J5; Q8BJX1;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Replication stress response regulator SDE2 {ECO:0000305};
DE Flags: Precursor;
GN Name=Sde2;
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 [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-205.
RC STRAIN=C57BL/6J; TISSUE=Muellerian duct;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND IDENTIFICATION BY
RP 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND IDENTIFICATION BY
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Lung;
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 both DNA replication and cell cycle control.
CC Unprocessed SDE2 interacts with PCNA via its PIP-box. The interaction
CC with PCNA prevents monoubiquitination of the latter thereby inhibiting
CC translesion DNA synthesis. The binding of SDE2 to PCNA also leads to
CC processing of SDE2 by an unidentified deubiquitinating enzyme, cleaving
CC off the N-terminal ubiquitin-like domain. The resulting mature SDE2 is
CC degraded by the DCX(DTL) complex in a cell cycle- and DNA damage
CC dependent manner. Binding of SDE2 to PCNA is necessary to counteract
CC damage due to ultraviolet light induced replication stress. The
CC complete degradation of SDE2 is necessary to allow S-phase progression.
CC {ECO:0000250|UniProtKB:Q6IQ49}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6IQ49}.
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:0000250|UniProtKB:Q6IQ49}.
CC -!- DOMAIN: The SAP domain is necessary for specific binding to DNA.
CC {ECO:0000250|UniProtKB:Q6IQ49}.
CC -!- DOMAIN: The propeptide displays a ubiquitin-like fold.
CC {ECO:0000250|UniProtKB:Q6IQ49}.
CC -!- PTM: The protein is cleaved at Gly-77 by a deubiquitinating enzyme to
CC form the active SDE2. {ECO:0000250|UniProtKB:Q6IQ49}.
CC -!- PTM: Both SDE2-UBL and the mature SDE2 are polyubiquitinated.
CC {ECO:0000250|UniProtKB:Q6IQ49}.
CC -!- SIMILARITY: Belongs to the SDE2 family. {ECO:0000305}.
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DR EMBL; BC031781; AAH31781.1; -; mRNA.
DR EMBL; AK078485; BAC37302.2; -; mRNA.
DR CCDS; CCDS15574.1; -.
DR RefSeq; NP_666055.1; NM_145943.1.
DR AlphaFoldDB; Q8K1J5; -.
DR BioGRID; 229012; 2.
DR IntAct; Q8K1J5; 1.
DR STRING; 10090.ENSMUSP00000037890; -.
DR iPTMnet; Q8K1J5; -.
DR PhosphoSitePlus; Q8K1J5; -.
DR EPD; Q8K1J5; -.
DR jPOST; Q8K1J5; -.
DR MaxQB; Q8K1J5; -.
DR PaxDb; Q8K1J5; -.
DR PeptideAtlas; Q8K1J5; -.
DR PRIDE; Q8K1J5; -.
DR ProteomicsDB; 256941; -.
DR Antibodypedia; 34648; 105 antibodies from 17 providers.
DR DNASU; 208768; -.
DR Ensembl; ENSMUST00000038091; ENSMUSP00000037890; ENSMUSG00000038806.
DR GeneID; 208768; -.
DR KEGG; mmu:208768; -.
DR UCSC; uc007dwt.1; mouse.
DR CTD; 163859; -.
DR MGI; MGI:2384788; Sde2.
DR VEuPathDB; HostDB:ENSMUSG00000038806; -.
DR eggNOG; KOG2827; Eukaryota.
DR GeneTree; ENSGT00530000063402; -.
DR HOGENOM; CLU_042333_0_0_1; -.
DR InParanoid; Q8K1J5; -.
DR OMA; QRQCHEM; -.
DR OrthoDB; 1446978at2759; -.
DR PhylomeDB; Q8K1J5; -.
DR TreeFam; TF314323; -.
DR BioGRID-ORCS; 208768; 23 hits in 73 CRISPR screens.
DR ChiTaRS; Sde2; mouse.
DR PRO; PR:Q8K1J5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8K1J5; protein.
DR Bgee; ENSMUSG00000038806; Expressed in metanephric renal vesicle and 222 other tissues.
DR Genevisible; Q8K1J5; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003684; F:damaged DNA binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034644; P:cellular response to UV; ISO:MGI.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; ISO:MGI.
DR GO; GO:0016485; P:protein processing; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR InterPro; IPR024974; Sde2_N.
DR Pfam; PF13019; Sde2_N_Ubi; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; DNA replication; DNA-binding;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT PROPEP 1..77
FT /note="UBL"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT /id="PRO_0000442522"
FT CHAIN 78..448
FT /note="Replication stress response regulator SDE2"
FT /id="PRO_0000286085"
FT DOMAIN 393..427
FT /note="SAP"
FT /evidence="ECO:0000255"
FT REGION 175..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..372
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:0000250|UniProtKB:Q6IQ49"
FT COMPBIAS 186..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 77..78
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 277
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT MOD_RES 324
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BJN8"
SQ SEQUENCE 448 AA; 48580 MW; B2A8DBDB795FFA36 CRC64;
MAEAAVVAWV RGPGTVWKAL PCASVGCSVR DVIYRHCQEQ EVPVECFFVT CNGVLVNAGD
KVQHGAVYSL EPRLRGGKGG FGSMLRALGA QIEKTTNREA CRDLSGRRLR DVNHEKAMAE
WVKQQAEREA EKEQRRLERL QRKLAEPAHC FTSPDYQRQC HEMAERLEDS VLKGMQAASS
KMVSAEITET RKRPNKSKTD QETSAKKRKR KCFWLGMDGL EAAEGSSTGS SEDSSEDDSE
DAPGTSEQSC CAREDGIDAV EVAADRPGSP RSSASGTHSE SPEKLQCPVT EPGQGILENT
GTEPGETSDK ECNERKTVTD PEETPARKET ESHEATEKDQ KTGMSGGDRA AMVLSGEDRK
SVPAANLEGN NSGDTALGLE AVDLSAFSSA AELESLGLER LKCELMVLGL KCGGTLQERA
ARLFSVRGLT KELIDPALFA KPSKGKKK
