DDI2_HUMAN
ID DDI2_HUMAN Reviewed; 399 AA.
AC Q5TDH0; A8KAE1; Q7RTZ0; Q9BRT1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Protein DDI1 homolog 2 {ECO:0000305};
DE EC=3.4.23.- {ECO:0000269|PubMed:27528193};
GN Name=DDI2 {ECO:0000312|HGNC:HGNC:24578};
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] (ISOFORM 1).
RC TISSUE=Trachea;
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 2).
RC TISSUE=Prostate;
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 IDENTIFICATION, AND ALTERNATIVE SPLICING (ISOFORM 3).
RX PubMed=12838346; DOI=10.1038/nrg1111;
RA Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C.;
RT "Human and mouse proteases: a comparative genomic approach.";
RL Nat. Rev. Genet. 4:544-558(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, 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].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-128 AND SER-194, AND
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-194, AND
RP IDENTIFICATION BY 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104; SER-106; SER-121;
RP SER-150 AND SER-194, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [14]
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 [15]
RP FUNCTION, AND MUTAGENESIS OF ASP-252.
RX PubMed=27676298; DOI=10.1016/j.cub.2016.08.030;
RA Sha Z., Goldberg A.L.;
RT "Reply to Vangala et al.: Complete inhibition of the proteasome reduces new
RT proteasome production by causing Nrf1 aggregation.";
RL Curr. Biol. 26:R836-R837(2016).
RN [16]
RP FUNCTION.
RX PubMed=27528193; DOI=10.7554/elife.18357;
RA Koizumi S., Irie T., Hirayama S., Sakurai Y., Yashiroda H., Naguro I.,
RA Ichijo H., Hamazaki J., Murata S.;
RT "The aspartyl protease DDI2 activates Nrf1 to compensate for proteasome
RT dysfunction.";
RL Elife 5:0-0(2016).
RN [17]
RP FUNCTION, INTERACTION WITH MCM6; PCNA; PSMD4; PSMD8; RPA2; RPN2 AND RTF2,
RP AND SUBCELLULAR LOCATION.
RX PubMed=29290612; DOI=10.1016/j.molcel.2017.11.035;
RA Kottemann M.C., Conti B.A., Lach F.P., Smogorzewska A.;
RT "Removal of RTF2 from Stalled Replisomes Promotes Maintenance of Genome
RT Integrity.";
RL Mol. Cell 69:24-35.E5(2018).
RN [18] {ECO:0007744|PDB:2N7D, ECO:0007744|PDB:4RGH, ECO:0007744|PDB:5K57}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 212-360, STRUCTURE BY NMR OF
RP 1-212, SUBUNIT, AND MOTIF.
RX PubMed=27461074; DOI=10.1038/srep30443;
RA Siva M., Svoboda M., Veverka V., Trempe J.F., Hofmann K., Kozisek M.,
RA Hexnerova R., Sedlak F., Belza J., Brynda J., Sacha P., Hubalek M.,
RA Starkova J., Flaisigova I., Konvalinka J., Saskova K.G.;
RT "Human DNA-damage-inducible 2 protein is structurally and functionally
RT distinct from its yeast ortholog.";
RL Sci. Rep. 6:30443-30443(2016).
CC -!- FUNCTION: Aspartic protease that mediates the cleavage of NFE2L1/NRF1
CC at 'Leu-104', thereby promoting release of NFE2L1/NRF1 from the
CC endoplasmic reticulum membrane (PubMed:27676298, PubMed:27528193).
CC Ubiquitination of NFE2L1/NRF1 is a prerequisite for cleavage,
CC suggesting that DDI2 specifically recognizes and binds ubiquitinated
CC NFE2L1/NRF1 (PubMed:27528193). Seems to act as a proteasomal shuttle
CC which links the proteasome and replication fork proteins like RTF2
CC (Probable). Required, with DDI1, for cellular survival following
CC replication stress. Together or redudantly with DDI1, removes RTF2 from
CC stalled forks to allow cell cycle progression after replication stress
CC and maintains genome integrity (PubMed:29290612).
CC {ECO:0000269|PubMed:27528193, ECO:0000269|PubMed:27676298,
CC ECO:0000269|PubMed:29290612, ECO:0000305|PubMed:29290612}.
CC -!- SUBUNIT: Homodimer (PubMed:27461074). Interacts with MCM6; PCNA; PSMD4;
CC PSMD8; RPA2 and RPN2 (PubMed:29290612). Interacts with RTF2
CC (PubMed:29290612). {ECO:0000269|PubMed:27461074,
CC ECO:0000269|PubMed:29290612}.
CC -!- INTERACTION:
CC Q5TDH0-2; P54253: ATXN1; NbExp=6; IntAct=EBI-25858598, EBI-930964;
CC Q5TDH0-2; P14136: GFAP; NbExp=3; IntAct=EBI-25858598, EBI-744302;
CC Q5TDH0-2; Q13148: TARDBP; NbExp=3; IntAct=EBI-25858598, EBI-372899;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:27528193}.
CC Chromosome {ECO:0000269|PubMed:29290612}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5TDH0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5TDH0-2; Sequence=VSP_025297;
CC Name=3;
CC IsoId=Q5TDH0-3; Sequence=VSP_025298;
CC -!- SIMILARITY: Belongs to the DDI1 family. {ECO:0000305}.
CC -!- CAUTION: The protein was initially thought to be catalytically inactive
CC (PubMed:27461074). It was later shown that it has aspartyl protease
CC activity and mediates cleavage of NFE2L1/NRF1 (PubMed:27676298).
CC {ECO:0000269|PubMed:27461074, ECO:0000269|PubMed:27676298}.
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DR EMBL; AK293006; BAF85695.1; -; mRNA.
DR EMBL; AL121992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471167; EAW51743.1; -; Genomic_DNA.
DR EMBL; BC006011; AAH06011.1; -; mRNA.
DR EMBL; BN000122; CAD67552.1; -; mRNA.
DR CCDS; CCDS30607.1; -. [Q5TDH0-1]
DR RefSeq; NP_115717.3; NM_032341.4. [Q5TDH0-1]
DR PDB; 2N7D; NMR; -; A=1-76.
DR PDB; 4RGH; X-ray; 1.90 A; A/B=212-360.
DR PDB; 5K57; NMR; -; A=116-212.
DR PDBsum; 2N7D; -.
DR PDBsum; 4RGH; -.
DR PDBsum; 5K57; -.
DR AlphaFoldDB; Q5TDH0; -.
DR SMR; Q5TDH0; -.
DR BioGRID; 124027; 56.
DR IntAct; Q5TDH0; 18.
DR STRING; 9606.ENSP00000417748; -.
DR MEROPS; A28.003; -.
DR GlyGen; Q5TDH0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5TDH0; -.
DR PhosphoSitePlus; Q5TDH0; -.
DR BioMuta; DDI2; -.
DR DMDM; 74746201; -.
DR EPD; Q5TDH0; -.
DR jPOST; Q5TDH0; -.
DR MassIVE; Q5TDH0; -.
DR MaxQB; Q5TDH0; -.
DR PaxDb; Q5TDH0; -.
DR PeptideAtlas; Q5TDH0; -.
DR PRIDE; Q5TDH0; -.
DR ProteomicsDB; 65023; -. [Q5TDH0-1]
DR ProteomicsDB; 65024; -. [Q5TDH0-2]
DR ProteomicsDB; 65025; -. [Q5TDH0-3]
DR Antibodypedia; 52916; 108 antibodies from 17 providers.
DR DNASU; 84301; -.
DR Ensembl; ENST00000480945.6; ENSP00000417748.1; ENSG00000197312.12. [Q5TDH0-1]
DR GeneID; 84301; -.
DR KEGG; hsa:84301; -.
DR MANE-Select; ENST00000480945.6; ENSP00000417748.1; NM_032341.5; NP_115717.3.
DR UCSC; uc001awz.4; human. [Q5TDH0-1]
DR CTD; 84301; -.
DR DisGeNET; 84301; -.
DR GeneCards; DDI2; -.
DR HGNC; HGNC:24578; DDI2.
DR HPA; ENSG00000197312; Low tissue specificity.
DR neXtProt; NX_Q5TDH0; -.
DR OpenTargets; ENSG00000197312; -.
DR PharmGKB; PA142672004; -.
DR VEuPathDB; HostDB:ENSG00000197312; -.
DR eggNOG; KOG0012; Eukaryota.
DR GeneTree; ENSGT00950000182999; -.
DR HOGENOM; CLU_020435_1_0_1; -.
DR InParanoid; Q5TDH0; -.
DR OMA; IHMVQIQ; -.
DR OrthoDB; 817208at2759; -.
DR PhylomeDB; Q5TDH0; -.
DR TreeFam; TF333421; -.
DR PathwayCommons; Q5TDH0; -.
DR SignaLink; Q5TDH0; -.
DR BioGRID-ORCS; 84301; 141 hits in 1076 CRISPR screens.
DR ChiTaRS; DDI2; human.
DR GenomeRNAi; 84301; -.
DR Pharos; Q5TDH0; Tbio.
DR PRO; PR:Q5TDH0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5TDH0; protein.
DR Bgee; ENSG00000197312; Expressed in tibialis anterior and 186 other tissues.
DR ExpressionAtlas; Q5TDH0; baseline and differential.
DR Genevisible; Q5TDH0; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
DR GO; GO:0072711; P:cellular response to hydroxyurea; IMP:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IMP:UniProtKB.
DR GO; GO:0016485; P:protein processing; IDA:UniProtKB.
DR GO; GO:0097752; P:regulation of DNA stability; IMP:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR CDD; cd05479; RP_DDI; 1.
DR CDD; cd01796; Ubl_Ddi1_like; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR InterPro; IPR033882; DDI1_N.
DR InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF09668; Asp_protease; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Aspartyl protease; Chromosome;
KW Cytoplasm; Hydrolase; Phosphoprotein; Protease; Reference proteome.
FT CHAIN 1..399
FT /note="Protein DDI1 homolog 2"
FT /id="PRO_0000287090"
FT DOMAIN 1..81
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 99..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 376..395
FT /note="Ubiquitin-binding"
FT /evidence="ECO:0000305|PubMed:27461074"
FT COMPBIAS 99..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 252
FT /evidence="ECO:0000305|PubMed:27528193"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 212..399
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025297"
FT VAR_SEQ 395..399
FT /note="ERQKP -> GIWDGQTLQYLLLMGKPGKCGLQKG (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_025298"
FT MUTAGEN 252
FT /note="D->N: Abolishes aspartic protease activity."
FT /evidence="ECO:0000269|PubMed:27528193"
FT STRAND 1..9
FT /evidence="ECO:0007829|PDB:2N7D"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:2N7D"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:2N7D"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:2N7D"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:2N7D"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:2N7D"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:2N7D"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:5K57"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:5K57"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:5K57"
FT HELIX 157..164
FT /evidence="ECO:0007829|PDB:5K57"
FT HELIX 168..190
FT /evidence="ECO:0007829|PDB:5K57"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:4RGH"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:4RGH"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:4RGH"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:4RGH"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:4RGH"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:4RGH"
FT STRAND 290..301
FT /evidence="ECO:0007829|PDB:4RGH"
FT STRAND 304..314
FT /evidence="ECO:0007829|PDB:4RGH"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:4RGH"
FT HELIX 324..329
FT /evidence="ECO:0007829|PDB:4RGH"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:4RGH"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:4RGH"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:4RGH"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:4RGH"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:4RGH"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:4RGH"
SQ SEQUENCE 399 AA; 44523 MW; D04FCA9ECECCD1D8 CRC64;
MLLTVYCVRR DLSEVTFSLQ VDADFELHNF RALCELESGI PAAESQIVYA ERPLTDNHRS
LASYGLKDGD VVILRQKENA DPRPPVQFPN LPRIDFSSIA VPGTSSPRQR QPPGTQQSHS
SPGEITSSPQ GLDNPALLRD MLLANPHELS LLKERNPPLA EALLSGDLEK FSRVLVEQQQ
DRARREQERI RLFSADPFDL EAQAKIEEDI RQQNIEENMT IAMEEAPESF GQVVMLYINC
KVNGHPVKAF VDSGAQMTIM SQACAERCNI MRLVDRRWAG IAKGVGTQKI IGRVHLAQVQ
IEGDFLPCSF SILEEQPMDM LLGLDMLKRH QCSIDLKKNV LVIGTTGSQT TFLPEGELPE
CARLAYGAGR EDVRPEEIAD QELAEALQKS AEDAERQKP
