DESI1_HUMAN
ID DESI1_HUMAN Reviewed; 168 AA.
AC Q6ICB0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Desumoylating isopeptidase 1 {ECO:0000250|UniProtKB:Q9CQT7};
DE Short=DeSI-1 {ECO:0000250|UniProtKB:Q9CQT7};
DE EC=3.4.-.- {ECO:0000250|UniProtKB:Q9CQT7};
DE AltName: Full=PPPDE peptidase domain-containing protein 2 {ECO:0000305};
DE AltName: Full=Polyubiquitinated substrate transporter {ECO:0000303|PubMed:29666234};
DE Short=POST {ECO:0000303|PubMed:29666234};
GN Name=DESI1 {ECO:0000312|HGNC:HGNC:24577};
GN Synonyms=FAM152B {ECO:0000312|HGNC:HGNC:24577},
GN PPPDE2 {ECO:0000312|HGNC:HGNC:24577};
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].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
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].
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 IDENTIFICATION BY 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 [6]
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UBQLN4.
RX PubMed=29666234; DOI=10.1073/pnas.1711017115;
RA Hirayama S., Sugihara M., Morito D., Iemura S.I., Natsume T., Murata S.,
RA Nagata K.;
RT "Nuclear export of ubiquitinated proteins via the UBIN-POST system.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E4199-E4208(2018).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RG Structural genomics consortium (SGC);
RT "Structure of human PPPDE1.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Protease which deconjugates SUMO1, SUMO2 and SUMO3 from some
CC substrate proteins. Has isopeptidase but not SUMO-processing activity
CC (By similarity). Desumoylates ZBTB46 (By similarity). Collaborates with
CC UBQLN4 in the export of ubiquitinated proteins from the nucleus to the
CC cytoplasm (PubMed:29666234). {ECO:0000250|UniProtKB:Q9CQT7,
CC ECO:0000269|PubMed:29666234}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with UBQLN4; leading to
CC the export of UBQLN4 from the nucleus (PubMed:29666234).
CC {ECO:0000250|UniProtKB:Q9CQT7, ECO:0000269|PubMed:29666234}.
CC -!- INTERACTION:
CC Q6ICB0; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-2806959, EBI-742038;
CC Q6ICB0; Q8TD06: AGR3; NbExp=3; IntAct=EBI-2806959, EBI-3925742;
CC Q6ICB0; Q9H305: CDIP1; NbExp=4; IntAct=EBI-2806959, EBI-2876678;
CC Q6ICB0; P78358: CTAG1B; NbExp=3; IntAct=EBI-2806959, EBI-1188472;
CC Q6ICB0; O75638-2: CTAG2; NbExp=6; IntAct=EBI-2806959, EBI-12265122;
CC Q6ICB0; Q15038: DAZAP2; NbExp=5; IntAct=EBI-2806959, EBI-724310;
CC Q6ICB0; P30040: ERP29; NbExp=3; IntAct=EBI-2806959, EBI-946830;
CC Q6ICB0; P34910-2: EVI2B; NbExp=3; IntAct=EBI-2806959, EBI-17640610;
CC Q6ICB0; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-2806959, EBI-712073;
CC Q6ICB0; Q4KN05: KLRF1; NbExp=3; IntAct=EBI-2806959, EBI-21690803;
CC Q6ICB0; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2806959, EBI-16439278;
CC Q6ICB0; Q13232: NME3; NbExp=6; IntAct=EBI-2806959, EBI-713684;
CC Q6ICB0; Q9H0P0: NT5C3A; NbExp=5; IntAct=EBI-2806959, EBI-3918356;
CC Q6ICB0; P85299-2: PRR5; NbExp=3; IntAct=EBI-2806959, EBI-12944296;
CC Q6ICB0; P78317: RNF4; NbExp=3; IntAct=EBI-2806959, EBI-2340927;
CC Q6ICB0; P62979: RPS27A; NbExp=3; IntAct=EBI-2806959, EBI-357375;
CC Q6ICB0; Q96DD7: SHISA4; NbExp=3; IntAct=EBI-2806959, EBI-18035902;
CC Q6ICB0; Q8N114-3: SHISA5; NbExp=3; IntAct=EBI-2806959, EBI-13369834;
CC Q6ICB0; Q3B7S5: SMIM21; NbExp=3; IntAct=EBI-2806959, EBI-23836218;
CC Q6ICB0; P59536: TAS2R41; NbExp=3; IntAct=EBI-2806959, EBI-13344991;
CC Q6ICB0; P62987: UBA52; NbExp=4; IntAct=EBI-2806959, EBI-357304;
CC Q6ICB0; P0CG47: UBB; NbExp=3; IntAct=EBI-2806959, EBI-413034;
CC Q6ICB0; P0CG48: UBC; NbExp=3; IntAct=EBI-2806959, EBI-3390054;
CC Q6ICB0; Q9UMX0: UBQLN1; NbExp=6; IntAct=EBI-2806959, EBI-741480;
CC Q6ICB0; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-2806959, EBI-947187;
CC Q6ICB0; Q8IYU4: UBQLNL; NbExp=6; IntAct=EBI-2806959, EBI-12295223;
CC Q6ICB0; Q96PU4-2: UHRF2; NbExp=3; IntAct=EBI-2806959, EBI-12878912;
CC Q6ICB0; A0A1U9X8X8; NbExp=3; IntAct=EBI-2806959, EBI-17234977;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29666234}. Nucleus
CC {ECO:0000269|PubMed:29666234}. Note=Shuttles between the nucleus and
CC the cytoplasm; exported from the nucleus in a XPO1/CRM1-dependent
CC manner via its nuclear export signal motifs.
CC {ECO:0000269|PubMed:29666234}.
CC -!- SIMILARITY: Belongs to the DeSI family. {ECO:0000305}.
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DR EMBL; CR456458; CAG30344.1; -; mRNA.
DR EMBL; Z83840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL023553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60445.1; -; Genomic_DNA.
DR EMBL; BC093956; AAH93956.1; -; mRNA.
DR EMBL; BC112179; AAI12180.1; -; mRNA.
DR CCDS; CCDS33652.1; -.
DR RefSeq; NP_056519.1; NM_015704.2.
DR PDB; 3EBQ; X-ray; 1.90 A; A=1-168.
DR PDBsum; 3EBQ; -.
DR AlphaFoldDB; Q6ICB0; -.
DR SMR; Q6ICB0; -.
DR BioGRID; 118163; 64.
DR IntAct; Q6ICB0; 36.
DR STRING; 9606.ENSP00000263256; -.
DR MEROPS; C97.001; -.
DR iPTMnet; Q6ICB0; -.
DR PhosphoSitePlus; Q6ICB0; -.
DR BioMuta; DESI1; -.
DR DMDM; 74757716; -.
DR EPD; Q6ICB0; -.
DR jPOST; Q6ICB0; -.
DR MassIVE; Q6ICB0; -.
DR MaxQB; Q6ICB0; -.
DR PaxDb; Q6ICB0; -.
DR PeptideAtlas; Q6ICB0; -.
DR PRIDE; Q6ICB0; -.
DR ProteomicsDB; 66382; -.
DR TopDownProteomics; Q6ICB0; -.
DR Antibodypedia; 55491; 33 antibodies from 13 providers.
DR DNASU; 27351; -.
DR Ensembl; ENST00000263256.7; ENSP00000263256.6; ENSG00000100418.8.
DR GeneID; 27351; -.
DR KEGG; hsa:27351; -.
DR MANE-Select; ENST00000263256.7; ENSP00000263256.6; NM_015704.3; NP_056519.1.
DR UCSC; uc003bam.3; human.
DR CTD; 27351; -.
DR DisGeNET; 27351; -.
DR GeneCards; DESI1; -.
DR HGNC; HGNC:24577; DESI1.
DR HPA; ENSG00000100418; Low tissue specificity.
DR MIM; 614637; gene.
DR neXtProt; NX_Q6ICB0; -.
DR OpenTargets; ENSG00000100418; -.
DR PharmGKB; PA164725008; -.
DR VEuPathDB; HostDB:ENSG00000100418; -.
DR eggNOG; KOG0324; Eukaryota.
DR GeneTree; ENSGT00730000111100; -.
DR HOGENOM; CLU_101028_0_0_1; -.
DR InParanoid; Q6ICB0; -.
DR OMA; LFDNNCN; -.
DR OrthoDB; 1214552at2759; -.
DR PhylomeDB; Q6ICB0; -.
DR TreeFam; TF328492; -.
DR PathwayCommons; Q6ICB0; -.
DR SignaLink; Q6ICB0; -.
DR BioGRID-ORCS; 27351; 35 hits in 1081 CRISPR screens.
DR ChiTaRS; DESI1; human.
DR EvolutionaryTrace; Q6ICB0; -.
DR GenomeRNAi; 27351; -.
DR Pharos; Q6ICB0; Tdark.
DR PRO; PR:Q6ICB0; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q6ICB0; protein.
DR Bgee; ENSG00000100418; Expressed in lower esophagus mucosa and 186 other tissues.
DR Genevisible; Q6ICB0; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0016929; F:deSUMOylase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0061676; F:importin-alpha family protein binding; IPI:UniProtKB.
DR GO; GO:0016926; P:protein desumoylation; IEA:Ensembl.
DR GO; GO:0006611; P:protein export from nucleus; IPI:UniProtKB.
DR GO; GO:0070646; P:protein modification by small protein removal; IBA:GO_Central.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR Gene3D; 3.90.1720.30; -; 1.
DR InterPro; IPR008580; PPPDE_dom.
DR InterPro; IPR042266; PPPDE_sf.
DR PANTHER; PTHR12378; PTHR12378; 1.
DR Pfam; PF05903; Peptidase_C97; 1.
DR SMART; SM01179; DUF862; 1.
DR PROSITE; PS51858; PPPDE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Nucleus; Protease; Reference proteome.
FT CHAIN 1..168
FT /note="Desumoylating isopeptidase 1"
FT /id="PRO_0000318150"
FT DOMAIN 7..149
FT /note="PPPDE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01205"
FT MOTIF 83..91
FT /note="Nuclear export signal 1"
FT /evidence="ECO:0000269|PubMed:29666234"
FT MOTIF 139..153
FT /note="Nuclear export signal 2"
FT /evidence="ECO:0000269|PubMed:29666234"
FT ACT_SITE 38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01205"
FT ACT_SITE 108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01205"
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:3EBQ"
FT TURN 16..19
FT /evidence="ECO:0007829|PDB:3EBQ"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:3EBQ"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:3EBQ"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:3EBQ"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:3EBQ"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:3EBQ"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:3EBQ"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:3EBQ"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3EBQ"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:3EBQ"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:3EBQ"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:3EBQ"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:3EBQ"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:3EBQ"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:3EBQ"
SQ SEQUENCE 168 AA; 18263 MW; D902AF6FE5DDA31A CRC64;
MEPPNLYPVK LYVYDLSKGL ARRLSPIMLG KQLEGIWHTS IVVHKDEFFF GSGGISSCPP
GGTLLGPPDS VVDVGSTEVT EEIFLEYLSS LGESLFRGEA YNLFEHNCNT FSNEVAQFLT
GRKIPSYITD LPSEVLSTPF GQALRPLLDS IQIQPPGGSS VGRPNGQS
