DSK2_YEAST
ID DSK2_YEAST Reviewed; 373 AA.
AC P48510; D6W0A3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Ubiquitin domain-containing protein DSK2;
GN Name=DSK2; Synonyms=SHE4; OrderedLocusNames=YMR276W; ORFNames=YM8021.02;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8682868; DOI=10.1083/jcb.133.6.1331;
RA Biggins S., Ivanovska I., Rose M.D.;
RT "Yeast ubiquitin-like genes are involved in duplication of the microtubule
RT organizing center.";
RL J. Cell Biol. 133:1331-1346(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [6]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-13 AND LYS-76, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [7]
RP STRUCTURE BY NMR OF 328-373.
RX PubMed=15837191; DOI=10.1016/j.str.2005.01.011;
RA Ohno A., Jee J., Fujiwara K., Tenno T., Goda N., Tochio H., Kobayashi H.,
RA Hiroaki H., Shirakawa M.;
RT "Structure of the UBA domain of Dsk2p in complex with ubiquitin molecular
RT determinants for ubiquitin recognition.";
RL Structure 13:521-532(2005).
CC -!- FUNCTION: Involved, with RAD23 in spindle pole body duplication.
CC Involved in the ubiquitin-proteasome proteolytic pathway.
CC -!- INTERACTION:
CC P48510; P34222: PTH2; NbExp=11; IntAct=EBI-6174, EBI-2345448;
CC P48510; P38886: RPN10; NbExp=5; IntAct=EBI-6174, EBI-15949;
CC P48510; O13563: RPN13; NbExp=8; IntAct=EBI-6174, EBI-32948;
CC P48510; P33299: RPT1; NbExp=3; IntAct=EBI-6174, EBI-13910;
CC P48510; P0CG63: UBI4; NbExp=3; IntAct=EBI-6174, EBI-7000452;
CC P48510; Q16186: ADRM1; Xeno; NbExp=4; IntAct=EBI-6174, EBI-954387;
CC P48510; O48726: RPN13; Xeno; NbExp=4; IntAct=EBI-6174, EBI-7710745;
CC P48510; P0CG48: UBC; Xeno; NbExp=2; IntAct=EBI-6174, EBI-3390054;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 3930 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L40587; AAB07267.1; -; Genomic_DNA.
DR EMBL; Z49704; CAA89774.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10177.1; -; Genomic_DNA.
DR PIR; S54583; S54583.
DR RefSeq; NP_014003.1; NM_001182783.1.
DR PDB; 1WR1; NMR; -; B=328-373.
DR PDB; 2BWB; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I=328-371.
DR PDB; 2BWE; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=328-373, S/T/U=1-75.
DR PDB; 2BWF; X-ray; 1.15 A; A/B=1-75.
DR PDB; 3M63; X-ray; 2.40 A; B=1-75.
DR PDB; 4UN2; X-ray; 1.51 A; B=328-373.
DR PDBsum; 1WR1; -.
DR PDBsum; 2BWB; -.
DR PDBsum; 2BWE; -.
DR PDBsum; 2BWF; -.
DR PDBsum; 3M63; -.
DR PDBsum; 4UN2; -.
DR AlphaFoldDB; P48510; -.
DR BMRB; P48510; -.
DR SMR; P48510; -.
DR BioGRID; 35455; 139.
DR DIP; DIP-4398N; -.
DR IntAct; P48510; 25.
DR MINT; P48510; -.
DR STRING; 4932.YMR276W; -.
DR iPTMnet; P48510; -.
DR MaxQB; P48510; -.
DR PaxDb; P48510; -.
DR PRIDE; P48510; -.
DR EnsemblFungi; YMR276W_mRNA; YMR276W; YMR276W.
DR GeneID; 855319; -.
DR KEGG; sce:YMR276W; -.
DR SGD; S000004889; DSK2.
DR VEuPathDB; FungiDB:YMR276W; -.
DR eggNOG; KOG0010; Eukaryota.
DR GeneTree; ENSGT00940000175001; -.
DR HOGENOM; CLU_024293_0_1_1; -.
DR InParanoid; P48510; -.
DR OMA; GMDMFGP; -.
DR BioCyc; YEAST:G3O-32947-MON; -.
DR Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR EvolutionaryTrace; P48510; -.
DR PRO; PR:P48510; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P48510; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IC:SGD.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:SGD.
DR GO; GO:0072665; P:protein localization to vacuole; IMP:SGD.
DR GO; GO:0030474; P:spindle pole body duplication; IGI:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00727; STI1; 2.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isopeptide bond; Nucleus; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..373
FT /note="Ubiquitin domain-containing protein DSK2"
FT /id="PRO_0000114900"
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 327..371
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 221..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 13
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 109
FT /note="A -> R (in Ref. 1; AAB07267)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="A -> R (in Ref. 1; AAB07267)"
FT /evidence="ECO:0000305"
FT STRAND 1..9
FT /evidence="ECO:0007829|PDB:2BWF"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:2BWF"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:2BWF"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:2BWF"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:2BWF"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2BWF"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:2BWF"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:4UN2"
FT HELIX 333..341
FT /evidence="ECO:0007829|PDB:4UN2"
FT HELIX 347..357
FT /evidence="ECO:0007829|PDB:4UN2"
FT HELIX 361..368
FT /evidence="ECO:0007829|PDB:4UN2"
SQ SEQUENCE 373 AA; 39346 MW; 3F8691BB95E46569 CRC64;
MSLNIHIKSG QDKWEVNVAP ESTVLQFKEA INKANGIPVA NQRLIYSGKI LKDDQTVESY
HIQDGHSVHL VKSQPKPQTA SAAGANNATA TGAAAGTGAT PNMSSGQSAG FNPLADLTSA
RYAGYLNMPS ADMFGPDGGA LNNDSNNQDE LLRMMENPIF QSQMNEMLSN PQMLDFMIQS
NPQLQAMGPQ ARQMLQSPMF RQMLTNPDMI RQSMQFARMM DPNAGMGSAG GAASAFPAPG
GDAPEEGSNT NTTSSSNTGN NAGTNAGTNA GANTAANPFA SLLNPALNPF ANAGNAASTG
MPAFDPALLA SMFQPPVQAS QAEDTRPPEE RYEHQLRQLN DMGFFDFDRN VAALRRSGGS
VQGALDSLLN GDV
