ULP2_YEAST
ID ULP2_YEAST Reviewed; 1034 AA.
AC P40537; D6VVQ0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Ubiquitin-like-specific protease 2;
DE EC=3.4.22.-;
GN Name=ULP2; Synonyms=SMT4; OrderedLocusNames=YIL031W;
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=S288c / YPH1;
RA Meluh P.B., Koshland D.E.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-788 AND SER-903, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983 AND SER-984, AND
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).
CC -!- FUNCTION: Insertion mutation in SMT4 confers temperature and benomyl
CC sensitivity; high copy suppressor of a temperature sensitive mutation
CC in MIF2.
CC -!- MISCELLANEOUS: Present with 450 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR EMBL; Z46861; CAA86920.1; -; Genomic_DNA.
DR EMBL; U27832; AAA69556.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08516.1; -; Genomic_DNA.
DR PIR; S49947; S49947.
DR RefSeq; NP_012233.1; NM_001179381.1.
DR PDB; 5LNB; X-ray; 2.30 A; B=411-710.
DR PDB; 5V1A; X-ray; 2.14 A; B=821-845.
DR PDBsum; 5LNB; -.
DR PDBsum; 5V1A; -.
DR AlphaFoldDB; P40537; -.
DR SMR; P40537; -.
DR BioGRID; 34958; 346.
DR DIP; DIP-5489N; -.
DR IntAct; P40537; 10.
DR STRING; 4932.YIL031W; -.
DR MEROPS; C48.005; -.
DR iPTMnet; P40537; -.
DR MaxQB; P40537; -.
DR PaxDb; P40537; -.
DR PRIDE; P40537; -.
DR EnsemblFungi; YIL031W_mRNA; YIL031W; YIL031W.
DR GeneID; 854780; -.
DR KEGG; sce:YIL031W; -.
DR SGD; S000001293; ULP2.
DR VEuPathDB; FungiDB:YIL031W; -.
DR eggNOG; KOG0779; Eukaryota.
DR GeneTree; ENSGT00940000172065; -.
DR HOGENOM; CLU_008911_0_0_1; -.
DR InParanoid; P40537; -.
DR OMA; FKPSLCY; -.
DR BioCyc; YEAST:G3O-31304-MON; -.
DR BRENDA; 3.4.22.B67; 984.
DR PRO; PR:P40537; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40537; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:SGD.
DR GO; GO:0016929; F:deSUMOylase activity; IDA:SGD.
DR GO; GO:0003711; F:transcription elongation regulator activity; IDA:SGD.
DR GO; GO:0030261; P:chromosome condensation; IMP:SGD.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:SGD.
DR GO; GO:0006276; P:plasmid maintenance; IMP:SGD.
DR GO; GO:0016926; P:protein desumoylation; IDA:SGD.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR Pfam; PF02902; Peptidase_C48; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Phosphoprotein; Protease; Reference proteome;
KW Thiol protease.
FT CHAIN 1..1034
FT /note="Ubiquitin-like-specific protease 2"
FT /id="PRO_0000101732"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 983
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 984
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:5LNB"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 446..449
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 460..476
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:5LNB"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 491..496
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 503..507
FT /evidence="ECO:0007829|PDB:5LNB"
FT TURN 508..513
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:5LNB"
FT STRAND 520..528
FT /evidence="ECO:0007829|PDB:5LNB"
FT STRAND 531..539
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 540..545
FT /evidence="ECO:0007829|PDB:5LNB"
FT STRAND 568..573
FT /evidence="ECO:0007829|PDB:5LNB"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 581..599
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 605..607
FT /evidence="ECO:0007829|PDB:5LNB"
FT STRAND 608..612
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 624..637
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 639..647
FT /evidence="ECO:0007829|PDB:5LNB"
FT TURN 648..650
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 654..664
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 667..670
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 673..694
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 698..703
FT /evidence="ECO:0007829|PDB:5LNB"
FT HELIX 832..839
FT /evidence="ECO:0007829|PDB:5V1A"
SQ SEQUENCE 1034 AA; 116883 MW; 782789B3B1DC37F6 CRC64;
MSARKRKFNS LKPLDTLNSS RASSPRSSAS LPPKRYNTFR KDPKIVDHLN NASTKDFLPV
LSMNSESKRQ IELSDNDVDN NDEGEGVNSG CSDQDFEPLQ SSPLKRHSSL KSTSNGLLFQ
MSNNLGNGSP EPAVASTSPN GSIISTKLNL NGQFSCVDSK TLRIYRHKAP CIMTFVSDHN
HPKFSLYFQQ SVIYNSQVNL LDDVELIILD KKNSFMAIIL KDLKKVKMIL DVNNSSININ
TNILIWSTAS SASNKKIKSI KRFLLMSYSS SIKVEILDHK EQILERLKHL IHPISSSSPS
LNMERAINST KNAFDSLRLK KTKLSTNDDE SPQIHTHFLS NKPHGLQSLT KRTRIASLGK
KEHSISVPKS NISPSDFYNT NGTETLQSHA VSQLRRSNRF KDVSDPANSN SNSEFDDATT
EFETPELFKP SLCYKFNDGS SYTITNQDFK CLFNKDWVND SILDFFTKFY IESSIEKSII
KREQVHLMSS FFYTKLISNP ADYYSNVKKW VNNTDLFSKK YVVIPINISY HWFSCIITNL
DAILDFHQNK DKNDAINSDE ISINNPLVNI LTFDSLRQTH SREIDPIKEF LISYALDKYS
IQLDKTQIKM KTCPVPQQPN MSDCGVHVIL NIRKFFENPV ETIDVWKNSK IKSKHFTAKM
INKYFDKNER NSARKNLRHT LKLLQLNYIS YLKKENLYEE VMQMEEKKST NINNNENYDD
DDEEIQIIEN IDQSSKDNNA QLTSEPPCSR SSSISTTERE PTELHNSVVR QPTGEIITDN
EDPVRAASPE TASVSPPIRH NILKSSSPFI SESANETEQE EFTSPYFGRP SLKTRAKQFE
GVSSPIKNDQ ALSSTHDIMM PSPKPKRIYP SKKIPQLSSH VQSLSTDSME RQSSPNNTNI
VISDTEQDSR LGVNSESKNT SGIVNRDDSD VNLIGSSLPN VAEKNHDNTQ ESNGNNDSLG
KILQNVDKEL NEKLVDIDDV AFSSPTRGIP RTSATSKGSN AQLLSNYGDE NNQSQDSVWD
EGRDNPILLE DEDP
