UBP1_HUMAN
ID UBP1_HUMAN Reviewed; 785 AA.
AC O94782; A0PJ95; D3DQ57; Q05BX7; Q59H66; Q9UFR0; Q9UNJ3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 1;
DE EC=3.4.19.12 {ECO:0000269|PubMed:15694335, ECO:0000269|PubMed:16531995, ECO:0000269|PubMed:18082604, ECO:0000269|PubMed:26388029, ECO:0000269|PubMed:9806842};
DE AltName: Full=Deubiquitinating enzyme 1;
DE Short=hUBP;
DE AltName: Full=Ubiquitin thioesterase 1;
DE AltName: Full=Ubiquitin-specific-processing protease 1;
DE Contains:
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 1, N-terminal fragment {ECO:0000303|PubMed:29775578};
GN Name=USP1;
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 [MRNA], AND CATALYTIC ACTIVITY.
RC TISSUE=Fetal brain;
RX PubMed=9806842; DOI=10.1006/geno.1998.5554;
RA Fjiwara T., Saito A., Suzuki M., Shinomiya H., Suzuki T., Takahashi E.,
RA Tanigami A., Ichiyama A., Chung C.H., Nakamura Y., Tanaka K.;
RT "Identification and chromosomal assignment of USP1, a novel gene encoding a
RT human ubiquitin-specific protease.";
RL Genomics 54:155-158(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Seibold S., Marx M.;
RT "Molecular cloning of a novel human ubiquitin-specific protease.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, Testis, and Uterus;
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, UBIQUITINATION,
RP INTERACTION WITH FANCD2, MUTAGENESIS OF CYS-90, CATALYTIC ACTIVITY, AND
RP ACTIVE SITE.
RX PubMed=15694335; DOI=10.1016/j.molcel.2005.01.008;
RA Nijman S.M.B., Huang T.T., Dirac A.M.G., Brummelkamp T.R., Kerkhoven R.M.,
RA D'Andrea A.D., Bernards R.;
RT "The deubiquitinating enzyme USP1 regulates the Fanconi Anemia pathway.";
RL Mol. Cell 17:331-339(2005).
RN [8]
RP FUNCTION, CLEAVAGE SITE, MUTAGENESIS OF CYS-90 AND 670-GLY-GLY-671,
RP CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX PubMed=16531995; DOI=10.1038/ncb1378;
RA Huang T.T., Nijman S.M.B., Mirchandani K.D., Galardy P.J., Cohn M.A.,
RA Haas W., Gygi S.P., Ploegh H.L., Bernards R., D'Andrea A.D.;
RT "Regulation of monoubiquitinated PCNA by DUB autocleavage.";
RL Nat. Cell Biol. 8:339-347(2006).
RN [9]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, INTERACTION
RP WITH WDR48, AND INDUCTION.
RX PubMed=18082604; DOI=10.1016/j.molcel.2007.09.031;
RA Cohn M.A., Kowal P., Yang K., Haas W., Huang T.T., Gygi S.P.,
RA D'Andrea A.D.;
RT "A UAF1-containing multisubunit protein complex regulates the Fanconi
RT anemia pathway.";
RL Mol. Cell 28:786-797(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, 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 [12]
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 [13]
RP FUNCTION, AND INTERACTION WITH ATAD5.
RX PubMed=20147293; DOI=10.1074/jbc.m109.092544;
RA Lee K.Y., Yang K., Cohn M.A., Sikdar N., D'Andrea A.D., Myung K.;
RT "Human ELG1 regulates the level of ubiquitinated proliferating cell nuclear
RT antigen (PCNA) through Its interactions with PCNA and USP1.";
RL J. Biol. Chem. 285:10362-10369(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-42; SER-67; SER-313
RP AND SER-475, 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 [17]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH WDR48, MUTAGENESIS OF CYS-90
RP AND GLU-444, AND ACTIVE SITE.
RX PubMed=26388029; DOI=10.1016/j.str.2015.08.010;
RA Yin J., Schoeffler A.J., Wickliffe K., Newton K., Starovasnik M.A.,
RA Dueber E.C., Harris S.F.;
RT "Structural insights into WD-repeat 48 activation of ubiquitin-specific
RT protease 46.";
RL Structure 23:2043-2054(2015).
RN [18]
RP UBIQUITINATION.
RX PubMed=29775578; DOI=10.1016/j.molcel.2018.04.006;
RA Lin H.C., Yeh C.W., Chen Y.F., Lee T.T., Hsieh P.Y., Rusnac D.V., Lin S.Y.,
RA Elledge S.J., Zheng N., Yen H.S.;
RT "C-terminal end-directed protein elimination by CRL2 ubiquitin ligases.";
RL Mol. Cell 70:602-613(2018).
RN [19] {ECO:0007744|PDB:6DO5}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 666-671 IN COMPLEX WITH KLHDC2,
RP AND UBIQUITINATION.
RX PubMed=30526872; DOI=10.1016/j.molcel.2018.10.021;
RA Rusnac D.V., Lin H.C., Canzani D., Tien K.X., Hinds T.R., Tsue A.F.,
RA Bush M.F., Yen H.S., Zheng N.;
RT "Recognition of the diglycine C-end degron by CRL2(KLHDC2) ubiquitin
RT ligase.";
RL Mol. Cell 72:813-822(2018).
CC -!- FUNCTION: Negative regulator of DNA damage repair which specifically
CC deubiquitinates monoubiquitinated FANCD2 (PubMed:15694335). Also
CC involved in PCNA-mediated translesion synthesis (TLS) by
CC deubiquitinating monoubiquitinated PCNA (PubMed:16531995,
CC PubMed:20147293). Has almost no deubiquitinating activity by itself and
CC requires the interaction with WDR48 to have a high activity
CC (PubMed:18082604, PubMed:26388029). {ECO:0000269|PubMed:15694335,
CC ECO:0000269|PubMed:16531995, ECO:0000269|PubMed:18082604,
CC ECO:0000269|PubMed:20147293, ECO:0000269|PubMed:26388029}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:15694335,
CC ECO:0000269|PubMed:16531995, ECO:0000269|PubMed:18082604,
CC ECO:0000269|PubMed:26388029, ECO:0000269|PubMed:9806842};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 uM for ubiquitin vinyl sulfone (in presence of WDR48)
CC {ECO:0000269|PubMed:18082604};
CC KM=1.4 uM for ubiquitin vinyl sulfone (in absence of WDR48)
CC {ECO:0000269|PubMed:18082604};
CC -!- SUBUNIT: Interacts with FANCD2 and PCNA (PubMed:15694335,
CC PubMed:16531995). Interacts with WDR48 (PubMed:18082604,
CC PubMed:26388029). Interacts with ATAD5; the interaction regulates USP1-
CC mediated PCNA deubiquitination (PubMed:20147293).
CC {ECO:0000269|PubMed:15694335, ECO:0000269|PubMed:16531995,
CC ECO:0000269|PubMed:18082604, ECO:0000269|PubMed:20147293,
CC ECO:0000269|PubMed:26388029}.
CC -!- INTERACTION:
CC O94782; Q8TAF3-1: WDR48; NbExp=2; IntAct=EBI-2513396, EBI-16178048;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15694335}.
CC -!- DEVELOPMENTAL STAGE: Cell cycle-regulated. Highest level during S
CC phase. {ECO:0000269|PubMed:15694335}.
CC -!- INDUCTION: Down-regulated following DNA damage.
CC {ECO:0000269|PubMed:18082604}.
CC -!- PTM: Autocatalytic cleavage of USP1 following UV irradiation
CC inactivates it leading to an increase in ubiquitinated PCNA,
CC recruitment of POLH and translesion synthesis.
CC {ECO:0000269|PubMed:15694335, ECO:0000269|PubMed:16531995}.
CC -!- PTM: [Ubiquitin carboxyl-terminal hydrolase 1, N-terminal fragment]:
CC Ubiquitinated by the CRL2(KLHDC2) complex following autocatalytic
CC cleavage, leading to its degradation: the CRL2(KLHDC2) complex
CC recognizes the diglycine (Gly-Gly) at the C-terminus.
CC {ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:30526872}.
CC -!- MISCELLANEOUS: HEK293T cells expressing reduced levels of USP1 show a
CC higher level of ubiquitinated PCNA and an increase in point mutations
CC upon UV irradiation.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH18745.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH32364.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAD92130.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB014458; BAA34703.1; -; mRNA.
DR EMBL; AF117386; AAD11441.1; -; mRNA.
DR EMBL; AL117575; CAB55999.1; -; mRNA.
DR EMBL; AL117503; CAB55967.1; -; mRNA.
DR EMBL; AB208893; BAD92130.1; ALT_FRAME; mRNA.
DR EMBL; CH471059; EAX06585.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06586.1; -; Genomic_DNA.
DR EMBL; BC050525; AAH50525.1; -; mRNA.
DR EMBL; BC018745; AAH18745.1; ALT_SEQ; mRNA.
DR EMBL; BC032364; AAH32364.1; ALT_SEQ; mRNA.
DR CCDS; CCDS621.1; -.
DR PIR; T17309; T17309.
DR RefSeq; NP_001017415.1; NM_001017415.1.
DR RefSeq; NP_001017416.1; NM_001017416.1.
DR RefSeq; NP_003359.3; NM_003368.4.
DR PDB; 6DO5; X-ray; 2.50 A; C/D=666-671.
DR PDB; 7AY0; X-ray; 3.60 A; B/D=67-785.
DR PDB; 7AY1; EM; 3.70 A; D=1-785.
DR PDB; 7AY2; X-ray; 3.20 A; B/E=67-785.
DR PDBsum; 6DO5; -.
DR PDBsum; 7AY0; -.
DR PDBsum; 7AY1; -.
DR PDBsum; 7AY2; -.
DR AlphaFoldDB; O94782; -.
DR SMR; O94782; -.
DR BioGRID; 113241; 106.
DR CORUM; O94782; -.
DR DIP; DIP-53609N; -.
DR IntAct; O94782; 37.
DR MINT; O94782; -.
DR STRING; 9606.ENSP00000343526; -.
DR BindingDB; O94782; -.
DR ChEMBL; CHEMBL1795087; -.
DR DrugCentral; O94782; -.
DR GuidetoPHARMACOLOGY; 2428; -.
DR MEROPS; C19.019; -.
DR iPTMnet; O94782; -.
DR PhosphoSitePlus; O94782; -.
DR BioMuta; USP1; -.
DR OGP; O94782; -.
DR CPTAC; CPTAC-952; -.
DR EPD; O94782; -.
DR jPOST; O94782; -.
DR MassIVE; O94782; -.
DR MaxQB; O94782; -.
DR PaxDb; O94782; -.
DR PeptideAtlas; O94782; -.
DR PRIDE; O94782; -.
DR ProteomicsDB; 50441; -.
DR Antibodypedia; 33332; 357 antibodies from 34 providers.
DR DNASU; 7398; -.
DR Ensembl; ENST00000339950.5; ENSP00000343526.4; ENSG00000162607.13.
DR Ensembl; ENST00000371146.5; ENSP00000360188.1; ENSG00000162607.13.
DR GeneID; 7398; -.
DR KEGG; hsa:7398; -.
DR MANE-Select; ENST00000339950.5; ENSP00000343526.4; NM_003368.5; NP_003359.3.
DR UCSC; uc001daj.3; human.
DR CTD; 7398; -.
DR DisGeNET; 7398; -.
DR GeneCards; USP1; -.
DR HGNC; HGNC:12607; USP1.
DR HPA; ENSG00000162607; Low tissue specificity.
DR MIM; 603478; gene.
DR neXtProt; NX_O94782; -.
DR OpenTargets; ENSG00000162607; -.
DR PharmGKB; PA37233; -.
DR VEuPathDB; HostDB:ENSG00000162607; -.
DR eggNOG; KOG1864; Eukaryota.
DR GeneTree; ENSGT00910000144243; -.
DR HOGENOM; CLU_019874_0_0_1; -.
DR InParanoid; O94782; -.
DR OMA; HAIQDVN; -.
DR OrthoDB; 439300at2759; -.
DR PhylomeDB; O94782; -.
DR TreeFam; TF331057; -.
DR PathwayCommons; O94782; -.
DR Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR SignaLink; O94782; -.
DR SIGNOR; O94782; -.
DR BioGRID-ORCS; 7398; 140 hits in 1123 CRISPR screens.
DR ChiTaRS; USP1; human.
DR GeneWiki; USP1; -.
DR GenomeRNAi; 7398; -.
DR Pharos; O94782; Tchem.
DR PRO; PR:O94782; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O94782; protein.
DR Bgee; ENSG00000162607; Expressed in secondary oocyte and 210 other tissues.
DR ExpressionAtlas; O94782; baseline and differential.
DR Genevisible; O94782; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; EXP:Reactome.
DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; IMP:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; IDA:UniProtKB.
DR GO; GO:0009411; P:response to UV; IDA:UniProtKB.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR GO; GO:0019985; P:translesion synthesis; TAS:Reactome.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd02671; Peptidase_C19O; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR033815; USP1.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; DNA damage; DNA repair; Hydrolase;
KW Nucleus; Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..785
FT /note="Ubiquitin carboxyl-terminal hydrolase 1"
FT /id="PRO_0000080615"
FT CHAIN 1..671
FT /note="Ubiquitin carboxyl-terminal hydrolase 1, N-terminal
FT fragment"
FT /id="PRO_0000453162"
FT DOMAIN 81..785
FT /note="USP"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:15694335,
FT ECO:0000269|PubMed:16531995, ECO:0000269|PubMed:26388029"
FT ACT_SITE 593
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT SITE 671..672
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:16531995"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJQ2"
FT MUTAGEN 90
FT /note="C->S: Loss of catalytic activity including
FT autolysis."
FT /evidence="ECO:0000269|PubMed:15694335,
FT ECO:0000269|PubMed:16531995, ECO:0000269|PubMed:26388029"
FT MUTAGEN 444
FT /note="E->K: Strongly reduces interaction with WDR48 and
FT activation by WDR48."
FT /evidence="ECO:0000269|PubMed:26388029"
FT MUTAGEN 670..671
FT /note="GG->AA: Loss of autolysis-mediated degradation upon
FT UV irradiation. No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:16531995"
FT CONFLICT 621
FT /note="I -> M (in Ref. 2; AAD11441)"
FT /evidence="ECO:0000305"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:7AY2"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:7AY2"
FT HELIX 105..118
FT /evidence="ECO:0007829|PDB:7AY2"
FT HELIX 141..165
FT /evidence="ECO:0007829|PDB:7AY2"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:7AY2"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:7AY2"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:7AY2"
FT HELIX 200..224
FT /evidence="ECO:0007829|PDB:7AY2"
FT HELIX 425..429
FT /evidence="ECO:0007829|PDB:7AY2"
FT STRAND 432..440
FT /evidence="ECO:0007829|PDB:7AY2"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:7AY2"
FT STRAND 446..461
FT /evidence="ECO:0007829|PDB:7AY2"
FT HELIX 485..493
FT /evidence="ECO:0007829|PDB:7AY2"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:7AY2"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:7AY2"
FT TURN 507..510
FT /evidence="ECO:0007829|PDB:7AY2"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:7AY2"
FT STRAND 515..521
FT /evidence="ECO:0007829|PDB:7AY2"
FT STRAND 526..533
FT /evidence="ECO:0007829|PDB:7AY2"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:7AY2"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:7AY2"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:7AY2"
FT HELIX 565..567
FT /evidence="ECO:0007829|PDB:7AY2"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:7AY2"
FT STRAND 576..585
FT /evidence="ECO:0007829|PDB:7AY2"
FT STRAND 587..591
FT /evidence="ECO:0007829|PDB:7AY2"
FT STRAND 593..599
FT /evidence="ECO:0007829|PDB:7AY2"
FT TURN 667..670
FT /evidence="ECO:0007829|PDB:6DO5"
FT STRAND 747..751
FT /evidence="ECO:0007829|PDB:7AY2"
FT STRAND 754..758
FT /evidence="ECO:0007829|PDB:7AY2"
FT HELIX 760..767
FT /evidence="ECO:0007829|PDB:7AY2"
FT STRAND 775..784
FT /evidence="ECO:0007829|PDB:7AY2"
SQ SEQUENCE 785 AA; 88207 MW; 50AA2817A60810AF CRC64;
MPGVIPSESN GLSRGSPSKK NRLSLKFFQK KETKRALDFT DSQENEEKAS EYRASEIDQV
VPAAQSSPIN CEKRENLLPF VGLNNLGNTC YLNSILQVLY FCPGFKSGVK HLFNIISRKK
EALKDEANQK DKGNCKEDSL ASYELICSLQ SLIISVEQLQ ASFLLNPEKY TDELATQPRR
LLNTLRELNP MYEGYLQHDA QEVLQCILGN IQETCQLLKK EEVKNVAELP TKVEEIPHPK
EEMNGINSIE MDSMRHSEDF KEKLPKGNGK RKSDTEFGNM KKKVKLSKEH QSLEENQRQT
RSKRKATSDT LESPPKIIPK YISENESPRP SQKKSRVKIN WLKSATKQPS ILSKFCSLGK
ITTNQGVKGQ SKENECDPEE DLGKCESDNT TNGCGLESPG NTVTPVNVNE VKPINKGEEQ
IGFELVEKLF QGQLVLRTRC LECESLTERR EDFQDISVPV QEDELSKVEE SSEISPEPKT
EMKTLRWAIS QFASVERIVG EDKYFCENCH HYTEAERSLL FDKMPEVITI HLKCFAASGL
EFDCYGGGLS KINTPLLTPL KLSLEEWSTK PTNDSYGLFA VVMHSGITIS SGHYTASVKV
TDLNSLELDK GNFVVDQMCE IGKPEPLNEE EARGVVENYN DEEVSIRVGG NTQPSKVLNK
KNVEAIGLLG GQKSKADYEL YNKASNPDKV ASTAFAENRN SETSDTTGTH ESDRNKESSD
QTGINISGFE NKISYVVQSL KEYEGKWLLF DDSEVKVTEE KDFLNSLSPS TSPTSTPYLL
FYKKL
