SGT1_HUMAN
ID SGT1_HUMAN Reviewed; 365 AA.
AC Q9Y2Z0; A2A303; Q5JAK5; Q5TAM6; Q6VXY6;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Protein SGT1 homolog {ECO:0000250|UniProtKB:Q08446};
DE AltName: Full=Protein 40-6-3 {ECO:0000312|EMBL:CAC51433.1};
DE AltName: Full=Sgt1 {ECO:0000303|PubMed:10445024};
DE AltName: Full=Suppressor of G2 allele of SKP1 homolog {ECO:0000250|UniProtKB:Q08446};
GN Name=SUGT1 {ECO:0000312|HGNC:HGNC:16987};
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] (ISOFORM 2), AND SUBUNIT.
RX PubMed=10445024; DOI=10.1016/s1097-2765(00)80184-7;
RA Kitagawa K., Skowyra D., Elledge S.J., Harper J.W., Hieter P.;
RT "SGT1 encodes an essential component of the yeast kinetochore assembly
RT pathway and a novel subunit of the SCF ubiquitin ligase complex.";
RL Mol. Cell 4:21-33(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=15018354; DOI=10.1080/10425170310001623644;
RA Niikura Y., Kitagawa K.;
RT "Identification of a novel splice variant: human SGT1B (SUGT1B).";
RL DNA Seq. 14:436-441(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15346769; DOI=10.1080/1042517032000160215;
RA Zou X., Ji C., Wang L., Wu M., Zheng H., Xu J., Jin F., Gu S., Ying K.,
RA Xie Y., Mao Y.;
RT "Molecular cloning and characterization of SGT1.2, a novel splice variant
RT of Homo sapiens SGT1.";
RL DNA Seq. 15:140-143(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Schmidt T.;
RL Thesis (2001), University of Goettingen, Germany.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cervix;
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 [9]
RP PROTEIN SEQUENCE OF 2-13.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [10]
RP PROTEIN SEQUENCE OF 2-13; 195-204; 222-236 AND 312-326, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [11]
RP INTERACTION WITH S100A6.
RX PubMed=12746458; DOI=10.1074/jbc.m211518200;
RA Nowotny M., Spiechowicz M., Jastrzebska B., Filipek A., Kitagawa K.,
RA Kuznicki J.;
RT "Calcium-regulated interaction of Sgt1 with S100A6 (calcyclin) and other
RT S100 proteins.";
RL J. Biol. Chem. 278:26923-26928(2003).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-265 AND SER-331, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [16]
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 [17]
RP PHOSPHORYLATION AT SER-281 AND SER-331, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH S100A6.
RX PubMed=21864708; DOI=10.1016/j.biocel.2011.08.010;
RA Prus W., Zabka M., Bieganowski P., Filipek A.;
RT "Nuclear translocation of Sgt1 depends on its phosphorylation state.";
RL Int. J. Biochem. Cell Biol. 43:1747-1753(2011).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-265 AND THR-284, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [21]
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 [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-295, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-295, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-295, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [26]
RP STRUCTURE BY NMR OF 167-276, AND INTERACTION WITH HSP90.
RX PubMed=14761955; DOI=10.1074/jbc.m400215200;
RA Lee Y.-T., Jacob J., Michowski W., Nowotny M., Kuznicki J., Chazin W.J.;
RT "Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the
RT tetratricopeptide repeat domain.";
RL J. Biol. Chem. 279:16511-16517(2004).
CC -!- FUNCTION: May play a role in ubiquitination and subsequent proteasomal
CC degradation of target proteins.
CC -!- SUBUNIT: Probably associates with SCF (SKP1-CUL1-F-box protein) complex
CC through interaction with SKP1. Interacts with S100A6. Interacts with
CC HSP90. {ECO:0000269|PubMed:10445024, ECO:0000269|PubMed:12746458,
CC ECO:0000269|PubMed:14761955, ECO:0000269|PubMed:21864708}.
CC -!- INTERACTION:
CC Q9Y2Z0; O75427: LRCH4; NbExp=2; IntAct=EBI-307008, EBI-718707;
CC Q9Y2Z0; Q9Y239: NOD1; NbExp=5; IntAct=EBI-307008, EBI-1051262;
CC Q9Y2Z0; A0A0H3NF38: sspH2; Xeno; NbExp=7; IntAct=EBI-307008, EBI-10689860;
CC Q9Y2Z0-2; P08238: HSP90AB1; NbExp=2; IntAct=EBI-10768076, EBI-352572;
CC Q9Y2Z0-2; P63208: SKP1; NbExp=2; IntAct=EBI-10768076, EBI-307486;
CC Q9Y2Z0-2; A0A0H3NF38: sspH2; Xeno; NbExp=2; IntAct=EBI-10768076, EBI-10689860;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21864708}. Nucleus
CC {ECO:0000269|PubMed:21864708}. Note=Translocates to the nucleus upon
CC heat shock, requiring S100A6.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=SGT1B {ECO:0000303|PubMed:15018354}, SUGT1B
CC {ECO:0000303|PubMed:15018354}, SGT1.2 {ECO:0000303|PubMed:15346769};
CC IsoId=Q9Y2Z0-1; Sequence=Displayed;
CC Name=2; Synonyms=SGT1A, SUGT1A {ECO:0000303|PubMed:15018354};
CC IsoId=Q9Y2Z0-2; Sequence=VSP_013420;
CC -!- DOMAIN: The CS domain mediates interaction with HSP90.
CC -!- PTM: Phosphorylated at Ser-281 and Ser-331, dephosphorylation promotes
CC nuclear translocation, most likely due to disruption of the SUGT1-HSP90
CC complex. {ECO:0000269|PubMed:21864708}.
CC -!- SIMILARITY: Belongs to the SGT1 family. {ECO:0000305}.
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DR EMBL; AF132856; AAD30062.1; -; mRNA.
DR EMBL; AJ344097; CAC51433.1; -; mRNA.
DR EMBL; AY321358; AAQ76039.1; -; mRNA.
DR EMBL; AY271314; AAQ01749.1; -; mRNA.
DR EMBL; BT009798; AAP88800.1; -; mRNA.
DR EMBL; AL139089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471124; EAW52045.1; -; Genomic_DNA.
DR EMBL; BC000911; AAH00911.1; -; mRNA.
DR CCDS; CCDS45050.1; -. [Q9Y2Z0-1]
DR CCDS; CCDS9436.1; -. [Q9Y2Z0-2]
DR RefSeq; NP_001124384.1; NM_001130912.2. [Q9Y2Z0-1]
DR RefSeq; NP_001307760.1; NM_001320831.1.
DR RefSeq; NP_006695.1; NM_006704.4. [Q9Y2Z0-2]
DR PDB; 1RL1; NMR; -; A=167-276.
DR PDBsum; 1RL1; -.
DR AlphaFoldDB; Q9Y2Z0; -.
DR BMRB; Q9Y2Z0; -.
DR SMR; Q9Y2Z0; -.
DR BioGRID; 116115; 199.
DR DIP; DIP-53799N; -.
DR IntAct; Q9Y2Z0; 107.
DR MINT; Q9Y2Z0; -.
DR STRING; 9606.ENSP00000367208; -.
DR GlyConnect; 638; 1 N-Linked glycan (1 site).
DR GlyGen; Q9Y2Z0; 2 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y2Z0; -.
DR MetOSite; Q9Y2Z0; -.
DR PhosphoSitePlus; Q9Y2Z0; -.
DR SwissPalm; Q9Y2Z0; -.
DR BioMuta; SUGT1; -.
DR DMDM; 62512186; -.
DR EPD; Q9Y2Z0; -.
DR jPOST; Q9Y2Z0; -.
DR MassIVE; Q9Y2Z0; -.
DR MaxQB; Q9Y2Z0; -.
DR PaxDb; Q9Y2Z0; -.
DR PeptideAtlas; Q9Y2Z0; -.
DR PRIDE; Q9Y2Z0; -.
DR ProteomicsDB; 85940; -. [Q9Y2Z0-1]
DR ProteomicsDB; 85941; -. [Q9Y2Z0-2]
DR Antibodypedia; 24223; 262 antibodies from 31 providers.
DR DNASU; 10910; -.
DR Ensembl; ENST00000310528.9; ENSP00000308067.7; ENSG00000165416.15. [Q9Y2Z0-2]
DR Ensembl; ENST00000343788.10; ENSP00000367208.4; ENSG00000165416.15. [Q9Y2Z0-1]
DR GeneID; 10910; -.
DR KEGG; hsa:10910; -.
DR MANE-Select; ENST00000310528.9; ENSP00000308067.7; NM_006704.5; NP_006695.1. [Q9Y2Z0-2]
DR UCSC; uc001vhb.3; human. [Q9Y2Z0-1]
DR CTD; 10910; -.
DR DisGeNET; 10910; -.
DR GeneCards; SUGT1; -.
DR HGNC; HGNC:16987; SUGT1.
DR HPA; ENSG00000165416; Low tissue specificity.
DR MIM; 604098; gene.
DR neXtProt; NX_Q9Y2Z0; -.
DR OpenTargets; ENSG00000165416; -.
DR PharmGKB; PA134880121; -.
DR VEuPathDB; HostDB:ENSG00000165416; -.
DR eggNOG; KOG0548; Eukaryota.
DR eggNOG; KOG1309; Eukaryota.
DR GeneTree; ENSGT00390000013700; -.
DR HOGENOM; CLU_039532_1_1_1; -.
DR InParanoid; Q9Y2Z0; -.
DR OMA; WDKLVGD; -.
DR PhylomeDB; Q9Y2Z0; -.
DR TreeFam; TF105979; -.
DR PathwayCommons; Q9Y2Z0; -.
DR Reactome; R-HSA-844456; The NLRP3 inflammasome.
DR Reactome; R-HSA-9660826; Purinergic signaling in leishmaniasis infection.
DR SignaLink; Q9Y2Z0; -.
DR SIGNOR; Q9Y2Z0; -.
DR BioGRID-ORCS; 10910; 445 hits in 1081 CRISPR screens.
DR ChiTaRS; SUGT1; human.
DR EvolutionaryTrace; Q9Y2Z0; -.
DR GeneWiki; SUGT1; -.
DR GenomeRNAi; 10910; -.
DR Pharos; Q9Y2Z0; Tbio.
DR PRO; PR:Q9Y2Z0; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9Y2Z0; protein.
DR Bgee; ENSG00000165416; Expressed in kidney epithelium and 192 other tissues.
DR Genevisible; Q9Y2Z0; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; TAS:ProtInc.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:ProtInc.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; IDA:AgBase.
DR DisProt; DP02834; -.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR007699; SGS_dom.
DR InterPro; IPR044563; Sgt1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45862; PTHR45862; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF05002; SGS; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
DR PROSITE; PS51048; SGS; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.10,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..365
FT /note="Protein SGT1 homolog"
FT /id="PRO_0000106332"
FT REPEAT 11..44
FT /note="TPR 1"
FT REPEAT 45..78
FT /note="TPR 2"
FT REPEAT 79..112
FT /note="TPR 3"
FT DOMAIN 169..258
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT DOMAIN 276..365
FT /note="SGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00386"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 265
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21864708"
FT MOD_RES 284
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21864708,
FT ECO:0007744|PubMed:20068231"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 110..142
FT /note="IETGFHRVGQAGLQLLTSSDPPALDSQSAGITG -> S (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:10445024,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4,
FT ECO:0000303|Ref.5"
FT /id="VSP_013420"
FT CONFLICT 120
FT /note="A -> V (in Ref. 3; AAQ01749)"
FT /evidence="ECO:0000305"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:1RL1"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:1RL1"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1RL1"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:1RL1"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1RL1"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1RL1"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:1RL1"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:1RL1"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:1RL1"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:1RL1"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:1RL1"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:1RL1"
SQ SEQUENCE 365 AA; 41024 MW; 4A5A413E70561D9A CRC64;
MAAAAAGTAT SQRFFQSFSD ALIDEDPQAA LEELTKALEQ KPDDAQYYCQ RAYCHILLGN
YCVAVADAKK SLELNPNNST AMLRKGICEY HEKNYAAALE TFTEGQKLDI ETGFHRVGQA
GLQLLTSSDP PALDSQSAGI TGADANFSVW IKRCQEAQNG SESEVWTHQS KIKYDWYQTE
SQVVITLMIK NVQKNDVNVE FSEKELSALV KLPSGEDYNL KLELLHPIIP EQSTFKVLST
KIEIKLKKPE AVRWEKLEGQ GDVPTPKQFV ADVKNLYPSS SPYTRNWDKL VGEIKEEEKN
EKLEGDAALN RLFQQIYSDG SDEVKRAMNK SFMESGGTVL STNWSDVGKR KVEINPPDDM
EWKKY
