Full text data of SUGT1
SUGT1
[Confidence: low (only semi-automatic identification from reviews)]
Suppressor of G2 allele of SKP1 homolog (Protein 40-6-3; Sgt1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Suppressor of G2 allele of SKP1 homolog (Protein 40-6-3; Sgt1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y2Z0
ID SUGT1_HUMAN Reviewed; 365 AA.
AC Q9Y2Z0; A2A303; Q5JAK5; Q5TAM6; Q6VXY6;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Suppressor of G2 allele of SKP1 homolog;
DE AltName: Full=Protein 40-6-3;
DE AltName: Full=Sgt1;
GN Name=SUGT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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 2).
RA Schmidt T.;
RL Thesis (2001), University of Goettingen, Germany.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Zou X., Mao Y., Xie Y.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
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
RT 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.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA 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.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA 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.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric 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 MASS 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
RT other 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
RT 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, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT THR-265 AND SER-331, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
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.,
RA 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
CC proteasomal degradation of target proteins.
CC -!- SUBUNIT: Probably associates with SCF (SKP1-CUL1-F-box protein)
CC complex through interaction with SKP1. Interacts with S100A6.
CC Interacts with HSP90.
CC -!- INTERACTION:
CC O75427:LRCH4; NbExp=2; IntAct=EBI-307008, EBI-718707;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates to the
CC nucleus upon heat shock, requiring S100A6.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y2Z0-1; Sequence=Displayed;
CC Name=2;
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
CC promotes nuclear translocation, most likely due to disruption of
CC the SUGT1-HSP90 complex.
CC -!- SIMILARITY: Belongs to the SUGT1 family.
CC -!- SIMILARITY: Contains 1 CS domain.
CC -!- SIMILARITY: Contains 1 SGS domain.
CC -!- SIMILARITY: Contains 3 TPR repeats.
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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; CAI17072.1; -; Genomic_DNA.
DR EMBL; AL139089; CAM23909.1; -; Genomic_DNA.
DR EMBL; CH471124; EAW52045.1; -; Genomic_DNA.
DR EMBL; BC000911; AAH00911.1; -; mRNA.
DR RefSeq; NP_001124384.1; NM_001130912.1.
DR RefSeq; NP_006695.1; NM_006704.3.
DR UniGene; Hs.281902; -.
DR PDB; 1RL1; NMR; -; A=167-276.
DR PDBsum; 1RL1; -.
DR ProteinModelPortal; Q9Y2Z0; -.
DR SMR; Q9Y2Z0; 30-111, 170-261.
DR IntAct; Q9Y2Z0; 12.
DR MINT; MINT-5005759; -.
DR STRING; 9606.ENSP00000367208; -.
DR PhosphoSite; Q9Y2Z0; -.
DR DMDM; 62512186; -.
DR PaxDb; Q9Y2Z0; -.
DR PRIDE; Q9Y2Z0; -.
DR DNASU; 10910; -.
DR Ensembl; ENST00000310528; ENSP00000308067; ENSG00000165416.
DR Ensembl; ENST00000343788; ENSP00000367208; ENSG00000165416.
DR GeneID; 10910; -.
DR KEGG; hsa:10910; -.
DR UCSC; uc001vhc.2; human.
DR CTD; 10910; -.
DR GeneCards; GC13P053226; -.
DR H-InvDB; HIX0026254; -.
DR H-InvDB; HIX0201992; -.
DR HGNC; HGNC:16987; SUGT1.
DR HPA; CAB015942; -.
DR MIM; 604098; gene.
DR neXtProt; NX_Q9Y2Z0; -.
DR PharmGKB; PA134880121; -.
DR eggNOG; COG0457; -.
DR HOGENOM; HOG000248210; -.
DR HOVERGEN; HBG055080; -.
DR InParanoid; Q9Y2Z0; -.
DR KO; K12795; -.
DR OMA; SFIDEDP; -.
DR OrthoDB; EOG7WX0B4; -.
DR Reactome; REACT_6900; Immune System.
DR EvolutionaryTrace; Q9Y2Z0; -.
DR GeneWiki; SUGT1; -.
DR GenomeRNAi; 10910; -.
DR NextBio; 41435; -.
DR PRO; PR:Q9Y2Z0; -.
DR ArrayExpress; Q9Y2Z0; -.
DR Bgee; Q9Y2Z0; -.
DR CleanEx; HS_SUGT1; -.
DR Genevestigator; Q9Y2Z0; -.
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:0000151; C:ubiquitin ligase complex; TAS:ProtInc.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0007067; P:mitosis; TAS:ProtInc.
DR GO; GO:0035872; P:nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; TAS:Reactome.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR007699; SGS.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF05002; SGS; 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; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 365 Suppressor of G2 allele of SKP1 homolog.
FT /FTId=PRO_0000106332.
FT REPEAT 11 44 TPR 1.
FT REPEAT 45 78 TPR 2.
FT REPEAT 79 112 TPR 3.
FT DOMAIN 169 258 CS.
FT DOMAIN 276 365 SGS.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 265 265 Phosphothreonine.
FT MOD_RES 281 281 Phosphoserine.
FT MOD_RES 331 331 Phosphoserine.
FT VAR_SEQ 110 142 IETGFHRVGQAGLQLLTSSDPPALDSQSAGITG -> S
FT (in isoform 2).
FT /FTId=VSP_013420.
FT CONFLICT 120 120 A -> V (in Ref. 4; AAQ01749).
FT STRAND 174 178
FT STRAND 180 187
FT HELIX 194 196
FT STRAND 197 200
FT STRAND 202 204
FT STRAND 206 211
FT STRAND 215 222
FT STRAND 224 226
FT HELIX 230 232
FT STRAND 233 237
FT STRAND 239 247
FT STRAND 255 258
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
//
ID SUGT1_HUMAN Reviewed; 365 AA.
AC Q9Y2Z0; A2A303; Q5JAK5; Q5TAM6; Q6VXY6;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Suppressor of G2 allele of SKP1 homolog;
DE AltName: Full=Protein 40-6-3;
DE AltName: Full=Sgt1;
GN Name=SUGT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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 2).
RA Schmidt T.;
RL Thesis (2001), University of Goettingen, Germany.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Zou X., Mao Y., Xie Y.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
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
RT 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.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA 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.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA 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.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric 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 MASS 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
RT other 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
RT 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, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT THR-265 AND SER-331, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
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.,
RA 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
CC proteasomal degradation of target proteins.
CC -!- SUBUNIT: Probably associates with SCF (SKP1-CUL1-F-box protein)
CC complex through interaction with SKP1. Interacts with S100A6.
CC Interacts with HSP90.
CC -!- INTERACTION:
CC O75427:LRCH4; NbExp=2; IntAct=EBI-307008, EBI-718707;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates to the
CC nucleus upon heat shock, requiring S100A6.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y2Z0-1; Sequence=Displayed;
CC Name=2;
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
CC promotes nuclear translocation, most likely due to disruption of
CC the SUGT1-HSP90 complex.
CC -!- SIMILARITY: Belongs to the SUGT1 family.
CC -!- SIMILARITY: Contains 1 CS domain.
CC -!- SIMILARITY: Contains 1 SGS domain.
CC -!- SIMILARITY: Contains 3 TPR repeats.
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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; CAI17072.1; -; Genomic_DNA.
DR EMBL; AL139089; CAM23909.1; -; Genomic_DNA.
DR EMBL; CH471124; EAW52045.1; -; Genomic_DNA.
DR EMBL; BC000911; AAH00911.1; -; mRNA.
DR RefSeq; NP_001124384.1; NM_001130912.1.
DR RefSeq; NP_006695.1; NM_006704.3.
DR UniGene; Hs.281902; -.
DR PDB; 1RL1; NMR; -; A=167-276.
DR PDBsum; 1RL1; -.
DR ProteinModelPortal; Q9Y2Z0; -.
DR SMR; Q9Y2Z0; 30-111, 170-261.
DR IntAct; Q9Y2Z0; 12.
DR MINT; MINT-5005759; -.
DR STRING; 9606.ENSP00000367208; -.
DR PhosphoSite; Q9Y2Z0; -.
DR DMDM; 62512186; -.
DR PaxDb; Q9Y2Z0; -.
DR PRIDE; Q9Y2Z0; -.
DR DNASU; 10910; -.
DR Ensembl; ENST00000310528; ENSP00000308067; ENSG00000165416.
DR Ensembl; ENST00000343788; ENSP00000367208; ENSG00000165416.
DR GeneID; 10910; -.
DR KEGG; hsa:10910; -.
DR UCSC; uc001vhc.2; human.
DR CTD; 10910; -.
DR GeneCards; GC13P053226; -.
DR H-InvDB; HIX0026254; -.
DR H-InvDB; HIX0201992; -.
DR HGNC; HGNC:16987; SUGT1.
DR HPA; CAB015942; -.
DR MIM; 604098; gene.
DR neXtProt; NX_Q9Y2Z0; -.
DR PharmGKB; PA134880121; -.
DR eggNOG; COG0457; -.
DR HOGENOM; HOG000248210; -.
DR HOVERGEN; HBG055080; -.
DR InParanoid; Q9Y2Z0; -.
DR KO; K12795; -.
DR OMA; SFIDEDP; -.
DR OrthoDB; EOG7WX0B4; -.
DR Reactome; REACT_6900; Immune System.
DR EvolutionaryTrace; Q9Y2Z0; -.
DR GeneWiki; SUGT1; -.
DR GenomeRNAi; 10910; -.
DR NextBio; 41435; -.
DR PRO; PR:Q9Y2Z0; -.
DR ArrayExpress; Q9Y2Z0; -.
DR Bgee; Q9Y2Z0; -.
DR CleanEx; HS_SUGT1; -.
DR Genevestigator; Q9Y2Z0; -.
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:0000151; C:ubiquitin ligase complex; TAS:ProtInc.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0007067; P:mitosis; TAS:ProtInc.
DR GO; GO:0035872; P:nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; TAS:Reactome.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR007699; SGS.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF05002; SGS; 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; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 365 Suppressor of G2 allele of SKP1 homolog.
FT /FTId=PRO_0000106332.
FT REPEAT 11 44 TPR 1.
FT REPEAT 45 78 TPR 2.
FT REPEAT 79 112 TPR 3.
FT DOMAIN 169 258 CS.
FT DOMAIN 276 365 SGS.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 265 265 Phosphothreonine.
FT MOD_RES 281 281 Phosphoserine.
FT MOD_RES 331 331 Phosphoserine.
FT VAR_SEQ 110 142 IETGFHRVGQAGLQLLTSSDPPALDSQSAGITG -> S
FT (in isoform 2).
FT /FTId=VSP_013420.
FT CONFLICT 120 120 A -> V (in Ref. 4; AAQ01749).
FT STRAND 174 178
FT STRAND 180 187
FT HELIX 194 196
FT STRAND 197 200
FT STRAND 202 204
FT STRAND 206 211
FT STRAND 215 222
FT STRAND 224 226
FT HELIX 230 232
FT STRAND 233 237
FT STRAND 239 247
FT STRAND 255 258
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
//
MIM
604098
*RECORD*
*FIELD* NO
604098
*FIELD* TI
*604098 SUPPRESSOR OF G2 ALLELE OF SKP1, S. CEREVISIAE, HOMOLOG OF; SUGT1
;;SGT1
*FIELD* TX
read more
CLONING
Kitagawa et al. (1999) identified the S. cerevisiae SGT1 (suppressor of
G2 allele of SKP1) gene, which, like SKP1 (see 601434), is required for
both the G1/S and G2/M transitions in the cell cycle. The SGT1 protein
physically associates with the SKP1 protein and the SCF (SKP1/Cdc53/F
box protein) ubiquitin ligase complex (see 603134) and is required for
kinetochore function, where it serves as an activator of the Ctf13
protein. Kitagawa et al. (1999) also cloned the human homolog of the
yeast SGT1 gene. The yeast and human SGT1 proteins share 26% identity
and 30% similarity. Human SGT1 could perform the essential functions of
SGT1 in budding yeast, indicating that SGT1 function is conserved
throughout eukaryotes.
MAPPING
Gross (2012) mapped the SUGT1 gene to chromosome 13q14.3 based on an
alignment of the SUGT1 sequence (GenBank GENBANK AF132856) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Gross, M. B.: Personal Communication. Baltimore, Md. 6/12/2012.
2. Kitagawa, K.; Skowyra, D.; Elledge, S. J.; Harper, J. W.; Hieter,
P.: SGT1 encodes an essential component of the yeast kinetochore
assembly pathway and a novel subunit of the SCF ubiquitin ligase complex. Molec.
Cell 4: 21-33, 1999.
*FIELD* CN
Matthew B. Gross - updated: 06/12/2012
*FIELD* CD
Stylianos E. Antonarakis: 8/3/1999
*FIELD* ED
mgross: 06/12/2012
carol: 6/8/2012
mgross: 11/12/2002
mgross: 8/3/1999
*RECORD*
*FIELD* NO
604098
*FIELD* TI
*604098 SUPPRESSOR OF G2 ALLELE OF SKP1, S. CEREVISIAE, HOMOLOG OF; SUGT1
;;SGT1
*FIELD* TX
read more
CLONING
Kitagawa et al. (1999) identified the S. cerevisiae SGT1 (suppressor of
G2 allele of SKP1) gene, which, like SKP1 (see 601434), is required for
both the G1/S and G2/M transitions in the cell cycle. The SGT1 protein
physically associates with the SKP1 protein and the SCF (SKP1/Cdc53/F
box protein) ubiquitin ligase complex (see 603134) and is required for
kinetochore function, where it serves as an activator of the Ctf13
protein. Kitagawa et al. (1999) also cloned the human homolog of the
yeast SGT1 gene. The yeast and human SGT1 proteins share 26% identity
and 30% similarity. Human SGT1 could perform the essential functions of
SGT1 in budding yeast, indicating that SGT1 function is conserved
throughout eukaryotes.
MAPPING
Gross (2012) mapped the SUGT1 gene to chromosome 13q14.3 based on an
alignment of the SUGT1 sequence (GenBank GENBANK AF132856) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Gross, M. B.: Personal Communication. Baltimore, Md. 6/12/2012.
2. Kitagawa, K.; Skowyra, D.; Elledge, S. J.; Harper, J. W.; Hieter,
P.: SGT1 encodes an essential component of the yeast kinetochore
assembly pathway and a novel subunit of the SCF ubiquitin ligase complex. Molec.
Cell 4: 21-33, 1999.
*FIELD* CN
Matthew B. Gross - updated: 06/12/2012
*FIELD* CD
Stylianos E. Antonarakis: 8/3/1999
*FIELD* ED
mgross: 06/12/2012
carol: 6/8/2012
mgross: 11/12/2002
mgross: 8/3/1999