SGT1_RAT
ID SGT1_RAT Reviewed; 336 AA.
AC B0BN85;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Protein SGT1 homolog {ECO:0000250|UniProtKB:Q08446};
DE AltName: Full=Suppressor of G2 allele of SKP1 homolog {ECO:0000250|UniProtKB:Q08446};
GN Name=Sugt1 {ECO:0000312|RGD:1307550};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Translocates the to nucleus upon heat shock, requiring S100A6.
CC {ECO:0000250}.
CC -!- DOMAIN: The CS domain mediates interaction with HSP90. {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-252 and Ser-302, dephosphorylation promotes
CC nuclear translocation, most likely due to disruption of the SUGT1-HSP90
CC complex. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SGT1 family. {ECO:0000305}.
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DR EMBL; BC158724; AAI58725.1; -; mRNA.
DR RefSeq; NP_001013069.1; NM_001013051.1.
DR AlphaFoldDB; B0BN85; -.
DR SMR; B0BN85; -.
DR BioGRID; 253191; 1.
DR STRING; 10116.ENSRNOP00000017086; -.
DR iPTMnet; B0BN85; -.
DR PhosphoSitePlus; B0BN85; -.
DR jPOST; B0BN85; -.
DR PaxDb; B0BN85; -.
DR PeptideAtlas; B0BN85; -.
DR PRIDE; B0BN85; -.
DR Ensembl; ENSRNOT00000118088; ENSRNOP00000095924; ENSRNOG00000012594.
DR GeneID; 290408; -.
DR KEGG; rno:290408; -.
DR UCSC; RGD:1307550; rat.
DR CTD; 10910; -.
DR RGD; 1307550; Sugt1.
DR eggNOG; KOG0548; Eukaryota.
DR eggNOG; KOG1309; Eukaryota.
DR GeneTree; ENSGT00390000013700; -.
DR HOGENOM; CLU_039532_1_1_1; -.
DR InParanoid; B0BN85; -.
DR OMA; WDKLVGD; -.
DR OrthoDB; 1426397at2759; -.
DR PhylomeDB; B0BN85; -.
DR TreeFam; TF105979; -.
DR Reactome; R-RNO-844456; The NLRP3 inflammasome.
DR PRO; PR:B0BN85; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000012594; Expressed in pancreas and 20 other tissues.
DR ExpressionAtlas; B0BN85; baseline and differential.
DR Genevisible; B0BN85; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; 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:0000250|UniProtKB:Q9Y2Z0"
FT CHAIN 2..336
FT /note="Protein SGT1 homolog"
FT /evidence="ECO:0000250"
FT /id="PRO_0000330902"
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 140..229
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT DOMAIN 247..336
FT /note="SGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00386"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z0"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z0"
FT MOD_RES 255
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z0"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z0"
FT CROSSLNK 266
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z0"
FT CROSSLNK 266
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z0"
SQ SEQUENCE 336 AA; 38091 MW; 8C4C4014113AEB9A CRC64;
MAAAAAGPAS SQRFFQSFPD ALIDGDPQAA LEELTKALEQ NPDDAQYYCQ RAYCHILLGK
YCDGIADVKK SLELNPNNST ALLRKGICEY YEKDYASALE TFAEGQKLDG TDTNFDIWIK
RCQEIQNGSE PEVSASQRTQ SKIKYDWYQT ESHVIITLMI KNVQKNDVRV DFSEKELSAV
VKIPSGEDCS LKLRLLHPII PEQSTFKVLS TKIEIKMKKP EAVRWEKLEG QGDVPAPKQF
TADVKNMYPS SSHYTRNWDK LVGEIKEEEK NEKLEGDAAL NKLFQQIYSD GSDEVKRAMN
KSFMESGGTV LSTNWSDVGK RKVEINPPDD MEWKQY
