SGT1_MOUSE
ID SGT1_MOUSE Reviewed; 336 AA.
AC Q9CX34; Q3UF88; Q9CRE7; Q9D8M6;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 161.
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|MGI:MGI:1915205};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Embryo, Pancreas, Spinal cord, and Sympathetic ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AK007881; BAB25326.1; -; mRNA.
DR EMBL; AK020433; BAB32098.1; -; mRNA.
DR EMBL; AK045153; BAC32241.1; -; mRNA.
DR EMBL; AK082328; BAC38466.1; -; mRNA.
DR EMBL; AK141416; BAE24677.1; -; mRNA.
DR EMBL; AK148838; BAE28673.1; -; mRNA.
DR EMBL; BC009167; AAH09167.1; -; mRNA.
DR CCDS; CCDS36988.1; -.
DR RefSeq; NP_080750.1; NM_026474.5.
DR AlphaFoldDB; Q9CX34; -.
DR SMR; Q9CX34; -.
DR BioGRID; 212563; 19.
DR IntAct; Q9CX34; 1.
DR STRING; 10090.ENSMUSP00000052942; -.
DR iPTMnet; Q9CX34; -.
DR PhosphoSitePlus; Q9CX34; -.
DR SwissPalm; Q9CX34; -.
DR REPRODUCTION-2DPAGE; Q9CX34; -.
DR EPD; Q9CX34; -.
DR jPOST; Q9CX34; -.
DR MaxQB; Q9CX34; -.
DR PaxDb; Q9CX34; -.
DR PeptideAtlas; Q9CX34; -.
DR PRIDE; Q9CX34; -.
DR ProteomicsDB; 261016; -.
DR Antibodypedia; 24223; 262 antibodies from 31 providers.
DR DNASU; 67955; -.
DR Ensembl; ENSMUST00000054908; ENSMUSP00000052942; ENSMUSG00000022024.
DR GeneID; 67955; -.
DR KEGG; mmu:67955; -.
DR UCSC; uc007ute.1; mouse.
DR CTD; 10910; -.
DR MGI; MGI:1915205; Sugt1.
DR VEuPathDB; HostDB:ENSMUSG00000022024; -.
DR eggNOG; KOG0548; Eukaryota.
DR eggNOG; KOG1309; Eukaryota.
DR GeneTree; ENSGT00390000013700; -.
DR HOGENOM; CLU_039532_1_1_1; -.
DR InParanoid; Q9CX34; -.
DR OMA; WDKLVGD; -.
DR OrthoDB; 1426397at2759; -.
DR PhylomeDB; Q9CX34; -.
DR TreeFam; TF105979; -.
DR Reactome; R-MMU-844456; The NLRP3 inflammasome.
DR BioGRID-ORCS; 67955; 19 hits in 74 CRISPR screens.
DR ChiTaRS; Sugt1; mouse.
DR PRO; PR:Q9CX34; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9CX34; protein.
DR Bgee; ENSMUSG00000022024; Expressed in morula and 260 other tissues.
DR Genevisible; Q9CX34; MM.
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:MGI.
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:MGI.
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 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 /id="PRO_0000106333"
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 236
FT /note="Phosphothreonine"
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"
FT CONFLICT 20
FT /note="D -> N (in Ref. 1; BAB25326)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="T -> I (in Ref. 1; BAB25326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 38159 MW; 2A06CA65E9EB6289 CRC64;
MAAAAAGPAS SQRLFQSFSD ALIDGDPQAA LEELTKALEQ NPDDAQYYCQ RAYCHILLGK
YRDGIADVKK SLELNPNNCT ALLRKGICEY HEKDYASALE TFAEGQKLDS TDTNFDTWIK
RCQEIQNGSE SEVSASQRTQ SKIKYDWYQT ESHVIITLMI KSVQKNDVRV GFSERELSAL
VKIPAGEDYS LKLRLLHPII PEQSTFKVLS TKIEIKMKKP EAVRWEKLEG QGDEPTPKQF
TADVKNMYPS SSHYTRNWDK LVGEIKEEEK NEKLEGDAAL NKLFQQIYSD GSDEVKRAMN
KSFMESGGTV LSTNWSDVGK RKVEINPPDD MEWKQY
