STIP1_MOUSE
ID STIP1_MOUSE Reviewed; 543 AA.
AC Q60864; Q3TT16; Q8BPH3; Q99L66;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Stress-induced-phosphoprotein 1;
DE Short=STI1;
DE Short=mSTI1;
DE AltName: Full=Hsc70/Hsp90-organizing protein;
DE Short=Hop;
GN Name=Stip1;
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 [MRNA].
RC TISSUE=Lung carcinoma;
RX PubMed=9272871; DOI=10.1016/s0378-1119(97)00206-0;
RA Blatch G.L., Laessle M., Zetter B.R., Kundra V.;
RT "Isolation of a mouse cDNA encoding mSTI1, a stress-inducible protein
RT containing the TPR motif.";
RL Gene 194:277-282(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Liver, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [4]
RP PROTEIN SEQUENCE OF 1-10; 94-109; 124-136; 145-169; 306-315; 352-364;
RP 435-446; 506-513 AND 534-543, ACETYLATION AT MET-1, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Kidney;
RA Bienvenut W.V., Frezza C., Gottlieb E.;
RL Submitted (MAY-2009) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 14-44, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH HSPA8; HSPCA AND
RP HSPCB.
RX PubMed=8999875; DOI=10.1074/jbc.272.3.1876;
RA Laessle M., Blatch G.L., Kundra V., Takatori T., Zetter B.R.;
RT "Stress-inducible, murine protein mSTI1. Characterization of binding
RT domains for heat shock proteins and in vitro phosphorylation by different
RT kinases.";
RL J. Biol. Chem. 272:1876-1884(1997).
RN [7]
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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-325, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Acts as a co-chaperone for HSP90AA1. Mediates the association
CC of the molecular chaperones HSPA8/HSC70 and HSP90.
CC {ECO:0000250|UniProtKB:O35814, ECO:0000250|UniProtKB:P31948}.
CC -!- SUBUNIT: Probably forms a complex composed of chaperones HSP90 and
CC HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and
CC client protein TSC2 (By similarity). Forms a complex with HSPA8/HSC70,
CC HSPCA/HSP-86 and HSPCB/HSP-84 (PubMed:8999875). Interacts with PACRG.
CC Interacts with EEF1AKMT3 (By similarity). Interacts with
CC HSP90/HSP90AA1; the interaction dissociates the PPP5C:HSP90AA1
CC interaction. Interacts with FLCN, FNIP1 and FNIP2. Interacts with
CC HSPA8/HSC70 (By similarity). Interacts with HSP90AB1; upon SMYD2-
CC dependent HSP90AB1 methylation (By similarity).
CC {ECO:0000250|UniProtKB:O35814, ECO:0000250|UniProtKB:P31948,
CC ECO:0000269|PubMed:8999875}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8999875}. Nucleus
CC {ECO:0000269|PubMed:8999875}. Dynein axonemal particle
CC {ECO:0000250|UniProtKB:Q7ZWU1}.
CC -!- DOMAIN: The TPR 1 repeat interacts with the C-terminal of HSC70. The
CC TPR 4, 5 and 6 repeats (also called TPR2A domain) and TPR 7, 8 and 9
CC repeats (also called TPR2B domain) interact with HSP90 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: In vitro kinase assay failed to detect phosphorylation by
CC MAPKAPK2.
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DR EMBL; U27830; AAC53267.1; -; mRNA.
DR EMBL; AK075988; BAC36100.1; -; mRNA.
DR EMBL; AK088494; BAC40389.1; -; mRNA.
DR EMBL; AK149493; BAE28916.1; -; mRNA.
DR EMBL; AK161645; BAE36509.1; -; mRNA.
DR EMBL; AK167273; BAE39385.1; -; mRNA.
DR EMBL; BC003794; AAH03794.1; -; mRNA.
DR CCDS; CCDS37901.1; -.
DR RefSeq; NP_058017.1; NM_016737.2.
DR AlphaFoldDB; Q60864; -.
DR SMR; Q60864; -.
DR BioGRID; 203539; 26.
DR IntAct; Q60864; 7.
DR MINT; Q60864; -.
DR STRING; 10090.ENSMUSP00000025918; -.
DR iPTMnet; Q60864; -.
DR PhosphoSitePlus; Q60864; -.
DR SwissPalm; Q60864; -.
DR REPRODUCTION-2DPAGE; IPI00121514; -.
DR REPRODUCTION-2DPAGE; Q60864; -.
DR UCD-2DPAGE; Q60864; -.
DR CPTAC; non-CPTAC-3673; -.
DR CPTAC; non-CPTAC-3674; -.
DR EPD; Q60864; -.
DR jPOST; Q60864; -.
DR MaxQB; Q60864; -.
DR PaxDb; Q60864; -.
DR PeptideAtlas; Q60864; -.
DR PRIDE; Q60864; -.
DR ProteomicsDB; 258755; -.
DR Antibodypedia; 15273; 437 antibodies from 40 providers.
DR DNASU; 20867; -.
DR Ensembl; ENSMUST00000025918; ENSMUSP00000025918; ENSMUSG00000024966.
DR GeneID; 20867; -.
DR KEGG; mmu:20867; -.
DR UCSC; uc008gke.2; mouse.
DR CTD; 10963; -.
DR MGI; MGI:109130; Stip1.
DR VEuPathDB; HostDB:ENSMUSG00000024966; -.
DR eggNOG; KOG0548; Eukaryota.
DR GeneTree; ENSGT00940000154911; -.
DR HOGENOM; CLU_000134_46_5_1; -.
DR InParanoid; Q60864; -.
DR OMA; HYSKAWE; -.
DR OrthoDB; 933764at2759; -.
DR PhylomeDB; Q60864; -.
DR TreeFam; TF300478; -.
DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 20867; 18 hits in 73 CRISPR screens.
DR ChiTaRS; Stip1; mouse.
DR PRO; PR:Q60864; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q60864; protein.
DR Bgee; ENSMUSG00000024966; Expressed in morula and 267 other tissues.
DR Genevisible; Q60864; MM.
DR GO; GO:0101031; C:chaperone complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
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; ISO:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0098761; P:cellular response to interleukin-7; IDA:MGI.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR041243; STI1.
DR InterPro; IPR045248; Sti1-like.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR22904; PTHR22904; 1.
DR Pfam; PF17830; STI1; 2.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00727; STI1; 2.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 9.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; TPR repeat;
KW Ubl conjugation.
FT CHAIN 1..543
FT /note="Stress-induced-phosphoprotein 1"
FT /id="PRO_0000106373"
FT REPEAT 4..37
FT /note="TPR 1"
FT REPEAT 39..71
FT /note="TPR 2"
FT REPEAT 73..105
FT /note="TPR 3"
FT DOMAIN 130..169
FT /note="STI1 1"
FT REPEAT 225..258
FT /note="TPR 4"
FT REPEAT 260..292
FT /note="TPR 5"
FT REPEAT 300..333
FT /note="TPR 6"
FT REPEAT 360..393
FT /note="TPR 7"
FT REPEAT 395..427
FT /note="TPR 8"
FT REPEAT 428..461
FT /note="TPR 9"
FT DOMAIN 492..531
FT /note="STI1 2"
FT REGION 191..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 222..239
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 208..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 198
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 301
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 312
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 325
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 332
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 344
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 354
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 446
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT CONFLICT 15
FT /note="L -> P (in Ref. 2; BAC36100)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="L -> V (in Ref. 3; AAH03794)"
FT /evidence="ECO:0000305"
FT CONFLICT 274..279
FT /note="DYNKCR -> RLYKCT (in Ref. 2; BAC36100)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="V -> S (in Ref. 2; BAC36100)"
FT /evidence="ECO:0000305"
FT CONFLICT 305..310
FT /note="RIGNSY -> PNWQFL (in Ref. 2; BAC36100)"
FT /evidence="ECO:0000305"
FT CONFLICT 316..317
FT /note="YK -> VQ (in Ref. 2; BAC36100)"
FT /evidence="ECO:0000305"
FT CONFLICT 333..347
FT /note="PDVLKKCQQAEKILK -> QMCSRSASSQRNSE (in Ref. 2;
FT BAC36100)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 543 AA; 62582 MW; B737FBA92B198D6C CRC64;
MEQVNELKEK GNKALSAGNI DDALQCYSEA IKLDPQNHVL YSNRSAAYAK KGDYQKAYED
GCKTVDLKPD WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNLQLKE GLQNMEARLA
ERKFMNPFNL PNLYQKLEND PRTRSLLSDP TYRELIEQLQ NKPSDLGTKL QDPRVMTTLS
VLLGVDLGSM DEEEEAATPP PPPPPKKEPK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD
FDKALKHYDR AKELDPTNMT YITNQAAVHF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA
KAYARIGNSY FKEEKYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE RLAYINPDLA
LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PRDAKLYSNR AACYTKLLEF QLALKDCEEC
IQLEPTFIKG YTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD
SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI
AIR
