ID STIP1_HUMAN Reviewed; 543 AA. AC P31948; B4DM70; F5H0T1; G3XAD8; Q3ZCU9; Q5TZU9; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 28-JAN-2026, entry version 239. DE RecName: Full=Stress-induced-phosphoprotein 1; DE Short=STI1; DE AltName: Full=Hsc70/Hsp90-organizing protein; DE Short=Hop; DE AltName: Full=Renal carcinoma antigen NY-REN-11; DE AltName: Full=Transformation-sensitive protein IEF SSP 3521; GN Name=STIP1 {ECO:0000312|HGNC:HGNC:11387}; 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 1), AND PARTIAL PROTEIN SEQUENCE. RX PubMed=1569099; DOI=10.1016/s0021-9258(18)42471-4; RA Honore B., Leffers H., Madsen P., Rasmussen H.H., Vandekerckhove J., RA Celis J.E.; RT "Molecular cloning and expression of a transformation-sensitive human RT protein containing the TPR motif and sharing identity to the stress- RT inducible yeast protein STI1."; RL J. Biol. Chem. 267:8485-8491(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Lung, and Testis; 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 [8] RP PROTEIN SEQUENCE OF 1-10; 110-118; 345-364; 382-389; 479-486 AND 534-543, RP ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (OCT-2004) to UniProtKB. RN [9] RP PROTEIN SEQUENCE OF 33-44; 64-73; 79-87; 154-160; 253-272; 306-312; RP 352-364; 407-429; 454-462; 489-513 AND 534-543, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [10] RP PROTEIN SEQUENCE OF 101-109; 352-364 AND 374-381. RC TISSUE=Keratinocyte; RX PubMed=1286667; DOI=10.1002/elps.11501301199; RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., RA Vandekerckhove J.; RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein RT database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). RN [11] RP INTERACTION WITH HSP90AA1. RX PubMed=9195923; DOI=10.1074/jbc.272.26.16224; RA Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K., RA Chinkers M., Pratt W.B.; RT "Protein phosphatase 5 is a major component of glucocorticoid RT receptor.hsp90 complexes with properties of an FK506-binding RT immunophilin."; RL J. Biol. Chem. 272:16224-16230(1997). RN [12] RP IDENTIFICATION AS A RENAL CANCER ANTIGEN. RC TISSUE=Renal cell carcinoma; RX PubMed=10508479; RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5; RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., RA Old L.J.; RT "Antigens recognized by autologous antibody in patients with renal-cell RT carcinoma."; RL Int. J. Cancer 83:456-464(1999). RN [13] RP INTERACTION WITH PACRG. RX PubMed=14532270; DOI=10.1074/jbc.m309655200; RA Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.; RT "A product of the human gene adjacent to parkin is a component of Lewy RT bodies and suppresses Pael receptor-induced cell death."; RL J. Biol. Chem. 278:51901-51910(2003). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-354, AND IDENTIFICATION BY RP 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY RP 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 [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [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 [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-301; LYS-312; LYS-325; RP LYS-344 AND LYS-446, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE 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 [19] 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-332 AND SER-481, 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 [23] RP INTERACTION WITH EEF1AKMT3. RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210; RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.; RT "A newly uncovered group of distantly related lysine methyltransferases RT preferentially interact with molecular chaperones to regulate their RT activity."; RL PLoS Genet. 9:E1003210-E1003210(2013). RN [24] RP INTERACTION WITH HSP90AB1. RX PubMed=24880080; DOI=10.1016/j.canlet.2014.05.014; RA Hamamoto R., Toyokawa G., Nakakido M., Ueda K., Nakamura Y.; RT "SMYD2-dependent HSP90 methylation promotes cancer cell proliferation by RT regulating the chaperone complex formation."; RL Cancer Lett. 351:126-133(2014). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-198, AND IDENTIFICATION BY RP 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 [26] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-123, 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 [27] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-123 AND LYS-210, AND RP IDENTIFICATION BY MASS 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 [28] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-123, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [29] RP IDENTIFICATION BY MASS SPECTROMETRY [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 [30] RP FUNCTION, AND INTERACTION WITH HSP90AA1; FLCN; FNIP1 AND FNIP2. RX PubMed=27353360; DOI=10.1038/ncomms12037; RA Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D., RA Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W., RA Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S., Marston Linehan W., RA Bratslavsky G., Mollapour M.; RT "The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance RT drug binding."; RL Nat. Commun. 7:12037-12037(2016). RN [31] RP IDENTIFICATION IN A COMPLEX WITH HSP90; HSP70; PTGES3; CDC37; PPP5C; TSC1 RP AND TSC2. RX PubMed=29127155; DOI=10.15252/embj.201796700; RA Woodford M.R., Sager R.A., Marris E., Dunn D.M., Blanden A.R., Murphy R.L., RA Rensing N., Shapiro O., Panaretou B., Prodromou C., Loh S.N., Gutmann D.H., RA Bourboulia D., Bratslavsky G., Wong M., Mollapour M.; RT "Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding RT of kinase and non-kinase clients."; RL EMBO J. 36:3650-3665(2017). RN [32] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-123 AND LYS-210, AND RP IDENTIFICATION BY MASS 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 [33] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 223-349. RX PubMed=10786835; DOI=10.1016/s0092-8674(00)80830-2; RA Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L., RA Bartunik H., Hartl F.U., Moarefi I.; RT "Structure of TPR domain-peptide complexes: critical elements in the RT assembly of the Hsp70-Hsp90 multichaperone machine."; RL Cell 101:199-210(2000). CC -!- FUNCTION: Acts as a co-chaperone for HSP90AA1 (PubMed:27353360). CC Mediates the association of the molecular chaperones HSPA8/HSC70 and CC HSP90 (By similarity). {ECO:0000250|UniProtKB:O35814, CC ECO:0000303|PubMed:27353360}. 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 (PubMed:29127155). Forms a complex with CC HSPA8/HSC70, HSPCA/HSP-86 and HSPCB/HSP-84 (By similarity). Interacts CC with PACRG (PubMed:14532270). Interacts with EEF1AKMT3 CC (PubMed:23349634). Interacts with HSP90/HSP90AA1; the interaction CC dissociates the PPP5C:HSP90AA1 interaction (PubMed:27353360, CC PubMed:9195923). Interacts with FLCN, FNIP1 and FNIP2 CC (PubMed:27353360). Interacts with HSPA8/HSC70 (By similarity). CC Interacts with HSP90AB1; upon SMYD2-dependent HSP90AB1 methylation CC (PubMed:24880080). {ECO:0000250|UniProtKB:O35814, CC ECO:0000250|UniProtKB:Q60864, ECO:0000269|PubMed:14532270, CC ECO:0000269|PubMed:23349634, ECO:0000269|PubMed:24880080, CC ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:29127155, CC ECO:0000269|PubMed:9195923}. CC -!- INTERACTION: CC P31948; Q96AP0: ACD; NbExp=2; IntAct=EBI-1054052, EBI-717666; CC P31948; Q6DHV7-2: ADAL; NbExp=3; IntAct=EBI-1054052, EBI-18899653; CC P31948; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-1054052, EBI-18036948; CC P31948; O15484: CAPN5; NbExp=2; IntAct=EBI-1054052, EBI-2932457; CC P31948; Q8IWD4: CCDC117; NbExp=6; IntAct=EBI-1054052, EBI-3387963; CC P31948; Q7L3B6: CDC37L1; NbExp=2; IntAct=EBI-1054052, EBI-2841876; CC P31948; O95674: CDS2; NbExp=3; IntAct=EBI-1054052, EBI-3913685; CC P31948; P00533: EGFR; NbExp=3; IntAct=EBI-1054052, EBI-297353; CC P31948; O00423: EML1; NbExp=3; IntAct=EBI-1054052, EBI-751327; CC P31948; P04626: ERBB2; NbExp=2; IntAct=EBI-1054052, EBI-641062; CC P31948; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-1054052, EBI-8468186; CC P31948; Q3SYB3: FOXD4L6; NbExp=3; IntAct=EBI-1054052, EBI-6425864; CC P31948; Q06547-3: GABPB1; NbExp=3; IntAct=EBI-1054052, EBI-9088619; CC P31948; P08238: HSP90AB1; NbExp=6; IntAct=EBI-1054052, EBI-352572; CC P31948; P01106: MYC; NbExp=3; IntAct=EBI-1054052, EBI-447544; CC P31948; Q14181: POLA2; NbExp=3; IntAct=EBI-1054052, EBI-712752; CC P31948; P53041: PPP5C; NbExp=4; IntAct=EBI-1054052, EBI-716663; CC P31948; Q09028: RBBP4; NbExp=3; IntAct=EBI-1054052, EBI-620823; CC P31948; Q9C004: SPRY4; NbExp=3; IntAct=EBI-1054052, EBI-354861; CC P31948; P54274-2: TERF1; NbExp=3; IntAct=EBI-1054052, EBI-711018; CC P31948; P04637: TP53; NbExp=4; IntAct=EBI-1054052, EBI-366083; CC P31948; O00463: TRAF5; NbExp=3; IntAct=EBI-1054052, EBI-523498; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q60864}. Nucleus CC {ECO:0000250|UniProtKB:Q60864}. Dynein axonemal particle CC {ECO:0000250|UniProtKB:Q7ZWU1}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P31948-1; Sequence=Displayed; CC Name=2; CC IsoId=P31948-2; Sequence=VSP_055034; CC Name=3; CC IsoId=P31948-3; Sequence=VSP_055035; 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M86752; AAA58682.1; -; mRNA. DR EMBL; BT020010; AAV38813.1; -; mRNA. DR EMBL; BT020011; AAV38814.1; -; mRNA. DR EMBL; CR536512; CAG38750.1; -; mRNA. DR EMBL; AK297319; BAG59782.1; -; mRNA. DR EMBL; AP005668; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471076; EAW74196.1; -; Genomic_DNA. DR EMBL; CH471076; EAW74197.1; -; Genomic_DNA. DR EMBL; BC002987; AAH02987.1; -; mRNA. DR EMBL; BC039299; AAH39299.1; -; mRNA. DR CCDS; CCDS60827.1; -. [P31948-2] DR CCDS; CCDS60828.1; -. [P31948-3] DR CCDS; CCDS8058.1; -. [P31948-1] DR PIR; A38093; A38093. DR RefSeq; NP_001269581.1; NM_001282652.2. [P31948-2] DR RefSeq; NP_001269582.1; NM_001282653.2. [P31948-3] DR RefSeq; NP_006810.1; NM_006819.3. [P31948-1] DR PDB; 1ELR; X-ray; 1.90 A; A=223-352. DR PDB; 1ELW; X-ray; 1.60 A; A/B=1-118. DR PDB; 2LNI; NMR; -; A=356-477. DR PDB; 2NC9; NMR; -; A=220-350. DR PDB; 3ESK; X-ray; 2.05 A; A=223-350. DR PDB; 3FWV; X-ray; 2.20 A; A/B=223-349. DR PDB; 7KW7; EM; 3.57 A; E=1-543. DR PDBsum; 1ELR; -. DR PDBsum; 1ELW; -. DR PDBsum; 2LNI; -. DR PDBsum; 2NC9; -. DR PDBsum; 3ESK; -. DR PDBsum; 3FWV; -. DR PDBsum; 7KW7; -. DR AlphaFoldDB; P31948; -. DR EMDB; EMD-23050; -. DR EMDB; EMD-5981; -. DR SMR; P31948; -. DR BioGRID; 116162; 1071. DR CORUM; P31948; -. DR DIP; DIP-41085N; -. DR FunCoup; P31948; 3000. DR IntAct; P31948; 259. DR MINT; P31948; -. DR STRING; 9606.ENSP00000351646; -. DR ChEMBL; CHEMBL4523216; -. DR DrugBank; DB09130; Copper. DR GlyCosmos; P31948; 2 sites, 1 glycan. DR GlyGen; P31948; 4 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (3 sites). DR iPTMnet; P31948; -. DR MetOSite; P31948; -. DR PhosphoSitePlus; P31948; -. DR SwissPalm; P31948; -. DR BioMuta; STIP1; -. DR DMDM; 400042; -. DR REPRODUCTION-2DPAGE; IPI00013894; -. DR jPOST; P31948; -. DR MassIVE; P31948; -. DR PaxDb; 9606-ENSP00000351646; -. DR PeptideAtlas; P31948; -. DR ProteomicsDB; 25436; -. DR ProteomicsDB; 33721; -. DR ProteomicsDB; 54820; -. [P31948-1] DR Pumba; P31948; -. DR TopDownProteomics; P31948-1; -. [P31948-1] DR Antibodypedia; 15273; 445 antibodies from 41 providers. DR DNASU; 10963; -. DR Ensembl; ENST00000305218.9; ENSP00000305958.5; ENSG00000168439.18. [P31948-1] DR Ensembl; ENST00000358794.9; ENSP00000351646.5; ENSG00000168439.18. [P31948-2] DR Ensembl; ENST00000538945.5; ENSP00000445957.1; ENSG00000168439.18. [P31948-3] DR GeneID; 10963; -. DR KEGG; hsa:10963; -. DR MANE-Select; ENST00000305218.9; ENSP00000305958.5; NM_006819.3; NP_006810.1. DR UCSC; uc010rnb.2; human. [P31948-1] DR AGR; HGNC:11387; -. DR ClinPGx; PA36196; -. DR CTD; 10963; -. DR DisGeNET; 10963; -. DR GeneCards; STIP1; -. DR HGNC; HGNC:11387; STIP1. DR HPA; ENSG00000168439; Low tissue specificity. DR MIM; 605063; gene. DR OpenTargets; ENSG00000168439; -. DR VEuPathDB; HostDB:ENSG00000168439; -. DR eggNOG; KOG0548; Eukaryota. DR GeneTree; ENSGT00940000154911; -. DR HOGENOM; CLU_000134_46_5_1; -. DR InParanoid; P31948; -. DR OMA; MYSAREN; -. DR OrthoDB; 2423701at2759; -. DR PAN-GO; P31948; 1 GO annotation based on evolutionary models. DR PhylomeDB; P31948; -. DR PathwayCommons; P31948; -. DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand. DR Reactome; R-HSA-9696273; RND1 GTPase cycle. DR SignaLink; P31948; -. DR SIGNOR; P31948; -. DR Agora; ENSG00000168439; -. DR BioGRID-ORCS; 10963; 106 hits in 1166 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; DEE660B4; Stress granule. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; STIP1; human. DR EvolutionaryTrace; P31948; -. DR GeneWiki; Hop_(protein); -. DR GenomeRNAi; 10963; -. DR Pharos; P31948; Tbio. DR PRO; PR:P31948; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P31948; protein. DR Bgee; ENSG00000168439; Expressed in adrenal tissue and 203 other cell types or tissues. DR ExpressionAtlas; P31948; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc. DR GO; GO:0005634; C:nucleus; TAS:UniProtKB. DR GO; GO:0101031; C:protein folding chaperone complex; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0051879; F:Hsp90 protein binding; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0098761; P:cellular response to interleukin-7; IEA:Ensembl. DR FunFam; 1.10.260.100:FF:000004; Putative stress-induced-phosphoprotein 1; 1. DR FunFam; 1.25.40.10:FF:000010; Stress-induced phosphoprotein 1; 1. DR FunFam; 1.25.40.10:FF:000020; Stress-induced phosphoprotein 1; 1. DR FunFam; 1.10.260.100:FF:000002; Stress-induced-phosphoprotein 1 (Hsp70/Hsp90-organizing); 1. DR FunFam; 1.25.40.10:FF:000027; stress-induced-phosphoprotein 1 isoform X1; 1. DR Gene3D; 1.10.260.100; -; 2. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3. DR IDEAL; IID00449; -. DR InterPro; IPR041243; STI1/HOP_DP. DR InterPro; IPR006636; STI1_HS-bd. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR013105; TPR_2. DR InterPro; IPR019734; TPR_rpt. DR PANTHER; PTHR22904:SF523; STRESS-INDUCED-PHOSPHOPROTEIN 1; 1. DR PANTHER; PTHR22904; TPR REPEAT CONTAINING PROTEIN; 1. DR Pfam; PF17830; STI1-HOP_DP; 2. DR Pfam; PF13414; TPR_11; 2. DR Pfam; PF13424; TPR_12; 1. DR Pfam; PF07719; TPR_2; 1. DR Pfam; PF13181; TPR_8; 1. DR SMART; SM00727; STI1; 2. DR SMART; SM00028; TPR; 9. DR SUPFAM; SSF48452; TPR-like; 3. DR PROSITE; PS50005; TPR; 9. DR PROSITE; PS50293; TPR_REGION; 2. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Repeat; TPR repeat; KW Ubl conjugation. FT CHAIN 1..543 FT /note="Stress-induced-phosphoprotein 1" FT /id="PRO_0000106372" FT REPEAT 4..37 FT /note="TPR 1" FT REPEAT 38..71 FT /note="TPR 2" FT REPEAT 72..105 FT /note="TPR 3" FT DOMAIN 130..169 FT /note="STI1 1" FT REPEAT 225..258 FT /note="TPR 4" FT REPEAT 259..292 FT /note="TPR 5" FT REPEAT 300..333 FT /note="TPR 6" FT REPEAT 360..393 FT /note="TPR 7" FT REPEAT 394..427 FT /note="TPR 8" FT REPEAT 428..461 FT /note="TPR 9" FT DOMAIN 492..531 FT /note="STI1 2" FT REGION 192..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 205..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.8, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT MOD_RES 8 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 16 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 198 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 301 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 312 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 325 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 332 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 344 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 354 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT MOD_RES 446 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 481 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT CROSSLNK 123 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 123 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:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 210 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 210 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..3 FT /note="MEQ -> MESGSPMGEVEISRTIRTNGRGQRGYDWQCKRPIRVAEVRSSLHS FT WSLRW (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_055034" FT VAR_SEQ 74..97 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055035" FT CONFLICT 84 FT /note="F -> L (in Ref. 7; AAH39299)" FT /evidence="ECO:0000305" FT CONFLICT 364 FT /note="K -> E (in Ref. 4; BAG59782)" FT /evidence="ECO:0000305" FT CONFLICT 533 FT /note="K -> R (in Ref. 4; BAG59782)" FT /evidence="ECO:0000305" FT HELIX 3..16 FT /evidence="ECO:0007829|PDB:1ELW" FT HELIX 20..33 FT /evidence="ECO:0007829|PDB:1ELW" FT HELIX 38..51 FT /evidence="ECO:0007829|PDB:1ELW" FT HELIX 54..67 FT /evidence="ECO:0007829|PDB:1ELW" FT HELIX 72..84 FT /evidence="ECO:0007829|PDB:1ELW" FT HELIX 88..99 FT /evidence="ECO:0007829|PDB:1ELW" FT HELIX 106..117 FT /evidence="ECO:0007829|PDB:1ELW" FT HELIX 223..237 FT /evidence="ECO:0007829|PDB:1ELR" FT HELIX 241..254 FT /evidence="ECO:0007829|PDB:1ELR" FT HELIX 259..272 FT /evidence="ECO:0007829|PDB:1ELR" FT HELIX 275..291 FT /evidence="ECO:0007829|PDB:1ELR" FT HELIX 296..312 FT /evidence="ECO:0007829|PDB:1ELR" FT HELIX 316..329 FT /evidence="ECO:0007829|PDB:1ELR" FT HELIX 333..348 FT /evidence="ECO:0007829|PDB:1ELR" FT HELIX 359..372 FT /evidence="ECO:0007829|PDB:2LNI" FT HELIX 377..387 FT /evidence="ECO:0007829|PDB:2LNI" FT HELIX 394..404 FT /evidence="ECO:0007829|PDB:2LNI" FT TURN 405..408 FT /evidence="ECO:0007829|PDB:2LNI" FT HELIX 410..423 FT /evidence="ECO:0007829|PDB:2LNI" FT HELIX 428..440 FT /evidence="ECO:0007829|PDB:2LNI" FT HELIX 444..457 FT /evidence="ECO:0007829|PDB:2LNI" FT HELIX 459..462 FT /evidence="ECO:0007829|PDB:2LNI" FT HELIX 463..475 FT /evidence="ECO:0007829|PDB:2LNI" SQ SEQUENCE 543 AA; 62639 MW; 8E58ECA13825CB0E CRC64; MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK KGDYQKAYED GCKTVDLKPD WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNPQLKE GLQNMEARLA ERKFMNPFNM PNLYQKLESD PRTRTLLSDP TYRELIEQLR NKPSDLGTKL QDPRIMTTLS VLLGVDLGSM DEEEEIATPP PPPPPKKETK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDTALKHYDK AKELDPTNMT YITNQAAVYF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA KAYARIGNSY FKEEKYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PKDAKLYSNR AACYTKLLEF QLALKDCEEC IQLEPTFIKG YTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR //