STIP1_HUMAN
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 03-AUG-2022, entry version 222.
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:9195923,
CC PubMed:27353360). 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; Q8IWD4: CCDC117; NbExp=2; 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=4; 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.
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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_001282652.1. [P31948-2]
DR RefSeq; NP_001269582.1; NM_001282653.1. [P31948-3]
DR RefSeq; NP_006810.1; NM_006819.2. [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 SMR; P31948; -.
DR BioGRID; 116162; 341.
DR DIP; DIP-41085N; -.
DR IntAct; P31948; 188.
DR MINT; P31948; -.
DR STRING; 9606.ENSP00000351646; -.
DR ChEMBL; CHEMBL4523216; -.
DR DrugBank; DB09130; Copper.
DR GlyGen; P31948; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P31948; -.
DR MetOSite; P31948; -.
DR PhosphoSitePlus; P31948; -.
DR SwissPalm; P31948; -.
DR BioMuta; STIP1; -.
DR DMDM; 400042; -.
DR REPRODUCTION-2DPAGE; IPI00013894; -.
DR UCD-2DPAGE; P31948; -.
DR EPD; P31948; -.
DR jPOST; P31948; -.
DR MassIVE; P31948; -.
DR MaxQB; P31948; -.
DR PaxDb; P31948; -.
DR PeptideAtlas; P31948; -.
DR PRIDE; P31948; -.
DR ProteomicsDB; 25436; -.
DR ProteomicsDB; 33721; -.
DR ProteomicsDB; 54820; -. [P31948-1]
DR TopDownProteomics; P31948-1; -. [P31948-1]
DR Antibodypedia; 15273; 437 antibodies from 40 providers.
DR DNASU; 10963; -.
DR Ensembl; ENST00000305218.9; ENSP00000305958.5; ENSG00000168439.17. [P31948-1]
DR Ensembl; ENST00000358794.9; ENSP00000351646.5; ENSG00000168439.17. [P31948-2]
DR Ensembl; ENST00000538945.5; ENSP00000445957.1; ENSG00000168439.17. [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 CTD; 10963; -.
DR DisGeNET; 10963; -.
DR GeneCards; STIP1; -.
DR HGNC; HGNC:11387; STIP1.
DR HPA; ENSG00000168439; Low tissue specificity.
DR MIM; 605063; gene.
DR neXtProt; NX_P31948; -.
DR OpenTargets; ENSG00000168439; -.
DR PharmGKB; PA36196; -.
DR VEuPathDB; HostDB:ENSG00000168439; -.
DR eggNOG; KOG0548; Eukaryota.
DR GeneTree; ENSGT00940000154911; -.
DR HOGENOM; CLU_000134_46_5_1; -.
DR InParanoid; P31948; -.
DR OMA; HYSKAWE; -.
DR OrthoDB; 933764at2759; -.
DR PhylomeDB; P31948; -.
DR TreeFam; TF300478; -.
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 BioGRID-ORCS; 10963; 94 hits in 1086 CRISPR screens.
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 201 other tissues.
DR ExpressionAtlas; P31948; baseline and differential.
DR Genevisible; P31948; HS.
DR GO; GO:0101031; C:chaperone complex; IDA:UniProtKB.
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:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
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 GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 3.
DR IDEAL; IID00449; -.
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; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR22904; PTHR22904; 1.
DR Pfam; PF17830; STI1; 2.
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; SSF48452; 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 Reference proteome; Repeat; TPR repeat; 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 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.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
