ID STIP1_HUMAN Reviewed; 543 AA. AC P31948; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 20-FEB-2007, entry version 76. DE Stress-induced-phosphoprotein 1 (STI1) (Hsc70/Hsp90-organizing DE protein) (Hop) (Transformation-sensitive protein IEF SSP 3521) (NY- DE REN-11 antigen). GN Name=STIP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RX MEDLINE=92235077; PubMed=1569099; 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]. RC TISSUE=Lung; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 1-10; 110-118; 345-364; 382-389; 479-486 AND RP 534-543, ACETYLATION AT MET-1, AND MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Unpublished observations (OCT-2004). RN [4] RP PROTEIN SEQUENCE OF 101-109; 352-364 AND 374-381. RC TISSUE=Keratinocyte; RX MEDLINE=93162043; PubMed=1286667; 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 RT protein database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). RN [5] RP IDENTIFICATION AS A RENAL CANCER ANTIGEN. RC TISSUE=Renal cell carcinoma; RX MEDLINE=99438124; 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- RT cell carcinoma."; RL Int. J. Cancer 83:456-464(1999). RN [6] 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-354, AND MASS RP SPECTROMETRY. 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 RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND MASS RP SPECTROMETRY. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-246, AND MASS SPECTROMETRY. RX PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026; RA Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., RA Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; RT "Substrate and functional diversity of lysine acetylation revealed by RT a proteomics survey."; RL Mol. Cell 23:607-618(2006). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 223-349. RX MEDLINE=20246507; 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: Mediates the association of the molecular chaperones CC HSC70 and HSP90 (HSPCA and HSPCB). CC -!- SUBUNIT: Forms a complex with HSC70 and HSPCA/HSP-86 and CC HSPCB/HSP-84. Interacts with PACRG. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- DOMAIN: The TPR 1 repeat interacts with the C-terminal of HSC70. CC The TPR 4, 5 and 6 repeats (also called TPR2A domain) and TPR 7, 8 CC and 9 repeats (also called TPR2B domain) interact with HSP90. CC -!- SIMILARITY: Contains 2 STI1 domains. CC -!- SIMILARITY: Contains 9 TPR repeats. 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; BC002987; AAH02987.1; -; mRNA. DR PIR; A38093; A38093. DR UniGene; Hs.337295; -. DR PDB; 1ELR; X-ray; A=223-352. DR PDB; 1ELW; X-ray; A/B=1-118. DR Aarhus/Ghent-2DPAGE; 2410; IEF. DR REPRODUCTION-2DPAGE; P31948; HUMAN. DR Ensembl; ENSG00000168439; Homo sapiens. DR KEGG; hsa:10963; -. DR H-InvDB; HIX0019658; -. DR HGNC; HGNC:11387; STIP1. DR MIM; 605063; gene. DR LinkHub; P31948; -. DR ArrayExpress; P31948; -. DR GermOnline; ENSG00000168439; Homo sapiens. DR RZPD-ProtExp; F0314; -. DR RZPD-ProtExp; RZPDo834C0722; -. DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc. DR GO; GO:0005634; C:nucleus; TAS:UniProtKB. DR GO; GO:0006950; P:response to stress; TAS:ProtInc. DR InterPro; IPR008940; Prenyl_trans. DR InterPro; IPR006636; STI1_HS_bd. DR InterPro; IPR011990; TPR-like_helical. DR InterPro; IPR001440; TPR_1. DR InterPro; IPR013026; TPR_region. DR Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2. DR Pfam; PF00515; TPR_1; 9. DR SMART; SM00727; STI1; 2. DR SMART; SM00028; TPR; 9. DR PROSITE; PS50005; TPR; 9. DR PROSITE; PS50293; TPR_REGION; 2. KW 3D-structure; Acetylation; Direct protein sequencing; Nuclear protein; KW Phosphorylation; Repeat; TPR repeat. FT CHAIN 1 543 Stress-induced-phosphoprotein 1. FT /FTId=PRO_0000106372. FT REPEAT 4 37 TPR 1. FT REPEAT 38 71 TPR 2. FT REPEAT 72 105 TPR 3. FT DOMAIN 130 169 STI1 1. FT REPEAT 225 258 TPR 4. FT REPEAT 259 292 TPR 5. FT REPEAT 300 333 TPR 6. FT REPEAT 360 393 TPR 7. FT REPEAT 394 427 TPR 8. FT REPEAT 428 461 TPR 9. FT DOMAIN 492 531 STI1 2. FT MOTIF 222 239 Bipartite nuclear localization signal FT (Potential). FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 246 246 N6-acetyllysine. FT MOD_RES 354 354 Phosphotyrosine. FT MOD_RES 481 481 Phosphoserine. FT HELIX 3 16 FT TURN 17 18 FT HELIX 20 33 FT TURN 35 36 FT HELIX 38 51 FT TURN 52 52 FT HELIX 54 67 FT TURN 69 70 FT HELIX 72 84 FT TURN 85 86 FT HELIX 88 99 FT TURN 100 101 FT TURN 103 104 FT HELIX 106 117 FT HELIX 223 237 FT TURN 238 239 FT HELIX 241 254 FT TURN 256 257 FT HELIX 259 272 FT TURN 273 273 FT HELIX 275 291 FT TURN 293 294 FT HELIX 296 312 FT TURN 313 314 FT HELIX 316 329 FT HELIX 333 348 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 //