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 27-MAY-2015, entry version 164. 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; 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] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE. RX 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] (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 RT 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RP 534-543, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS RP 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 RP MASS 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 RT protein 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- RT cell 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 RP BY 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 RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION RP BY 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 RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-8; LYS-301; LYS-312; RP LYS-325; LYS-344 AND LYS-446, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., 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 RP BY 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation 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., RA Buerckstuemmer T., 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 RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome 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 RP MASS 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., RA Meinnel T., 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 INTERACTION WITH METTL21B. 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 RT methyltransferases preferentially interact with molecular chaperones RT to regulate their activity."; RL PLoS Genet. 9:E1003210-E1003210(2013). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-198, AND IDENTIFICATION RP BY 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [24] 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: 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. Interacts with METTL21B. CC Interacts with HSP90/HSP90AA1; the interaction dissociates the CC PPP5C:HSP90AA1 interaction. {ECO:0000269|PubMed:14532270, CC ECO:0000269|PubMed:23349634, ECO:0000269|PubMed:9195923}. CC -!- INTERACTION: CC Q8IWD4:CCDC117; NbExp=2; IntAct=EBI-1054052, EBI-3387963; CC Q7L3B6:CDC37L1; NbExp=2; IntAct=EBI-1054052, EBI-2841876; CC P00533:EGFR; NbExp=2; IntAct=EBI-1054052, EBI-297353; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus CC {ECO:0000250}. 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. 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. {ECO:0000305}. CC -!- SIMILARITY: Contains 9 TPR repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00339}. 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_001282652.1. [P31948-2] DR RefSeq; NP_001269582.1; NM_001282653.1. [P31948-3] DR RefSeq; NP_006810.1; NM_006819.2. [P31948-1] DR UniGene; Hs.337295; -. 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; 3ESK; X-ray; 2.05 A; A=223-350. DR PDB; 3FWV; X-ray; 2.20 A; A/B=223-349. DR PDBsum; 1ELR; -. DR PDBsum; 1ELW; -. DR PDBsum; 2LNI; -. DR PDBsum; 3ESK; -. DR PDBsum; 3FWV; -. DR ProteinModelPortal; P31948; -. DR SMR; P31948; 2-118, 223-540. DR BioGrid; 116162; 66. DR DIP; DIP-41085N; -. DR IntAct; P31948; 78. DR MINT; MINT-132047; -. DR STRING; 9606.ENSP00000305958; -. DR PhosphoSite; P31948; -. DR BioMuta; STIP1; -. DR DMDM; 400042; -. DR REPRODUCTION-2DPAGE; IPI00013894; -. DR UCD-2DPAGE; P31948; -. DR PaxDb; P31948; -. DR PRIDE; P31948; -. DR DNASU; 10963; -. DR Ensembl; ENST00000305218; ENSP00000305958; ENSG00000168439. [P31948-1] DR Ensembl; ENST00000358794; ENSP00000351646; ENSG00000168439. [P31948-2] DR Ensembl; ENST00000538945; ENSP00000445957; ENSG00000168439. [P31948-3] DR GeneID; 10963; -. DR KEGG; hsa:10963; -. DR UCSC; uc001nyk.1; human. [P31948-1] DR CTD; 10963; -. DR GeneCards; GC11P063953; -. DR HGNC; HGNC:11387; STIP1. DR HPA; CAB017448; -. DR HPA; HPA039291; -. DR HPA; HPA044062; -. DR MIM; 605063; gene. DR neXtProt; NX_P31948; -. DR PharmGKB; PA36196; -. DR eggNOG; COG0457; -. DR GeneTree; ENSGT00790000122996; -. DR HOGENOM; HOG000186562; -. DR HOVERGEN; HBG057820; -. DR InParanoid; P31948; -. DR KO; K09553; -. DR OMA; CEKAIDV; -. DR OrthoDB; EOG7BGHM5; -. DR PhylomeDB; P31948; -. DR TreeFam; TF300478; -. DR ChiTaRS; STIP1; human. DR EvolutionaryTrace; P31948; -. DR GeneWiki; Hop_(protein); -. DR GenomeRNAi; 10963; -. DR NextBio; 35473239; -. DR PRO; PR:P31948; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; P31948; -. DR CleanEx; HS_STIP1; -. DR ExpressionAtlas; P31948; baseline and differential. DR Genevestigator; P31948; -. DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc. DR GO; GO:0005634; C:nucleus; TAS:UniProtKB. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0006950; P:response to stress; TAS:ProtInc. DR Gene3D; 1.25.40.10; -; 3. DR InterPro; IPR006636; STI1_HS-bd. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR001440; TPR_1. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF00515; TPR_1; 8. DR Pfam; PF13181; TPR_8; 1. DR SMART; SM00727; STI1; 2. DR SMART; SM00028; TPR; 9. DR PROSITE; PS50005; TPR; 9. DR PROSITE; PS50293; TPR_REGION; 2. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Complete proteome; KW Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein; KW Reference proteome; 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 {ECO:0000255}. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000269|PubMed:19413330, FT ECO:0000269|PubMed:19608861, FT ECO:0000269|PubMed:22223895, FT ECO:0000269|Ref.8}. FT MOD_RES 8 8 N6-acetyllysine. FT {ECO:0000269|PubMed:19608861}. FT MOD_RES 16 16 Phosphoserine. FT {ECO:0000269|PubMed:18669648}. FT MOD_RES 198 198 Phosphothreonine. FT {ECO:0000269|PubMed:24275569}. FT MOD_RES 301 301 N6-acetyllysine. FT {ECO:0000269|PubMed:19608861}. FT MOD_RES 312 312 N6-acetyllysine. FT {ECO:0000269|PubMed:19608861}. FT MOD_RES 325 325 N6-acetyllysine. FT {ECO:0000269|PubMed:19608861}. FT MOD_RES 344 344 N6-acetyllysine. FT {ECO:0000269|PubMed:19608861}. FT MOD_RES 354 354 Phosphotyrosine. FT {ECO:0000269|PubMed:15592455}. FT MOD_RES 446 446 N6-acetyllysine. FT {ECO:0000269|PubMed:19608861}. FT MOD_RES 481 481 Phosphoserine. FT {ECO:0000269|PubMed:20068231, FT ECO:0000269|PubMed:21406692}. FT VAR_SEQ 1 3 MEQ -> MESGSPMGEVEISRTIRTNGRGQRGYDWQCKRPI FT RVAEVRSSLHSWSLRW (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_055034. FT VAR_SEQ 74 97 Missing (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_055035. FT CONFLICT 84 84 F -> L (in Ref. 7; AAH39299). FT {ECO:0000305}. FT CONFLICT 364 364 K -> E (in Ref. 4; BAG59782). FT {ECO:0000305}. FT CONFLICT 533 533 K -> R (in Ref. 4; BAG59782). FT {ECO:0000305}. FT HELIX 3 16 {ECO:0000244|PDB:1ELW}. FT HELIX 20 33 {ECO:0000244|PDB:1ELW}. FT HELIX 38 51 {ECO:0000244|PDB:1ELW}. FT HELIX 54 67 {ECO:0000244|PDB:1ELW}. FT HELIX 72 84 {ECO:0000244|PDB:1ELW}. FT HELIX 88 99 {ECO:0000244|PDB:1ELW}. FT HELIX 106 117 {ECO:0000244|PDB:1ELW}. FT HELIX 223 237 {ECO:0000244|PDB:1ELR}. FT HELIX 241 254 {ECO:0000244|PDB:1ELR}. FT HELIX 259 272 {ECO:0000244|PDB:1ELR}. FT HELIX 275 291 {ECO:0000244|PDB:1ELR}. FT HELIX 296 312 {ECO:0000244|PDB:1ELR}. FT HELIX 316 329 {ECO:0000244|PDB:1ELR}. FT HELIX 333 348 {ECO:0000244|PDB:1ELR}. FT HELIX 359 372 {ECO:0000244|PDB:2LNI}. FT HELIX 377 387 {ECO:0000244|PDB:2LNI}. FT HELIX 394 404 {ECO:0000244|PDB:2LNI}. FT TURN 405 408 {ECO:0000244|PDB:2LNI}. FT HELIX 410 423 {ECO:0000244|PDB:2LNI}. FT HELIX 428 440 {ECO:0000244|PDB:2LNI}. FT HELIX 444 457 {ECO:0000244|PDB:2LNI}. FT HELIX 459 462 {ECO:0000244|PDB:2LNI}. FT HELIX 463 475 {ECO:0000244|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 //