UniProt Accession

 STIP1_HUMAN; P31948; Q5TZU9 

Genbank Protein ID

 M86752; BT020010; BT020011; CR536512; CH471076; BC002987 

Genbank Nucleotide ID

 AAA58682.1; AAV38813.1; AAV38814.1; CAG38750.1; EAW74196.1; AAH02987.1 

Protein Name

 Stress-induced-phosphoprotein 1 

Protein Synonyms/Alias

 STI1; Hsc70/Hsp90-organizing protein; Hop; Renal carcinoma antigen NY-REN-11; Transformation-sensitive protein IEF SSP 3521 

Gene Name

 STIP1 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
8	MEQVNELKEKGNKAL	acetylation	[1]
10	QVNELKEKGNKALSV	ubiquitination	[2]
13	ELKEKGNKALSVGNI	ubiquitination	[2, 3]
32	QCYSEAIKLDPHNHV	ubiquitination	[2]
50	NRSAAYAKKGDYQKA	ubiquitination	[3]
56	AKKGDYQKAYEDGCK	ubiquitination	[2]
68	GCKTVDLKPDWGKGY	acetylation	[1]
68	GCKTVDLKPDWGKGY	ubiquitination	[2, 4, 5, 6]
73	DLKPDWGKGYSRKAA	acetylation	[1]
78	WGKGYSRKAAALEFL	ubiquitination	[4]
100	RTYEEGLKHEANNPQ	acetylation	[1]
100	RTYEEGLKHEANNPQ	ubiquitination	[2, 5, 6]
109	EANNPQLKEGLQNME	ubiquitination	[4, 5, 6]
123	EARLAERKFMNPFNM	ubiquitination	[2, 4, 5]
136	NMPNLYQKLESDPRT	ubiquitination	[2]
169	KPSDLGTKLQDPRIM	ubiquitination	[2, 5]
246	KDFDTALKHYDKAKE	acetylation	[7, 8]
246	KDFDTALKHYDKAKE	ubiquitination	[2]
272	QAAVYFEKGDYNKCR	ubiquitination	[6]
284	KCRELCEKAIEVGRE	ubiquitination	[2]
301	EDYRQIAKAYARIGN	acetylation	[1]
312	RIGNSYFKEEKYKDA	acetylation	[1]
317	YFKEEKYKDAIHFYN	ubiquitination	[2]
325	DAIHFYNKSLAEHRT	acetylation	[1]
325	DAIHFYNKSLAEHRT	ubiquitination	[4]
337	HRTPDVLKKCQQAEK	ubiquitination	[2]
344	KKCQQAEKILKEQER	acetylation	[1]
344	KKCQQAEKILKEQER	ubiquitination	[2]
364	PDLALEEKNKGNECF	acetylation	[1]
381	GDYPQAMKHYTEAIK	acetylation	[1]
388	KHYTEAIKRNPKDAK	acetylation	[1]
429	QLEPTFIKGYTRKAA	ubiquitination	[2]
434	FIKGYTRKAAALEAM	ubiquitination	[2]
442	AAALEAMKDYTKAMD	ubiquitination	[4]
446	EAMKDYTKAMDVYQK	acetylation	[1]
446	EAMKDYTKAMDVYQK	ubiquitination	[4]
462	LDLDSSCKEAADGYQ	ubiquitination	[2, 5]
486	HDSPEDVKRRAMADP	ubiquitination	[5]
513	LILEQMQKDPQALSE	ubiquitination	[2]
523	QALSEHLKNPVIAQK	ubiquitination	[6]
533	VIAQKIQKLMDVGLI	ubiquitination	[2]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [8] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 

Functional Description

 Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB). 

Sequence Annotation

 REPEAT 4 37 TPR 1.
 REPEAT 38 71 TPR 2.
 REPEAT 72 105 TPR 3.
 DOMAIN 130 169 STI1 1.
 REPEAT 225 258 TPR 4.
 REPEAT 259 292 TPR 5.
 REPEAT 300 333 TPR 6.
 REPEAT 360 393 TPR 7.
 REPEAT 394 427 TPR 8.
 REPEAT 428 461 TPR 9.
 DOMAIN 492 531 STI1 2.
 MOTIF 222 239 Bipartite nuclear localization signal
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 8 8 N6-acetyllysine.
 MOD_RES 16 16 Phosphoserine.
 MOD_RES 301 301 N6-acetyllysine.
 MOD_RES 312 312 N6-acetyllysine.
 MOD_RES 325 325 N6-acetyllysine.
 MOD_RES 344 344 N6-acetyllysine.
 MOD_RES 354 354 Phosphotyrosine.
 MOD_RES 446 446 N6-acetyllysine.
 MOD_RES 481 481 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome; Repeat; TPR repeat. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 543 AA 

Protein Sequence

Gene Ontology

 GO:0005794; C:Golgi apparatus; TAS:ProtInc.
 GO:0005634; C:nucleus; TAS:UniProtKB.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0006950; P:response to stress; TAS:ProtInc. 

Interpro

 IPR006636; STI1_HS-bd.
 IPR001440; TPR-1.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR019734; TPR_repeat. 

Pfam

 PF00515; TPR_1
 PF13181; TPR_8 

SMART

 SM00727; STI1
 SM00028; TPR 

PROSITE

 PS50005; TPR
 PS50293; TPR_REGION 

PRINTS