Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Stress-induced-phosphoprotein 1  

UniProtKB / Swiss-Prot ID :  STIP1_HUMAN

Gene Name (Synonyms) : 
STIP1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm (By similarity). Nucleus (By similarity). 

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

Protein Sequence MEQVNELKEKGNKALSVGNIDDALQCYSEAIKLDPHNHVLYSNRSAAYAKKGDYQKAYEDGCKTVDLKPD...
Predicted Secondary Structure CHHHHHHHHHHHHHHHHCCHHHHHHHHHHHHHHCCCCHHHHHHHHHHHHHHCCHHHHHHHHHHHHHHCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
1N-acetylmethionine.----MEQVN
----CHHHH
7.99UniProtKB
Link-
8N6-acetyllysineVNELKEKGN
HHHHHHHHH
51.72HPRD
Link-
8N6-acetyllysineVNELKEKGN
HHHHHHHHH
51.72Phosphositeplus
Link-
8N6-acetyllysine.VNELKEKGN
HHHHHHHHH
51.72UniProtKB
Link-
16PhosphoserineNKALSVGNI
HHHHHHCCH
32.60HPRD
Link-
16PhosphoserineNKALSVGNI
HHHHHHCCH
32.60PhosphoELM
Link-
16PhosphoserineNKALSVGNI
HHHHHHCCH
32.60Phosphositeplus
Link-
16PhosphoserineNKALSVGNI
HHHHHHCCH
32.60SysPTM
Link-
16Phosphoserine.NKALSVGNI
HHHHHHCCH
32.60UniProtKB
Link-
26S-nitrosocysteineDALQCYSEA
HHHHHHHHH
4.14dbSNO
Link-
41PhosphotyrosineNHVLYSNRS
CHHHHHHHH
11.65Phosphositeplus
Link-
48PhosphotyrosineRSAAYAKKG
HHHHHHHHC
20.76Phosphositeplus
Link-
54PhosphotyrosineKKGDYQKAY
HHCCHHHHH
22.15Phosphositeplus
Link-
62S-nitrosocysteineYEDGCKTVD
HHHHHHHHH
5.30dbSNO
Link-
68Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TVDLKPDWG
HHHHCCCCH
36.15Phosphositeplus
Link-
68N6-acetyllysineTVDLKPDWG
HHHHCCCCH
36.15HPRD
Link-
68N6-acetyllysineTVDLKPDWG
HHHHCCCCH
36.15Phosphositeplus
Link-
68N6-acetyllysine.TVDLKPDWG
HHHHCCCCH
36.15UniProtKB
Link-
73N6-acetyllysinePDWGKGYSR
CCCHHHHHH
50.88HPRD
Link-
73N6-acetyllysinePDWGKGYSR
CCCHHHHHH
50.88Phosphositeplus
Link-
73N6-acetyllysine.PDWGKGYSR
CCCHHHHHH
50.88UniProtKB
Link-
78Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GYSRKAAAL
HHHHHHHHH
36.11Phosphositeplus
Link-
100Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EEGLKHEAN
HHHHHHCCC
50.70Phosphositeplus
Link-
100N6-acetyllysineEEGLKHEAN
HHHHHHCCC
50.70HPRD
Link-
100N6-acetyllysineEEGLKHEAN
HHHHHHCCC
50.70Phosphositeplus
Link-
100N6-acetyllysine.EEGLKHEAN
HHHHHHCCC
50.70UniProtKB
Link-
109Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NPQLKEGLQ
CHHHHHHHH
44.48Phosphositeplus
Link-
123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LAERKFMNP
HHHHHHHHH
40.23Phosphositeplus
Link-
169Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DLGTKLQDP
HHHHHHHHH
42.21Phosphositeplus
Link-
198PhosphothreonineEEIATPPPP
HHHHHHCCC
41.82HPRD
Link-
198PhosphothreonineEEIATPPPP
HHHHHHCCC
41.82PhosphoELM
Link-
198PhosphothreonineEEIATPPPP
HHHHHHCCC
41.82Phosphositeplus
Link-
198Phosphothreonine.EEIATPPPP
HHHHHHCCC
41.82UniProtKB
Link-
246N6-acetyllysineDTALKHYDK
HHHHHHHHH
37.34Phosphositeplus
Link
246N6-acetyllysine.DTALKHYDK
HHHHHHHHH
37.34UniProtKB
Link
255Caspase cleavage aspartic acidAKELDPTNM
HHHHCCCCH
49.41Phosphositeplus
Link
301N6-acetyllysineRQIAKAYAR
HHHHHHHHH
43.49HPRD
Link
301N6-acetyllysineRQIAKAYAR
HHHHHHHHH
43.49Phosphositeplus
Link
301N6-acetyllysine.RQIAKAYAR
HHHHHHHHH
43.49UniProtKB
Link
312N6-acetyllysineNSYFKEEKY
HHHHHHHHH
57.65HPRD
Link
312N6-acetyllysineNSYFKEEKY
HHHHHHHHH
57.65Phosphositeplus
Link
312N6-acetyllysine.NSYFKEEKY
HHHHHHHHH
57.65UniProtKB
Link
325Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)HFYNKSLAE
HHHHHHHHH
35.15Phosphositeplus
Link
325N6-acetyllysineHFYNKSLAE
HHHHHHHHH
35.15HPRD
Link
325N6-acetyllysineHFYNKSLAE
HHHHHHHHH
35.15Phosphositeplus
Link
325N6-acetyllysine.HFYNKSLAE
HHHHHHHHH
35.15UniProtKB
Link
344N6-acetyllysineQQAEKILKE
HHHHHHHHH
57.25HPRD
Link
344N6-acetyllysineQQAEKILKE
HHHHHHHHH
57.25Phosphositeplus
Link
344N6-acetyllysine.QQAEKILKE
HHHHHHHHH
57.25UniProtKB
Link
354PhosphotyrosineERLAYINPD
HHHHHHHHH
13.06HPRD
Link-
354PhosphotyrosineERLAYINPD
HHHHHHHHH
13.06PhosphoELM
Link-
354PhosphotyrosineERLAYINPD
HHHHHHHHH
13.06Phosphositeplus
Link-
354Phosphotyrosine.ERLAYINPD
HHHHHHHHH
13.06UniProtKB
Link-
364N6-acetyllysineALEEKNKGN
HHHHHHHHH
55.36HPRD
Link-
381N6-acetyllysinePQAMKHYTE
HHHHHHHHH
36.15HPRD
Link-
381N6-acetyllysinePQAMKHYTE
HHHHHHHHH
36.15Phosphositeplus
Link-
383PhosphotyrosineAMKHYTEAI
HHHHHHHHH
10.76Phosphositeplus
Link-
384PhosphothreonineMKHYTEAIK
HHHHHHHHH
20.75Phosphositeplus
Link-
388N6-acetyllysineTEAIKRNPK
HHHHHHCCC
53.85HPRD
Link-
388N6-acetyllysineTEAIKRNPK
HHHHHHCCC
53.85Phosphositeplus
Link-
388N6-acetyllysine.TEAIKRNPK
HHHHHHCCC
53.85UniProtKB
Link-
442Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LEAMKDYTK
HHHHCCHHH
55.41Phosphositeplus
Link-
444PhosphotyrosineAMKDYTKAM
HHCCHHHHH
12.48Phosphositeplus
Link-
446Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KDYTKAMDV
CCHHHHHHH
35.17Phosphositeplus
Link-
446N6-acetyllysineKDYTKAMDV
CCHHHHHHH
35.17HPRD
Link-
446N6-acetyllysineKDYTKAMDV
CCHHHHHHH
35.17Phosphositeplus
Link-
446N6-acetyllysine.KDYTKAMDV
CCHHHHHHH
35.17UniProtKB
Link-
462Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DSSCKEAAD
CCCCHHHHH
52.95Phosphositeplus
Link-
476PhosphotyrosineMMAQYNRHD
HHHHHHHHH
12.48HPRD
Link-
476PhosphotyrosineMMAQYNRHD
HHHHHHHHH
12.48Phosphositeplus
Link-
476PhosphotyrosineMMAQYNRHD
HHHHHHHHH
12.48SysPTM
Link-
481PhosphoserineNRHDSPEDV
HHHHHHHHH
24.86HPRD
Link-
481PhosphoserineNRHDSPEDV
HHHHHHHHH
24.86PhosphoELM
Link-
481PhosphoserineNRHDSPEDV
HHHHHHHHH
24.86Phosphositeplus
Link-
481PhosphoserineNRHDSPEDV
HHHHHHHHH
24.86SysPTM
Link-
481Phosphoserine.NRHDSPEDV
HHHHHHHHH
24.86UniProtKB
Link-
486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PEDVKRRAM
HHHHHHHHH
48.79Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
HS90A_HUMANin vitro
in vivo
HPRD:05454HPRD10786835
PRIO_HUMANin vivoHPRD:05454HPRD12093732
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-246, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-8; LYS-68; LYS-73;LYS-100; LYS-301; LYS-312; LYS-325; LYS-344; LYS-388 AND LYS-446, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-354, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-198, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-481, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-354, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures