Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Heat shock protein HSP 90-beta  

UniProtKB / Swiss-Prot ID :  HS90B_HUMAN

Gene Name (Synonyms) : 
HSP90AB1, HSP90B, HSPC2, HSPCB  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. 

Protein Function :  Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. 

Protein Sequence MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKE...
Predicted Secondary Structure CCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHHHHHHHHHCCCHHHCCCCCC...
Protein Variant
LocationDescription
349K -> E (in dbSNP:rs11538975). VAR_049624
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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
Protein Variant
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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
36Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FYSNKEIFL
HCCCCCHHH
46.37Phosphositeplus
Link-
45PhosphoserineRELISNASD
HHHHHHHHH
38.68Phosphositeplus
Link-
48PhosphoserineISNASDALD
HHHHHHHHH
27.89Phosphositeplus
Link-
53Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DALDKIRYE
HHHHHHHHH
29.90Phosphositeplus
Link-
56PhosphotyrosineDKIRYESLT
HHHHHHHCC
17.22Phosphositeplus
Link-
60PhosphothreonineYESLTDPSK
HHHCCCHHH
55.96HPRD
Link-
64Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TDPSKLDSG
CCHHHCCCC
62.80Phosphositeplus
Link-
69Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LDSGKELKI
CCCCCCCEE
64.92Phosphositeplus
Link-
89PhosphothreonineTLVDTGIGM
EEEECCCCC
24.18Phosphositeplus
Link-
95Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IGMTKADLI
CCCCHHHHH
30.89Phosphositeplus
Link-
107Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GTIAKSGTK
CHHHHHHHH
45.64Phosphositeplus
Link-
148Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VVITKHNDD
EEEEEECCC
29.32Phosphositeplus
Link-
180Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GRGTKVILH
CCCCEEEEE
30.06Phosphositeplus
Link-
186Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ILHLKEDQT
EEEECCCCH
48.80Phosphositeplus
Link-
192PhosphotyrosineDQTEYLEER
CCHHHHHHH
23.85Phosphositeplus
Link-
204Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EVVKKHSQF
HHHHHHHCC
36.56Phosphositeplus
Link-
219Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LYLEKEREK
EEEECCCCC
60.52Phosphositeplus
Link-
226PhosphoserineEKEISDDEA
CCCCCCCCC
39.85HPRD
Link-
226PhosphoserineEKEISDDEA
CCCCCCCCC
39.85Phosphositeplus
Link-
226PhosphoserineEKEISDDEA
CCCCCCCCC
39.85SysPTM
Link-
226Phosphoserine (CK2_group;CK2_alpha)EKEISDDEA
CCCCCCCCC
39.85PhosphoELM
Link-
226Phosphoserine.EKEISDDEA
CCCCCCCCC
39.85UniProtKB
Link-
237Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EKGEKEEED
CCCCCCCCC
78.19Phosphositeplus
Link-
255PhosphoserineEDVGSDEED
CCCCCCHHH
41.52HPRD
Link-
255PhosphoserineEDVGSDEED
CCCCCCHHH
41.52Phosphositeplus
Link-
255PhosphoserineEDVGSDEED
CCCCCCHHH
41.52SysPTM
Link-
255Phosphoserine (CK2_group;CK2_alpha)EDVGSDEED
CCCCCCHHH
41.52PhosphoELM
Link-
255Phosphoserine.EDVGSDEED
CCCCCCHHH
41.52UniProtKB
Link-
261PhosphoserineEEDDSGKDK
HHHHHHCCC
61.13HPRD
Link-
261PhosphoserineEEDDSGKDK
HHHHHHCCC
61.13PhosphoELM
Link-
261PhosphoserineEEDDSGKDK
HHHHHHCCC
61.13Phosphositeplus
Link-
261PhosphoserineEEDDSGKDK
HHHHHHCCC
61.13SysPTM
Link-
261Phosphoserine.EEDDSGKDK
HHHHHHCCC
61.13UniProtKB
Link-
275Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KIKEKYIDQ
CCCCCCCCC
42.37Phosphositeplus
Link-
275N6-acetyllysineKIKEKYIDQ
CCCCCCCCC
42.37Phosphositeplus
Link-
275N6-acetyllysine.KIKEKYIDQ
CCCCCCCCC
42.37UniProtKB
Link-
276PhosphotyrosineIKEKYIDQE
CCCCCCCCC
15.72Phosphositeplus
Link-
284Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EELNKTKPI
CEECCCCCC
71.23Phosphositeplus
Link-
284N6-acetyllysineEELNKTKPI
CEECCCCCC
71.23Phosphositeplus
Link-
284N6-acetyllysine.EELNKTKPI
CEECCCCCC
71.23UniProtKB
Link-
285PhosphothreonineELNKTKPIW
EECCCCCCC
40.76HPRD
Link-
297PhosphothreoninePDDITQEEY
CCCCCHHHH
36.60HPRD
Link-
297PhosphothreoninePDDITQEEY
CCCCCHHHH
36.60PhosphoELM
Link-
297PhosphothreoninePDDITQEEY
CCCCCHHHH
36.60Phosphositeplus
Link-
297Phosphothreonine.PDDITQEEY
CCCCCHHHH
36.60UniProtKB
Link-
301PhosphotyrosineTQEEYGEFY
CHHHHHHHH
22.62Phosphositeplus
Link-
306Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GEFYKSLTN
HHHHHHHHC
44.29Phosphositeplus
Link-
307PhosphoserineEFYKSLTND
HHHHHHHCC
29.10HPRD
Link-
307PhosphoserineEFYKSLTND
HHHHHHHCC
29.10Phosphositeplus
Link-
307Phosphoserine.EFYKSLTND
HHHHHHHCC
29.10UniProtKB
Link-
309PhosphothreonineYKSLTNDWE
HHHHHCCCC
37.92HPRD
Link-
319Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)HLAVKHFSV
CCEEEEEEE
33.07Phosphositeplus
Link-
347Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LFENKKKKN
CCCCCCCCC
59.79Phosphositeplus
Link-
347N6-methyllysineLFENKKKKN
CCCCCCCCC
59.79Phosphositeplus
Link-
354Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KNNIKLYVR
CCCCEEEEE
35.57Phosphositeplus
Link-
354N6-acetyllysine.KNNIKLYVR
CCCCEEEEE
35.57UniProtKB
Link-
391PhosphoserinePLNISREML
CCHHHHHHH
22.55Phosphositeplus
Link-
399Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LQQSKILKV
HHCCHHHHH
47.95Phosphositeplus
Link-
399N6-acetyllysine; alternate.LQQSKILKV
HHCCHHHHH
47.95UniProtKB
Link-
399N6-malonyllysine; alternate.LQQSKILKV
HHCCHHHHH
47.95UniProtKB
Link-
402N6-acetyllysine.SKILKVIRK
CHHHHHHHH
38.80UniProtKB
Link-
411Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NIVKKCLEL
HHHHHHHHH
32.91Phosphositeplus
Link-
412S-nitrosocysteineIVKKCLELF
HHHHHHHHH
2.71dbSNO
Link-
428Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ENYKKFYEA
HHHHHHHHH
42.70Phosphositeplus
Link-
435Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EAFSKNLKL
HHHHHHHHC
60.90Phosphositeplus
Link-
435N6-acetyllysineEAFSKNLKL
HHHHHHHHC
60.90HPRD
Link-
435N6-acetyllysineEAFSKNLKL
HHHHHHHHC
60.90Phosphositeplus
Link-
435N6-acetyllysine.EAFSKNLKL
HHHHHHHHC
60.90UniProtKB
Link-
438Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SKNLKLGIH
HHHHHCCCC
54.80Phosphositeplus
Link-
445PhosphoserineIHEDSTNRR
CCCCHHHHH
25.29HPRD
Link-
452PhosphoserineRRRLSELLR
HHHHHHHHH
25.12HPRD
Link-
452PhosphoserineRRRLSELLR
HHHHHHHHH
25.12Phosphositeplus
Link-
452Phosphoserine.RRRLSELLR
HHHHHHHHH
25.12UniProtKB
Link-
477Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VSRMKETQK
HHHCCCCCC
57.40Phosphositeplus
Link-
481Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KETQKSIYY
CCCCCEEEE
46.36Phosphositeplus
Link-
481N6-acetyllysineKETQKSIYY
CCCCCEEEE
46.36HPRD
Link-
481N6-acetyllysineKETQKSIYY
CCCCCEEEE
46.36Phosphositeplus
Link-
481N6-acetyllysine.KETQKSIYY
CCCCCEEEE
46.36UniProtKB
Link-
482PhosphoserineETQKSIYYI
CCCCEEEEE
13.15Phosphositeplus
Link-
484PhosphotyrosineQKSIYYITG
CCEEEEEEC
8.91HPRD
Link-
484PhosphotyrosineQKSIYYITG
CCEEEEEEC
8.91PhosphoELM
Link-
484PhosphotyrosineQKSIYYITG
CCEEEEEEC
8.91Phosphositeplus
Link-
484Phosphotyrosine.QKSIYYITG
CCEEEEEEC
8.91UniProtKB
Link-
485PhosphotyrosineKSIYYITGE
CEEEEEECC
7.13Phosphositeplus
Link-
491Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TGESKEQVA
ECCCHHHHH
48.11Phosphositeplus
Link-
514PhosphothreonineVVYMTEPID
EEEECCCHH
22.41HPRD
Link-
531Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EFDGKSLVS
HCCCCCEEE
42.32Phosphositeplus
Link-
532PhosphoserineFDGKSLVSV
CCCCCEEEE
39.26HPRD
Link-
532PhosphoserineFDGKSLVSV
CCCCCEEEE
39.26Phosphositeplus
Link-
532Phosphoserine.FDGKSLVSV
CCCCCEEEE
39.26UniProtKB
Link-
535PhosphoserineKSLVSVTKE
CCEEEECCC
29.39HPRD
Link-
538Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VSVTKEGLE
EEECCCCCC
47.86Phosphositeplus
Link-
550Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DEEEKKKME
CCHHHHHHH
62.06Phosphositeplus
Link-
559Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ESKAKFENL
HHHHHHHHH
57.88Phosphositeplus
Link-
565Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ENLCKLMKE
HHHHHHHHH
55.57Phosphositeplus
Link-
568Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)CKLMKEILD
HHHHHHHCC
52.63Phosphositeplus
Link-
568N6-acetyllysineCKLMKEILD
HHHHHHHCC
52.63HPRD
Link-
568N6-acetyllysineCKLMKEILD
HHHHHHHCC
52.63Phosphositeplus
Link-
568N6-acetyllysine.CKLMKEILD
HHHHHHHCC
52.63UniProtKB
Link-
577Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KKVEKVTIS
CCEEEEEEE
47.90Phosphositeplus
Link-
596PhosphotyrosineVTSTYGWTA
EECCCCCCH
15.50HPRD
Link-
596PhosphotyrosineVTSTYGWTA
EECCCCCCH
15.50Phosphositeplus
Link-
607Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ERIMKAQAL
HHHHHHHCC
34.67Phosphositeplus
Link-
619PhosphotyrosineSTMGYMMAK
CCCCCCCCC
3.48Phosphositeplus
Link-
623Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YMMAKKHLE
CCCCCCEEE
23.88Phosphositeplus
Link-
624Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MMAKKHLEI
CCCCCEEEE
43.83Phosphositeplus
Link-
624N6-acetyllysineMMAKKHLEI
CCCCCEEEE
43.83Phosphositeplus
Link-
624N6-acetyllysine.MMAKKHLEI
CCCCCEEEE
43.83UniProtKB
Link-
685Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YRMIKLGLG
HHHHHHHCC
27.45Phosphositeplus
Link-
718PhosphoserineDEDASRMEE
CCCCCCCCC
44.47HPRD
Link
718PhosphoserineDEDASRMEE
CCCCCCCCC
44.47Phosphositeplus
Link
718PhosphoserineDEDASRMEE
CCCCCCCCC
44.47SysPTM
Link
718Phosphoserine.DEDASRMEE
CCCCCCCCC
44.47UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
XPO1_HUMANphysical interactionMINT-72646MINT16263121
IKKA_HUMANphysical interactionMINT-47954MINT14743216
EIF3H_HUMANphysical interactionMINT-72672MINT16263121
LDHA_HUMANphysical interactionMINT-72650MINT16263121
PGK1_HUMANphysical interactionMINT-72649MINT16263121
ALDOA_HUMANphysical interactionMINT-72651MINT16263121
G3P_HUMANphysical interactionMINT-72648MINT16263121
RLA0_HUMANphysical interactionMINT-72674MINT16263121
HSP71_HUMANphysical interactionMINT-72641MINT16263121
RSSA_HUMANphysical interactionMINT-72673MINT16263121
C1TC_HUMANphysical interactionMINT-72655MINT16263121
TCPA_HUMANphysical interactionMINT-72642MINT16263121
UBA1_HUMANphysical interactionMINT-72666MINT16263121
AKT2_HUMANphysical interactionMINT-18409MINT11988487
STAT3_HUMANphysical interactionMINT-15155MINT12559950
FAS_HUMANphysical interactionMINT-72654MINT16263121
ACTG_HUMANphysical interactionMINT-72659MINT16263121
PRKDC_HUMANphysical interactionMINT-72644MINT16263121
NUMA1_HUMANphysical interactionMINT-72664MINT16263121
CDC37_HUMANphysical interactionMINT-16429MINT11864612
HS105_HUMANphysical interactionMINT-72643MINT16263121
PSMD1_HUMANphysical interactionMINT-72667MINT16263121
M3K14_HUMANphysical interactionMINT-47998MINT14743216
SIAS_HUMANphysical interactionMINT-72658MINT16263121
E2IG5_HUMANphysical interactionMINT-2567472MINT16698020
E2IG5_HUMANphysical interactionMINT-2567397MINT16698020
E2IG5_HUMANcolocalizationMINT-2567511MINT16698020
NEMO_HUMANphysical interactionMINT-47969MINT14743216
NEMO_HUMANphysical interactionMINT-48175MINT14743216
1433Z_HUMANphysical interactionMINT-3319575MINT15161933
TRADD_HUMANphysical interactionMINT-49497MINT14743216
TBK1_HUMANphysical interactionMINT-49292MINT14743216
RIPK3_HUMANphysical interactionMINT-49154MINT14743216
NEMO_HUMANphysical interactionMINT-48239MINT14743216
HS90B_HUMANphysical interactionDIP:762EDIP7588731
HSP71_HUMANphysical interactionEBI-709762
intact16263121
TCPA_HUMANphysical interactionEBI-709762
intact16263121
HS105_HUMANphysical interactionEBI-709762
intact16263121
PRKDC_HUMANphysical interactionEBI-709762
intact16263121
GNAI2_HUMANphysical interactionEBI-709762
intact16263121
XPO1_HUMANphysical interactionEBI-709762
intact16263121
KPYM_HUMANphysical interactionEBI-709762
intact16263121
G3P_HUMANphysical interactionEBI-709762
intact16263121
PGK1_HUMANphysical interactionEBI-709762
intact16263121
LDHA_HUMANphysical interactionEBI-709762
intact16263121
ALDOA_HUMANphysical interactionEBI-709762
intact16263121
MDHC_HUMANphysical interactionEBI-709762
intact16263121
FAS_HUMANphysical interactionEBI-709762
intact16263121
C1TC_HUMANphysical interactionEBI-709762
intact16263121
SERC_HUMANphysical interactionEBI-709762
intact16263121
SIAS_HUMANphysical interactionEBI-709762
intact16263121
ACTG_HUMANphysical interactionEBI-709762
intact16263121
TPM3_HUMANphysical interactionEBI-709762
intact16263121
FLNA_HUMANphysical interactionEBI-709762
intact16263121
MYH9_HUMANphysical interactionEBI-709762
intact16263121
SPTA2_HUMANphysical interactionEBI-709762
intact16263121
NUMA1_HUMANphysical interactionEBI-709762
intact16263121
ACTN1_HUMANphysical interactionEBI-709762
intact16263121
UBA1_HUMANphysical interactionEBI-709762
intact16263121
PSMD1_HUMANphysical interactionEBI-709762
intact16263121
PSB5_HUMANphysical interactionEBI-709762
intact16263121
SYAC_HUMANphysical interactionEBI-709762
intact16263121
SYIM_HUMANphysical interactionEBI-709762
intact16263121
EF2_HUMANphysical interactionEBI-709762
intact16263121
EIF3H_HUMANphysical interactionEBI-709762
intact16263121
RSSA_HUMANphysical interactionEBI-709762
intact16263121
RLA0_HUMANphysical interactionEBI-709762
intact16263121
RS6_HUMANphysical interactionEBI-709762
intact16263121
RS4X_HUMANphysical interactionEBI-709762
intact16263121
RL7_HUMANphysical interactionEBI-709762
intact16263121
RS3A_HUMANphysical interactionEBI-709762
intact16263121
RL5_HUMANphysical interactionEBI-709762
intact16263121
MYG1_HUMANphysical interactionEBI-709762
intact16263121
IKKA_HUMANphysical interaction
physical interaction
EBI-365533
EBI-361215
intact14743216
14743216
ESR1_HUMANin vitroHPRD:06763HPRD11795466
AKT1_HUMANin vivoHPRD:06763HPRD10995457
P53_HUMANin vitro
in vivo
HPRD:06763HPRD11707401
RHG01_HUMANyeast 2-hybridHPRD:06763HPRD14697242
WASL_HUMANin vitro
in vivo
HPRD:06763HPRD15791211
HS90B_HUMANin vitroHPRD:06763HPRD7588731
STAT3_HUMANin vivoHPRD:06763HPRD12559950
DDX24_HUMANyeast 2-hybridHPRD:06763HPRD16169070
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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-624, 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 LYS-275; LYS-284; LYS-354;LYS-399; LYS-402; LYS-435; LYS-481 AND LYS-568, AND MASS SPECTROMETRY.
N6-malonyllysine
ReferencePubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme.";
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.;
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
Cited for: MALONYLATION AT LYS-399.
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-261, ANDMASS SPECTROMETRY.
"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-484, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of synaptosomes from human cerebralcortex.";
DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P.,Pant H.C., Dosemeci A.;
J. Proteome Res. 4:306-315(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASSSPECTROMETRY.
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, 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-226 AND SER-255, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-255 ANDSER-261, AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-484, AND MASSSPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-297, 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 SER-226 AND SER-255, ANDMASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, ANDMASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, ANDMASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-255 ANDSER-261, AND MASS SPECTROMETRY.
"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-226; SER-255; SER-261;SER-307; SER-452; SER-532 AND SER-718, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, ANDMASS SPECTROMETRY.
"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-484, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASSSPECTROMETRY.
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