Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Heat shock cognate 71 kDa protein  

UniProtKB / Swiss-Prot ID :  HSP7C_HUMAN

Gene Name (Synonyms) : 
HSPA8, HSC70, HSP73, HSPA10  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Melanosome. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock. Identified by mass spectrometry in melanosome fracti 

Protein Function :  Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Isoform 2 may function as an endogenous inhibitory regulator of HSC70 by competing the co- chaperones. 

Protein Sequence MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDA...
Predicted Secondary Structure CCCCCEEEEEECCCCEEEEEEECCEEEEEECCCCCEECCEEEEECCCCEEECHHHHHHHHCCHHHHHHHH...
Protein Variant
LocationDescription
32D -> Y (in dbSNP:rs11551602). VAR_049619
459F -> L (in dbSNP:rs11551598). VAR_049620
- top -

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
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylserine---MSKGPA
---CCCCCE
46.44HPRD
Link-
2N-acetylserine.---MSKGPA
---CCCCCE
46.44UniProtKB
Link-
3Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)--MSKGPAV
--CCCCCEE
68.56Phosphositeplus
Link-
15PhosphotyrosineLGTTYSCVG
ECCCCEEEE
10.42Phosphositeplus
Link-
15Phosphotyrosine.LGTTYSCVG
ECCCCEEEE
10.42UniProtKB
Link-
41PhosphotyrosineTTPSYVAFT
ECCEEEEEC
9.30PhosphoELM
Link-
41PhosphotyrosineTTPSYVAFT
ECCEEEEEC
9.30Phosphositeplus
Link-
41Phosphotyrosine.TTPSYVAFT
ECCEEEEEC
9.30UniProtKB
Link-
56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GDAAKNQVA
CHHHHHHHH
50.02Phosphositeplus
Link-
66PhosphothreonineNPTNTVFDA
CHHHHHHHH
25.65Phosphositeplus
Link-
71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VFDAKRLIG
HHHHHHHHC
49.97Phosphositeplus
Link-
88Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QSDMKHWPF
HHHHHHCCE
47.73Phosphositeplus
Link-
88N6-acetyllysineQSDMKHWPF
HHHHHHCCE
47.73HPRD
Link-
88N6-acetyllysineQSDMKHWPF
HHHHHHCCE
47.73Phosphositeplus
Link-
88N6-acetyllysine.QSDMKHWPF
HHHHHHCCE
47.73UniProtKB
Link-
107PhosphotyrosineVQVEYKGET
EEEEECCCC
25.99PhosphoELM
Link-
107PhosphotyrosineVQVEYKGET
EEEEECCCC
25.99Phosphositeplus
Link-
107Phosphotyrosine.VQVEYKGET
EEEEECCCC
25.99UniProtKB
Link-
108Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QVEYKGETK
EEEECCCCC
36.44Phosphositeplus
Link-
108N6-acetyllysineQVEYKGETK
EEEECCCCC
36.44HPRD
Link-
108N6-acetyllysineQVEYKGETK
EEEECCCCC
36.44Phosphositeplus
Link-
108N6-acetyllysine.QVEYKGETK
EEEECCCCC
36.44UniProtKB
Link-
112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KGETKSFYP
CCCCCEECH
33.98Phosphositeplus
Link-
113Phosphoserine.GETKSFYPE
CCCCEECHH
37.12UniProtKB
Link-
115Phosphotyrosine.TKSFYPEEV
CCEECHHHH
19.47UniProtKB
Link-
120Phosphoserine.PEEVSSMVL
HHHHHHHHH
18.92UniProtKB
Link-
121Phosphoserine.EEVSSMVLT
HHHHHHHHH
20.34UniProtKB
Link-
126Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MVLTKMKEI
HHHHHHHHH
43.76Phosphositeplus
Link-
128Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LTKMKEIAE
HHHHHHHHH
47.74Phosphositeplus
Link-
134PhosphotyrosineIAEAYLGKT
HHHHHHCCC
13.90Phosphositeplus
Link-
137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AYLGKTVTN
HHHCCCCCC
36.91Phosphositeplus
Link-
137N6-acetyllysineAYLGKTVTN
HHHCCCCCC
36.91HPRD
Link-
153PhosphoserineYFNDSQRQA
CCCHHHHHH
28.50HPRD
Link-
153PhosphoserineYFNDSQRQA
CCCHHHHHH
28.50PhosphoELM
Link-
153PhosphoserineYFNDSQRQA
CCCHHHHHH
28.50Phosphositeplus
Link-
153Phosphoserine.YFNDSQRQA
CCCHHHHHH
28.50UniProtKB
Link-
158PhosphothreonineQRQATKDAG
HHHHHHHHH
22.56Phosphositeplus
Link-
159Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RQATKDAGT
HHHHHHHHH
48.90Phosphositeplus
Link-
163PhosphothreonineKDAGTIAGL
HHHHHHCCC
14.90Phosphositeplus
Link-
177PhosphothreonineINEPTAAAI
EECHHHHHH
23.81Phosphositeplus
Link-
187Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YGLDKKVGA
HHCCCCCCC
55.17Phosphositeplus
Link-
188Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GLDKKVGAE
HCCCCCCCC
45.64Phosphositeplus
Link-
246Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IAEFKRKHK
HHHHHHHHC
52.63Phosphositeplus
Link-
246N6-acetyllysineIAEFKRKHK
HHHHHHHHC
52.63HPRD
Link-
246N6-acetyllysineIAEFKRKHK
HHHHHHHHC
52.63Phosphositeplus
Link-
246N6-acetyllysine.IAEFKRKHK
HHHHHHHHC
52.63UniProtKB
Link-
251Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RKHKKDISE
HHHCCCCCC
61.07Phosphositeplus
Link-
254PhosphoserineKKDISENKR
CCCCCCCHH
45.29HPRD
Link-
254PhosphoserineKKDISENKR
CCCCCCCHH
45.29Phosphositeplus
Link-
257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ISENKRAVR
CCCCHHHHH
37.37Phosphositeplus
Link-
265PhosphothreonineRRLRTACER
HHHHHHHHH
40.01Phosphositeplus
Link-
277PhosphoserineTLSSSTQAS
HHCCCCEEE
22.59Phosphositeplus
Link-
313PhosphothreonineLFRGTLDPV
HHHHHHHHH
24.59Phosphositeplus
Link-
319Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DPVEKALRD
HHHHHHHHH
53.61Phosphositeplus
Link-
319N6-acetyllysineDPVEKALRD
HHHHHHHHH
53.61HPRD
Link-
319N6-acetyllysineDPVEKALRD
HHHHHHHHH
53.61Phosphositeplus
Link-
319N6-acetyllysine.DPVEKALRD
HHHHHHHHH
53.61UniProtKB
Link-
325Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LRDAKLDKS
HHHCCCCHH
62.60Phosphositeplus
Link-
328Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AKLDKSQIH
CCCCHHHCC
55.48Phosphositeplus
Link-
329PhosphoserineKLDKSQIHD
CCCHHHCCE
33.75HPRD
Link-
329PhosphoserineKLDKSQIHD
CCCHHHCCE
33.75Phosphositeplus
Link-
341PhosphothreonineVGGSTRIPK
ECCCCHHHH
35.57Phosphositeplus
Link-
348Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PKIQKLLQD
HHHHHHHHH
55.42Phosphositeplus
Link-
348N6-acetyllysinePKIQKLLQD
HHHHHHHHH
55.42HPRD
Link-
348N6-acetyllysinePKIQKLLQD
HHHHHHHHH
55.42Phosphositeplus
Link-
348N6-acetyllysine.PKIQKLLQD
HHHHHHHHH
55.42UniProtKB
Link-
357Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FFNGKELNK
HCCCCCCCC
61.20Phosphositeplus
Link-
361Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KELNKSINP
CCCCCCCCH
66.39Phosphositeplus
Link-
362PhosphoserineELNKSINPD
CCCCCCCHH
26.90HPRD
Link-
362PhosphoserineELNKSINPD
CCCCCCCHH
26.90Phosphositeplus
Link-
385PhosphoserineSGDKSENVQ
CCCCCCCCC
38.86HPRD
Link-
397PhosphothreonineLLDVTPLSL
EEEECCCCE
20.41HPRD
Link-
400PhosphoserineVTPLSLGIE
ECCCCEEEE
26.25Phosphositeplus
Link-
423Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TIPTKQTQT
CCCCEEEEE
46.09Phosphositeplus
Link-
451Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RAMTKDNNL
CCCCCCCCC
45.43Phosphositeplus
Link-
458Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NLLGKFELT
CCEEEEEEC
35.32Phosphositeplus
Link-
462PhosphothreonineKFELTGIPP
EEEECCCCC
26.35HPRD
Link-
477PhosphothreonineQIEVTFDID
EEEEEEEEC
11.64HPRD
Link-
477PhosphothreonineQIEVTFDID
EEEEEEEEC
11.64PhosphoELM
Link-
477PhosphothreonineQIEVTFDID
EEEEEEEEC
11.64Phosphositeplus
Link-
477PhosphothreonineQIEVTFDID
EEEEEEEEC
11.64SysPTM
Link-
477Phosphothreonine.QIEVTFDID
EEEEEEEEC
11.64UniProtKB
Link-
500Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GKENKITIT
CCCCEEEEE
42.17Phosphositeplus
Link-
502PhosphothreonineENKITITND
CCEEEEECC
24.29Phosphositeplus
Link-
507Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ITNDKGRLS
EECCCCCCC
48.26Phosphositeplus
Link-
512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GRLSKEDIE
CCCCHHHHH
65.09Phosphositeplus
Link-
512N6-acetyllysineGRLSKEDIE
CCCCHHHHH
65.09HPRD
Link-
512N6-acetyllysineGRLSKEDIE
CCCCHHHHH
65.09Phosphositeplus
Link-
512N6-acetyllysine.GRLSKEDIE
CCCCHHHHH
65.09UniProtKB
Link-
524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QEAEKYKAE
HHHHHHHHH
60.13Phosphositeplus
Link-
524N6-acetyllysineQEAEKYKAE
HHHHHHHHH
60.13HPRD
Link-
524N6-acetyllysineQEAEKYKAE
HHHHHHHHH
60.13Phosphositeplus
Link-
524N6-acetyllysine.QEAEKYKAE
HHHHHHHHH
60.13UniProtKB
Link-
526Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AEKYKAEDE
HHHHHHHHH
57.26Phosphositeplus
Link-
531Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AEDEKQRDK
HHHHHHHHH
64.06Phosphositeplus
Link-
539Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KVSSKNSLE
HHHHHHHHH
42.95Phosphositeplus
Link-
541PhosphoserineSSKNSLESY
HHHHHHHHH
36.93HPRD
Link-
541Phosphoserine.SSKNSLESY
HHHHHHHHH
36.93UniProtKB
Link-
550Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AFNMKATVE
HHHHHHHHC
41.85Phosphositeplus
Link-
557Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VEDEKLQGK
HCCCCCCCC
59.43Phosphositeplus
Link-
561Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KLQGKINDE
CCCCCCCHH
25.94Phosphositeplus
Link-
573Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KILDKCNEI
HHHHHHHHH
35.20Phosphositeplus
Link-
574S-nitrosocysteineILDKCNEII
HHHHHHHHH
5.73dbSNO
Link-
583Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NWLDKNQTA
HHHHCCCCC
49.11Phosphositeplus
Link-
589Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QTAEKEEFE
CCCCHHHHH
61.14Phosphositeplus
Link-
589N6-acetyllysineQTAEKEEFE
CCCCHHHHH
61.14HPRD
Link-
589N6-acetyllysineQTAEKEEFE
CCCCHHHHH
61.14Phosphositeplus
Link-
589N6-acetyllysine.QTAEKEEFE
CCCCHHHHH
61.14UniProtKB
Link-
597Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EHQQKELEK
HHHHHHHHH
58.66Phosphositeplus
Link-
597N6-acetyllysineEHQQKELEK
HHHHHHHHH
58.66HPRD
Link-
597N6-acetyllysineEHQQKELEK
HHHHHHHHH
58.66Phosphositeplus
Link-
597N6-acetyllysine.EHQQKELEK
HHHHHHHHH
58.66UniProtKB
Link-
601Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KELEKVCNP
HHHHHHHHH
65.79Phosphositeplus
Link-
601N6-acetyllysineKELEKVCNP
HHHHHHHHH
65.79HPRD
Link-
601N6-acetyllysineKELEKVCNP
HHHHHHHHH
65.79Phosphositeplus
Link-
601N6-acetyllysine.KELEKVCNP
HHHHHHHHH
65.79UniProtKB
Link-
603S-nitrosocysteineLEKVCNPII
HHHHHHHHH
8.10dbSNO
Link-
611PhosphotyrosineITKLYQSAG
HHHHHHHHC
11.28HPRD
Link-
613PhosphoserineKLYQSAGGM
HHHHHHCCC
18.48Phosphositeplus
Link-
633PhosphoserineGAPPSGGAS
CCCCCCCCC
49.12HPRD
Link-
637PhosphoserineSGGASSGPT
CCCCCCCCC
38.82HPRD
Link-
637Phosphoserine.SGGASSGPT
CCCCCCCCC
38.82UniProtKB
Link-
638PhosphoserineGGASSGPTI
CCCCCCCCE
48.54HPRD
Link
638Phosphoserine.GGASSGPTI
CCCCCCCCE
48.54UniProtKB
Link
641PhosphothreonineSSGPTIEEV
CCCCCEEEC
44.54HPRD
Link
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
IKKB_HUMANphysical interactionMINT-48068MINT14743216
TAD3L_HUMANphysical interactionMINT-63208MINT16169070
APOB_HUMANphysical interactionMINT-16980MINT9694898
RB_HUMANphysical interactionMINT-17355MINT7673249
SP1_HUMANphysical interactionMINT-17728MINT10976766
NFKB1_HUMANphysical interactionMINT-48532MINT14743216
TNR1B_HUMANphysical interactionMINT-49374MINT14743216
1433T_HUMANphysical interactionMINT-50373MINT15324660
RGS2_HUMANphysical interactionMINT-63728MINT16169070
1433Z_HUMANphysical interactionMINT-3319337MINT15161933
NFKB2_HUMANphysical interactionMINT-48696MINT14743216
TRAF2_HUMANphysical interactionMINT-49534MINT14743216
TRAF1_HUMANphysical interactionMINT-49502MINT14743216
M3K1_HUMANphysical interactionMINT-48277MINT14743216
IKKE_HUMANphysical interactionMINT-48094MINT14743216
TRADD_HUMANphysical interactionMINT-49466MINT14743216
Q59EM9_HUMANphysical interactionMINT-63449MINT16169070
Q5VZC3_HUMANphysical interactionMINT-63451MINT16169070
Q6N083_HUMANphysical interactionMINT-63452MINT16169070
TANK_HUMANphysical interactionMINT-48249MINT14743216
M3K3_HUMANphysical interactionMINT-48380MINT14743216
HPBP1_HUMANphysical interactionMINT-63285MINT16169070
TRAF6_HUMANphysical interactionMINT-49568MINT14743216
NEMO_HUMANphysical interactionMINT-48134MINT14743216
ERH_HUMANphysical interactionEBI-730171
intact16169070
F16P1_HUMANphysical interactionEBI-730174
intact16169070
UBIQ_HUMANphysical interactionEBI-730177
intact16169070
T4S1_HUMANphysical interactionEBI-732157
intact16169070
DPP3_HUMANphysical interactionEBI-736928
intact16169070
PHC1_HUMANphysical interactionEBI-736931
intact16169070
TRADD_HUMANphysical interactionEBI-364822
intact14743216
APOB_HUMANin vivoHPRD:07205HPRD9694898
CLCA_HUMANin vitroHPRD:07205HPRD1975516
CYC_HUMANin vitro
in vivo
HPRD:07205HPRD8663341
AATM_HUMANin vitro
in vivo
HPRD:07205HPRD7559589
HS90A_HUMANin vivoHPRD:07205HPRD9269769
HSF1_HUMANin vitro
in vivo
HPRD:07205HPRD7639722
1433T_HUMANin vivoHPRD:07205HPRD15324660
JAK2_HUMANin vivoHPRD:07205HPRD11679576
STMN1_HUMANin vitro
in vivo
HPRD:07205HPRD10197448
REL_HUMANin vitroHPRD:07205HPRD2155506
CITE1_HUMANin vitro
in vivo
HPRD:07205HPRD10722728
SP1_HUMANin vitroHPRD:07205HPRD10976766
RB_HUMANin vitro
in vivo
HPRD:07205HPRD7673249
ALDOB_HUMANin vivoHPRD:07205HPRD11241348
BAG1_HUMANin vitro
yeast 2-hybrid
HPRD:07205HPRD9305631
11741305
CXCR4_HUMANin vitro
in vivo
HPRD:07205HPRD16365278
DYL1_HUMANin vitroHPRD:07205HPRD14760703
DNJA1_HUMANin vivoHPRD:07205HPRD10075921
BAG2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:07205HPRD9873016
BAG3_HUMANin vitro
in vivo
HPRD:07205HPRD9873016
ABI1_HUMANin vitroHPRD:07205HPRD15048123
GAK_HUMANin vitro
in vivo
HPRD:07205HPRD10625686
STUB1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:07205HPRD10330192
ERH_HUMANyeast 2-hybridHPRD:07205HPRD16169070
HDAC3_HUMANin vivoHPRD:07205HPRD12502735
HSP7C_HUMANin vitro
in vivo
HPRD:07205HPRD11679576
14993262
7578144
T4S1_HUMANyeast 2-hybridHPRD:07205HPRD16169070
TAD3L_HUMANyeast 2-hybridHPRD:07205HPRD16169070
DPP3_HUMANyeast 2-hybridHPRD:07205HPRD16169070
CD014_HUMANyeast 2-hybridHPRD:07205HPRD16169070
E2AK1_HUMANENSP00000227378STRING
STUB1_HUMANENSP00000227378STRING
BAG1_HUMANENSP00000227378STRING
TTC1_HUMANENSP00000227378STRING
CXCR4_HUMANENSP00000227378STRING
AATM_HUMANENSP00000227378STRING
AATM_HUMANENSP00000227378STRING
LRRC4_HUMANENSP00000227378STRING
DNJB1_HUMANENSP00000227378STRING
DNJCD_HUMANENSP00000227378STRING
DNJA3_HUMANENSP00000227378STRING
GRPE1_HUMANENSP00000227378STRING
DJB11_HUMANENSP00000227378STRING
P53_HUMANENSP00000227378STRING
BAG4_HUMANENSP00000227378STRING
CYC_HUMANENSP00000227378STRING
CYC_HUMANENSP00000227378STRING
ISCU_HUMANENSP00000227378STRING
DNJB5_HUMANENSP00000227378STRING
DNJB5_HUMANENSP00000227378STRING
HNRPD_HUMANENSP00000227378STRING
DNJA2_HUMANENSP00000227378STRING
GAK_HUMANENSP00000227378STRING
HS105_HUMANENSP00000227378STRING
IF4G1_HUMANENSP00000227378STRING
HSF1_HUMANENSP00000227378STRING
HS90A_HUMANENSP00000227378STRING
HS90A_HUMANENSP00000227378STRING
HS90A_HUMANENSP00000227378STRING
DNJA4_HUMANENSP00000227378STRING
CH60_HUMANENSP00000227378STRING
- top -

Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
- top -
Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-88; LYS-108; LYS-246;LYS-319; LYS-348; LYS-512; LYS-524; LYS-589; LYS-597 AND LYS-601, ANDMASS SPECTROMETRY.
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 THR-477, AND MASSSPECTROMETRY.
"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-15, 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-41 AND TYR-107, 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 SER-153, 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-113; TYR-115; SER-120AND SER-121, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541; SER-637 ANDSER-638, AND MASS SPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures