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-alpha  

UniProtKB / Swiss-Prot ID :  HS90A_HUMAN

Gene Name (Synonyms) : 
HSP90AA1, HSP90A, HSPC1, HSPCA  

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 MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKL...
Predicted Secondary Structure CCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHHHHHHHHHCCCHHHH...
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
5PhosphothreonineMPEETQTQD
CCCCCCCCC
34.94PhosphoELM
Link-
5PhosphothreonineMPEETQTQD
CCCCCCCCC
34.94Phosphositeplus
Link-
5Phosphothreonine (PRKDC)MPEETQTQD
CCCCCCCCC
34.94HPRD
Link-
5Phosphothreonine; by PRKDC.MPEETQTQD
CCCCCCCCC
34.94UniProtKB
Link-
7PhosphothreonineEETQTQDQP
CCCCCCCCC
41.34Phosphositeplus
Link-
7Phosphothreonine (DNA-PK;DNA-PK)EETQTQDQP
CCCCCCCCC
41.34PhosphoELM
Link-
7Phosphothreonine (PRKDC)EETQTQDQP
CCCCCCCCC
41.34HPRD
Link-
7Phosphothreonine; by PRKDC.EETQTQDQP
CCCCCCCCC
41.34UniProtKB
Link-
41Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FYSNKEIFL
HCCCCCHHH
46.37Phosphositeplus
Link
58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DALDKIRYE
HHHHHHHHH
29.90Phosphositeplus
Link
61PhosphotyrosineDKIRYESLT
HHHHHHHCC
17.22Phosphositeplus
Link
69Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TDPSKLDSG
CCHHHHCCC
62.80Phosphositeplus
Link
69N6-acetyllysineTDPSKLDSG
CCHHHHCCC
62.80HPRD
Link
69N6-acetyllysineTDPSKLDSG
CCHHHHCCC
62.80Phosphositeplus
Link
74Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LDSGKELHI
HCCCCCCEE
62.14Phosphositeplus
Link
84Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LIPNKQDRT
EEEECCCCE
48.50Phosphositeplus
Link
88PhosphothreonineKQDRTLTIV
CCCCEEEEE
36.22HPRD
Link
88PhosphothreonineKQDRTLTIV
CCCCEEEEE
36.22Phosphositeplus
Link
90PhosphothreonineDRTLTIVDT
CCEEEEEEC
20.52HPRD
Link
90PhosphothreonineDRTLTIVDT
CCEEEEEEC
20.52Phosphositeplus
Link
100N6-acetyllysineIGMTKADLI
CCCCHHHHH
30.89Phosphositeplus
Link
112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GTIAKSGTK
CHHHHHHHH
45.64Phosphositeplus
Link
185Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GRGTKVILH
CCCCEEEEE
30.06Phosphositeplus
Link
191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ILHLKEDQT
EEEECCCCH
48.80Phosphositeplus
Link
191N6-acetyllysineILHLKEDQT
EEEECCCCH
48.80HPRD
Link
197PhosphotyrosineDQTEYLEER
CCHHHHHHH
23.85Phosphositeplus
Link
209Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EIVKKHSQF
HHHHHHHCC
37.28Phosphositeplus
Link
224Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LFVEKERDK
EEEECCCCC
53.39Phosphositeplus
Link-
224N6-acetyllysineLFVEKERDK
EEEECCCCC
53.39HPRD
Link-
224N6-acetyllysineLFVEKERDK
EEEECCCCC
53.39Phosphositeplus
Link-
224N6-acetyllysine.LFVEKERDK
EEEECCCCC
53.39UniProtKB
Link-
228Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KERDKEVSD
CCCCCCCCC
67.26Phosphositeplus
Link-
231PhosphoserineDKEVSDDEA
CCCCCCCCC
40.20HPRD
Link-
231PhosphoserineDKEVSDDEA
CCCCCCCCC
40.20Phosphositeplus
Link-
231PhosphoserineDKEVSDDEA
CCCCCCCCC
40.20SysPTM
Link-
231Phosphoserine (CK2_group)DKEVSDDEA
CCCCCCCCC
40.20PhosphoELM
Link-
231Phosphoserine (CSNK2A1)DKEVSDDEA
CCCCCCCCC
40.20HPRD
Link-
231Phosphoserine.DKEVSDDEA
CCCCCCCCC
40.20UniProtKB
Link-
252PhosphoserineEEKESEDKP
HHHHHHHHH
63.26HPRD
Link-
252PhosphoserineEEKESEDKP
HHHHHHHHH
63.26PhosphoELM
Link-
252PhosphoserineEEKESEDKP
HHHHHHHHH
63.26Phosphositeplus
Link-
252PhosphoserineEEKESEDKP
HHHHHHHHH
63.26SysPTM
Link-
252Phosphoserine.EEKESEDKP
HHHHHHHHH
63.26UniProtKB
Link-
263PhosphoserineEDVGSDEEE
CCCCCCCHH
41.52HPRD
Link-
263PhosphoserineEDVGSDEEE
CCCCCCCHH
41.52Phosphositeplus
Link-
263PhosphoserineEDVGSDEEE
CCCCCCCHH
41.52SysPTM
Link-
263Phosphoserine (CK2_group;CK2_group;CK2_alpha;CK2_alpha)EDVGSDEEE
CCCCCCCHH
41.52PhosphoELM
Link-
263Phosphoserine (CSNK2A1)EDVGSDEEE
CCCCCCCHH
41.52HPRD
Link-
263Phosphoserine.EDVGSDEEE
CCCCCCCHH
41.52UniProtKB
Link-
274N6-acetyllysineKDGDKKKKK
CCCCCCCCC
72.52Phosphositeplus
Link-
276N6-acetyllysineGDKKKKKKI
CCCCCCCCC
75.47Phosphositeplus
Link-
283Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KIKEKYIDQ
CCCEEEECH
42.37Phosphositeplus
Link-
283N6-acetyllysineKIKEKYIDQ
CCCEEEECH
42.37HPRD
Link-
283N6-acetyllysineKIKEKYIDQ
CCCEEEECH
42.37Phosphositeplus
Link-
284PhosphotyrosineIKEKYIDQE
CCEEEECHH
15.72Phosphositeplus
Link-
292Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EELNKTKPI
HCCCCCCCC
71.23Phosphositeplus
Link-
292N6-acetyllysineEELNKTKPI
HCCCCCCCC
71.23HPRD
Link-
292N6-acetyllysineEELNKTKPI
HCCCCCCCC
71.23Phosphositeplus
Link-
294N6-acetyllysineLNKTKPIWT
CCCCCCCCC
35.79Phosphositeplus
Link-
314Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GEFYKSLTN
HHHHHHHHC
44.29Phosphositeplus
Link-
315PhosphoserineEFYKSLTND
HHHHHHHCC
29.10HPRD
Link-
315PhosphoserineEFYKSLTND
HHHHHHHCC
29.10Phosphositeplus
Link-
317PhosphothreonineYKSLTNDWE
HHHHHCCHH
37.92Phosphositeplus
Link-
327Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)HLAVKHFSV
HHHHHHEEE
33.07Phosphositeplus
Link-
327N6-acetyllysineHLAVKHFSV
HHHHHHEEE
33.07Phosphositeplus
Link-
362Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KNNIKLYVR
CCCCEEEEE
35.57Phosphositeplus
Link-
362N6-acetyllysineKNNIKLYVR
CCCCEEEEE
35.57HPRD
Link-
391PhosphoserineGVVDSEDLP
CEECCCCCC
22.77Phosphositeplus
Link-
399PhosphoserinePLNISREML
CCHHHHHHH
22.55Phosphositeplus
Link-
399Phosphoserine.PLNISREML
CCHHHHHHH
22.55UniProtKB
Link-
407Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LQQSKILKV
HHCCHHHHH
47.95Phosphositeplus
Link-
407N6-acetyllysineLQQSKILKV
HHCCHHHHH
47.95HPRD
Link-
410N6-acetyllysineSKILKVIRK
CHHHHHHHH
38.80HPRD
Link-
410N6-acetyllysine.SKILKVIRK
CHHHHHHHH
38.80UniProtKB
Link-
414N6-acetyllysineKVIRKNLVK
HHHHHHHHH
43.43HPRD
Link-
419Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NLVKKCLEL
HHHHHHHHH
36.25Phosphositeplus
Link-
420S-nitrosocysteineLVKKCLELF
HHHHHHHHH
2.71dbSNO
Link-
436Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ENYKKFYEQ
HHHHHHHHH
42.70Phosphositeplus
Link-
443Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EQFSKNIKL
HHHHHHHHC
65.07Phosphositeplus
Link-
443N6-acetyllysineEQFSKNIKL
HHHHHHHHC
65.07HPRD
Link-
443N6-acetyllysineEQFSKNIKL
HHHHHHHHC
65.07Phosphositeplus
Link-
443N6-acetyllysine.EQFSKNIKL
HHHHHHHHC
65.07UniProtKB
Link-
446Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SKNIKLGIH
HHHHHCCCC
50.48Phosphositeplus
Link-
458N6-acetyllysineQNRKKLSEL
HHHHHHHHH
54.75HPRD
Link-
458N6-acetyllysineQNRKKLSEL
HHHHHHHHH
54.75Phosphositeplus
Link-
458N6-acetyllysine.QNRKKLSEL
HHHHHHHHH
54.75UniProtKB
Link-
466PhosphotyrosineLLRYYTSAS
HHHHHCCCC
6.44Phosphositeplus
Link-
478N6-acetyllysineMVSLKDYCT
CEEHHHHHH
38.86Phosphositeplus
Link-
481S-nitrosocysteineLKDYCTRMK
HHHHHHHCC
2.52dbSNO
Link-
489Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KENQKHIYY
CCCCCEEEE
43.48Phosphositeplus
Link-
489N6-acetyllysineKENQKHIYY
CCCCCEEEE
43.48HPRD
Link-
489N6-acetyllysineKENQKHIYY
CCCCCEEEE
43.48Phosphositeplus
Link-
489N6-acetyllysine.KENQKHIYY
CCCCCEEEE
43.48UniProtKB
Link-
492PhosphotyrosineQKHIYYITG
CCEEEEEEC
6.63Phosphositeplus
Link-
499Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TGETKDQVA
ECCCHHHHH
41.69Phosphositeplus
Link-
505PhosphoserineQVANSAFVE
HHHHCCHHH
17.22Phosphositeplus
Link-
539Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EFEGKTLVS
HCCCCEEEE
31.33Phosphositeplus
Link-
546Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VSVTKEGLE
EEECCCCCC
47.86Phosphositeplus
Link-
546N6-acetyllysineVSVTKEGLE
EEECCCCCC
47.86Phosphositeplus
Link-
558Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DEEEKKKQE
CCHHHHHHH
69.42Phosphositeplus
Link-
558N6-acetyllysineDEEEKKKQE
CCHHHHHHH
69.42HPRD
Link-
558N6-acetyllysineDEEEKKKQE
CCHHHHHHH
69.42Phosphositeplus
Link-
565N6-acetyllysineQEEKKTKFE
HHHHHHHHH
61.29HPRD
Link-
566PhosphothreonineEEKKTKFEN
HHHHHHHHH
52.62Phosphositeplus
Link-
573N6-acetyllysineENLCKIMKD
HHHHHHHHH
49.34HPRD
Link-
576N6-acetyllysineCKIMKDILE
HHHHHHHCC
45.12HPRD
Link-
576N6-acetyllysineCKIMKDILE
HHHHHHHCC
45.12Phosphositeplus
Link-
576N6-acetyllysine.CKIMKDILE
HHHHHHHCC
45.12UniProtKB
Link-
585N6-acetyllysineKKVEKVVVS
CCEEEEEEE
43.23HPRD
Link-
585N6-acetyllysineKKVEKVVVS
CCEEEEEEE
43.23Phosphositeplus
Link-
585N6-acetyllysine.KKVEKVVVS
CCEEEEEEE
43.23UniProtKB
Link-
589PhosphoserineKVVVSNRLV
EEEEEEEEC
12.48HPRD
Link-
589PhosphoserineKVVVSNRLV
EEEEEEEEC
12.48Phosphositeplus
Link-
597S-nitrosocysteineVTSPCCIVT
CCCCEEEEE
2.18dbSNO
Link-
598S-nitrosocysteineTSPCCIVTS
CCCEEEEEC
2.96dbSNO
Link-
598S-nitrosocysteine.TSPCCIVTS
CCCEEEEEC
2.96UniProtKB
Link-
604PhosphotyrosineVTSTYGWTA
EECCCCCCH
15.50Phosphositeplus
Link-
615Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ERIMKAQAL
HHHHHHHCC
34.67Phosphositeplus
Link-
624PhosphothreonineRDNSTMGYM
CCCCCCCCC
22.37Phosphositeplus
Link-
627PhosphotyrosineSTMGYMAAK
CCCCCCCCC
3.46Phosphositeplus
Link-
631Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YMAAKKHLE
CCCCCCEEE
31.05Phosphositeplus
Link-
632Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MAAKKHLEI
CCCCCEEEE
49.01Phosphositeplus
Link-
641PhosphoserineNPDHSIIET
CCCCHHHHH
32.42HPRD
Link-
667PhosphotyrosineVILLYETAL
HHHHHHHHH
14.05HPRD
Link-
673PhosphoserineTALLSSGFS
HHHHHCCCC
29.30HPRD
Link-
674PhosphoserineALLSSGFSL
HHHHCCCCC
43.77HPRD
Link-
677PhosphoserineSSGFSLEDP
HCCCCCCCH
34.08HPRD
Link-
683PhosphothreonineEDPQTHANR
CCHHHHHHH
28.48HPRD
Link-
689PhosphotyrosineANRIYRMIK
HHHHHHHHH
7.29Phosphositeplus
Link-
704PhosphothreonineEDDPTADDT
CCCCCCCCC
50.11HPRD
Link-
708PhosphothreonineTADDTSAAV
CCCCCCCCC
22.32HPRD
Link-
709PhosphoserineADDTSAAVT
CCCCCCCCC
22.64HPRD
Link-
725PhosphothreonineGDDDTSRME
CCCCCCCCC
25.81HPRD
Link-
725PhosphothreonineGDDDTSRME
CCCCCCCCC
25.81PhosphoELM
Link-
726PhosphoserineDDDTSRMEE
CCCCCCCCC
36.30HPRD
Link-
726PhosphoserineDDDTSRMEE
CCCCCCCCC
36.30PhosphoELM
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
IKKB_HUMANphysical interactionMINT-47957MINT14743216
LCK_HUMANphysical interactionMINT-3373863MINT16888650
HS90A_HUMANphysical interactionMINT-64380MINT16169070
NOS3_HUMANphysical interactionMINT-17171MINT11744239
STIP1_HUMANphysical interactionMINT-15879MINT10786835
ZAP70_HUMANphysical interactionMINT-3374106MINT16888650
SYQ_HUMANphysical interactionMINT-17385MINT10913161
NFKB2_HUMANphysical interactionMINT-48760MINT14743216
M3K1_HUMANphysical interactionMINT-47979MINT14743216
IKKE_HUMANphysical interactionMINT-47962MINT14743216
IKKE_HUMANphysical interactionMINT-48120MINT14743216
Q14342_HUMANphysical interactionMINT-3373882MINT16888650
TRADD_HUMANphysical interactionMINT-49493MINT14743216
TAB1_HUMANphysical interactionMINT-49177MINT14743216
NOD1_HUMANphysical interactionMINT-62547MINT16083881
CDK4_HUMANphysical interactionDIP:817EDIP8703009
TEBP_HUMANphysical interactionDIP:821EDIP8114727
PRGR_HUMANphysical interactionDIP:822EDIP9178755
SRC_HUMANphysical interactionDIP:830EDIP1310678
GCR_HUMANphysical interactionDIP:753EDIP8089152
HS90A_HUMANphysical interactionDIP:761EDIP7588731
M3K1_HUMANphysical interactionDIP:44903EDIP14743216
M3K3_HUMANphysical interactionDIP:44914EDIP14743216
M3K7_HUMANphysical interactionDIP:44949EDIP14743216
IKKA_HUMANphysical interactionDIP:44882EDIP14743216
MMP2_HUMANphysical interactionEBI-1176756
intact15146192
HS90A_HUMANphysical interactionEBI-732202
intact16169070
STAT3_HUMANin vivoHPRD:00777HPRD12559950
APOB_HUMANin vitro
in vivo
HPRD:00777HPRD11333259
ASGR1_HUMANin vitro
in vivo
HPRD:00777HPRD12167617
CSK22_HUMANin vitroHPRD:00777HPRD7794926
ESR1_HUMANin vivoHPRD:00777HPRD11911945
MTG8_HUMANin vitro
in vivo
HPRD:00777HPRD10076566
GCR_HUMANin vitroHPRD:00777HPRD8898375
9334248
8645634
10066374
8621522
SYEP_HUMANin vitro
in vivo
HPRD:00777HPRD10913161
HS90A_HUMANin vitro
in vivo
HPRD:00777HPRD12504007
11779851
12167617
12482202
GCYB1_HUMANin vitro
in vivo
HPRD:00777HPRD12676772
BIRC5_HUMANin vivoHPRD:00777HPRD15894266
WASL_HUMANin vitro
in vivo
HPRD:00777HPRD15791211
IRAK1_HUMANin vitroHPRD:00777HPRD15647277
RS3A_HUMANyeast 2-hybridHPRD:00777HPRD16169070
SRC_HUMANin vivoHPRD:00777HPRD1310678
NOS1_HUMANin vitro
in vivo
HPRD:00777HPRD11284722
9880522
NR2C2_HUMANin vitroHPRD:00777HPRD14743216
M3K3_HUMANin vitroHPRD:00777HPRD14743216
M3K14_HUMANin vitroHPRD:00777HPRD14743216
TBK1_HUMANin vitroHPRD:00777HPRD14743216
IKKE_HUMANin vivoHPRD:00777HPRD14743216
FKBP4_HUMANENSP00000335153STRING
FKBP4_HUMANENSP00000335153STRING
FKBP4_HUMANENSP00000335153STRING
PPP5_HUMANENSP00000335153STRING
PPP5_HUMANENSP00000335153STRING
PPP5_HUMANENSP00000335153STRING
AHSA1_HUMANENSP00000335153STRING
AHSA1_HUMANENSP00000335153STRING
AHSA1_HUMANENSP00000335153STRING
STUB1_HUMANENSP00000335153STRING
STUB1_HUMANENSP00000335153STRING
STUB1_HUMANENSP00000335153STRING
CDC37_HUMANENSP00000335153STRING
CDC37_HUMANENSP00000335153STRING
CDC37_HUMANENSP00000335153STRING
HSP7C_HUMANENSP00000335153STRING
HSP7C_HUMANENSP00000335153STRING
HSP7C_HUMANENSP00000335153STRING
AHR_HUMANENSP00000335153STRING
AHR_HUMANENSP00000335153STRING
AHR_HUMANENSP00000335153STRING
RAF1_HUMANENSP00000335153STRING
RAF1_HUMANENSP00000335153STRING
RAF1_HUMANENSP00000335153STRING
DNJB1_HUMANENSP00000335153STRING
DNJB1_HUMANENSP00000335153STRING
DNJB1_HUMANENSP00000335153STRING
MDM2_HUMANENSP00000335153STRING
MDM2_HUMANENSP00000335153STRING
MDM2_HUMANENSP00000335153STRING
P53_HUMANENSP00000335153STRING
P53_HUMANENSP00000335153STRING
P53_HUMANENSP00000335153STRING
AKT1_HUMANENSP00000335153STRING
AKT1_HUMANENSP00000335153STRING
AKT1_HUMANENSP00000335153STRING
GNA12_HUMANENSP00000335153STRING
GNA12_HUMANENSP00000335153STRING
GNA12_HUMANENSP00000335153STRING
AIP_HUMANENSP00000335153STRING
AIP_HUMANENSP00000335153STRING
AIP_HUMANENSP00000335153STRING
HSP74_HUMANENSP00000335153STRING
HSP74_HUMANENSP00000335153STRING
HSP74_HUMANENSP00000335153STRING
PPID_HUMANENSP00000335153STRING
PPID_HUMANENSP00000335153STRING
PPID_HUMANENSP00000335153STRING
TERT_HUMANENSP00000335153STRING
TERT_HUMANENSP00000335153STRING
TERT_HUMANENSP00000335153STRING
CHRD1_HUMANENSP00000335153STRING
CHRD1_HUMANENSP00000335153STRING
CHRD1_HUMANENSP00000335153STRING
CHRD1_HUMANENSP00000335153STRING
CHRD1_HUMANENSP00000335153STRING
CHRD1_HUMANENSP00000335153STRING
CHRD1_HUMANENSP00000335153STRING
CHRD1_HUMANENSP00000335153STRING
CHRD1_HUMANENSP00000335153STRING
SMYD3_HUMANENSP00000335153STRING
SMYD3_HUMANENSP00000335153STRING
SMYD3_HUMANENSP00000335153STRING
HIF1A_HUMANENSP00000335153STRING
HIF1A_HUMANENSP00000335153STRING
HIF1A_HUMANENSP00000335153STRING
HIF1A_HUMANENSP00000335153STRING
HIF1A_HUMANENSP00000335153STRING
HIF1A_HUMANENSP00000335153STRING
CH60_HUMANENSP00000335153STRING
CH60_HUMANENSP00000335153STRING
CH60_HUMANENSP00000335153STRING
FKBP5_HUMANENSP00000335153STRING
FKBP5_HUMANENSP00000335153STRING
FKBP5_HUMANENSP00000335153STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00716Nedocromil
DB00615Rifabutin
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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-224; LYS-410; LYS-443;LYS-458; LYS-489; LYS-576 AND LYS-585, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"The human double-stranded DNA-activated protein kinase phosphorylatesthe 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminalthreonine residues.";
Lees-Miller S.P., Anderson C.W.;
J. Biol. Chem. 264:17275-17280(1989).
Cited for: PHOSPHORYLATION AT THR-5 AND THR-7.
"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-231 AND SER-263, ANDMASS SPECTROMETRY.
"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-231; SER-252 ANDSER-263, AND MASS SPECTROMETRY.
"Phosphoproteomic analysis of the human pituitary.";
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
Pituitary 9:109-120(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, 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-231 AND SER-263, 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-231; SER-252 ANDSER-263, AND MASS 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-263, 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-263, 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-263, AND MASSSPECTROMETRY.
"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-231 AND SER-263, ANDMASS 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-263, 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-399, AND MASSSPECTROMETRY.
S-nitrosylation
ReferencePubMed
"S-nitrosylation of Hsp90 promotes the inhibition of its ATPase andendothelial nitric oxide synthase regulatory activities.";
Martinez-Ruiz A., Villanueva L., Gonzalez de Orduna C.,Lopez-Ferrer D., Higueras M.A., Tarin C., Rodriguez-Crespo I.,Vazquez J., Lamas S.;
Proc. Natl. Acad. Sci. U.S.A. 102:8525-8530(2005).
Cited for: PROTEIN SEQUENCE OF 592-612, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESISOF CYS-598, AND S-NITROSYLATION AT CYS-598.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures