CHZ1_YEAST - dbPTM
CHZ1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHZ1_YEAST
UniProt AC P40019
Protein Name Histone H2A.Z-specific chaperone CHZ1
Gene Name CHZ1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 153
Subcellular Localization Nucleus .
Protein Description Forms a chaperone-bound H2A.Z-H2B complex that acts as a source for SWR1 complex-dependent H2A to H2A.Z histone replacement in chromatin..
Protein Sequence MSDEAKEKRELESQKESSHNKSEKSVEPKPKRRRRRNYDDYDAEVAKEETKAKNGLTKSENNGTVEDSESDMDDAKLDALMGNEGEEEEDDLAEIDTSNIITSGRRTRGKVIDYKKTAEELDKKEPSTGSKDDVGYGEKEEDDEDEEDDDFKE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MSDEAKEKR
------CCHHHHHHH
44.1322814378
6Acetylation--MSDEAKEKRELES
--CCHHHHHHHHHHH
62.8225381059
13PhosphorylationKEKRELESQKESSHN
HHHHHHHHHHHHHCC
60.2130377154
15AcetylationKRELESQKESSHNKS
HHHHHHHHHHHCCCC
69.6924489116
17PhosphorylationELESQKESSHNKSEK
HHHHHHHHHCCCCCC
43.8930377154
18PhosphorylationLESQKESSHNKSEKS
HHHHHHHHCCCCCCC
31.9730377154
22PhosphorylationKESSHNKSEKSVEPK
HHHHCCCCCCCCCCC
56.4229136822
24AcetylationSSHNKSEKSVEPKPK
HHCCCCCCCCCCCCC
67.8825381059
25PhosphorylationSHNKSEKSVEPKPKR
HCCCCCCCCCCCCCH
27.8824909858
29AcetylationSEKSVEPKPKRRRRR
CCCCCCCCCCHHHCC
50.0624489116
47AcetylationDYDAEVAKEETKAKN
HHHHHHHHHHHHHHC
62.3524489116
51AcetylationEVAKEETKAKNGLTK
HHHHHHHHHHCCCCC
61.7222865919
59PhosphorylationAKNGLTKSENNGTVE
HHCCCCCCCCCCCCC
40.0821126336
64PhosphorylationTKSENNGTVEDSESD
CCCCCCCCCCCCHHH
23.8922369663
68PhosphorylationNNGTVEDSESDMDDA
CCCCCCCCHHHCCHH
26.0322369663
70PhosphorylationGTVEDSESDMDDAKL
CCCCCCHHHCCHHHH
42.0322369663
97PhosphorylationDDLAEIDTSNIITSG
CCHHCCCCCCCCCCC
29.3622369663
98PhosphorylationDLAEIDTSNIITSGR
CHHCCCCCCCCCCCC
23.4522369663
102PhosphorylationIDTSNIITSGRRTRG
CCCCCCCCCCCCCCC
22.7222369663
103PhosphorylationDTSNIITSGRRTRGK
CCCCCCCCCCCCCCC
21.6422369663
110AcetylationSGRRTRGKVIDYKKT
CCCCCCCCEEEHHHH
32.5025381059
117PhosphorylationKVIDYKKTAEELDKK
CEEEHHHHHHHHHCC
34.8430377154
123AcetylationKTAEELDKKEPSTGS
HHHHHHHCCCCCCCC
72.2124489116
124AcetylationTAEELDKKEPSTGSK
HHHHHHCCCCCCCCC
74.6225381059
131AcetylationKEPSTGSKDDVGYGE
CCCCCCCCCCCCCCC
60.3324489116

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CHZ1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHZ1_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CHZ1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EIF3B_YEASTPRT1physical
16554755
NUP84_YEASTNUP84genetic
17314980
SLX5_YEASTSLX5genetic
17314980
VPS72_YEASTVPS72genetic
17314980
H2AZ_YEASTHTZ1physical
17289584
H2B1_YEASTHTB1physical
17289584
H2B2_YEASTHTB2physical
17289584
H2AZ_YEASTHTZ1physical
18641662
H2AZ_YEASTHTZ1physical
19385041
H2B1_YEASTHTB1physical
19385041
H2B2_YEASTHTB2physical
19385041
VPS8_YEASTVPS8genetic
20093466
EF1A_YEASTTEF2genetic
20093466
SLX5_YEASTSLX5genetic
20093466
UME6_YEASTUME6genetic
20093466
SWR1_YEASTSWR1genetic
20093466
EAF1_YEASTEAF1genetic
20093466
VMA21_YEASTVMA21genetic
20093466
SIN3_YEASTSIN3genetic
20093466
RS28A_YEASTRPS28Agenetic
20093466
YAR1_YEASTYAR1genetic
20093466
UBP10_YEASTUBP10genetic
20008511
NAB3_YEASTNAB3genetic
27708008
UME6_YEASTUME6genetic
27708008
VMA21_YEASTVMA21genetic
27708008
TRS23_YEASTTRS23genetic
27708008
ACT_YEASTACT1genetic
27708008
RFC2_YEASTRFC2genetic
27708008
PRP24_YEASTPRP24genetic
27708008
VPS8_YEASTVPS8genetic
27708008
EF1A_YEASTTEF2genetic
27708008
SWC5_YEASTSWC5genetic
27708008
SLX5_YEASTSLX5genetic
27708008
SWR1_YEASTSWR1genetic
27708008
ASK10_YEASTASK10genetic
27708008
SET2_YEASTSET2genetic
27708008
ARP6_YEASTARP6genetic
27708008
VPS9_YEASTVPS9genetic
27708008
SIN3_YEASTSIN3genetic
27708008
RS28A_YEASTRPS28Agenetic
27708008
CHL1_YEASTCHL1genetic
27708008
RL21B_YEASTRPL21Bgenetic
27708008
KA120_YEASTKAP120genetic
27708008
ALG5_YEASTALG5genetic
27708008
H2AZ_YEASTHTZ1physical
28883625
H2AZ_YEASTHTZ1genetic
28883625

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CHZ1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-70 AND SER-98,AND MASS SPECTROMETRY.

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