H1_YEAST - dbPTM
H1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H1_YEAST
UniProt AC P53551
Protein Name Histone H1
Gene Name HHO1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 258
Subcellular Localization Nucleus . Chromosome .
Protein Description Could act as an H1-type linker histone. Has been shown to bind DNA..
Protein Sequence MAPKKSTTKTTSKGKKPATSKGKEKSTSKAAIKKTTAKKEEASSKSYRELIIEGLTALKERKGSSRPALKKFIKENYPIVGSASNFDLYFNNAIKKGVEAGDFEQPKGPAGAVKLAKKKSPEVKKEKEVSPKPKQAATSVSATASKAKAASTKLAPKKVVKKKSPTVTAKKASSPSSLTYKEMILKSMPQLNDGKGSSRIVLKKYVKDTFSSKLKTSSNFDYLFNSAIKKCVENGELVQPKGPSGIIKLNKKKVKLST
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
26PhosphorylationTSKGKEKSTSKAAIK
CCCCCCCCCCHHHHH
38.7221440633
27PhosphorylationSKGKEKSTSKAAIKK
CCCCCCCCCHHHHHH
45.3621440633
28PhosphorylationKGKEKSTSKAAIKKT
CCCCCCCCHHHHHHH
27.6421440633
47PhosphorylationEEASSKSYRELIIEG
HHHCCHHHHHHHHHH
16.3121440633
64PhosphorylationALKERKGSSRPALKK
HHHHCCCCCCHHHHH
26.6419823750
65PhosphorylationLKERKGSSRPALKKF
HHHCCCCCCHHHHHH
51.4521551504
82PhosphorylationENYPIVGSASNFDLY
HCCCCCCCCCCCHHH
20.0330377154
96AcetylationYFNNAIKKGVEAGDF
HHCHHHHCCCCCCCC
63.1724489116
127AcetylationSPEVKKEKEVSPKPK
CHHHHCCCCCCCCCC
72.7525381059
130PhosphorylationVKKEKEVSPKPKQAA
HHCCCCCCCCCCHHH
28.4419823750
138PhosphorylationPKPKQAATSVSATAS
CCCCHHHHHHHHHHH
32.4530377154
141PhosphorylationKQAATSVSATASKAK
CHHHHHHHHHHHHHH
21.4823749301
143PhosphorylationAATSVSATASKAKAA
HHHHHHHHHHHHHHH
24.7730377154
145PhosphorylationTSVSATASKAKAAST
HHHHHHHHHHHHHHC
28.8830377154
164PhosphorylationKKVVKKKSPTVTAKK
HHHCCCCCCCCEECC
34.3828889911
166PhosphorylationVVKKKSPTVTAKKAS
HCCCCCCCCEECCCC
37.2627717283
168PhosphorylationKKKSPTVTAKKASSP
CCCCCCCEECCCCCC
34.9327717283
173PhosphorylationTVTAKKASSPSSLTY
CCEECCCCCCCCCCH
52.2222369663
174PhosphorylationVTAKKASSPSSLTYK
CEECCCCCCCCCCHH
33.3922369663
176PhosphorylationAKKASSPSSLTYKEM
ECCCCCCCCCCHHHH
39.6722890988
177PhosphorylationKKASSPSSLTYKEMI
CCCCCCCCCCHHHHH
28.2822890988
179PhosphorylationASSPSSLTYKEMILK
CCCCCCCCHHHHHHH
34.2022890988
180PhosphorylationSSPSSLTYKEMILKS
CCCCCCCHHHHHHHH
15.3928132839
186AcetylationTYKEMILKSMPQLND
CHHHHHHHHCCCCCC
33.5124489116
207AcetylationIVLKKYVKDTFSSKL
EEEEHHHHHHHHHHC
48.2222865919
213AcetylationVKDTFSSKLKTSSNF
HHHHHHHHCCCCCCH
53.4522865919
216PhosphorylationTFSSKLKTSSNFDYL
HHHHHCCCCCCHHHH
48.0730377154
217PhosphorylationFSSKLKTSSNFDYLF
HHHHCCCCCCHHHHH
23.0030377154
218PhosphorylationSSKLKTSSNFDYLFN
HHHCCCCCCHHHHHH
46.9130377154
222PhosphorylationKTSSNFDYLFNSAIK
CCCCCHHHHHHHHHH
14.7330377154
226PhosphorylationNFDYLFNSAIKKCVE
CHHHHHHHHHHHHHH
24.8430377154
229AcetylationYLFNSAIKKCVENGE
HHHHHHHHHHHHCCC
39.5824489116
248AcetylationKGPSGIIKLNKKKVK
CCCCCEEEECCCCCC
44.0525381059

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 H1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of H1_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 H1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VPH2_YEASTVPH2genetic
17314980
PFD1_YEASTPFD1genetic
17314980
RAS2_YEASTRAS2genetic
17314980
SUS1_YEASTSUS1genetic
17314980
PCNA_YEASTPOL30genetic
17314980
ELP4_YEASTELP4genetic
17314980
ARO1_YEASTARO1genetic
17314980
DPB3_YEASTDPB3genetic
17314980
NHP6A_YEASTNHP6Aphysical
18467557
ARP4_YEASTARP4physical
25542182
METW_YEASTYLL058Wgenetic
27708008
CS111_YEASTCOS111genetic
27708008
PHO89_YEASTPHO89genetic
27708008
RPN4_YEASTRPN4genetic
27708008
PEX19_YEASTPEX19genetic
27708008
MNN10_YEASTMNN10genetic
27708008
GNTK_YEASTYDR248Cgenetic
27708008
PEX10_YEASTPEX10genetic
27708008
RAD4_YEASTRAD4genetic
27708008
BLM10_YEASTBLM10genetic
27708008
YFF1_YEASTYFL051Cgenetic
27708008
NPY1_YEASTNPY1genetic
27708008
ASK10_YEASTASK10genetic
27708008
RL8A_YEASTRPL8Agenetic
27708008
RL17B_YEASTRPL17Bgenetic
27708008
YK104_YEASTYKR104Wgenetic
27708008
PAU23_YEASTPAU23genetic
27708008
ENV10_YEASTENV10genetic
27708008
YL225_YEASTYLR225Cgenetic
27708008
NDE1_YEASTNDL1genetic
27708008
YPT6_YEASTYPT6genetic
27708008
VPS9_YEASTVPS9genetic
27708008
RAD14_YEASTRAD14genetic
27708008
SIW14_YEASTSIW14genetic
27708008
MSO1_YEASTMSO1genetic
27708008
MDM12_YEASTMDM12genetic
27708008
YO075_YEASTYOL075Cgenetic
27708008
INO4_YEASTINO4genetic
27708008
WHI5_YEASTWHI5genetic
27708008
SUCA_YEASTLSC1genetic
27708008
FCY1_YEASTFCY1genetic
27708008
PPAL_YEASTLTP1genetic
27708008
YPR09_YEASTYPR109Wgenetic
27708008
KAR3_YEASTKAR3genetic
27708008
DOM34_YEASTDOM34genetic
29158977

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of H1_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-174, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, AND MASSSPECTROMETRY.

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