HPC2_YEAST - dbPTM
HPC2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HPC2_YEAST
UniProt AC Q01448
Protein Name Histone promoter control protein 2
Gene Name HPC2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 625
Subcellular Localization Nucleus .
Protein Description Component of the HIR complex, which functions as a histone chaperone that cooperates with ASF1 to promote replication-independent chromatin assembly. The HIR complex is also required for the periodic repression of three of the four histone gene loci during cell cycle as well as for autogenous regulation of the HTA1-HTB1 locus by H2A and H2B. DNA-binding by the HIR complex may repress transcription by inhibiting nucleosome remodeling by the SWI/SNF complex. The HIR complex may also be required for transcriptional silencing of centromeric, telomeric and mating-type loci in the absence of CAF-1..
Protein Sequence MDQKAIVLDNSKSGSKQTKSSGKMQTQTDTNAEVLNTDNSIKKETGSDSEDLFNKFSNKKTNRKIPNIAEELAKNRNYVKGASPSPIIISGSSSTSPSGPSSSSTNPMGIPTNRFNKNTVELYQHSPSPVMTTNKTDTEEKRQNNRNMDNKNTPERGSSSFAAKQLKISSLLTISSNEDSKTLHINDTNGNKNSNAASNNIPSAYAELHTEGNSIESLIKPPSSPRNKSLTPKVILPTQNMDGTIAKDPHLGDNTPGILIAKTSSPVNLDVESTAQSLGKFNKSTNSLKAALTKAPAEKVSLKRSISSVTNSDSNISSSKKPTSEKAKKSSSASAILPKPTTTKTSKKAASNSSDSTRKKNASNKTTSAIKKESNAGSKLNTVKKENSSLSSIKATEKEKDKGGNSTEAKNSTSNVRKEPTAKSPKRLVAAPTVSPPKILQTAETKAKEPSILIDVPLYQADTNDYLDENGQVIFNLSTLIKEKYHPKSKELAQLKDSKRNLLMQLSDHSNGSLEKEKDEEGDVIELDDDEDMEEDEGEIDTETNTVTTTISPKKKSHPMKGKNLIGKYDVEDPFIDDSELLWEEQRAATKDGFFVYFGPLIEKGHYASLERANGTMKRGGVKNK
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
13PhosphorylationIVLDNSKSGSKQTKS
EEECCCCCCCCCCCC		48.3928889911
40PhosphorylationEVLNTDNSIKKETGS
HHHCCCCCCCHHHCC		38.3019779198
45PhosphorylationDNSIKKETGSDSEDL
CCCCCHHHCCCHHHH		51.3622369663
47PhosphorylationSIKKETGSDSEDLFN
CCCHHHCCCHHHHHH		45.4422369663
49PhosphorylationKKETGSDSEDLFNKF
CHHHCCCHHHHHHHH		34.4125521595
74AcetylationNIAEELAKNRNYVKG
CHHHHHHHCCCCCCC		69.8924489116
83PhosphorylationRNYVKGASPSPIIIS
CCCCCCCCCCCEEEE		34.2822369663
85PhosphorylationYVKGASPSPIIISGS
CCCCCCCCCEEEECC		26.6622369663
90PhosphorylationSPSPIIISGSSSTSP
CCCCEEEECCCCCCC		23.3922369663
92PhosphorylationSPIIISGSSSTSPSG
CCEEEECCCCCCCCC		17.8322369663
93PhosphorylationPIIISGSSSTSPSGP
CEEEECCCCCCCCCC		40.9522369663
94PhosphorylationIIISGSSSTSPSGPS
EEEECCCCCCCCCCC		34.3021440633
95PhosphorylationIISGSSSTSPSGPSS
EEECCCCCCCCCCCC		46.7521440633
96PhosphorylationISGSSSTSPSGPSSS
EECCCCCCCCCCCCC		21.0122369663
98PhosphorylationGSSSTSPSGPSSSST
CCCCCCCCCCCCCCC		64.2021440633
101PhosphorylationSTSPSGPSSSSTNPM
CCCCCCCCCCCCCCC		46.5122369663
102PhosphorylationTSPSGPSSSSTNPMG
CCCCCCCCCCCCCCC		31.2921440633
103PhosphorylationSPSGPSSSSTNPMGI
CCCCCCCCCCCCCCC		45.5822369663
104PhosphorylationPSGPSSSSTNPMGIP
CCCCCCCCCCCCCCC		33.8622369663
105PhosphorylationSGPSSSSTNPMGIPT
CCCCCCCCCCCCCCC		45.3422369663
112PhosphorylationTNPMGIPTNRFNKNT
CCCCCCCCCCCCCCC		36.7922369663
117AcetylationIPTNRFNKNTVELYQ
CCCCCCCCCCEEEHH		51.8122865919
123PhosphorylationNKNTVELYQHSPSPV
CCCCEEEHHCCCCCC		7.2321440633
126PhosphorylationTVELYQHSPSPVMTT
CEEEHHCCCCCCCCC		16.1422369663
128PhosphorylationELYQHSPSPVMTTNK
EEHHCCCCCCCCCCC		32.8922369663
132PhosphorylationHSPSPVMTTNKTDTE
CCCCCCCCCCCCCHH		27.7028132839
133PhosphorylationSPSPVMTTNKTDTEE
CCCCCCCCCCCCHHH		19.3428132839
151UbiquitinationNNRNMDNKNTPERGS
HCCCCCCCCCCCCCC		58.9115699485
153PhosphorylationRNMDNKNTPERGSSS
CCCCCCCCCCCCCCH		28.3021440633
160PhosphorylationTPERGSSSFAAKQLK
CCCCCCCHHHHHHCE		22.1721551504
164UbiquitinationGSSSFAAKQLKISSL
CCCHHHHHHCEECCE		53.3815699485
164AcetylationGSSSFAAKQLKISSL
CCCHHHHHHCEECCE		53.3824489116
167UbiquitinationSFAAKQLKISSLLTI
HHHHHHCEECCEEEE		37.7415699485
169PhosphorylationAAKQLKISSLLTISS
HHHHCEECCEEEEEC		17.2224961812
170PhosphorylationAKQLKISSLLTISSN
HHHCEECCEEEEECC		30.7624961812
194PhosphorylationDTNGNKNSNAASNNI
CCCCCCCCCHHHCCC		29.4722369663
198PhosphorylationNKNSNAASNNIPSAY
CCCCCHHHCCCCHHH		28.1822369663
203PhosphorylationAASNNIPSAYAELHT
HHHCCCCHHHHHHHC		30.0721440633
205PhosphorylationSNNIPSAYAELHTEG
HCCCCHHHHHHHCCC		12.6322369663
210PhosphorylationSAYAELHTEGNSIES
HHHHHHHCCCCCHHH		59.2022369663
214PhosphorylationELHTEGNSIESLIKP
HHHCCCCCHHHHCCC		38.2920377248
217PhosphorylationTEGNSIESLIKPPSS
CCCCCHHHHCCCCCC		33.4522369663
223PhosphorylationESLIKPPSSPRNKSL
HHHCCCCCCCCCCCC		62.5922369663
224PhosphorylationSLIKPPSSPRNKSLT
HHCCCCCCCCCCCCC		33.3822369663
263PhosphorylationPGILIAKTSSPVNLD
CCEEEEECCCCCCCC		25.9722369663
264PhosphorylationGILIAKTSSPVNLDV
CEEEEECCCCCCCCH		31.7522369663
265PhosphorylationILIAKTSSPVNLDVE
EEEEECCCCCCCCHH		37.7922369663
280AcetylationSTAQSLGKFNKSTNS
HHHHHHCCCCCCCHH		51.5724489116
284PhosphorylationSLGKFNKSTNSLKAA
HHCCCCCCCHHHHHH		33.6522369663
285PhosphorylationLGKFNKSTNSLKAAL
HCCCCCCCHHHHHHH		30.3621440633
287PhosphorylationKFNKSTNSLKAALTK
CCCCCCHHHHHHHHH		31.1922369663
299AcetylationLTKAPAEKVSLKRSI
HHHCCHHHHCCCHHH		38.9525381059
303AcetylationPAEKVSLKRSISSVT
CHHHHCCCHHHHHCC		36.2725381059
305PhosphorylationEKVSLKRSISSVTNS
HHHCCCHHHHHCCCC		25.8222369663
307PhosphorylationVSLKRSISSVTNSDS
HCCCHHHHHCCCCCC		21.7222369663
308PhosphorylationSLKRSISSVTNSDSN
CCCHHHHHCCCCCCC		31.1522369663
310PhosphorylationKRSISSVTNSDSNIS
CHHHHHCCCCCCCCC		30.8422369663
312PhosphorylationSISSVTNSDSNISSS
HHHHCCCCCCCCCCC		32.8122369663
314PhosphorylationSSVTNSDSNISSSKK
HHCCCCCCCCCCCCC		35.5622369663
317PhosphorylationTNSDSNISSSKKPTS
CCCCCCCCCCCCCCC		32.5822369663
318PhosphorylationNSDSNISSSKKPTSE
CCCCCCCCCCCCCCH		42.2422369663
319PhosphorylationSDSNISSSKKPTSEK
CCCCCCCCCCCCCHH		37.6022369663
330PhosphorylationTSEKAKKSSSASAIL
CCHHHHHCCCCCCCC		28.9017287358
331PhosphorylationSEKAKKSSSASAILP
CHHHHHCCCCCCCCC		38.5117287358
332PhosphorylationEKAKKSSSASAILPK
HHHHHCCCCCCCCCC		33.0821551504
334PhosphorylationAKKSSSASAILPKPT
HHHCCCCCCCCCCCC		20.1429136822
366PhosphorylationKKNASNKTTSAIKKE
HHHCCCCHHHHHHHH		30.1821126336
368PhosphorylationNASNKTTSAIKKESN
HCCCCHHHHHHHHHC		32.9830377154
379AcetylationKESNAGSKLNTVKKE
HHHCCCCCCHHHHHH		44.8525381059
388PhosphorylationNTVKKENSSLSSIKA
HHHHHHCCCCHHCCC		33.4720190278
389PhosphorylationTVKKENSSLSSIKAT
HHHHHCCCCHHCCCC		43.8027214570
391PhosphorylationKKENSSLSSIKATEK
HHHCCCCHHCCCCCC		31.7830377154
421PhosphorylationSNVRKEPTAKSPKRL
CCCCCCCCCCCCCEE		48.0530377154
424PhosphorylationRKEPTAKSPKRLVAA
CCCCCCCCCCEEEEC		32.9421440633
433PhosphorylationKRLVAAPTVSPPKIL
CEEEECCCCCCCHHH		28.9622369663
435PhosphorylationLVAAPTVSPPKILQT
EEECCCCCCCHHHHC		37.6522369663
507PhosphorylationRNLLMQLSDHSNGSL
HHHHHHHHCCCCCCC		19.1819795423
510PhosphorylationLMQLSDHSNGSLEKE
HHHHHCCCCCCCCCC		48.1219795423
513PhosphorylationLSDHSNGSLEKEKDE
HHCCCCCCCCCCCCC		37.2919795423
563AcetylationKSHPMKGKNLIGKYD
CCCCCCCCCCCCCCC		42.9625381059
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 HPC2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HPC2_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 HPC2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YRA1_YEASTYRA1physical
16554755
HIR2_YEASTHIR2physical
16554755
HIR1_YEASTHIR1physical
16264190
HIR2_YEASTHIR2physical
16264190
HIR3_YEASTHIR3physical
16264190
H3_YEASTHHT1genetic
17314980
H4_YEASTHHF1genetic
17314980
SWD3_YEASTSWD3genetic
17314980
DEP1_YEASTDEP1genetic
17314980
PCNA_YEASTPOL30genetic
17314980
HIR1_YEASTHIR1genetic
17314980
DBP3_YEASTDBP3physical
18467557
HSP71_YEASTSSA1physical
19536198
NHP10_YEASTNHP10genetic
19547744
RSC8_YEASTRSC8physical
21698254
SNF2_YEASTSNF2physical
21698254
PHO84_YEASTPHO84genetic
22281500
YD132_YEASTYDR132Cgenetic
27708008
CRF1_YEASTCRF1genetic
27708008
PALF_YEASTRIM8genetic
27708008
MRM2_YEASTMRM2genetic
27708008
ASK10_YEASTASK10genetic
27708008
STB5_YEASTSTB5genetic
27708008
RL17B_YEASTRPL17Bgenetic
27708008
IZH2_YEASTIZH2genetic
27708008
ELO2_YEASTELO2genetic
27708008
PAT1_YEASTPAT1genetic
27708008
NHP10_YEASTNHP10genetic
27708008
SLX5_YEASTSLX5genetic
27708008
RPN4_YEASTRPN4genetic
27708008
H2A1_YEASTHTA1genetic
27708008
LSM6_YEASTLSM6genetic
27708008
SLX8_YEASTSLX8genetic
27708008
SPT2_YEASTSPT2genetic
27708008
RIM15_YEASTRIM15genetic
27708008
PUF4_YEASTPUF4genetic
27708008
MON1_YEASTMON1genetic
27708008
ATC1_YEASTPMR1genetic
27708008
HUR1_YEASTHUR1genetic
27708008
MSC7_YEASTMSC7genetic
27708008
DAL81_YEASTDAL81genetic
27708008
LSM1_YEASTLSM1genetic
27708008
FEN1_YEASTRAD27genetic
27708008
ELF1_YEASTELF1genetic
27708008
RM49_YEASTMRP49genetic
27708008
NU133_YEASTNUP133genetic
27708008
CDC73_YEASTCDC73genetic
27708008
CAC2_YEASTCAC2genetic
27708008
MSC1_YEASTMSC1genetic
27708008
ARMT1_YEASTYMR027Wgenetic
27708008
YM24_YEASTYMR147Wgenetic
27708008
LSM7_YEASTLSM7genetic
27708008
RCF2_YEASTRCF2genetic
27708008
COQ2_YEASTCOQ2genetic
27708008
DIA2_YEASTDIA2genetic
27708008
LEO1_YEASTLEO1genetic
27708008
DSE3_YEASTDSE3genetic
27708008
SPS4_YEASTSPS4genetic
27708008
KIP2_YEASTKIP2genetic
27708008
RLF2_YEASTRLF2genetic
27708008
MED1_YEASTMED1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HPC2_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 THR-45; SER-47; SER-49;SER-85; SER-223; SER-224; SER-265; SER-307; THR-310; SER-312; SER-332;SER-388 AND SER-435, AND MASS SPECTROMETRY.
"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 THR-45; SER-47; SER-332;SER-388 AND SER-435, AND MASS SPECTROMETRY.

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