DOHH_YEAST - dbPTM
DOHH_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DOHH_YEAST
UniProt AC P47120
Protein Name Deoxyhypusine hydroxylase {ECO:0000255|HAMAP-Rule:MF_03101}
Gene Name LIA1 {ECO:0000255|HAMAP-Rule:MF_03101}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 325
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor..
Protein Sequence MSTNFEKHFQENVDECTLEQLRDILVNKSGKTVLANRFRALFNLKTVAEEFATKPEEAKKAIEYIAESFVNDKSELLKHEVAYVLGQTKNLDAAPTLRHVMLDQNQEPMVRHEAAEALGALGDKDSLDDLNKAAKEDPHVAVRETCELAINRINWTHGGAKDKENLQQSLYSSIDPAPPLPLEKDATIPELQALLNDPKQPLFQRYRAMFRLRDIGTDEAILALATGFSAESSLFKHEIAYVFGQIGSPAAVPSLIEVLGRKEEAPMVRHEAAEALGAIASPEVVDVLKSYLNDEVDVVRESCIVALDMYDYENSNELEYAPTAN
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------MSTNFEKHF
------CCCHHHHHH		31.879298649
2Phosphorylation------MSTNFEKHF
------CCCHHHHHH		31.8727717283
3Phosphorylation-----MSTNFEKHFQ
-----CCCHHHHHHH		42.5027717283
7Acetylation-MSTNFEKHFQENVD
-CCCHHHHHHHHCCC		45.6524489116
45UbiquitinationFRALFNLKTVAEEFA
HHHHHCHHHHHHHHC		41.9024961812
45AcetylationFRALFNLKTVAEEFA
HHHHHCHHHHHHHHC		41.9024489116
54AcetylationVAEEFATKPEEAKKA
HHHHHCCCHHHHHHH		47.1824489116
73AcetylationAESFVNDKSELLKHE
HHHHCCCHHHHHHHH		40.4024489116
78AcetylationNDKSELLKHEVAYVL
CCHHHHHHHHHHHHH		50.7924489116
89AcetylationAYVLGQTKNLDAAPT
HHHHCCCCCCCCCCC		47.8524489116
96PhosphorylationKNLDAAPTLRHVMLD
CCCCCCCCHHHHHCC		31.5325704821
124AcetylationALGALGDKDSLDDLN
HHHHCCCCCCHHHHH		47.6324489116
126PhosphorylationGALGDKDSLDDLNKA
HHCCCCCCHHHHHHH		39.1627214570
132AcetylationDSLDDLNKAAKEDPH
CCHHHHHHHHHHCCC		57.9524489116
161AcetylationNWTHGGAKDKENLQQ
CCCCCCCCCHHHHHH		73.0224489116
163AcetylationTHGGAKDKENLQQSL
CCCCCCCHHHHHHHH		48.0424489116
169PhosphorylationDKENLQQSLYSSIDP
CHHHHHHHHHHCCCC		19.1322369663
171PhosphorylationENLQQSLYSSIDPAP
HHHHHHHHHCCCCCC		12.9622369663
172PhosphorylationNLQQSLYSSIDPAPP
HHHHHHHHCCCCCCC		26.5522369663
173PhosphorylationLQQSLYSSIDPAPPL
HHHHHHHCCCCCCCC		19.9022369663
187PhosphorylationLPLEKDATIPELQAL
CCCCCCCCHHHHHHH		47.3928889911
199AcetylationQALLNDPKQPLFQRY
HHHHCCCCCHHHHHH		68.3724489116
248PhosphorylationYVFGQIGSPAAVPSL
HHHHHCCCCCHHHHH		17.0022369663
281PhosphorylationEALGAIASPEVVDVL
HHHHHHCCHHHHHHH		18.5822369663
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 DOHH_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DOHH_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 DOHH_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRO9_YEASTSRO9genetic
14764870
ARF1_YEASTARF1genetic
14764870
MED31_YEASTSOH1genetic
14764870
IF5A1_YEASTHYP2physical
14675757
HSL1_YEASTHSL1physical
18467557
TRPE_YEASTTRP2physical
18719252
PRTB_YEASTPRB1genetic
14764870
RMD9_YEASTRMD9genetic
14764870
RTF1_YEASTRTF1genetic
14764870
MED20_YEASTSRB2genetic
14764870
TMA23_YEASTTMA23genetic
14764870
ADE_YEASTAAH1genetic
14764870
IF5A1_YEASTHYP2physical
19956996
BOS1_YEASTBOS1genetic
27708008
SEC63_YEASTSEC63genetic
27708008
YG1I_YEASTYGR026Wgenetic
27708008
YG2G_YEASTYGR079Wgenetic
27708008
MRT4_YEASTMRT4genetic
27708008
MID2_YEASTMID2genetic
27708008
EOS1_YEASTEOS1genetic
27708008
STU1_YEASTSTU1genetic
27708008
SYIC_YEASTILS1genetic
27708008
PRP6_YEASTPRP6genetic
27708008
CALM_YEASTCMD1genetic
27708008
CDK1_YEASTCDC28genetic
27708008
CDC10_YEASTCDC10genetic
27708008
PRP9_YEASTPRP9genetic
27708008
PRP11_YEASTPRP11genetic
27708008
RRP1_YEASTRRP1genetic
27708008
CDC1_YEASTCDC1genetic
27708008
SP110_YEASTSPC110genetic
27708008
PRS8_YEASTRPT6genetic
27708008
RCC1_YEASTSRM1genetic
27708008
SWC4_YEASTSWC4genetic
27708008
PRP18_YEASTPRP18genetic
27708008
RPF2_YEASTRPF2genetic
27708008
DCA13_YEASTSOF1genetic
27708008
COFI_YEASTCOF1genetic
27708008
GSP1_YEASTGSP1genetic
27708008
RU1C_YEASTYHC1genetic
27708008
MED11_YEASTMED11genetic
27708008
CBF3B_YEASTCEP3genetic
27708008
NOP2_YEASTNOP2genetic
27708008
HRP1_YEASTHRP1genetic
27708008
THIL_YEASTERG10genetic
27708008
IPL1_YEASTIPL1genetic
27708008
NSL1_YEASTNSL1genetic
27708008
TF2B_YEASTSUA7genetic
27708008
RS8A_YEASTRPS8Agenetic
27708008
RS8B_YEASTRPS8Agenetic
27708008
RL4A_YEASTRPL4Agenetic
27708008
CSG2_YEASTCSG2genetic
27708008
ELO2_YEASTELO2genetic
27708008
PAT1_YEASTPAT1genetic
27708008
RPN4_YEASTRPN4genetic
27708008
VMS1_YEASTVMS1genetic
27708008
SWF1_YEASTSWF1genetic
27708008
SNX41_YEASTSNX41genetic
27708008
PPN1_YEASTPPN1genetic
27708008
PUF6_YEASTPUF6genetic
27708008
CAJ1_YEASTCAJ1genetic
27708008
BLM10_YEASTBLM10genetic
27708008
FAB1_YEASTFAB1genetic
27708008
SDS23_YEASTSDS23genetic
27708008
SGF73_YEASTSGF73genetic
27708008
ATC1_YEASTPMR1genetic
27708008
STF2_YEASTSTF2genetic
27708008
YG1T_YEASTYGR042Wgenetic
27708008
ASK10_YEASTASK10genetic
27708008
CPD1_YEASTCPD1genetic
27708008
URM1_YEASTURM1genetic
27708008
PIG2_YEASTPIG2genetic
27708008
REV7_YEASTREV7genetic
27708008
YJV8_YEASTYJL218Wgenetic
27708008
AIM26_YEASTAIM26genetic
27708008
MDM35_YEASTMDM35genetic
27708008
YET1_YEASTYET1genetic
27708008
CYT2_YEASTCYT2genetic
27708008
TGL1_YEASTTGL1genetic
27708008
PYRD_YEASTURA1genetic
27708008
RL40A_YEASTRPL40Bgenetic
27708008
RL40B_YEASTRPL40Bgenetic
27708008
LCL2_YEASTLCL2genetic
27708008
SWI6_YEASTSWI6genetic
27708008
EFM7_YEASTNNT1genetic
27708008
RS30A_YEASTRPS30Agenetic
27708008
RS30B_YEASTRPS30Agenetic
27708008
ELO3_YEASTELO3genetic
27708008
CDC73_YEASTCDC73genetic
27708008
RS3A2_YEASTRPS1Bgenetic
27708008
HMDH1_YEASTHMG1genetic
27708008
ARMT1_YEASTYMR027Wgenetic
27708008
IOC4_YEASTIOC4genetic
27708008
ADT1_YEASTAAC1genetic
27708008
SCS7_YEASTSCS7genetic
27708008
JNM1_YEASTJNM1genetic
27708008
SIW14_YEASTSIW14genetic
27708008
APJ1_YEASTAPJ1genetic
27708008
HMI1_YEASTHMI1genetic
27708008
SFL1_YEASTSFL1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
TGS1_YEASTTGS1genetic
27708008
RKM1_YEASTRKM1genetic
27708008
NEW1_YEASTNEW1genetic
27708008
BRR1_YEASTBRR1genetic
27708008
SPEE_YEASTSPE3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DOHH_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins.";
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.;
Electrophoresis 18:1347-1360(1997).
Cited for: ACETYLATION AT SER-2.
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-169 AND SER-281, ANDMASS 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 SER-281, 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-281, AND MASSSPECTROMETRY.

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