SRP72_YEAST - dbPTM
SRP72_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRP72_YEAST
UniProt AC P38688
Protein Name Signal recognition particle subunit SRP72
Gene Name SRP72
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 640
Subcellular Localization Cytoplasm. Endoplasmic reticulum membrane. Nucleus. Transiently localizes to the nucleolus during biogenesis of the SRP. The SRP-RNC complex is bound to the endoplasmic reticulum membrane due to the interaction of the SRP with the membrane SRP-recept
Protein Description Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the arrest of nascent chain elongation during membrane targeting. SRP72 binds the 7S RNA only in presence of SRP68..
Protein Sequence MAKDNLTNLLSQLNIQLSQDEHSQVEQTCVKLLDSGCENPADVFRRCLVAVIQQDKYQKALHYLKKFKHIDDKYGRKFALEKLYIFYKLNMPDEFNTLYTAIITDDLDTVLKKDIESLRGILHVRAQYCYKNGLYQEAFKIYQHLASHNEKDQDSQIELSCNERVPLSVATELMNRSPLVTPMDESSYDLLFNESFIMASVGKYDKAIELLEKALQGATNEGYQNDINTIKLQLSFVLQMVGKTAQSKEILKGLLQELKADSPFSLICQNNLNAFVDFSKYNTNFNLLLRELNVEKLNTFNLQTFTHEQWSNIQRNVLFLRLFNNVKIHSQESLLSRTFDKYSKLVDNVTLESYKTQAKKLYHHTTKTILSGTDGSTIGILLLTIQLLIIEKEWENAIRIGELFLNESWKSSFEKFNDSQAIVCYILFELYKIKGRNNSKSVLLKKLGSVRVQLSGKIQENIPFWKHVGFELLSMGNAKESKALLREISNFSKGDADVLVDRVVSSDSLDIAQGIDLVRDIDIDKLIQLGVKPLESSAKRSKNTAVSKVQKRKVLELKKKRKIKRLEKFLQGRDTSKLPDPERWLPLRDRSTYRPKKKQQGAKQTQGGAMNKKSEQALDISKKGKPTVNKKPKNKKKGRK
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
73AcetylationKFKHIDDKYGRKFAL
HCCCCCCCCCHHHHH		45.9525381059
97PhosphorylationNMPDEFNTLYTAIIT
CCCCHHHHHHHHHHC		26.8530377154
99PhosphorylationPDEFNTLYTAIITDD
CCHHHHHHHHHHCCC		7.6530377154
100PhosphorylationDEFNTLYTAIITDDL
CHHHHHHHHHHCCCH		17.9430377154
109PhosphorylationIITDDLDTVLKKDIE
HHCCCHHHHHHHHHH		34.7330377154
151AcetylationHLASHNEKDQDSQIE
HHHHCCCCCCCCCEE		67.0424489116
155PhosphorylationHNEKDQDSQIELSCN
CCCCCCCCCEECCCC		27.6828889911
206AcetylationASVGKYDKAIELLEK
HHCCCHHHHHHHHHH		48.4524489116
265PhosphorylationLKADSPFSLICQNNL
HCCCCCCEEEECCCC		21.8721440633
279PhosphorylationLNAFVDFSKYNTNFN
CCCCCCHHHHCCCHH		29.7521440633
327AcetylationLRLFNNVKIHSQESL
HHHHCCCCCCCCHHH		36.5024489116
411PhosphorylationFLNESWKSSFEKFND
HCCCHHHHHHHHCCH		33.7219795423
412PhosphorylationLNESWKSSFEKFNDS
CCCHHHHHHHHCCHH		33.4319795423
505PhosphorylationVLVDRVVSSDSLDIA
HHHEEECCCCCCCHH		26.1029688323
506PhosphorylationLVDRVVSSDSLDIAQ
HHEEECCCCCCCHHH		21.4329734811
508PhosphorylationDRVVSSDSLDIAQGI
EEECCCCCCCHHHCC		29.8628889911
614PhosphorylationGGAMNKKSEQALDIS
CCCCCHHHHHHHHHH		36.2321440633
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 SRP72_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRP72_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 SRP72_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BEM2_YEASTBEM2physical
16429126
HSP82_YEASTHSP82physical
16429126
LHP1_YEASTLHP1physical
16429126
SEC65_YEASTSEC65physical
16429126
SRP14_YEASTSRP14physical
16429126
SRP21_YEASTSRP21physical
16429126
SRP54_YEASTSRP54physical
16429126
SRP68_YEASTSRP68physical
16429126
GET3_YEASTGET3genetic
16269340
GET1_YEASTGET1genetic
16269340
CHO2_YEASTCHO2genetic
16269340
SSH1_YEASTSSH1genetic
16269340
SC6B2_YEASTSBH2genetic
16269340
RL3_YEASTRPL3physical
21765803
NACA_YEASTEGD2physical
21765803
G3P3_YEASTTDH3physical
22940862
YCZ2_YEASTYCR102Cgenetic
27708008
APT2_YEASTAPT2genetic
27708008
SAC1_YEASTSAC1genetic
27708008
YL287_YEASTYLR287Cgenetic
27708008
SEI1_YEASTFLD1genetic
27708008
HIR1_YEASTHIR1genetic
27708008
FMP23_YEASTFMP23genetic
27708008
SSH1_YEASTSSH1genetic
27708008
ERS1_YEASTERS1genetic
27708008
RL13A_YEASTRPL13Agenetic
27708008
BAP3_YEASTBAP3genetic
27708008
MNN10_YEASTMNN10genetic
27708008
HSP78_YEASTHSP78genetic
27708008
CEM1_YEASTCEM1genetic
27708008
GET2_YEASTGET2genetic
27708008
AIM11_YEASTAIM11genetic
27708008
MSH4_YEASTMSH4genetic
27708008
GET1_YEASTGET1genetic
27708008
CGR1_YEASTCGR1genetic
27708008
XRN1_YEASTXRN1genetic
27708008
RME1_YEASTRME1genetic
27708008
YG1X_YEASTYGR050Cgenetic
27708008
MUP1_YEASTMUP1genetic
27708008
OPI1_YEASTOPI1genetic
27708008
HTD2_YEASTHTD2genetic
27708008
KC11_YEASTYCK1genetic
27708008
AIM18_YEASTAIM18genetic
27708008
SNL1_YEASTSNL1genetic
27708008
SDS3_YEASTSDS3genetic
27708008
THIK_YEASTPOT1genetic
27708008
NCA3_YEASTNCA3genetic
27708008
IF4A_YEASTTIF2genetic
27708008
RPA34_YEASTRPA34genetic
27708008
YJY1_YEASTYJR011Cgenetic
27708008
UBL1_YEASTYUH1genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
TCD2_YEASTTCD2genetic
27708008
FABG_YEASTOAR1genetic
27708008
MUD2_YEASTMUD2genetic
27708008
KTI12_YEASTKTI12genetic
27708008
MCR1_YEASTMCR1genetic
27708008
ELF1_YEASTELF1genetic
27708008
DCOR_YEASTSPE1genetic
27708008
CBT1_YEASTCBT1genetic
27708008
ENV10_YEASTENV10genetic
27708008
ENT2_YEASTENT2genetic
27708008
LIPB_YEASTLIP2genetic
27708008
YL278_YEASTYLR278Cgenetic
27708008
EFM7_YEASTNNT1genetic
27708008
COX8_YEASTCOX8genetic
27708008
GBLP_YEASTASC1genetic
27708008
RAD14_YEASTRAD14genetic
27708008
BRE5_YEASTBRE5genetic
27708008
PHO80_YEASTPHO80genetic
27708008
LIPA_YEASTLIP5genetic
27708008
FABD_YEASTMCT1genetic
27708008
PMT3_YEASTPMT3genetic
27708008
HAP5_YEASTHAP5genetic
27708008
SUE1_YEASTSUE1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SRP72_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-508, AND MASSSPECTROMETRY.

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