SRP68_YEAST - dbPTM
SRP68_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRP68_YEAST
UniProt AC P38687
Protein Name Signal recognition particle subunit SRP68
Gene Name SRP68
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 599
Subcellular Localization Cytoplasm. Nucleus .
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. SRP68 binds the 7S RNA, SRP72 binds to this complex subsequently..
Protein Sequence MVAYSPIIATYGNRAEQFLETDSDFAKYHAKLNKKLQHLRSRCHLVTKDTKKYSSKNKYGEINSEDYDNKTKLIGVLILLHAERDLALAETLKLRARQRGKLKKSEEKVLSTRLKKACKTADKLVNVTQNEQQWITRAQYLAFAKLVHSEYLINGKRFKRKDNAKISNNLALVFAALEHLKNLSLLAEEVVDNIVNKYQYSLKQYAGNLITTPEINNFIVERVQSDENKDDELVKLLLDNGFNMKKITTSTEDQKVTTNINWRSFNAKIIDAEVAQFLEQGLSIHPTQITQYTQRLSKLEKALDRHEFFIANHDDQDDIDEMVENSSENNQIILAYIKYNILLTSISRERDLFTHLWNQWLKLNTSLPSKLTKYKEMERIVKNLTKYLSDIMELPGVYSDDELLSQLDLCKLYFQLFLNTGCLSVLYQSKGRYMEALALYVDAYRRLENKLSEIESLDEILLPANLLSLNSVRSLQKRIENGGNSVITLAEYEKRNHGGSLGKYDLTVIEKLDSKKILPTDIQLKNLFPLKPKMLPIPSKPTLFDLAFNYITYDKQEPSASQVKDSVTETESISQTPISNEQTEGEPKKKRGFLGLFGR
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
23PhosphorylationEQFLETDSDFAKYHA
HHHHHCCHHHHHHHH		41.8927214570
27AcetylationETDSDFAKYHAKLNK
HCCHHHHHHHHHHHH		37.2524489116
53PhosphorylationVTKDTKKYSSKNKYG
EECCCCCCCCCCCCC		21.5219823750
54PhosphorylationTKDTKKYSSKNKYGE
ECCCCCCCCCCCCCC		43.6519823750
55PhosphorylationKDTKKYSSKNKYGEI
CCCCCCCCCCCCCCC		36.8419823750
59PhosphorylationKYSSKNKYGEINSED
CCCCCCCCCCCCHHH		29.4119823750
64PhosphorylationNKYGEINSEDYDNKT
CCCCCCCHHHCCCHH		37.1919823750
67PhosphorylationGEINSEDYDNKTKLI
CCCCHHHCCCHHHHH		19.8419823750
249PhosphorylationFNMKKITTSTEDQKV
CCEEECCCCCCCCEE		36.8023749301
250PhosphorylationNMKKITTSTEDQKVT
CEEECCCCCCCCEEE		22.5827717283
251PhosphorylationMKKITTSTEDQKVTT
EEECCCCCCCCEEEE		41.3027717283
369PhosphorylationKLNTSLPSKLTKYKE
HHCCCCCHHHHHHHH		45.6627214570
494AcetylationITLAEYEKRNHGGSL
EEEEEEEHHHCCCCC		58.5624489116
503AcetylationNHGGSLGKYDLTVIE
HCCCCCCCCCEEEEE		40.6724489116
531AcetylationLKNLFPLKPKMLPIP
CCCCCCCCCCCCCCC		42.7124489116
566PhosphorylationSASQVKDSVTETESI
CHHHCCCCCCCCCCC		25.8127717283
568PhosphorylationSQVKDSVTETESISQ
HHCCCCCCCCCCCCC		40.9328889911
570PhosphorylationVKDSVTETESISQTP
CCCCCCCCCCCCCCC		26.1822369663
572PhosphorylationDSVTETESISQTPIS
CCCCCCCCCCCCCCC		34.6525521595
574PhosphorylationVTETESISQTPISNE
CCCCCCCCCCCCCCC		36.9625521595
576PhosphorylationETESISQTPISNEQT
CCCCCCCCCCCCCCC		18.7922369663
579PhosphorylationSISQTPISNEQTEGE
CCCCCCCCCCCCCCC		35.2025521595
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 SRP68_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRP68_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 SRP68_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC73_YEASTCDC73physical
16554755
SEC65_YEASTSEC65physical
16554755
SRP72_YEASTSRP72physical
16554755
AHA1_YEASTAHA1physical
16429126
LHP1_YEASTLHP1physical
16429126
SEC65_YEASTSEC65physical
16429126
SRP14_YEASTSRP14physical
16429126
SRP54_YEASTSRP54physical
16429126
SRP72_YEASTSRP72physical
16429126
RDS1_YEASTRDS1physical
18719252
RL3_YEASTRPL3physical
21765803
NACA_YEASTEGD2physical
21765803
MCM1_YEASTMCM1genetic
27708008
VPS41_YEASTVPS41genetic
27708008
PET8_YEASTPET8genetic
27708008
STU1_YEASTSTU1genetic
27708008
PRP6_YEASTPRP6genetic
27708008
CDC37_YEASTCDC37genetic
27708008
SEC65_YEASTSEC65genetic
27708008
BUR1_YEASTSGV1genetic
27708008
YAJ9_YEASTYAR029Wgenetic
27708008
ICS2_YEASTICS2genetic
27708008
SSH1_YEASTSSH1genetic
27708008
GPR1_YEASTGPR1genetic
27708008
GET3_YEASTGET3genetic
27708008
BAP3_YEASTBAP3genetic
27708008
ACL4_YEASTYDR161Wgenetic
27708008
APT2_YEASTAPT2genetic
27708008
GET1_YEASTGET1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
YGZ2_YEASTYGL242Cgenetic
27708008
YG1X_YEASTYGR050Cgenetic
27708008
TNA1_YEASTTNA1genetic
27708008
MAL12_YEASTMAL12genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
YJ90_YEASTYJR120Wgenetic
27708008
MCR1_YEASTMCR1genetic
27708008
ELF1_YEASTELF1genetic
27708008
DCOR_YEASTSPE1genetic
27708008
SAC1_YEASTSAC1genetic
27708008
PCKA_YEASTPCK1genetic
27708008
PUR91_YEASTADE16genetic
27708008
ENV10_YEASTENV10genetic
27708008
APTH1_YEASTYLR118Cgenetic
27708008
COX7_YEASTCOX7genetic
27708008
MKT1_YEASTMKT1genetic
27708008
PHO23_YEASTPHO23genetic
27708008
BRE5_YEASTBRE5genetic
27708008
LDS2_YEASTLDS2genetic
27708008
CY1_YEASTCYT1genetic
27708008
PMT3_YEASTPMT3genetic
27708008
YP089_YEASTYPR089Wgenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SRP68_YEAST

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Related Literatures of Post-Translational Modification

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