SRP14_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SRP14_YEAST
• UniProt AC: P38985
• Protein Name: Signal recognition particle subunit SRP14
• Gene Name: SRP14
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 146
• 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. SRP14 binds scR1 RNA to form the probable Alu domain of SRP responsible for elongation arrest..
• Protein Sequence: MANTGCLSPGAFLSKVPEFFQTANEKHITVRLTAKRLIEHDPVEGNLEFDSTNHPDYDVSKKASEISVSSRSDREYPLLIRMSYGSHDKKTKCSTVVKASELDQFWQEYSSVFKGGMQNLIKKKKKKSKNGTISKTGKKNKVAKKN

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
4	Phosphorylation	----MANTGCLSPGA ----CCCCCCCCCCH	21.53	19823750
8	Phosphorylation	MANTGCLSPGAFLSK CCCCCCCCCCHHHHC	25.93	19823750
14	Phosphorylation	LSPGAFLSKVPEFFQ CCCCHHHHCCHHHHH	25.75	30377154
26	Acetylation	FFQTANEKHITVRLT HHHHCCCCCEEEEEE	39.86	24489116
61	Acetylation	HPDYDVSKKASEISV CCCCCHHHHHHEEEE	52.81	24489116
64	Phosphorylation	YDVSKKASEISVSSR CCHHHHHHEEEECCC	44.32	21126336
67	Phosphorylation	SKKASEISVSSRSDR HHHHHEEEECCCCCC	16.34	30377154
69	Phosphorylation	KASEISVSSRSDREY HHHEEEECCCCCCCC	17.16	28889911
70	Phosphorylation	ASEISVSSRSDREYP HHEEEECCCCCCCCE	33.38	27214570

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SRP14_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SRP14_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SRP14_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LHP1_YEAST	LHP1	physical	16554755
YRA1_YEAST	YRA1	physical	16554755
SRP21_YEAST	SRP21	physical	16554755
SEC65_YEAST	SEC65	physical	16554755
SRP72_YEAST	SRP72	physical	16554755
SRP68_YEAST	SRP68	physical	16554755
SRP54_YEAST	SRP54	physical	16554755
LHP1_YEAST	LHP1	physical	16429126
SEC65_YEAST	SEC65	physical	16429126
SRP54_YEAST	SRP54	physical	16429126
SRP68_YEAST	SRP68	physical	16429126
SRP72_YEAST	SRP72	physical	16429126
SST2_YEAST	SST2	physical	16429126
CP51_YEAST	ERG11	physical	18467557
MIM1_YEAST	MIM1	physical	18467557
SRP72_YEAST	SRP72	physical	18467557
SRP54_YEAST	SRP54	physical	22940862
SEC65_YEAST	SEC65	physical	22940862
SRP68_YEAST	SRP68	physical	22940862
PAP2_YEAST	PAP2	genetic	25159613
RRP6_YEAST	RRP6	genetic	25159613
RRP44_YEAST	DIS3	genetic	25159613

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-8 AND SER-69, AND MASSSPECTROMETRY.
PubMed: 18407956