dbPTM

SRP21_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SRP21_YEAST
UniProt AC	P32342
Protein Name	Signal recognition particle subunit SRP21
Gene Name	SRP21
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	167
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..
Protein Sequence	MSVKPIDNYITNSVRLFEVNPSQTLFSISYKPPTQKTDTKVSFRTHNSHLSLNYKFTTNKSKDVSRLLSALGPRGVSITPGKIEKIAQSKKKNNKIKESSKKIKGKSIQDIVGLATLIVNTDVEKSDPAAKKTATEPKQKANAVQNNNGNSAASKKKKNKNKGKKKR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSVKPIDNY ------CCCCCCCCC	38.56	22814378
2	Phosphorylation	------MSVKPIDNY ------CCCCCCCCC	38.56	26447709
9	Phosphorylation	SVKPIDNYITNSVRL CCCCCCCCCCCCEEE	12.84	26447709
11	Phosphorylation	KPIDNYITNSVRLFE CCCCCCCCCCEEEEE	15.87	24909858
13	Phosphorylation	IDNYITNSVRLFEVN CCCCCCCCEEEEEEC	10.44	26447709
22	Phosphorylation	RLFEVNPSQTLFSIS EEEEECCCCCEEEEE	30.50	22369663
24	Phosphorylation	FEVNPSQTLFSISYK EEECCCCCEEEEEEC	33.82	22369663
27	Phosphorylation	NPSQTLFSISYKPPT CCCCCEEEEEECCCC	17.46	22369663
29	Phosphorylation	SQTLFSISYKPPTQK CCCEEEEEECCCCCC	26.38	22369663
30	Phosphorylation	QTLFSISYKPPTQKT CCEEEEEECCCCCCC	26.33	22369663
31	Ubiquitination	TLFSISYKPPTQKTD CEEEEEECCCCCCCC	37.42	23749301
34	Phosphorylation	SISYKPPTQKTDTKV EEEECCCCCCCCCEE	51.75	22369663
36	Ubiquitination	SYKPPTQKTDTKVSF EECCCCCCCCCEEEE	51.34	23749301
39	Phosphorylation	PPTQKTDTKVSFRTH CCCCCCCCEEEEECC	38.28	23749301
45	Phosphorylation	DTKVSFRTHNSHLSL CCEEEEECCCCCEEE	24.33	30377154
48	Phosphorylation	VSFRTHNSHLSLNYK EEEECCCCCEEEEEE	20.43	17287358
51	Phosphorylation	RTHNSHLSLNYKFTT ECCCCCEEEEEEECC	14.78	30377154
85	Acetylation	ITPGKIEKIAQSKKK CCCHHHHHHHHHHHH	46.98	24489116
106	Ubiquitination	SSKKIKGKSIQDIVG HHHHHCCCCHHHHHH	39.11	23749301
121	Phosphorylation	LATLIVNTDVEKSDP HHHEEECCCHHHCCH	30.44	23749301

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 SRP21_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SRP21_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 SRP21_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CALM_YEAST	CMD1	physical	16554755
MYO3_YEAST	MYO3	physical	16554755
SEC65_YEAST	SEC65	physical	16554755
SRP72_YEAST	SRP72	physical	16554755
SRP68_YEAST	SRP68	physical	16554755
SRP54_YEAST	SRP54	physical	16554755
SRP14_YEAST	SRP14	physical	18719252
SDCB2_HUMAN	SDCBP2	physical	27107014

Drug and Disease Associations

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

Regulatory Network of SRP21_YEAST

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Subunits of the Saccharomyces cerevisiae signal recognition particlerequired for its functional expression."; Brown J.D., Hann B.C., Medzihradszky K.F., Niwa M., Burlingame A.L.,Walter P.; EMBO J. 13:4390-4400(1994). Cited for: PROTEIN SEQUENCE OF 2-15; 45-55; 75-85 AND 107-120, IDENTIFICATION INTHE SRP COMPLEX, AND ACETYLATION AT SER-2.	7925282 [Abstract]
Phosphorylation
Reference	PubMed
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASSSPECTROMETRY.	17287358 [Abstract]