dbPTM

NACA_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NACA_SCHPO
UniProt AC	P87147
Protein Name	Nascent polypeptide-associated complex subunit alpha
Gene Name	egd2
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	173
Subcellular Localization	Cytoplasm. Nucleus. Predominantly cytoplasmic, may also transiently localize to the nucleus..
Protein Description	Component of the nascent polypeptide-associated complex (NAC), a dynamic component of the ribosomal exit tunnel, protecting the emerging polypeptides from interaction with other cytoplasmic proteins to ensure appropriate nascent protein targeting. The NAC complex also promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane and blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum. Ucp15 may also be involved in transcription regulation (By similarity)..
Protein Sequence	MSVESQPVEKISELPAGSTTVVHAEKAQKLIQKLGLKRVEGITRVAMRRPKNILLIINEPIVYKSSNNAYIVLGKVTVEDMAAQARAFNESQKQATETKEEAAITEESGDAQPADTAKIEESFEQEKAVDETGVDAKDIELVMAQANVSRAKAVTALKENNSDVVNAIMSLTM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSVESQPVE ------CCCCCCCCC	34.29	24763107
5	Phosphorylation	---MSVESQPVEKIS ---CCCCCCCCCHHH	37.31	24763107
18	Phosphorylation	ISELPAGSTTVVHAE HHCCCCCCEEEEEHH	24.02	25720772
19	Phosphorylation	SELPAGSTTVVHAEK HCCCCCCEEEEEHHH	23.77	24763107
20	Phosphorylation	ELPAGSTTVVHAEKA CCCCCCEEEEEHHHH	23.41	29996109
66	Phosphorylation	EPIVYKSSNNAYIVL CCEEEECCCCEEEEE	29.92	25720772
91	Phosphorylation	QARAFNESQKQATET HHHHHCHHHHHHHHC	43.72	27738172
105	Phosphorylation	TKEEAAITEESGDAQ CHHHHHHCCCCCCCC	29.04	25720772
108	Phosphorylation	EAAITEESGDAQPAD HHHHCCCCCCCCCCC	35.42	25720772
116	Phosphorylation	GDAQPADTAKIEESF CCCCCCCCHHHHHHH	31.77	21712547
122	Phosphorylation	DTAKIEESFEQEKAV CCHHHHHHHHHHHCC	22.69	28889911
149	Phosphorylation	VMAQANVSRAKAVTA HHHHCCCCHHHHHHH	26.74	25720772

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 NACA_SCHPO !!

Functions of PTM Sites

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

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 NACA_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of NACA_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of NACA_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of fission yeast."; Wilson-Grady J.T., Villen J., Gygi S.P.; J. Proteome Res. 7:1088-1097(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND MASSSPECTROMETRY.	18257517 [Abstract]