NACA2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NACA2_HUMAN
• UniProt AC: Q9H009
• Protein Name: Nascent polypeptide-associated complex subunit alpha-2
• Gene Name: NACA2
• Organism: Homo sapiens (Human).
• Sequence Length: 215
• Subcellular Localization: Cytoplasm. Nucleus.
• Protein Description: Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites) (By similarity)..
• Protein Sequence: MPGEATETVPATEQELPQSQAETGSGTASDSGESVPGIEEQDSTQTTTQKAWLVAAAEIDEEPVGKAKQSRSEKRARKAMSKLGLLQVTGVTRVTIWKSKNILFVITKLDVYKSPASDAYIVFGEAKIQDLSQQAQLAAAEKFRVQGEAVGNIQENTQTPTVQEESEEEEVDETGVEVKDVKLVMSQANVSRAKAVRALKNNSNDIVNAIMELTV

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
43	Phosphorylation	PGIEEQDSTQTTTQK CCCCCCCCCCHHHHH	23.31	-
68	Ubiquitination	EEPVGKAKQSRSEKR CCCCCCHHHCHHHHH	52.90	-
82	Ubiquitination	RARKAMSKLGLLQVT HHHHHHHHHCCCHHC	33.23	-
89	Phosphorylation	KLGLLQVTGVTRVTI HHCCCHHCCCCEEEE	16.99	20068231
92	Phosphorylation	LLQVTGVTRVTIWKS CCHHCCCCEEEEECC	22.29	20068231
100	Ubiquitination	RVTIWKSKNILFVIT EEEEECCCCEEEEEE	44.26	21906983
108	Acetylation	NILFVITKLDVYKSP CEEEEEEEEEECCCC	31.40	26051181
108	Ubiquitination	NILFVITKLDVYKSP CEEEEEEEEEECCCC	31.40	21906983
113	Ubiquitination	ITKLDVYKSPASDAY EEEEEECCCCCCCCE	50.22	-
127	Ubiquitination	YIVFGEAKIQDLSQQ EEEEEEHHHHHHHHH	36.28	-
132	Phosphorylation	EAKIQDLSQQAQLAA EHHHHHHHHHHHHHH	28.65	-
142	Ubiquitination	AQLAAAEKFRVQGEA HHHHHHHHHHCCCEE	33.47	21906983
142	Acetylation	AQLAAAEKFRVQGEA HHHHHHHHHHCCCEE	33.47	-
157	Phosphorylation	VGNIQENTQTPTVQE ECCCCCCCCCCCCCC	32.82	26657352
159	Phosphorylation	NIQENTQTPTVQEES CCCCCCCCCCCCCHH	20.91	15005626
161	Phosphorylation	QENTQTPTVQEESEE CCCCCCCCCCCHHHH	37.90	25159151
166	Phosphorylation	TPTVQEESEEEEVDE CCCCCCHHHHHCCCC	49.94	25159151
174	Phosphorylation	EEEEVDETGVEVKDV HHHCCCCCCCCHHHH	41.90	22496350
186	Phosphorylation	KDVKLVMSQANVSRA HHHEEEEECCCHHHH	20.75	-
191	Phosphorylation	VMSQANVSRAKAVRA EEECCCHHHHHHHHH	26.74	20068231
200	Ubiquitination	AKAVRALKNNSNDIV HHHHHHHHCCCHHHH	53.77	-
203	Phosphorylation	VRALKNNSNDIVNAI HHHHHCCCHHHHHHH	45.32	28112733
214	Phosphorylation	VNAIMELTV------ HHHHHHHCC------	15.74	28464451

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

Oops, there are no upstream regulatory protein records of NACA2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NACA2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of NACA2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RL32_HUMAN	RPL32	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
TERA_HUMAN	VCP	physical	22939629
RL23_HUMAN	RPL23	physical	22939629
RS25_HUMAN	RPS25	physical	22939629

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-214, AND MASSSPECTROMETRY.
PubMed: 19690332