dbPTM

NSA2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NSA2_HUMAN
UniProt AC	O95478
Protein Name	Ribosome biogenesis protein NSA2 homolog
Gene Name	NSA2
Organism	Homo sapiens (Human).
Sequence Length	260
Subcellular Localization	Nucleus, nucleolus .
Protein Description	Involved in the biogenesis of the 60S ribosomal subunit. May play a part in the quality control of pre-60S particles (By similarity)..
Protein Sequence	MPQNEYIELHRKRYGYRLDYHEKKRKKESREAHERSKKAKKMIGLKAKLYHKQRHAEKIQMKKTIKMHEKRNTKQKNDEKTPQGAVPAYLLDREGQSRAKVLSNMIKQKRKEKAGKWEVPLPKVRAQGETEVLKVIRTGKRKKKAWKRMVTKVCFVGDGFTRKPPKYERFIRPMGLRFKKAHVTHPELKATFCLPILGVKKNPSSPLYTTLGVITKGTVIEVNVSELGLVTQGGKVIWGKYAQVTNNPENDGCINAVLLV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MPQNEYIELHRKR --CCHHHHHHHHHHH	13.77	28064214
80	Sumoylation	TKQKNDEKTPQGAVP CCCCCCCCCCCCCCC	69.26	28112733
80	Ubiquitination	TKQKNDEKTPQGAVP CCCCCCCCCCCCCCC	69.26	-
81	Phosphorylation	KQKNDEKTPQGAVPA CCCCCCCCCCCCCCH	20.85	25159151
93	Methylation	VPAYLLDREGQSRAK CCHHHCCCCCHHHHH	50.33	115918509
100	Ubiquitination	REGQSRAKVLSNMIK CCCHHHHHHHHHHHH	42.47	-
107	Ubiquitination	KVLSNMIKQKRKEKA HHHHHHHHHHHHHHC	38.71	-
109	Ubiquitination	LSNMIKQKRKEKAGK HHHHHHHHHHHHCCC	61.51	-
116	Ubiquitination	KRKEKAGKWEVPLPK HHHHHCCCCCCCCHH	45.07	-
123	Ubiquitination	KWEVPLPKVRAQGET CCCCCCHHHHCCCCC	52.62	-
134	Ubiquitination	QGETEVLKVIRTGKR CCCCEEHHHHHCCCC	40.57	-
134	2-Hydroxyisobutyrylation	QGETEVLKVIRTGKR CCCCEEHHHHHCCCC	40.57	-
152	Ubiquitination	AWKRMVTKVCFVGDG HHHHHCCEEEECCCC	26.12	-
179	Ubiquitination	RPMGLRFKKAHVTHP CCCCCEEEECCCCCH	42.49	-
180	Ubiquitination	PMGLRFKKAHVTHPE CCCCEEEECCCCCHH	40.80	-
189	Ubiquitination	HVTHPELKATFCLPI CCCCHHHHHEEEEEH	43.66	-
200	Ubiquitination	CLPILGVKKNPSSPL EEEHHCCCCCCCCCC	45.06	-
200	Acetylation	CLPILGVKKNPSSPL EEEHHCCCCCCCCCC	45.06	26051181
201	Ubiquitination	LPILGVKKNPSSPLY EEHHCCCCCCCCCCE	72.23	-
204	Phosphorylation	LGVKKNPSSPLYTTL HCCCCCCCCCCEEEE	54.72	25159151
205	Phosphorylation	GVKKNPSSPLYTTLG CCCCCCCCCCEEEEE	21.85	21815630
208	Phosphorylation	KNPSSPLYTTLGVIT CCCCCCCEEEEEEEE	10.89	21406692
209	Phosphorylation	NPSSPLYTTLGVITK CCCCCCEEEEEEEEC	24.19	21406692
210	Phosphorylation	PSSPLYTTLGVITKG CCCCCEEEEEEEECC	14.14	21406692
215	Phosphorylation	YTTLGVITKGTVIEV EEEEEEEECCEEEEE	22.48	20068231

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 NSA2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NSA2_HUMAN !!

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 NSA2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RL26L_HUMAN	RPL26L1	physical	26186194
NPM_HUMAN	NPM1	physical	26186194
RRS1_HUMAN	RRS1	physical	26186194
PTCD3_HUMAN	PTCD3	physical	26186194
PABP4_HUMAN	PABPC4	physical	26186194
NOG2_HUMAN	GNL2	physical	26186194
NOG1_HUMAN	GTPBP4	physical	26186194
RT09_HUMAN	MRPS9	physical	26186194
CCD86_HUMAN	CCDC86	physical	26186194
MRT4_HUMAN	MRTO4	physical	26186194
RS8_HUMAN	RPS8	physical	26186194
RLP24_HUMAN	RSL24D1	physical	26186194
TYW5_HUMAN	TYW5	physical	26186194
LN28B_HUMAN	LIN28B	physical	26186194
RPF2_HUMAN	RPF2	physical	26186194
NLE1_HUMAN	NLE1	physical	26186194
ZN646_HUMAN	ZNF646	physical	26186194
NOC2L_HUMAN	NOC2L	physical	26344197
RPF2_HUMAN	RPF2	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
SDA1_HUMAN	SDAD1	physical	26344197
NLE1_HUMAN	NLE1	physical	28514442
ZN646_HUMAN	ZNF646	physical	28514442
TYW5_HUMAN	TYW5	physical	28514442
NOG2_HUMAN	GNL2	physical	28514442
RL30_HUMAN	RPL30	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
NOG1_HUMAN	GTPBP4	physical	28514442
RPF2_HUMAN	RPF2	physical	28514442
NOP53_HUMAN	GLTSCR2	physical	28514442
RBM34_HUMAN	RBM34	physical	28514442
RBM4_HUMAN	RBM4	physical	28514442
RL18A_HUMAN	RPL18A	physical	28514442
ZCCHV_HUMAN	ZC3HAV1	physical	28514442
CCD86_HUMAN	CCDC86	physical	28514442
RL7_HUMAN	RPL7	physical	28514442
RENT1_HUMAN	UPF1	physical	28514442

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.

Regulatory Network of NSA2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-81, AND MASSSPECTROMETRY.	18669648 [Abstract]