dbPTM

NRBF2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NRBF2_HUMAN
UniProt AC	Q96F24
Protein Name	Nuclear receptor-binding factor 2
Gene Name	NRBF2
Organism	Homo sapiens (Human).
Sequence Length	287
Subcellular Localization	Nucleus . Cytoplasm . Cytoplasmic vesicle . Cytoplasmic vesicle, autophagosome .
Protein Description	May modulate transcriptional activation by target nuclear receptors. Can act as transcriptional activator (in vitro).; Involved in starvation-induced autophagy probably by its association with PI3K complex I (PI3KC3-C1). However, effects has been described variably. Involved in the induction of starvation-induced autophagy. [PubMed: 24785657 Stabilzes PI3KC3-C1 assembly and enhances ATG14-linked lipid kinase activity of PIK3C3 (By similarity Proposed to negatively regulate basal and starvation-induced autophagy and to inhibit PIK3C3 activity by modulating interactions in PI3KC3-C1]
Protein Sequence	MEVMEGPLNLAHQQSRRADRLLAAGKYEEAISCHKKAAAYLSEAMKLTQSEQAHLSLELQRDSHMKQLLLIQERWKRAQREERLKAQQNTDKDAAAHLQTSHKPSAEDAEGQSPLSQKYSPSTEKCLPEIQGIFDRDPDTLLYLLQQKSEPAEPCIGSKAPKDDKTIIEEQATKIADLKRHVEFLVAENERLRKENKQLKAEKARLLKGPIEKELDVDADFVETSELWSLPPHAETATASSTWQKFAANTGKAKDIPIPNLPPLDFPSPELPLMELSEDILKGFMNN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
85	Acetylation	AQREERLKAQQNTDK HHHHHHHHHHHHCCH	50.82	7663087
90	Phosphorylation	RLKAQQNTDKDAAAH HHHHHHHCCHHHHHH	39.84	23927012
100	Phosphorylation	DAAAHLQTSHKPSAE HHHHHHHHCCCCCHH	38.88	23927012
101	Phosphorylation	AAAHLQTSHKPSAED HHHHHHHCCCCCHHH	19.29	23927012
103	Acetylation	AHLQTSHKPSAEDAE HHHHHCCCCCHHHCC	40.20	7663095
105	Phosphorylation	LQTSHKPSAEDAEGQ HHHCCCCCHHHCCCC	49.44	23927012
108	Ubiquitination	SHKPSAEDAEGQSPL CCCCCHHHCCCCCCC	50.03	29967540
113	Phosphorylation	AEDAEGQSPLSQKYS HHHCCCCCCCHHCCC	38.37	29255136
116	Phosphorylation	AEGQSPLSQKYSPST CCCCCCCHHCCCCCH	28.19	29255136
118	Ubiquitination	GQSPLSQKYSPSTEK CCCCCHHCCCCCHHH	44.30	29967540
119	Phosphorylation	QSPLSQKYSPSTEKC CCCCHHCCCCCHHHH	20.41	23898821
120	Phosphorylation	SPLSQKYSPSTEKCL CCCHHCCCCCHHHHH	21.29	25159151
122	Phosphorylation	LSQKYSPSTEKCLPE CHHCCCCCHHHHHHH	43.17	27794612
123	Phosphorylation	SQKYSPSTEKCLPEI HHCCCCCHHHHHHHH	42.73	27794612
138	Ubiquitination	QGIFDRDPDTLLYLL CCCCCCCHHHHHHHH	37.06	29967540
143	Phosphorylation	RDPDTLLYLLQQKSE CCHHHHHHHHHCCCC	14.42	28674151
148	Ubiquitination	LLYLLQQKSEPAEPC HHHHHHCCCCCCCCC	43.77	29967540
149	Phosphorylation	LYLLQQKSEPAEPCI HHHHHCCCCCCCCCC	44.46	27251275
156	Ubiquitination	SEPAEPCIGSKAPKD CCCCCCCCCCCCCCC	11.61	24816145
190	Ubiquitination	EFLVAENERLRKENK HHHHHHHHHHHHHHH	44.60	24816145
200	Ubiquitination	RKENKQLKAEKARLL HHHHHHHHHHHHHHH	52.59	24816145
250	Phosphorylation	WQKFAANTGKAKDIP HHHHHHHCCCCCCCC	35.02	29396449
268	Phosphorylation	LPPLDFPSPELPLME CCCCCCCCCCCCHHH	30.88	25159151
277	Phosphorylation	ELPLMELSEDILKGF CCCHHHCCHHHHHHH	21.66	27732954

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
113	S	Phosphorylation	Kinase	MTOR	P42345	PSP
120	S	Phosphorylation	Kinase	MTOR	P42345	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NRBF2_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 NRBF2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PPARA_HUMAN	PPARA	physical	10786636
RXRA_HUMAN	RXRA	physical	10786636
THB_HUMAN	THRB	physical	10786636
CPVL_HUMAN	CPVL	physical	20562859
PA2G4_HUMAN	PA2G4	physical	20562859
PGK1_HUMAN	PGK1	physical	20562859
CA216_HUMAN	C1orf216	physical	25416956
PI3R4_HUMAN	PIK3R4	physical	26186194
PK3C3_HUMAN	PIK3C3	physical	26186194
CACO2_HUMAN	CALCOCO2	physical	26186194
TGFA1_HUMAN	TGFBRAP1	physical	26186194
BECN1_HUMAN	BECN1	physical	26186194
GALT_HUMAN	GALT	physical	26186194
BAKOR_HUMAN	ATG14	physical	26186194
SOGA3_HUMAN	SOGA3	physical	26186194
BAKOR_HUMAN	ATG14	physical	28514442
PK3C3_HUMAN	PIK3C3	physical	28514442
BECN1_HUMAN	BECN1	physical	28514442
GALT_HUMAN	GALT	physical	28514442
SOGA3_HUMAN	SOGA3	physical	28514442
PI3R4_HUMAN	PIK3R4	physical	28514442
TGFA1_HUMAN	TGFBRAP1	physical	28514442
NRBF2_HUMAN	NRBF2	physical	27630019

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 NRBF2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-90; SER-105; SER-113;SER-268 AND SER-277, AND MASS SPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND MASSSPECTROMETRY.	17287340 [Abstract]