dbPTM

NUCB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NUCB2_HUMAN
UniProt AC	P80303
Protein Name	Nucleobindin-2
Gene Name	NUCB2
Organism	Homo sapiens (Human).
Sequence Length	420
Subcellular Localization	Golgi apparatus . Membrane Peripheral membrane protein . Cytoplasm . Secreted . Endoplasmic reticulum. Nucleus envelope. Golgi retention is mediated by its N-terminal region. Nesfatin-1: Secreted.
Protein Description	Calcium-binding protein. May have a role in calcium homeostasis.; Nesfatin-1: Anorexigenic peptide, seems to play an important role in hypothalamic pathways regulating food intake and energy homeostasis, acting in a leptin-independent manner. May also exert hypertensive roles and modulate blood pressure through directly acting on peripheral arterial resistance (By similarity)..
Protein Sequence	MRWRTILLQYCFLLITCLLTALEAVPIDIDKTKVQNIHPVESAKIEPPDTGLYYDEYLKQVIDVLETDKHFREKLQKADIEEIKSGRLSKELDLVSHHVRTKLDELKRQEVGRLRMLIKAKLDSLQDIGMDHQALLKQFDHLNHLNPDKFESTDLDMLIKAATSDLEHYDKTRHEEFKKYEMMKEHERREYLKTLNEEKRKEEESKFEEMKKKHENHPKVNHPGSKDQLKEVWEETDGLDPNDFDPKTFFKLHDVNSDGFLDEQELEALFTKELEKVYDPKNEEDDMVEMEEERLRMREHVMNEVDTNKDRLVTLEEFLKATEKKEFLEPDSWETLDQQQFFTEEELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQKLEYHQVIQQMEQKKLQQGIPPSGPAGELKFEPHI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
32	O-linked_Glycosylation	VPIDIDKTKVQNIHP CCCCCCCCCCCCCCC	32.47	OGP
42	Phosphorylation	QNIHPVESAKIEPPD CCCCCCCCCCCCCCC	34.79	25159151
42	O-linked_Glycosylation	QNIHPVESAKIEPPD CCCCCCCCCCCCCCC	34.79	72260553
50	O-linked_Glycosylation	AKIEPPDTGLYYDEY CCCCCCCCCCCHHHH	34.56	OGP
53	Phosphorylation	EPPDTGLYYDEYLKQ CCCCCCCCHHHHHHH	15.37	22817900
54	Phosphorylation	PPDTGLYYDEYLKQV CCCCCCCHHHHHHHH	13.82	22817900
59	Ubiquitination	LYYDEYLKQVIDVLE CCHHHHHHHHHHHHH	41.43	-
67	Phosphorylation	QVIDVLETDKHFREK HHHHHHHHCHHHHHH	46.30	21406692
77	Ubiquitination	HFREKLQKADIEEIK HHHHHHHHCCHHHHH	59.47	-
84	Ubiquitination	KADIEEIKSGRLSKE HCCHHHHHCCCCCHH	50.57	-
84	Acetylation	KADIEEIKSGRLSKE HCCHHHHHCCCCCHH	50.57	27452117
85	Phosphorylation	ADIEEIKSGRLSKEL CCHHHHHCCCCCHHH	34.50	29116813
89	Phosphorylation	EIKSGRLSKELDLVS HHHCCCCCHHHHHHH	23.79	29116813
90	Ubiquitination	IKSGRLSKELDLVSH HHCCCCCHHHHHHHH	67.88	21890473
90 (in isoform 1)	Ubiquitination	-	67.88	21890473
90 (in isoform 2)	Ubiquitination	-	67.88	21890473
96	O-linked_Glycosylation	SKELDLVSHHVRTKL CHHHHHHHHHHHHHH	18.38	55825665
101	Phosphorylation	LVSHHVRTKLDELKR HHHHHHHHHHHHHHH	34.57	22964224
124	Phosphorylation	LIKAKLDSLQDIGMD HHHHHHHHHHHCCCC	38.06	28450419
130	Sulfoxidation	DSLQDIGMDHQALLK HHHHHCCCCHHHHHH	4.20	21406390
152	Phosphorylation	LNPDKFESTDLDMLI CCHHHCCCCCHHHHH	30.29	24275569
163	Phosphorylation	DMLIKAATSDLEHYD HHHHHHHCCCHHHHH	27.86	23312004
163	O-linked_Glycosylation	DMLIKAATSDLEHYD HHHHHHHCCCHHHHH	27.86	55825219
164	Phosphorylation	MLIKAATSDLEHYDK HHHHHHCCCHHHHHH	35.16	23312004
169	Phosphorylation	ATSDLEHYDKTRHEE HCCCHHHHHHHCHHH	15.12	25884760
171	Acetylation	SDLEHYDKTRHEEFK CCHHHHHHHCHHHHH	40.05	27452117
171	Ubiquitination	SDLEHYDKTRHEEFK CCHHHHHHHCHHHHH	40.05	-
172	O-linked_Glycosylation	DLEHYDKTRHEEFKK CHHHHHHHCHHHHHH	34.07	55827625
172	Phosphorylation	DLEHYDKTRHEEFKK CHHHHHHHCHHHHHH	34.07	28442448
178	Acetylation	KTRHEEFKKYEMMKE HHCHHHHHHHHHHHH	58.69	7695173
201	Acetylation	TLNEEKRKEEESKFE HHCHHHHHHHHHHHH	79.24	12431389
247 (in isoform 2)	Ubiquitination	-	60.86	21890473
247 (in isoform 1)	Ubiquitination	-	60.86	21890473
247	Ubiquitination	DPNDFDPKTFFKLHD CCCCCCHHHHHEEEC	60.86	21890473
257	Phosphorylation	FKLHDVNSDGFLDEQ HEEECCCCCCCCCHH	38.67	22817900
272	Ubiquitination	ELEALFTKELEKVYD HHHHHHHHHHHHHCC	53.63	-
278	Phosphorylation	TKELEKVYDPKNEED HHHHHHHCCCCCCCC	37.28	-
287	Sulfoxidation	PKNEEDDMVEMEEER CCCCCCCCHHHHHHH	4.21	28465586
314	O-linked_Glycosylation	TNKDRLVTLEEFLKA CCHHHEECHHHHHHH	32.80	55833709
322	O-linked_Glycosylation	LEEFLKATEKKEFLE HHHHHHHHCCHHHCC	46.91	55833715
332	Phosphorylation	KEFLEPDSWETLDQQ HHHCCCCCHHHHCHH	37.21	28176443
335	Phosphorylation	LEPDSWETLDQQQFF CCCCCHHHHCHHHCC	29.40	23403867
343	Phosphorylation	LDQQQFFTEEELKEY HCHHHCCCHHHHHHH	43.72	28176443
350	Phosphorylation	TEEELKEYENIIALQ CHHHHHHHHHHHHHC	16.82	30622161
386	Ubiquitination	HDQLEAQKLEYHQVI HHHHHHHHHHHHHHH	50.78	-
389	Phosphorylation	LEAQKLEYHQVIQQM HHHHHHHHHHHHHHH	14.16	27642862
389	O-linked_Glycosylation	LEAQKLEYHQVIQQM HHHHHHHHHHHHHHH	14.16	46512301
396	Sulfoxidation	YHQVIQQMEQKKLQQ HHHHHHHHHHHHHHC	3.18	30846556
399	Ubiquitination	VIQQMEQKKLQQGIP HHHHHHHHHHHCCCC	41.99	-
408	O-linked_Glycosylation	LQQGIPPSGPAGELK HHCCCCCCCCCCCCC	52.64	55454029

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 NUCB2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NUCB2_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
332	Phosphorylation	338 (6)	Q ⇒ E	rs757081	Systolic blood pressure	28739976
335	Phosphorylation	338 (3)	Q ⇒ E	rs757081	Systolic blood pressure	28739976

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NECD_HUMAN	NDN	physical	10915798
SMRD1_HUMAN	SMARCD1	physical	21988832
XPO1_HUMAN	XPO1	physical	21988832
HS71L_HUMAN	HSPA1L	physical	22863883
ULA1_HUMAN	NAE1	physical	22863883
TBB6_HUMAN	TUBB6	physical	22863883
CALU_HUMAN	CALU	physical	26344197
SPTN1_HUMAN	SPTAN1	physical	26344197
SSA27_HUMAN	SSSCA1	physical	26344197

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 NUCB2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-257, AND MASSSPECTROMETRY.	19690332 [Abstract]