dbPTM

NUCB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NUCB1_HUMAN
UniProt AC	Q02818
Protein Name	Nucleobindin-1
Gene Name	NUCB1
Organism	Homo sapiens (Human).
Sequence Length	461
Subcellular Localization	Golgi apparatus, cis-Golgi network membrane Peripheral membrane protein Lumenal side . Cytoplasm . Secreted . A small fraction of the protein may be cytoplasmic.
Protein Description	Major calcium-binding protein of the Golgi. May have a role in calcium homeostasis (By similarity)..
Protein Sequence	MPPSGPRGTLLLLPLLLLLLLRAVLAVPLERGAPNKEETPATESPDTGLYYHRYLQEVIDVLETDGHFREKLQAANAEDIKSGKLSRELDFVSHHVRTKLDELKRQEVSRLRMLLKAKMDAEQDPNVQVDHLNLLKQFEHLDPQNQHTFEARDLELLIQTATRDLAQYDAAHHEEFKRYEMLKEHERRRYLESLGEEQRKEAERKLEEQQRRHREHPKVNVPGSQAQLKEVWEELDGLDPNRFNPKTFFILHDINSDGVLDEQELEALFTKELEKVYDPKNEEDDMREMEEERLRMREHVMKNVDTNQDRLVTLEEFLASTQRKEFGDTGEGWETVEMHPAYTEEELRRFEEELAAREAELNAKAQRLSQETEALGRSQGRLEAQKRELQQAVLHMEQRKQQQQQQQGHKAPAAHPEGQLKFHPDTDDVPVPAPAGDQKEVDTSEKKLLERLPEVEVPQHL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MPPSGPRGTLL ----CCCCCHHHHHH	56.40	20068231
39	O-linked_Glycosylation	GAPNKEETPATESPD CCCCCCCCCCCCCCC	21.22	30059200
39	Phosphorylation	GAPNKEETPATESPD CCCCCCCCCCCCCCC	21.22	23898821
42	O-linked_Glycosylation	NKEETPATESPDTGL CCCCCCCCCCCCCCH	37.89	30059200
42	Phosphorylation	NKEETPATESPDTGL CCCCCCCCCCCCCCH	37.89	23898821
44	Phosphorylation	EETPATESPDTGLYY CCCCCCCCCCCCHHH	24.58	23898821
44	O-linked_Glycosylation	EETPATESPDTGLYY CCCCCCCCCCCCHHH	24.58	30059200
47	Phosphorylation	PATESPDTGLYYHRY CCCCCCCCCHHHHHH	32.25	23898821
47	O-linked_Glycosylation	PATESPDTGLYYHRY CCCCCCCCCHHHHHH	32.25	30059200
50	O-linked_Glycosylation	ESPDTGLYYHRYLQE CCCCCCHHHHHHHHH	9.89	55826313
50	Phosphorylation	ESPDTGLYYHRYLQE CCCCCCHHHHHHHHH	9.89	23898821
51	Phosphorylation	SPDTGLYYHRYLQEV CCCCCHHHHHHHHHH	5.71	23898821
64	Phosphorylation	EVIDVLETDGHFREK HHHHHHHCCCHHHHH	43.02	-
71	2-Hydroxyisobutyrylation	TDGHFREKLQAANAE CCCHHHHHHHHCCHH	41.46	-
81	2-Hydroxyisobutyrylation	AANAEDIKSGKLSRE HCCHHHHHCCCCHHH	66.53	-
81	Ubiquitination	AANAEDIKSGKLSRE HCCHHHHHCCCCHHH	66.53	-
82	Phosphorylation	ANAEDIKSGKLSREL CCHHHHHCCCCHHHH	41.30	23927012
86	Phosphorylation	DIKSGKLSRELDFVS HHHCCCCHHHHHHHH	27.48	23927012
93	O-linked_Glycosylation	SRELDFVSHHVRTKL HHHHHHHHHHHHHHH	14.10	20068231
93	Phosphorylation	SRELDFVSHHVRTKL HHHHHHHHHHHHHHH	14.10	20068231
104	2-Hydroxyisobutyrylation	RTKLDELKRQEVSRL HHHHHHHHHHHHHHH	50.41	-
119	Sulfoxidation	RMLLKAKMDAEQDPN HHHHHHHCCCCCCCC	7.63	30846556
148	Phosphorylation	LDPQNQHTFEARDLE CCCCCCCCCHHHHHH	17.26	28355574
148	O-linked_Glycosylation	LDPQNQHTFEARDLE CCCCCCCCCHHHHHH	17.26	54914103
160	O-linked_Glycosylation	DLELLIQTATRDLAQ HHHHHHHHHHHHHHH	24.01	55824735
162	O-linked_Glycosylation	ELLIQTATRDLAQYD HHHHHHHHHHHHHHH	28.27	55824741
168	O-linked_Glycosylation	ATRDLAQYDAAHHEE HHHHHHHHHHHCHHH	11.27	70957953
168	Phosphorylation	ATRDLAQYDAAHHEE HHHHHHHHHHHCHHH	11.27	-
177	Acetylation	AAHHEEFKRYEMLKE HHCHHHHHHHHHHHH	58.30	25825284
179	Phosphorylation	HHEEFKRYEMLKEHE CHHHHHHHHHHHHHH	13.28	22817900
183	2-Hydroxyisobutyrylation	FKRYEMLKEHERRRY HHHHHHHHHHHHHHH	56.57	-
190	Phosphorylation	KEHERRRYLESLGEE HHHHHHHHHHHHCHH	17.01	28152594
224	O-linked_Glycosylation	PKVNVPGSQAQLKEV CCCCCCCCHHHHHHH	19.10	17525332
224	Phosphorylation	PKVNVPGSQAQLKEV CCCCCCCCHHHHHHH	19.10	17525332
229	Ubiquitination	PGSQAQLKEVWEELD CCCHHHHHHHHHHHC	37.83	-
277	Phosphorylation	TKELEKVYDPKNEED HHHHHHHHCCCCCHH	37.28	-
302	Ubiquitination	RMREHVMKNVDTNQD HHHHHHHHHCCCCHH	53.37	-
310	Methylation	NVDTNQDRLVTLEEF HCCCCHHHHHHHHHH	22.69	115485705
313	O-linked_Glycosylation	TNQDRLVTLEEFLAS CCHHHHHHHHHHHHH	32.80	55832629
320	O-linked_Glycosylation	TLEEFLASTQRKEFG HHHHHHHHHCHHHHC	27.50	55832635
320	Phosphorylation	TLEEFLASTQRKEFG HHHHHHHHHCHHHHC	27.50	28348404
321	Phosphorylation	LEEFLASTQRKEFGD HHHHHHHHCHHHHCC	27.13	28348404
321	O-linked_Glycosylation	LEEFLASTQRKEFGD HHHHHHHHCHHHHCC	27.13	55832641
335	Phosphorylation	DTGEGWETVEMHPAY CCCCCCEEEECCCCC	18.43	29507054
338	Sulfoxidation	EGWETVEMHPAYTEE CCCEEEECCCCCCHH	3.89	30846556
343	Phosphorylation	VEMHPAYTEEELRRF EECCCCCCHHHHHHH	38.74	-
369	Phosphorylation	NAKAQRLSQETEALG HHHHHHHHHHHHHHH	28.32	29255136
369	O-linked_Glycosylation	NAKAQRLSQETEALG HHHHHHHHHHHHHHH	28.32	17525332
372	Phosphorylation	AQRLSQETEALGRSQ HHHHHHHHHHHHHHH	20.94	23927012
372	O-linked_Glycosylation	AQRLSQETEALGRSQ HHHHHHHHHHHHHHH	20.94	29134961
378	O-linked_Glycosylation	ETEALGRSQGRLEAQ HHHHHHHHHHHHHHH	34.88	55828285
378	Phosphorylation	ETEALGRSQGRLEAQ HHHHHHHHHHHHHHH	34.88	-
396	Sulfoxidation	LQQAVLHMEQRKQQQ HHHHHHHHHHHHHHH	4.03	30846556
426	O-linked_Glycosylation	QLKFHPDTDDVPVPA CCCCCCCCCCCCCCC	38.25	55832931
443	Phosphorylation	GDQKEVDTSEKKLLE CCCCCCCHHHHHHHH	43.92	26699800
444	O-linked_Glycosylation	DQKEVDTSEKKLLER CCCCCCHHHHHHHHH	42.85	55834541
444	Phosphorylation	DQKEVDTSEKKLLER CCCCCCHHHHHHHHH	42.85	26699800

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
86	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
148	T	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
369	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NUCB1_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 NUCB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RBL1_HUMAN	RBL1	physical	21988832
SET_HUMAN	SET	physical	21988832
XPO1_HUMAN	XPO1	physical	21988832
PGH2_HUMAN	PTGS2	physical	18493301
CBS_HUMAN	CBS	physical	22863883
PYRG2_HUMAN	CTPS2	physical	22863883
GTF2I_HUMAN	GTF2I	physical	22863883
PRKDC_HUMAN	PRKDC	physical	22863883
RD23B_HUMAN	RAD23B	physical	22863883
SYWC_HUMAN	WARS	physical	22863883
REL_HUMAN	REL	physical	25416956

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 NUCB1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-369, ANDMASS SPECTROMETRY.	17525332 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-179, AND MASSSPECTROMETRY.	18083107 [Abstract]