dbPTM

SCG1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SCG1_HUMAN
UniProt AC	P05060
Protein Name	Secretogranin-1
Gene Name	CHGB
Organism	Homo sapiens (Human).
Sequence Length	677
Subcellular Localization	Secreted. Neuroendocrine and endocrine secretory granules.
Protein Description	Secretogranin-1 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides..
Protein Sequence	MQPTLLLSLLGAVGLAAVNSMPVDNRNHNEGMVTRCIIEVLSNALSKSSAPPITPECRQVLKTSRKDVKDKETTENENTKFEVRLLRDPADASEAHESSSRGEAGAPGEEDIQGPTKADTEKWAEGGGHSRERADEPQWSLYPSDSQVSEEVKTRHSEKSQREDEEEEEGENYQKGERGEDSSEEKHLEEPGETQNAFLNERKQASAIKKEELVARSETHAAGHSQEKTHSREKSSQESGEETGSQENHPQESKGQPRSQEESEEGEEDATSEVDKRRTRPRHHHGRSRPDRSSQGGSLPSEEKGHPQEESEESNVSMASLGEKRDHHSTHYRASEEEPEYGEEIKGYPGVQAPEDLEWERYRGRGSEEYRAPRPQSEESWDEEDKRNYPSLELDKMAHGYGEESEEERGLEPGKGRHHRGRGGEPRAYFMSDTREEKRFLGEGHHRVQENQMDKARRHPQGAWKELDRNYLNYGEEGAPGKWQQQGDLQDTKENREEARFQDKQYSSHHTAEKRKRLGELFNPYYDPLQWKSSHFERRDNMNDNFLEGEEENELTLNEKNFFPEYNYDWWEKKPFSEDVNWGYEKRNLARVPKLDLKRQYDRVAQLDQLLHYRKKSAEFPDFYDSEEPVSTHQEAENEKDRADQTVLTEDEKKELENLAAMDLELQKIAEKFSQRG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
46	Phosphorylation	EVLSNALSKSSAPPI HHHHHHHHCCCCCCC	28.25	27251275
73	Phosphorylation	KDVKDKETTENENTK HHCCCCCCCCCCCCC	45.19	29507054
74	Phosphorylation	DVKDKETTENENTKF HCCCCCCCCCCCCCE	37.59	29507054
79	Phosphorylation	ETTENENTKFEVRLL CCCCCCCCCEEEEEE	30.82	-
93	Phosphorylation	LRDPADASEAHESSS ECCCCCHHHHHHHCC	35.54	29691806
98	Phosphorylation	DASEAHESSSRGEAG CHHHHHHHCCCCCCC	24.60	29691806
99	Phosphorylation	ASEAHESSSRGEAGA HHHHHHHCCCCCCCC	22.52	29691806
100	Phosphorylation	SEAHESSSRGEAGAP HHHHHHCCCCCCCCC	54.29	29691806
117	Acetylation	EDIQGPTKADTEKWA CCCCCCCCHHHHHHH	47.61	7680037
130	Phosphorylation	WAEGGGHSRERADEP HHCCCCCCCCCCCCC	38.83	24670416
140	Phosphorylation	RADEPQWSLYPSDSQ CCCCCCCCCCCCHHH	16.87	29691806
142	Phosphorylation	DEPQWSLYPSDSQVS CCCCCCCCCCHHHHC	8.65	26657352
144	Phosphorylation	PQWSLYPSDSQVSEE CCCCCCCCHHHHCHH	36.02	26657352
146	Phosphorylation	WSLYPSDSQVSEEVK CCCCCCHHHHCHHHH	36.50	26657352
149	Phosphorylation	YPSDSQVSEEVKTRH CCCHHHHCHHHHHHC	22.02	14997482
173	Phosphorylation	EEEEGENYQKGERGE HHHHHCHHCCCCCCC	13.80	22817900
182	Phosphorylation	KGERGEDSSEEKHLE CCCCCCCCHHHHHCC	35.03	26657352
183	Phosphorylation	GERGEDSSEEKHLEE CCCCCCCHHHHHCCC	63.20	26657352
194	Phosphorylation	HLEEPGETQNAFLNE HCCCCCHHHHHHHHH	32.79	29691806
217	Phosphorylation	KEELVARSETHAAGH HHHHHHHHHHHHCCC	36.79	29691806
219	Phosphorylation	ELVARSETHAAGHSQ HHHHHHHHHHCCCCH	20.33	29691806
225	Phosphorylation	ETHAAGHSQEKTHSR HHHHCCCCHHHCCCC	38.83	29691806
229	Phosphorylation	AGHSQEKTHSREKSS CCCCHHHCCCCCHHH	25.08	29691806
231	Phosphorylation	HSQEKTHSREKSSQE CCHHHCCCCCHHHHH	47.57	29691806
235	Phosphorylation	KTHSREKSSQESGEE HCCCCCHHHHHCCCC	32.28	30177828
236	Phosphorylation	THSREKSSQESGEET CCCCCHHHHHCCCCC	49.38	30177828
239	Phosphorylation	REKSSQESGEETGSQ CCHHHHHCCCCCCCC	43.82	30177828
243	Phosphorylation	SQESGEETGSQENHP HHHCCCCCCCCCCCC	37.52	30177828
245	Phosphorylation	ESGEETGSQENHPQE HCCCCCCCCCCCCCC	41.56	30177828
259	Phosphorylation	ESKGQPRSQEESEEG CCCCCCCCHHHCCCC	48.94	29691806
263	Phosphorylation	QPRSQEESEEGEEDA CCCCHHHCCCCCCCC	39.95	21082442
271	Phosphorylation	EEGEEDATSEVDKRR CCCCCCCCHHHHHHH	37.43	29691806
272	Phosphorylation	EGEEDATSEVDKRRT CCCCCCCHHHHHHHC	37.03	29691806
293	Phosphorylation	GRSRPDRSSQGGSLP CCCCCCCCCCCCCCC	34.10	29691806
294	Phosphorylation	RSRPDRSSQGGSLPS CCCCCCCCCCCCCCC	33.47	29691806
298	Phosphorylation	DRSSQGGSLPSEEKG CCCCCCCCCCCCCCC	43.88	29691806
301	Phosphorylation	SQGGSLPSEEKGHPQ CCCCCCCCCCCCCCC	64.78	29691806
311	Phosphorylation	KGHPQEESEESNVSM CCCCCHHCHHCCCCC	46.00	28348404
314	Phosphorylation	PQEESEESNVSMASL CCHHCHHCCCCCHHH	38.18	26657352
317	Phosphorylation	ESEESNVSMASLGEK HCHHCCCCCHHHCCC	16.93	26657352
320	Phosphorylation	ESNVSMASLGEKRDH HCCCCCHHHCCCCCC	28.41	26657352
329	Phosphorylation	GEKRDHHSTHYRASE CCCCCCCCCCCCCCC	17.29	26657352
330	Phosphorylation	EKRDHHSTHYRASEE CCCCCCCCCCCCCCC	20.69	26657352
332	Phosphorylation	RDHHSTHYRASEEEP CCCCCCCCCCCCCCC	14.15	26657352
335	Phosphorylation	HSTHYRASEEEPEYG CCCCCCCCCCCCCCC	36.22	26657352
341	Sulfation	ASEEEPEYGEEIKGY CCCCCCCCCCCCCCC	40.32	-
341	Phosphorylation	ASEEEPEYGEEIKGY CCCCCCCCCCCCCCC	40.32	26657352
341	Sulfation	ASEEEPEYGEEIKGY CCCCCCCCCCCCCCC	40.32	-
367	Phosphorylation	ERYRGRGSEEYRAPR HHHCCCCCCCCCCCC	26.37	29691806
377	Phosphorylation	YRAPRPQSEESWDEE CCCCCCCCCCCCCHH	46.12	18702456
380	Phosphorylation	PRPQSEESWDEEDKR CCCCCCCCCCHHHHH	35.46	26657352
389	Phosphorylation	DEEDKRNYPSLELDK CHHHHHCCCCHHHHH	9.76	26657352
391	Phosphorylation	EDKRNYPSLELDKMA HHHHCCCCHHHHHHH	24.90	26657352
401	Phosphorylation	LDKMAHGYGEESEEE HHHHHCCCCCCCHHH	16.11	26657352
405	Phosphorylation	AHGYGEESEEERGLE HCCCCCCCHHHHCCC	46.11	22617229
429	Phosphorylation	RGGEPRAYFMSDTRE CCCCCCCCCCCCCHH	10.90	24670416
432	Phosphorylation	EPRAYFMSDTREEKR CCCCCCCCCCHHHHH	26.40	24670416
471	Sulfation	WKELDRNYLNYGEEG HHHHHHHCCCCCCCC	9.38	-
474	Sulfation	LDRNYLNYGEEGAPG HHHHCCCCCCCCCCC	24.26	-
474	Sulfation	LDRNYLNYGEEGAPG HHHHCCCCCCCCCCC	24.26	-
482	Ubiquitination	GEEGAPGKWQQQGDL CCCCCCCCCCCCCCC	40.55	23503661
492	Phosphorylation	QQGDLQDTKENREEA CCCCCCCCHHHHHHH	27.57	26657352
506	Phosphorylation	ARFQDKQYSSHHTAE HHHCHHHHHHHHHHH	20.20	22817900
525	Phosphorylation	LGELFNPYYDPLQWK HHHHHCCCCCHHHCH	22.92	-
526	Phosphorylation	GELFNPYYDPLQWKS HHHHCCCCCHHHCHH	16.61	22817900
533	Phosphorylation	YDPLQWKSSHFERRD CCHHHCHHHHHHCCC	26.53	-
534	Phosphorylation	DPLQWKSSHFERRDN CHHHCHHHHHHCCCC	28.59	-
566	Sulfation	EKNFFPEYNYDWWEK CCCCCCCCCCCHHHH	21.18	-
566	Phosphorylation	EKNFFPEYNYDWWEK CCCCCCCCCCCHHHH	21.18	29691806
566	Sulfation	EKNFFPEYNYDWWEK CCCCCCCCCCCHHHH	21.18	-
568	Sulfation	NFFPEYNYDWWEKKP CCCCCCCCCHHHHCC	16.43	-
568	Phosphorylation	NFFPEYNYDWWEKKP CCCCCCCCCHHHHCC	16.43	29691806
577	Phosphorylation	WWEKKPFSEDVNWGY HHHHCCCCCCCCCCH	41.22	27251275
586	Ubiquitination	DVNWGYEKRNLARVP CCCCCHHHCCCCCCC	37.80	23503661
598	Acetylation	RVPKLDLKRQYDRVA CCCCCCHHHHHHHHH	36.80	20167786
613	Phosphorylation	QLDQLLHYRKKSAEF HHHHHHHHHHHCCCC	24.89	-
617	Phosphorylation	LLHYRKKSAEFPDFY HHHHHHHCCCCCCCC	35.75	26657352
624	Sulfation	SAEFPDFYDSEEPVS CCCCCCCCCCCCCCC	26.41	-
624	Sulfation	SAEFPDFYDSEEPVS CCCCCCCCCCCCCCC	26.41	-
624	Phosphorylation	SAEFPDFYDSEEPVS CCCCCCCCCCCCCCC	26.41	26657352
626	Phosphorylation	EFPDFYDSEEPVSTH CCCCCCCCCCCCCCH	32.26	26657352
631	Phosphorylation	YDSEEPVSTHQEAEN CCCCCCCCCHHHHHH	30.78	29691806
632	Phosphorylation	DSEEPVSTHQEAENE CCCCCCCCHHHHHHH	28.01	29691806

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
130	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
225	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
367	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
377	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
380	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 SCG1_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 SCG1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
A4_HUMAN	APP	physical	21832049

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 SCG1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteomic analysis of the human pituitary."; Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.; Pituitary 9:109-120(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-182; SER-183;SER-259; SER-263; SER-311; SER-335; SER-377; SER-405; SER-617 ANDSER-626, AND MASS SPECTROMETRY.	16807684 [Abstract]
"Identification and characterization of phosphorylated proteins in thehuman pituitary."; Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.; Proteomics 4:587-598(2004). Cited for: PHOSPHORYLATION AT SER-149 AND SER-405.	14997482 [Abstract]