ERC2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ERC2_HUMAN
• UniProt AC: O15083
• Protein Name: ERC protein 2
• Gene Name: ERC2
• Organism: Homo sapiens (Human).
• Sequence Length: 957
• Subcellular Localization: Cytoplasm . Cell junction, synapse . Cell junction, synapse, synaptosome . Cytoplasm, cytoskeleton . In neurons, localized to synapses, and colocalizes with PCLO. Localized to the active zone of presynaptic density (By similarity)..
• Protein Description: Thought to be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. Seems to act together with BSN. May recruit liprin-alpha proteins to the CAZ..
• Protein Sequence: MYGSARTITNLEGSPSRSPRLPRSPRLGHRRTSSGGGGGTGKTLSMENIQSLNAAYATSGPMYLSDHEGVASTTYPKGTMTLGRATNRAVYGGRVTAMGSSPNIASAGLSHTDVLSYTDQHGGLTGSSHHHHHQVPSMLRQVRDSTMLDLQAQLKELQRENDLLRKELDIKDSKLGSSMNSIKTFWSPELKKERVLRKEEAARMSVLKEQMRVSHEENQHLQLTIQALQDELRTQRDLNHLLQQESGNRGAEHFTIELTEENFRRLQAEHDRQAKELFLLRKTLEEMELRIETQKQTLNARDESIKKLLEMLQSKGLPSKSLEDDNERTRRMAEAESQVSHLEVILDQKEKENIHLREELHRRSQLQPEPAKTKALQTVIEMKDTKIASLERNIRDLEDEIQMLKANGVLNTEDREEEIKQIEVYKSHSKFMKTKIDQLKQELSKKESELLALQTKLETLSNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKGTLAGEIRDMKDMLEVKERKINVLQKKIENLQEQLRDKDKQLTNLKDRVKSLQTDSSNTDTALATLEEALSEKERIIERLKEQRERDDRERLEEIESFRKENKDLKEKVNALQAELTEKESSLIDLKEHASSLASAGLKRDSKLKSLEIAIEQKKEECSKLEAQLKKAHNIEDDSRMNPEFADQIKQLDKEASYYRDECGKAQAEVDRLLEILKEVENEKNDKDKKIAELESLTLRHMKDQNKKVANLKHNQQLEKKKNAQLLEEVRRREDSMADNSQHLQIEELMNALEKTRQELDATKARLASTQQSLAEKEAHLANLRIERRKQLEEILEMKQEALLAAISEKDANIALLELSASKKKKTQEEVMALKREKDRLVHQLKQQTQNRMKLMADNYDDDHHHYHHHHHHHHHRSPGRSQHSNHRPSPDQDDEEGIWA

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MYGSARTITNL ----CCCCCCCCCCC	9.33	24719451
7	Phosphorylation	-MYGSARTITNLEGS -CCCCCCCCCCCCCC	31.69	27732954
7	O-linked_Glycosylation	-MYGSARTITNLEGS -CCCCCCCCCCCCCC	31.69	28657654
9	Phosphorylation	YGSARTITNLEGSPS CCCCCCCCCCCCCCC	32.89	27732954
14	Phosphorylation	TITNLEGSPSRSPRL CCCCCCCCCCCCCCC	15.44	29116813
16	Phosphorylation	TNLEGSPSRSPRLPR CCCCCCCCCCCCCCC	47.27	29116813
18	Phosphorylation	LEGSPSRSPRLPRSP CCCCCCCCCCCCCCC	20.79	20068231
24	Phosphorylation	RSPRLPRSPRLGHRR CCCCCCCCCCCCCCC	16.66	28355574
32	Phosphorylation	PRLGHRRTSSGGGGG CCCCCCCCCCCCCCC	27.48	18452278
34	Phosphorylation	LGHRRTSSGGGGGTG CCCCCCCCCCCCCCC	40.62	18452278
65	Phosphorylation	TSGPMYLSDHEGVAS CCCCEECCCCCCCCC	21.31	-
178	Phosphorylation	KDSKLGSSMNSIKTF CHHCCCCCHHHHHHH	21.86	-
183	Ubiquitination	GSSMNSIKTFWSPEL CCCHHHHHHHCCHHH	37.17	21963094
184	Phosphorylation	SSMNSIKTFWSPELK CCHHHHHHHCCHHHH	28.77	30266825
187	Phosphorylation	NSIKTFWSPELKKER HHHHHHCCHHHHHHH	12.33	19664994
192	Ubiquitination	FWSPELKKERVLRKE HCCHHHHHHHHHCHH	64.48	21963094
194	Methylation	SPELKKERVLRKEEA CHHHHHHHHHCHHHH	41.47	-
197	Methylation	LKKERVLRKEEAARM HHHHHHHCHHHHHHH	41.29	-
198	Acetylation	KKERVLRKEEAARMS HHHHHHCHHHHHHHH	56.60	155991
203	Dimethylation	LRKEEAARMSVLKEQ HCHHHHHHHHHHHHH	25.59	-
295	Ubiquitination	ELRIETQKQTLNARD HHHHHHHHHHHHHCH	53.31	29967540
314	Phosphorylation	KLLEMLQSKGLPSKS HHHHHHHHCCCCCCC	25.40	20068231
319	Phosphorylation	LQSKGLPSKSLEDDN HHHCCCCCCCCCCHH	39.66	20068231
321	Phosphorylation	SKGLPSKSLEDDNER HCCCCCCCCCCHHHH	41.13	-
382	Sulfoxidation	ALQTVIEMKDTKIAS HHHHHHHHCHHHHHH	3.06	21406390
389	Phosphorylation	MKDTKIASLERNIRD HCHHHHHHHHHHHCH	33.95	24719451
412	Phosphorylation	KANGVLNTEDREEEI HHCCCCCCCCHHHHH	34.79	29255136
440	Ubiquitination	KTKIDQLKQELSKKE HHHHHHHHHHHHHHH	35.77	30230243
531	Ubiquitination	AGEIRDMKDMLEVKE HHHHHCHHHHHHHHH	44.25	29967540
547	Malonylation	KINVLQKKIENLQEQ HHHHHHHHHHHHHHH	42.14	26320211
585	Phosphorylation	NTDTALATLEEALSE CHHHHHHHHHHHHHH	35.24	25311616
591	Phosphorylation	ATLEEALSEKERIIE HHHHHHHHHHHHHHH	54.38	25311616
666	Phosphorylation	KRDSKLKSLEIAIEQ CCHHHCHHHHHHHHH	41.49	-
713	Phosphorylation	KQLDKEASYYRDECG HHHHHHHHHHHHCHH	24.64	-
734	Ubiquitination	DRLLEILKEVENEKN HHHHHHHHHHHHHCC	66.43	-
752	Phosphorylation	KKIAELESLTLRHMK HHHHHHHHHHHHHHH	39.00	25072903
754	Phosphorylation	IAELESLTLRHMKDQ HHHHHHHHHHHHHHC	30.90	25072903
877	Acetylation	IALLELSASKKKKTQ HHHHHHCCCCCCCCH	37.68	-
879	Acetylation	LLELSASKKKKTQEE HHHHCCCCCCCCHHH	69.22	20167786

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ERC2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ERC2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ERC2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LIPA4_HUMAN	PPFIA4	physical	12923177
BSN_HUMAN	BSN	physical	14734538
RIMS1_HUMAN	RIMS1	physical	14734538
UN13A_HUMAN	UNC13A	physical	14734538
PCLO_HUMAN	PCLO	physical	14734538
LIPA1_HUMAN	PPFIA1	physical	12923177
GIT1_HUMAN	GIT1	physical	12923177
GRIP2_HUMAN	GRIP2	physical	12923177
RIMS1_HUMAN	RIMS1	physical	12163476
LSP1_HUMAN	LSP1	physical	15090600
RB6I2_HUMAN	ERC1	physical	22939629

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND MASSSPECTROMETRY.
PubMed: 17924679