UniProt ID | ERC2_MOUSE | |
---|---|---|
UniProt AC | Q6PH08 | |
Protein Name | ERC protein 2 | |
Gene Name | Erc2 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 957 | |
Subcellular Localization | Cytoplasm . Cell junction, synapse . Cell junction, synapse, synaptosome . Cytoplasm, cytoskeleton . Localized to the active zone of presynaptic density. | |
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 | MYGSARTISNLEGSPSRSPRLPRSPRLGHRRTSSGGGGGTGKTLSMENIQSLNAAYATSGPMYLSDHEGVASTTYPKGTMTLGRATNRAVYGGRVTAMGSSPNIASAGLSHTDVLSYTDQHGGLSGSSHHHHHQVPSMLRQVRDSTMLDLQAQLKELQRENDLLRKELDIKDSKLGSSMNSIKTFWSPELKKERVLRKEEAARMSVLKEQMRVSHEENQHLQLTIQALQDELRTQRDLNHLLQQESGNRGAEHFTIELTEENFRRLQAEHDRQAKELFLLRKTLEEMELRIETQKQTLNARDESIKKLLEMLQSKGLPSKSLEDDNERTRRMAEAESQVSHLEVILDQKEKENIHLREELHRRSQLQPEPAKTKALQTVIEMKDTKIASLERNIRDLEDEVQMLKANGVLNTEDREEEIKQIEVYKSHSKFMKTKIDQLKQELSKKESELLALQTKLETLSNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKGTLAGEIRDMKDMLEVKERKINVLQKKIENLQEQLRDKDKQLTNLKDRVKSLQTDSSNTDTALATLEEALSEKERIIERLKEQRERDDRERLEEIESFRKENKDLKEKVNALQAELTEKESSLIDLKEHASSLASAGLKRDSKLKSLEIAIEQKKEECNKLEAQLKKAHNIEDDSRMNPEFADRLKQLDKEASYYRDECGKAQAEVDRLLEILKEVENEKNDKDKKIAELESLTLRHMKDQNKKVANLKYNQQLEKKKNAQLLEEVRRREDSMVDNSQHLQIEELMNALEKTRQELDATKARLASTQQSLAEKEAHLANLRIERRKQLEEILEMKQEALLAAISEKDANIALLELSASKKKKTQEEVMALKREKDRLVHQLKQQTQNRMKLMADNYDEDHHHYHHHHHHHHHRSPGRSQHSNHRPSPDQDDEEGIWA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MYGSARTIS ------CCCCCCCCC | 21.56 | 21183079 | |
7 | O-linked_Glycosylation | -MYGSARTISNLEGS -CCCCCCCCCCCCCC | 28.59 | 55411901 | |
7 | Phosphorylation | -MYGSARTISNLEGS -CCCCCCCCCCCCCC | 28.59 | - | |
9 | Phosphorylation | YGSARTISNLEGSPS CCCCCCCCCCCCCCC | 34.45 | 29472430 | |
14 | Phosphorylation | TISNLEGSPSRSPRL CCCCCCCCCCCCCCC | 15.44 | 25521595 | |
16 | Phosphorylation | SNLEGSPSRSPRLPR CCCCCCCCCCCCCCC | 47.27 | 29472430 | |
18 | Phosphorylation | LEGSPSRSPRLPRSP CCCCCCCCCCCCCCC | 20.79 | 25521595 | |
24 | Phosphorylation | RSPRLPRSPRLGHRR CCCCCCCCCCCCCCC | 16.66 | 27149854 | |
32 | Phosphorylation | PRLGHRRTSSGGGGG CCCCCCCCCCCCCCC | 27.48 | 29899451 | |
33 | Phosphorylation | RLGHRRTSSGGGGGT CCCCCCCCCCCCCCC | 25.77 | 29899451 | |
43 | Phosphorylation | GGGGTGKTLSMENIQ CCCCCCCCCCHHHHH | 25.96 | 19060867 | |
45 | Phosphorylation | GGTGKTLSMENIQSL CCCCCCCCHHHHHHH | 29.31 | 19060867 | |
51 | Phosphorylation | LSMENIQSLNAAYAT CCHHHHHHHHHHHCC | 21.57 | 29899451 | |
63 | Phosphorylation | YATSGPMYLSDHEGV HCCCCCEECCCCCCC | 13.24 | 29899451 | |
65 | Phosphorylation | TSGPMYLSDHEGVAS CCCCEECCCCCCCCC | 21.31 | 21183079 | |
178 | Phosphorylation | KDSKLGSSMNSIKTF CHHCCCCCHHHHHHH | 21.86 | - | |
184 | Phosphorylation | SSMNSIKTFWSPELK CCHHHHHHHCCHHHH | 28.77 | 25777480 | |
187 | Phosphorylation | NSIKTFWSPELKKER HHHHHHCCHHHHHHH | 12.33 | 27149854 | |
198 | Acetylation | KKERVLRKEEAARMS HHHHHHCHHHHHHHH | 56.60 | 155993 | |
319 | Phosphorylation | LQSKGLPSKSLEDDN HHHCCCCCCCCCCHH | 39.66 | 20415495 | |
321 | Phosphorylation | SKGLPSKSLEDDNER HCCCCCCCCCCHHHH | 41.13 | 20415495 | |
364 | Phosphorylation | REELHRRSQLQPEPA HHHHHHHHCCCCCCH | 34.89 | 29899451 | |
373 | O-linked_Glycosylation | LQPEPAKTKALQTVI CCCCCHHHHHHHHHH | 24.53 | 55411909 | |
389 | Phosphorylation | MKDTKIASLERNIRD HCHHHHHHHHHHHCH | 33.95 | - | |
427 | Phosphorylation | KQIEVYKSHSKFMKT HHHHHHHHHHHHHHH | 18.46 | 29899451 | |
547 | Malonylation | KINVLQKKIENLQEQ HHHHHHHHHHHHHHH | 42.14 | 26320211 | |
579 | Phosphorylation | LQTDSSNTDTALATL HHCCCCCHHHHHHHH | 36.35 | 29899451 | |
647 | Ubiquitination | ESSLIDLKEHASSLA HHCHHHHHHHHHHHH | 43.64 | - | |
651 | Phosphorylation | IDLKEHASSLASAGL HHHHHHHHHHHHHCC | 28.00 | 25338131 | |
652 | Phosphorylation | DLKEHASSLASAGLK HHHHHHHHHHHHCCC | 28.83 | 25338131 | |
666 | Phosphorylation | KRDSKLKSLEIAIEQ CCHHHCHHHHHHHHH | 41.49 | 16141072 | |
752 | Phosphorylation | KKIAELESLTLRHMK HHHHHHHHHHHHHHH | 39.00 | 22324799 | |
754 | Phosphorylation | IAELESLTLRHMKDQ HHHHHHHHHHHHHHC | 30.90 | 22324799 | |
792 | Phosphorylation | EVRRREDSMVDNSQH HHHHHHHHCCCCCHH | 18.89 | 29899451 | |
797 | Phosphorylation | EDSMVDNSQHLQIEE HHHCCCCCHHHCHHH | 17.95 | 29899451 | |
812 | Phosphorylation | LMNALEKTRQELDAT HHHHHHHHHHHHHHH | 28.36 | - | |
876 | Phosphorylation | NIALLELSASKKKKT HHHHHHHCCCCCCCC | 22.56 | 29899451 | |
934 (in isoform 3) | Phosphorylation | - | 27.61 | 29233185 | |
937 (in isoform 3) | Phosphorylation | - | 36.21 | 29233185 | |
942 (in isoform 3) | Phosphorylation | - | 32.82 | 29233185 | |
946 | Phosphorylation | QHSNHRPSPDQDDEE CCCCCCCCCCCCCCC | 40.85 | 29899451 |
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 ERC2_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ERC2_MOUSE !! |
* 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 ERC2_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ERC2_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY. |