ERC2_MOUSE - dbPTM
ERC2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MYGSARTIS
------CCCCCCCCC
21.5621183079
7O-linked_Glycosylation-MYGSARTISNLEGS
-CCCCCCCCCCCCCC
28.5955411901
7Phosphorylation-MYGSARTISNLEGS
-CCCCCCCCCCCCCC
28.59-
9PhosphorylationYGSARTISNLEGSPS
CCCCCCCCCCCCCCC
34.4529472430
14PhosphorylationTISNLEGSPSRSPRL
CCCCCCCCCCCCCCC
15.4425521595
16PhosphorylationSNLEGSPSRSPRLPR
CCCCCCCCCCCCCCC
47.2729472430
18PhosphorylationLEGSPSRSPRLPRSP
CCCCCCCCCCCCCCC
20.7925521595
24PhosphorylationRSPRLPRSPRLGHRR
CCCCCCCCCCCCCCC
16.6627149854
32PhosphorylationPRLGHRRTSSGGGGG
CCCCCCCCCCCCCCC
27.4829899451
33PhosphorylationRLGHRRTSSGGGGGT
CCCCCCCCCCCCCCC
25.7729899451
43PhosphorylationGGGGTGKTLSMENIQ
CCCCCCCCCCHHHHH
25.9619060867
45PhosphorylationGGTGKTLSMENIQSL
CCCCCCCCHHHHHHH
29.3119060867
51PhosphorylationLSMENIQSLNAAYAT
CCHHHHHHHHHHHCC
21.5729899451
63PhosphorylationYATSGPMYLSDHEGV
HCCCCCEECCCCCCC
13.2429899451
65PhosphorylationTSGPMYLSDHEGVAS
CCCCEECCCCCCCCC
21.3121183079
178PhosphorylationKDSKLGSSMNSIKTF
CHHCCCCCHHHHHHH
21.86-
184PhosphorylationSSMNSIKTFWSPELK
CCHHHHHHHCCHHHH
28.7725777480
187PhosphorylationNSIKTFWSPELKKER
HHHHHHCCHHHHHHH
12.3327149854
198AcetylationKKERVLRKEEAARMS
HHHHHHCHHHHHHHH
56.60155993
319PhosphorylationLQSKGLPSKSLEDDN
HHHCCCCCCCCCCHH
39.6620415495
321PhosphorylationSKGLPSKSLEDDNER
HCCCCCCCCCCHHHH
41.1320415495
364PhosphorylationREELHRRSQLQPEPA
HHHHHHHHCCCCCCH
34.8929899451
373O-linked_GlycosylationLQPEPAKTKALQTVI
CCCCCHHHHHHHHHH
24.5355411909
389PhosphorylationMKDTKIASLERNIRD
HCHHHHHHHHHHHCH
33.95-
427PhosphorylationKQIEVYKSHSKFMKT
HHHHHHHHHHHHHHH
18.4629899451
547MalonylationKINVLQKKIENLQEQ
HHHHHHHHHHHHHHH
42.1426320211
579PhosphorylationLQTDSSNTDTALATL
HHCCCCCHHHHHHHH
36.3529899451
647UbiquitinationESSLIDLKEHASSLA
HHCHHHHHHHHHHHH
43.64-
651PhosphorylationIDLKEHASSLASAGL
HHHHHHHHHHHHHCC
28.0025338131
652PhosphorylationDLKEHASSLASAGLK
HHHHHHHHHHHHCCC
28.8325338131
666PhosphorylationKRDSKLKSLEIAIEQ
CCHHHCHHHHHHHHH
41.4916141072
752PhosphorylationKKIAELESLTLRHMK
HHHHHHHHHHHHHHH
39.0022324799
754PhosphorylationIAELESLTLRHMKDQ
HHHHHHHHHHHHHHC
30.9022324799
792PhosphorylationEVRRREDSMVDNSQH
HHHHHHHHCCCCCHH
18.8929899451
797PhosphorylationEDSMVDNSQHLQIEE
HHHCCCCCHHHCHHH
17.9529899451
812PhosphorylationLMNALEKTRQELDAT
HHHHHHHHHHHHHHH
28.36-
876PhosphorylationNIALLELSASKKKKT
HHHHHHHCCCCCCCC
22.5629899451
934 (in isoform 3)Phosphorylation-27.6129233185
937 (in isoform 3)Phosphorylation-36.2129233185
942 (in isoform 3)Phosphorylation-32.8229233185
946PhosphorylationQHSNHRPSPDQDDEE
CCCCCCCCCCCCCCC
40.8529899451

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 ERC2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERC2_MOUSE !!

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 ERC2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ERC2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERC2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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