COPD_MOUSE - dbPTM
COPD_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COPD_MOUSE
UniProt AC Q5XJY5
Protein Name Coatomer subunit delta
Gene Name Arcn1
Organism Mus musculus (Mouse).
Sequence Length 511
Subcellular Localization Cytoplasm. Golgi apparatus membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane
Peripheral membrane protein
Cytoplasmic side. The coatomer is cytoplasmic or polymerized on the cytoplasmic side o
Protein Description The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity)..
Protein Sequence MVLLAAAVCTKAGKAIVSRQFVEMTRTRIEGLLAAFPKLMNTGKQHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDLETLRLFSRVIPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTFTEMDSHEEKVFRAVRETQEREAKAEMRRKAKELQQARRDAERQGKKAPGFGGFGSSAVSGGSTAAMITETIIETDKPKVAPAPARPSGPSKALKLGAKGKEVDNFVDKLKSEGETIMSSNMGKRTSEATKVHAPPINMESVHMKIEEKITLTCGRDGGLQNMELHGMIMLRISDDKFGRIRLHVENEDKKGVQLQTHPNVDKKLFTAESLIGLKNPEKSFPVNSDVGVLKWRLQTTEESFIPLTINCWPSESGNGCDVNIEYELQEDNLELNDVVITIPLPSGVGAPVIGEIDGEYRHDSRRNTLEWCLPVIDAKNKSGSLEFSIPGQPNDFFPVQVSFISKKNYCNIQVTKVTQVDGNSPVRFSTETTFLVDKYEIL
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
56PhosphorylationVETESVRYVYQPMEK
EEECCEEEEECCHHH
11.0122817900
65PhosphorylationYQPMEKLYMVLITTK
ECCHHHEEEEEEEEC
9.0322817900
71PhosphorylationLYMVLITTKNSNILE
EEEEEEEECCCCHHH
22.6419854140
138PhosphorylationRTFTEMDSHEEKVFR
EEEECCCCHHHHHHH
31.3324719451
142UbiquitinationEMDSHEEKVFRAVRE
CCCCHHHHHHHHHHH
43.6322790023
142AcetylationEMDSHEEKVFRAVRE
CCCCHHHHHHHHHHH
43.6323236377
164MalonylationAEMRRKAKELQQARR
HHHHHHHHHHHHHHH
63.0926320211
188PhosphorylationPGFGGFGSSAVSGGS
CCCCCCCCCCCCCCC
16.9221082442
192PhosphorylationGFGSSAVSGGSTAAM
CCCCCCCCCCCHHEE
36.8322817900
195PhosphorylationSSAVSGGSTAAMITE
CCCCCCCCHHEEEEE
20.5623984901
196PhosphorylationSAVSGGSTAAMITET
CCCCCCCHHEEEEEE
23.0123984901
201PhosphorylationGSTAAMITETIIETD
CCHHEEEEEEHHHCC
17.6223984901
203PhosphorylationTAAMITETIIETDKP
HHEEEEEEHHHCCCC
20.7123984901
207PhosphorylationITETIIETDKPKVAP
EEEEHHHCCCCCCCC
38.6323984901
220PhosphorylationAPAPARPSGPSKALK
CCCCCCCCCCCCCCC
58.7529895711
223PhosphorylationPARPSGPSKALKLGA
CCCCCCCCCCCCCCC
33.8024719451
224UbiquitinationARPSGPSKALKLGAK
CCCCCCCCCCCCCCC
61.9527667366
224MalonylationARPSGPSKALKLGAK
CCCCCCCCCCCCCCC
61.9526320211
227MalonylationSGPSKALKLGAKGKE
CCCCCCCCCCCCCCC
50.1326320211
233AcetylationLKLGAKGKEVDNFVD
CCCCCCCCCCHHHHH
54.5823806337
233UbiquitinationLKLGAKGKEVDNFVD
CCCCCCCCCCHHHHH
54.5822790023
241AcetylationEVDNFVDKLKSEGET
CCHHHHHHHHHHCCC
53.1423806337
241UbiquitinationEVDNFVDKLKSEGET
CCHHHHHHHHHHCCC
53.1422790023
243UbiquitinationDNFVDKLKSEGETIM
HHHHHHHHHHCCCEE
52.8022790023
244PhosphorylationNFVDKLKSEGETIMS
HHHHHHHHHCCCEEC
62.3625338131
256UbiquitinationIMSSNMGKRTSEATK
EECCCCCCCCCCCCC
41.56-
256MalonylationIMSSNMGKRTSEATK
EECCCCCCCCCCCCC
41.5626320211
259PhosphorylationSNMGKRTSEATKVHA
CCCCCCCCCCCCCCC
29.3024719451
286GlutathionylationEEKITLTCGRDGGLQ
EEEEEEEECCCCCCC
4.7824333276
286S-nitrosylationEEKITLTCGRDGGLQ
EEEEEEEECCCCCCC
4.7820925432
286S-nitrosocysteineEEKITLTCGRDGGLQ
EEEEEEEECCCCCCC
4.78-
309UbiquitinationMLRISDDKFGRIRLH
EEEECCCCCCEEEEE
55.5022790023
309AcetylationMLRISDDKFGRIRLH
EEEECCCCCCEEEEE
55.50-
322UbiquitinationLHVENEDKKGVQLQT
EEEECCCCCCCCCCC
45.29-
329PhosphorylationKKGVQLQTHPNVDKK
CCCCCCCCCCCCCHH
48.14-
335MalonylationQTHPNVDKKLFTAES
CCCCCCCHHCEEHHH
47.2826073543
335AcetylationQTHPNVDKKLFTAES
CCCCCCCHHCEEHHH
47.2823201123
336UbiquitinationTHPNVDKKLFTAESL
CCCCCCHHCEEHHHH
44.3522790023
342PhosphorylationKKLFTAESLIGLKNP
HHCEEHHHHHCCCCC
23.8722802335
347UbiquitinationAESLIGLKNPEKSFP
HHHHHCCCCCCCCCC
66.3022790023
351UbiquitinationIGLKNPEKSFPVNSD
HCCCCCCCCCCCCCC
59.6727667366
351AcetylationIGLKNPEKSFPVNSD
HCCCCCCCCCCCCCC
59.6723806337
351SuccinylationIGLKNPEKSFPVNSD
HCCCCCCCCCCCCCC
59.6723806337
363AcetylationNSDVGVLKWRLQTTE
CCCCCEEEEEEEECC
28.0622826441
363MalonylationNSDVGVLKWRLQTTE
CCCCCEEEEEEEECC
28.0626320211
441S-nitrosylationRRNTLEWCLPVIDAK
CCCCEEEEEEEEECC
1.9420925432
441S-nitrosocysteineRRNTLEWCLPVIDAK
CCCCEEEEEEEEECC
1.94-
448UbiquitinationCLPVIDAKNKSGSLE
EEEEEECCCCCCCEE
62.2522790023
450UbiquitinationPVIDAKNKSGSLEFS
EEEECCCCCCCEEEE
56.33-
479S-nitrosylationFISKKNYCNIQVTKV
EEECCCCEEEEEEEE
5.1721278135
479S-nitrosocysteineFISKKNYCNIQVTKV
EEECCCCEEEEEEEE
5.17-
485UbiquitinationYCNIQVTKVTQVDGN
CEEEEEEEEEEECCC
44.4122790023
487PhosphorylationNIQVTKVTQVDGNSP
EEEEEEEEEECCCCC
25.1629899451
493PhosphorylationVTQVDGNSPVRFSTE
EEEECCCCCEEEEEE
30.2425521595
498PhosphorylationGNSPVRFSTETTFLV
CCCCEEEEEEEEEEE
18.1226745281
499PhosphorylationNSPVRFSTETTFLVD
CCCEEEEEEEEEEEE
34.3426745281
501PhosphorylationPVRFSTETTFLVDKY
CEEEEEEEEEEEEEE
23.9626745281
502PhosphorylationVRFSTETTFLVDKYE
EEEEEEEEEEEEEEE
14.5626745281

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 COPD_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COPD_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 COPD_MOUSE !!

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

Oops, there are no PPI records of COPD_MOUSE !!

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

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Related Literatures of Post-Translational Modification

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