GP107_HUMAN - dbPTM
GP107_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GP107_HUMAN
UniProt AC Q5VW38
Protein Name Protein GPR107
Gene Name GPR107
Organism Homo sapiens (Human).
Sequence Length 600
Subcellular Localization Golgi apparatus, trans-Golgi network membrane
Multi-pass membrane protein .
Protein Description Involved in Golgi-to-ER retrograde transport. Functions as a host factor required for infection by Pseudomonas aeruginosa exotoxin A and Campylobacter jejuni CDT toxins..
Protein Sequence MAALAPVGSPASRGPRLAAGLRLLPMLGLLQLLAEPGLGRVHHLALKDDVRHKVHLNTFGFFKDGYMVVNVSSLSLNEPEDKDVTIGFSLDRTKNDGFSSYLDEDVNYCILKKQSVSVTLLILDISRSEVRVKSPPEAGTQLPKIIFSRDEKVLGQSQEPNVNPASAGNQTQKTQDGGKSKRSTVDSKAMGEKSFSVHNNGGAVSFQFFFNISTDDQEGLYSLYFHKCLGKELPSDKFTFSLDIEITEKNPDSYLSAGEIPLPKLYISMAFFFFLSGTIWIHILRKRRNDVFKIHWLMAALPFTKSLSLVFHAIDYHYISSQGFPIEGWAVVYYITHLLKGALLFITIALIGTGWAFIKHILSDKDKKIFMIVIPLQVLANVAYIIIESTEEGTTEYGLWKDSLFLVDLLCCGAILFPVVWSIRHLQEASATDGKGDSMGPLQQRANLRAGSRIESHHFAQADLELLASSCPPASVSQRAGITAAINLAKLKLFRHYYVLIVCYIYFTRIIAFLLKLAVPFQWKWLYQLLDETATLVFFVLTGYKFRPASDNPYLQLSQEEEDLEMESVVTTSGVMESMKKVKKVTNGSVEPQGEWEGAV
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
70N-linked_GlycosylationKDGYMVVNVSSLSLN
CCCEEEEEEEEECCC
19.28UniProtKB CARBOHYD
85PhosphorylationEPEDKDVTIGFSLDR
CCCCCCCEEEEEEEC
26.05-
89PhosphorylationKDVTIGFSLDRTKND
CCCEEEEEEECCCCC
24.9324719451
115PhosphorylationYCILKKQSVSVTLLI
EEEEECCCEEEEEEE
25.8223403867
126PhosphorylationTLLILDISRSEVRVK
EEEEEEECCCCCEEC
29.4423403867
144UbiquitinationEAGTQLPKIIFSRDE
CCCCCCCEEEECCCC
57.96-
157O-linked_GlycosylationDEKVLGQSQEPNVNP
CCCCCCCCCCCCCCC
34.4155826041
166O-linked_GlycosylationEPNVNPASAGNQTQK
CCCCCCCCCCCCCEE
37.6655826047
169N-linked_GlycosylationVNPASAGNQTQKTQD
CCCCCCCCCCEECCC
41.25UniProtKB CARBOHYD
171O-linked_GlycosylationPASAGNQTQKTQDGG
CCCCCCCCEECCCCC
35.7155826051
183PhosphorylationDGGKSKRSTVDSKAM
CCCCCCCCCCCHHHH
36.2025072903
184PhosphorylationGGKSKRSTVDSKAMG
CCCCCCCCCCHHHHC
32.1525072903
211N-linked_GlycosylationVSFQFFFNISTDDQE
EEEEEEEEECCCCCC
23.34UniProtKB CARBOHYD
432PhosphorylationHLQEASATDGKGDSM
HHHHHHCCCCCCCCC
42.67-
435 (in isoform 2)Ubiquitination-63.4521906983
435UbiquitinationEASATDGKGDSMGPL
HHHCCCCCCCCCCHH
63.45-
536 (in isoform 2)Ubiquitination-2.6821906983
578PhosphorylationTTSGVMESMKKVKKV
EEHHHHHHHHHEEEC
20.1524275569
584UbiquitinationESMKKVKKVTNGSVE
HHHHHEEECCCCCCC
58.2321906983
584 (in isoform 1)Ubiquitination-58.2321906983
589PhosphorylationVKKVTNGSVEPQGEW
EEECCCCCCCCCCCC
25.9425627689

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 GP107_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GP107_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 GP107_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRAF2_HUMANTRAF2physical
28514442
BIRC2_HUMANBIRC2physical
28514442
LCAP_HUMANLNPEPphysical
28514442
NDUAC_HUMANNDUFA12physical
28514442
NEK7_HUMANNEK7physical
28514442

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 GP107_HUMAN

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Related Literatures of Post-Translational Modification

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