RFT1_HUMAN - dbPTM
RFT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RFT1_HUMAN
UniProt AC Q96AA3
Protein Name Protein RFT1 homolog
Gene Name RFT1
Organism Homo sapiens (Human).
Sequence Length 541
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description May be involved in N-linked oligosaccharide assembly. May participate in the translocation of oligosaccharide from the cytoplasmic side to the lumenal side of the endoplasmic reticulum membrane..
Protein Sequence MGSQEVLGHAARLASSGLLLQVLFRLITFVLNAFILRFLSKEIVGVVNVRLTLLYSTTLFLAREAFRRACLSGGTQRDWSQTLNLLWLTVPLGVFWSLFLGWIWLQLLEVPDPNVVPHYATGVVLFGLSAVVELLGEPFWVLAQAHMFVKLKVIAESLSVILKSVLTAFLVLWLPHWGLYIFSLAQLFYTTVLVLCYVIYFTKLLGSPESTKLQTLPVSRITDLLPNITRNGAFINWKEAKLTWSFFKQSFLKQILTEGERYVMTFLNVLNFGDQGVYDIVNNLGSLVARLIFQPIEESFYIFFAKVLERGKDATLQKQEDVAVAAAVLESLLKLALLAGLTITVFGFAYSQLALDIYGGTMLSSGSGPVLLRSYCLYVLLLAINGVTECFTFAAMSKEEVDRYNFVMLALSSSFLVLSYLLTRWCGSVGFILANCFNMGIRITQSLCFIHRYYRRSPHRPLAGLHLSPVLLGTFALSGGVTAVSEVFLCCEQGWPARLAHIAVGAFCLGATLGTAFLTETKLIHFLRTQLGVPRRTDKMT
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
3Phosphorylation-----MGSQEVLGHA
-----CCHHHHHHHH
23.1322985185
19UbiquitinationRLASSGLLLQVLFRL
HHHHHHHHHHHHHHH
3.4222817900
22UbiquitinationSSGLLLQVLFRLITF
HHHHHHHHHHHHHHH
5.7122817900
29UbiquitinationVLFRLITFVLNAFIL
HHHHHHHHHHHHHHH
4.7022817900
34UbiquitinationITFVLNAFILRFLSK
HHHHHHHHHHHHHCC
5.4221963094
52PhosphorylationGVVNVRLTLLYSTTL
HHHHHHHHHHHHHHH
12.2627174698
55PhosphorylationNVRLTLLYSTTLFLA
HHHHHHHHHHHHHHH
13.6919835603
56PhosphorylationVRLTLLYSTTLFLAR
HHHHHHHHHHHHHHH
18.1919835603
57PhosphorylationRLTLLYSTTLFLARE
HHHHHHHHHHHHHHH
17.6019835603
58PhosphorylationLTLLYSTTLFLAREA
HHHHHHHHHHHHHHH
15.0127174698
93UbiquitinationLWLTVPLGVFWSLFL
HHHHHHHHHHHHHHH
13.4027667366
99UbiquitinationLGVFWSLFLGWIWLQ
HHHHHHHHHHHHHHH
5.0423503661
207PhosphorylationYFTKLLGSPESTKLQ
HHHHHHCCCCCCCCC
26.0121406692
210PhosphorylationKLLGSPESTKLQTLP
HHHCCCCCCCCCCCC
33.9421406692
211PhosphorylationLLGSPESTKLQTLPV
HHCCCCCCCCCCCCH
33.8321406692
212UbiquitinationLGSPESTKLQTLPVS
HCCCCCCCCCCCCHH
48.1221906983
215PhosphorylationPESTKLQTLPVSRIT
CCCCCCCCCCHHHHH
43.3921406692
219PhosphorylationKLQTLPVSRITDLLP
CCCCCCHHHHHHCCC
18.9421406692
238UbiquitinationNGAFINWKEAKLTWS
CCCCCCHHHCHHHHH
43.2221906983
241UbiquitinationFINWKEAKLTWSFFK
CCCHHHCHHHHHHHH
47.7622817900
248UbiquitinationKLTWSFFKQSFLKQI
HHHHHHHHHHHHHHH
42.9222817900
250PhosphorylationTWSFFKQSFLKQILT
HHHHHHHHHHHHHCC
32.8924719451
253UbiquitinationFFKQSFLKQILTEGE
HHHHHHHHHHCCCCH
33.0321963094
262PhosphorylationILTEGERYVMTFLNV
HCCCCHHHHHHHHHH
7.1126503514
265PhosphorylationEGERYVMTFLNVLNF
CCHHHHHHHHHHHCC
18.2226503514
312UbiquitinationAKVLERGKDATLQKQ
HHHHHHCCCCCCCCH
50.8727667366
318UbiquitinationGKDATLQKQEDVAVA
CCCCCCCCHHHHHHH
59.7823503661
331PhosphorylationVAAAVLESLLKLALL
HHHHHHHHHHHHHHH
34.5421406692
404PhosphorylationSKEEVDRYNFVMLAL
CHHHHHHHHHHHHHH
14.42-

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 RFT1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RFT1_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 RFT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STOM_HUMANSTOMphysical
27173435

Drug and Disease Associations
Kegg Disease
H00118 Congenital disorders of glycosylation (CDG) type I
OMIM Disease
612015Congenital disorder of glycosylation 1N (CDG1N)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RFT1_HUMAN

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Related Literatures of Post-Translational Modification

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