RFTN1_HUMAN - dbPTM
RFTN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RFTN1_HUMAN
UniProt AC Q14699
Protein Name Raftlin
Gene Name RFTN1
Organism Homo sapiens (Human).
Sequence Length 578
Subcellular Localization Cell membrane
Lipid-anchor . Cytoplasm . Membrane raft . Endosome . Early endosome . Translocates from cytoplasm to cell membrane where it colocalizes with poly (I:C) and then moves to endosomes where it colocalizes with TLR3 (PubMed:21266579). Tra
Protein Description Involved in protein trafficking via association with clathrin and AP2 complex. [PubMed: 27022195]
Protein Sequence MGCGLNKLEKRDEKRPGNIYSTLKRPQVETKIDVSYEYRFLEFTTLSAAELPGSSAVRLASLRDLPAQLLELYQQGFSLAALHPFVQPTHEREKTPLEHIFRAILIKKTDRSQKTDLHNEGYILELDCCSSLDHPTDQKLIPEFIKKIQEAASQGLKFVGVIPQYHSSVNSAGSSAPVSTANSTEDARDAKNARGDHASLENEKPGTGDVCSAPAGRNQSPEPSSGPRGEVPLAKQPSSPSGEGDGGELSPQGVSKTLDGPESNPLEVHEEPLSGKMEIFTLFNKPKSHQKCRQYYPVTIPLHVSKNGQTVSGLDANWLEHMSDHFRKGGMLVNAVFYLGIVNDSLHGLTDGVFIFEAVSTEDSKTIQGYDAIVVEQWTVLEGVEVQTDYVPLLNSLAAYGWQLTCVLPTPVVKTTSEGSVSTKQIVFLQRPCLPQKIKKKESKFQWRFSREEMHNRQMRKSKGKLSARDKQQAEENEKNLEDQSSKAGDMGNCVSGQQQEGGVSEEMKGPVQEDKGEQLSPGGLLCGVGVEGEAVQNGPASHSRALVGICTGHSNPGEDARDGDAEEVRELGTVEEN
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
2Myristoylation------MGCGLNKLE
------CCCCCCHHC		17.7512805216
2N-myristoyl glycine------MGCGLNKLE
------CCCCCCHHC		17.75-
3S-palmitoylation-----MGCGLNKLEK
-----CCCCCCHHCC		5.6012805216
14UbiquitinationKLEKRDEKRPGNIYS
HHCCCCCCCCCCHHH		69.08-
20PhosphorylationEKRPGNIYSTLKRPQ
CCCCCCHHHCCCCCC		10.2928796482
21PhosphorylationKRPGNIYSTLKRPQV
CCCCCHHHCCCCCCC		24.3828796482
22PhosphorylationRPGNIYSTLKRPQVE
CCCCHHHCCCCCCCE		21.2324702127
35PhosphorylationVETKIDVSYEYRFLE
CEEEEEEEEEEEEEE		14.4330108239
36PhosphorylationETKIDVSYEYRFLEF
EEEEEEEEEEEEEEE		19.4830108239
61PhosphorylationSSAVRLASLRDLPAQ
CHHHHHHHHCCCHHH		28.6425394399
114UbiquitinationKKTDRSQKTDLHNEG
CCCCCCCCCCCCCCC		45.30-
122PhosphorylationTDLHNEGYILELDCC
CCCCCCCEEEEEEEE		8.9925884760
130PhosphorylationILELDCCSSLDHPTD
EEEEEEECCCCCCCC		40.0222210691
131PhosphorylationLELDCCSSLDHPTDQ
EEEEEECCCCCCCCH		24.7322210691
136PhosphorylationCSSLDHPTDQKLIPE
ECCCCCCCCHHHHHH		47.8722210691
139UbiquitinationLDHPTDQKLIPEFIK
CCCCCCHHHHHHHHH		51.71-
146UbiquitinationKLIPEFIKKIQEAAS
HHHHHHHHHHHHHHH		49.50-
147UbiquitinationLIPEFIKKIQEAASQ
HHHHHHHHHHHHHHC		44.82-
165PhosphorylationFVGVIPQYHSSVNSA
EEEEECCCCCCCCCC		9.7930108239
167PhosphorylationGVIPQYHSSVNSAGS
EEECCCCCCCCCCCC		30.9228450419
168PhosphorylationVIPQYHSSVNSAGSS
EECCCCCCCCCCCCC		16.4128450419
171PhosphorylationQYHSSVNSAGSSAPV
CCCCCCCCCCCCCCC		31.6728450419
174PhosphorylationSSVNSAGSSAPVSTA
CCCCCCCCCCCCCCC		24.0426657352
175PhosphorylationSVNSAGSSAPVSTAN
CCCCCCCCCCCCCCC		35.3630108239
179PhosphorylationAGSSAPVSTANSTED
CCCCCCCCCCCCHHH		22.2728450419
180PhosphorylationGSSAPVSTANSTEDA
CCCCCCCCCCCHHHH		30.0528450419
183PhosphorylationAPVSTANSTEDARDA
CCCCCCCCHHHHHHH		30.6130108239
184PhosphorylationPVSTANSTEDARDAK
CCCCCCCHHHHHHHH		37.3830108239
199PhosphorylationNARGDHASLENEKPG
HCCCCCCCCCCCCCC		32.5629255136
204UbiquitinationHASLENEKPGTGDVC
CCCCCCCCCCCCCCC		61.40-
207PhosphorylationLENEKPGTGDVCSAP
CCCCCCCCCCCCCCC		38.4429255136
211S-nitrosylationKPGTGDVCSAPAGRN
CCCCCCCCCCCCCCC		3.2322178444
212PhosphorylationPGTGDVCSAPAGRNQ
CCCCCCCCCCCCCCC		36.8223927012
220PhosphorylationAPAGRNQSPEPSSGP
CCCCCCCCCCCCCCC		34.4829255136
224PhosphorylationRNQSPEPSSGPRGEV
CCCCCCCCCCCCCCC		46.3930266825
225PhosphorylationNQSPEPSSGPRGEVP
CCCCCCCCCCCCCCC		64.6330266825
235UbiquitinationRGEVPLAKQPSSPSG
CCCCCCCCCCCCCCC		71.12-
238PhosphorylationVPLAKQPSSPSGEGD
CCCCCCCCCCCCCCC		53.0023401153
239PhosphorylationPLAKQPSSPSGEGDG
CCCCCCCCCCCCCCC		29.7521712546
241PhosphorylationAKQPSSPSGEGDGGE
CCCCCCCCCCCCCCC		51.9620164059
250PhosphorylationEGDGGELSPQGVSKT
CCCCCCCCCCCCCCC		15.7521712546
255PhosphorylationELSPQGVSKTLDGPE
CCCCCCCCCCCCCCC		27.0929978859
257PhosphorylationSPQGVSKTLDGPESN
CCCCCCCCCCCCCCC		23.6827732954
263PhosphorylationKTLDGPESNPLEVHE
CCCCCCCCCCCEECC		47.0527732954
274PhosphorylationEVHEEPLSGKMEIFT
EECCCCCCCCEEEEE		47.2730108239
276UbiquitinationHEEPLSGKMEIFTLF
CCCCCCCCEEEEECC		29.95-
285UbiquitinationEIFTLFNKPKSHQKC
EEEECCCCCCCCCCC		46.63-
415PhosphorylationLPTPVVKTTSEGSVS
ECCCEEEECCCCCCC		24.7625332170
424UbiquitinationSEGSVSTKQIVFLQR
CCCCCCCCEEEEEEC		30.44-
437UbiquitinationQRPCLPQKIKKKESK
ECCCCCHHHHHCCCC		55.33-
444UbiquitinationKIKKKESKFQWRFSR
HHHHCCCCHHHHCCH		42.54-
450PhosphorylationSKFQWRFSREEMHNR
CCHHHHCCHHHHHHH		30.1523401153
462PhosphorylationHNRQMRKSKGKLSAR
HHHHHHHHHCCCCHH		35.9522798277
467PhosphorylationRKSKGKLSARDKQQA
HHHHCCCCHHHHHHH		25.4130242111
479UbiquitinationQQAEENEKNLEDQSS
HHHHHHHHCHHHHHH		77.68-
485PhosphorylationEKNLEDQSSKAGDMG
HHCHHHHHHCCCCCC		46.2423401153
486PhosphorylationKNLEDQSSKAGDMGN
HCHHHHHHCCCCCCC		22.3830576142
487UbiquitinationNLEDQSSKAGDMGNC
CHHHHHHCCCCCCCC		62.73-
505PhosphorylationQQQEGGVSEEMKGPV
CCCCCCCCHHHCCCC		30.9826471730
516UbiquitinationKGPVQEDKGEQLSPG
CCCCCCCCCCCCCCC		64.69-
521PhosphorylationEDKGEQLSPGGLLCG
CCCCCCCCCCCEEEE		22.6130108239
552PhosphorylationRALVGICTGHSNPGE
EEEEEECCCCCCCCC		35.6930266825
555PhosphorylationVGICTGHSNPGEDAR
EEECCCCCCCCCCCC		46.1730266825
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 RFTN1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RFTN1_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 RFTN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBG10_HUMANRABGAP1Lphysical
28514442
RBG1L_HUMANRABGAP1Lphysical
28514442
ATG2A_HUMANATG2Aphysical
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 RFTN1_HUMAN

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"Strategy for comprehensive identification of human N-myristoylatedproteins using an insect cell-free protein synthesis system.";
Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,Tsunasawa S., Utsumi T.;
Proteomics 10:1780-1793(2010).
Cited for: MYRISTOYLATION AT GLY-2.
"The B cell-specific major raft protein, Raftlin, is necessary for theintegrity of lipid raft and BCR signal transduction.";
Saeki K., Miura Y., Aki D., Kurosaki T., Yoshimura A.;
EMBO J. 22:3015-3026(2003).
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, TISSUE SPECIFICITY,SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2 AND CYS-3, MYRISTOYLATIONAT GLY-2, AND PALMITOYLATION AT CYS-3.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-220, ANDMASS SPECTROMETRY.

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