RFTN2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RFTN2_HUMAN
• UniProt AC: Q52LD8
• Protein Name: Raftlin-2
• Gene Name: RFTN2
• Organism: Homo sapiens (Human).
• Sequence Length: 501
• Subcellular Localization: Cell membrane ; Lipid-anchor .
• Protein Description: Upon bacterial lipopolysaccharide stimulation, mediates clathrin-dependent internalization of TLR4 in dendritic cells, resulting in activation of TICAM1-mediated signaling and subsequent IFNB1 production. May regulate B-cell antigen receptor-mediated signaling..
• Protein Sequence: MGCGLRKLEDPDDSSPGKIFSTLKRPQVETKTEFAYEYVLLDFTLQASSNPEVIKINSILDIVTKVENYYLKGYIVGAIHPVIQPVGQRKHLPASYLYRVVLLRLKLSPKNSAAPSGQRRPRLVIEECPLTSEAQTNDAAKELIEKINVAAKRGMKFVGFISQHYSPSKFCNGTNHDGDIESMLHVRHGSDENCRSWNEGTLSGQSSESGIEEELHHESGQYQMEQNGSPTSSKSRKGEASDNKLYTVFNAFDDDSTSWAYQEGILSMKVTRKGSVISTLDADWLELTTFYYKQGLSLIDSFVFWETSKGEHLPKSLEGFFIYEEEGSGVPGSSRKGNDAIVVEQWTVIEGCEIKTDYGPLLHTLAEFGWLLTSVLPTPVLRHDSEGNLATKQIVFLQRPVMWNSAAQTPDKKASRHIKGEDKNKATSRSIGLDTTSSQPAESRHLPEECRLSPSRECWTKEGRLAQHNSFSGFSSSDNVLRELDDGQFDQEDGVTQVTCM

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
2	Myristoylation	------MGCGLRKLE ------CCCCCCCCC	17.75	-
3	S-palmitoylation	-----MGCGLRKLED -----CCCCCCCCCC	4.47	-
58	Phosphorylation	PEVIKINSILDIVTK CCEEEEHHHHHHHHH	28.18	26270265
64	Phosphorylation	NSILDIVTKVENYYL HHHHHHHHHHHHHHH	29.70	26270265
108	Phosphorylation	VLLRLKLSPKNSAAP HHHHHCCCCCCCCCC	32.04	24719451
112	Phosphorylation	LKLSPKNSAAPSGQR HCCCCCCCCCCCCCC	31.75	27174698
116	Phosphorylation	PKNSAAPSGQRRPRL CCCCCCCCCCCCCCE	42.71	27174698
222	Phosphorylation	LHHESGQYQMEQNGS HHHHCCCEEHHHCCC	17.22	22817900
235	Phosphorylation	GSPTSSKSRKGEASD CCCCCCCCCCCCCCC	40.97	22817900
246	Phosphorylation	EASDNKLYTVFNAFD CCCCCCEEEEEECCC	11.49	28387310
247	Phosphorylation	ASDNKLYTVFNAFDD CCCCCEEEEEECCCC	29.11	28387310
256	Phosphorylation	FNAFDDDSTSWAYQE EECCCCCCCCCHHHC	31.19	28387310
323	Phosphorylation	SLEGFFIYEEEGSGV CEEEEEEEEECCCCC	16.48	-
334	Phosphorylation	GSGVPGSSRKGNDAI CCCCCCCCCCCCCEE	43.88	-
405	Phosphorylation	QRPVMWNSAAQTPDK ECCCCCCCCCCCCCH	14.96	23403867
409	Phosphorylation	MWNSAAQTPDKKASR CCCCCCCCCCHHHHH	28.82	23403867
427	Phosphorylation	GEDKNKATSRSIGLD CCCCCCCCCCCCCCC	26.70	-
430	Phosphorylation	KNKATSRSIGLDTTS CCCCCCCCCCCCCCC	22.30	29255136
435	Phosphorylation	SRSIGLDTTSSQPAE CCCCCCCCCCCCCCH	33.35	25850435
436	Phosphorylation	RSIGLDTTSSQPAES CCCCCCCCCCCCCHH	26.50	25850435
437	Phosphorylation	SIGLDTTSSQPAESR CCCCCCCCCCCCHHC	29.12	25850435
438	Phosphorylation	IGLDTTSSQPAESRH CCCCCCCCCCCHHCC	37.78	25850435
443	Phosphorylation	TSSQPAESRHLPEEC CCCCCCHHCCCCCHH	27.40	-
453	Phosphorylation	LPEECRLSPSRECWT CCCHHCCCCCCCCCC	11.07	29255136
455	Phosphorylation	EECRLSPSRECWTKE CHHCCCCCCCCCCCC	37.02	29255136
470	Phosphorylation	GRLAQHNSFSGFSSS CCCCCCCCCCCCCCC	20.75	26657352
472	Phosphorylation	LAQHNSFSGFSSSDN CCCCCCCCCCCCCCC	38.46	25307156

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RFTN2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RFTN2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RFTN2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
POMT2_HUMAN	POMT2	physical	28514442
RBG10_HUMAN	RABGAP1L	physical	28514442
RBG1L_HUMAN	RABGAP1L	physical	28514442
POMT1_HUMAN	POMT1	physical	28514442
GRDN_HUMAN	CCDC88A	physical	28514442
UBP30_HUMAN	USP30	physical	28514442
NMT1_HUMAN	NMT1	physical	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-222 AND SER-235, ANDMASS SPECTROMETRY.
PubMed: 17287340