dbPTM

RFX1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RFX1_HUMAN
UniProt AC	P22670
Protein Name	MHC class II regulatory factor RFX1
Gene Name	RFX1
Organism	Homo sapiens (Human).
Sequence Length	979
Subcellular Localization	Nucleus.
Protein Description	Regulatory factor essential for MHC class II genes expression. Binds to the X boxes of MHC class II genes. Also binds to an inverted repeat (ENH1) required for hepatitis B virus genes expression and to the most upstream element (alpha) of the RPL30 promoter..
Protein Sequence	MATQAYTELQAAPPPSQPPQAPPQAQPQPPPPPPPAAPQPPQPPTAAATPQPQYVTELQSPQPQAQPPGGQKQYVTELPAVPAPSQPTGAPTPSPAPQQYIVVTVSEGAMRASETVSEASPGSTASQTGVPTQVVQQVQGTQQRLLVQTSVQAKPGHVSPLQLTNIQVPQQALPTQRLVVQSAAPGSKGGQVSLTVHGTQQVHSPPEQSPVQANSSSSKTAGAPTGTVPQQLQVHGVQQSVPVTQERSVVQATPQAPKPGPVQPLTVQGLQPVHVAQEVQQLQQVPVPHVYSSQVQYVEGGDASYTASAIRSSTYSYPETPLYTQTASTSYYEAAGTATQVSTPATSQAVASSGSMPMYVSGSQVVASSTSTGAGASNSSGGGGSGGGGGGGGGGGGGGSGSTGGGGSGAGTYVIQGGYMLGSASQSYSHTTRASPATVQWLLDNYETAEGVSLPRSTLYCHYLLHCQEQKLEPVNAASFGKLIRSVFMGLRTRRLGTRGNSKYHYYGLRIKASSPLLRLMEDQQHMAMRGQPFSQKQRLKPIQKMEGMTNGVAVGQQPSTGLSDISAQVQQYQQFLDASRSLPDFTELDLQGKVLPEGVGPGDIKAFQVLYREHCEAIVDVMVNLQFTLVETLWKTFWRYNLSQPSEAPPLAVHDEAEKRLPKAILVLLSKFEPVLQWTKHCDNVLYQGLVEILIPDVLRPIPSALTQAIRNFAKSLESWLTHAMVNIPEEMLRVKVAAAGAFAQTLRRYTSLNHLAQAARAVLQNTAQINQMLSDLNRVDFANVQEQASWVCRCEDRVVQRLEQDFKVTLQQQNSLEQWAAWLDGVVSQVLKPYQGSAGFPKAAKLFLLKWSFYSSMVIRDLTLRSAASFGSFHLIRLLYDEYMYYLIEHRVAQAKGETPIAVMGEFANLATSLNPLDPDKDEEEEEEEESEDELPQDISLAAGGESPALGPETLEPPAKLARTDARGLFVQALPSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
60	Phosphorylation	QYVTELQSPQPQAQP CEEEECCCCCCCCCC	37.82	24275569
85	Phosphorylation	LPAVPAPSQPTGAPT CCCCCCCCCCCCCCC	51.39	27251275
94	Phosphorylation	PTGAPTPSPAPQQYI CCCCCCCCCCCCCEE	35.85	27251275
113	Phosphorylation	SEGAMRASETVSEAS CCCCHHCCCCCHHCC	24.36	25159151
115	Phosphorylation	GAMRASETVSEASPG CCHHCCCCCHHCCCC	27.17	25159151
117	Phosphorylation	MRASETVSEASPGST HHCCCCCHHCCCCCC	34.56	25159151
120	Phosphorylation	SETVSEASPGSTASQ CCCCHHCCCCCCHHH	26.24	30278072
123	Phosphorylation	VSEASPGSTASQTGV CHHCCCCCCHHHCCC	24.96	30278072
124	Phosphorylation	SEASPGSTASQTGVP HHCCCCCCHHHCCCC	35.92	30278072
126	Phosphorylation	ASPGSTASQTGVPTQ CCCCCCHHHCCCCHH	28.50	30278072
128	Phosphorylation	PGSTASQTGVPTQVV CCCCHHHCCCCHHHH	37.34	30278072
132	Phosphorylation	ASQTGVPTQVVQQVQ HHHCCCCHHHHHHCC	31.43	30108239
149	Phosphorylation	QQRLLVQTSVQAKPG CEEEEEEEEECCCCC	24.32	28450419
150	O-linked_Glycosylation	QRLLVQTSVQAKPGH EEEEEEEEECCCCCC	8.64	31492838
150	Phosphorylation	QRLLVQTSVQAKPGH EEEEEEEEECCCCCC	8.64	22210691
154	Acetylation	VQTSVQAKPGHVSPL EEEEECCCCCCCCCC	34.15	26051181
159	Phosphorylation	QAKPGHVSPLQLTNI CCCCCCCCCCCCCCC	17.76	23401153
164	Phosphorylation	HVSPLQLTNIQVPQQ CCCCCCCCCCCCCCC	19.81	30266825
188	Acetylation	QSAAPGSKGGQVSLT EECCCCCCCCEEEEE	73.33	26051181
193	Phosphorylation	GSKGGQVSLTVHGTQ CCCCCEEEEEECCCC	15.50	23401153
195	Phosphorylation	KGGQVSLTVHGTQQV CCCEEEEEECCCCEE	11.71	25159151
199	Phosphorylation	VSLTVHGTQQVHSPP EEEEECCCCEECCCC	10.84	25159151
204	Phosphorylation	HGTQQVHSPPEQSPV CCCCEECCCCCCCCC	43.20	23401153
209	Phosphorylation	VHSPPEQSPVQANSS ECCCCCCCCCCCCCC	25.94	25159151
215	Phosphorylation	QSPVQANSSSSKTAG CCCCCCCCCCCCCCC	34.31	20068231
216	Phosphorylation	SPVQANSSSSKTAGA CCCCCCCCCCCCCCC	38.14	20068231
217	Phosphorylation	PVQANSSSSKTAGAP CCCCCCCCCCCCCCC	35.36	20068231
218	Phosphorylation	VQANSSSSKTAGAPT CCCCCCCCCCCCCCC	35.65	20068231
220	Phosphorylation	ANSSSSKTAGAPTGT CCCCCCCCCCCCCCC	32.07	26074081
244	O-linked_Glycosylation	VQQSVPVTQERSVVQ EECCCCCCCCCEEEE	20.74	31492838
253	Phosphorylation	ERSVVQATPQAPKPG CCEEEEECCCCCCCC	9.99	25159151
453	Phosphorylation	YETAEGVSLPRSTLY CCCCCCCCCCHHHHH	43.44	24719451
471	Acetylation	LLHCQEQKLEPVNAA HHHCHHCCCCCCCHH	54.81	26051181
486	Phosphorylation	SFGKLIRSVFMGLRT HHHHHHHHHHHHHCC	16.83	22210691
502	Phosphorylation	RLGTRGNSKYHYYGL ECCCCCCCCCEEEEE	37.10	-
514	Phosphorylation	YGLRIKASSPLLRLM EEEEEECCCHHHHHH	27.73	27966365
515	Phosphorylation	GLRIKASSPLLRLME EEEEECCCHHHHHHH	25.15	26699800
537	Ubiquitination	RGQPFSQKQRLKPIQ CCCCCCHHHCCCCHH	35.87	29967540
537	Acetylation	RGQPFSQKQRLKPIQ CCCCCCHHHCCCCHH	35.87	25953088
594	Ubiquitination	TELDLQGKVLPEGVG CEEECCCCCCCCCCC	27.86	29967540
660	Ubiquitination	AVHDEAEKRLPKAIL CCCCHHHHHCCHHHH	67.30	29967540
660	Acetylation	AVHDEAEKRLPKAIL CCCCHHHHHCCHHHH	67.30	26051181
751	Phosphorylation	FAQTLRRYTSLNHLA HHHHHHHHHCHHHHH	8.34	23312004
752	Phosphorylation	AQTLRRYTSLNHLAQ HHHHHHHHCHHHHHH	25.56	23312004
753	Phosphorylation	QTLRRYTSLNHLAQA HHHHHHHCHHHHHHH	20.45	23312004
768	Phosphorylation	ARAVLQNTAQINQML HHHHHHHHHHHHHHH	13.64	-
776	Phosphorylation	AQINQMLSDLNRVDF HHHHHHHHHHCCCCC	34.41	-
868	Phosphorylation	IRDLTLRSAASFGSF HHHHHHHHHHHCCCH	31.16	28122231
871	Phosphorylation	LTLRSAASFGSFHLI HHHHHHHHCCCHHHH	29.83	28122231
942	Phosphorylation	DELPQDISLAAGGES CCCCCCCHHHCCCCC	21.90	26074081
949	Phosphorylation	SLAAGGESPALGPET HHHCCCCCCCCCCCC	20.81	26074081
956	Phosphorylation	SPALGPETLEPPAKL CCCCCCCCCCCCHHH	39.28	26074081
966	Phosphorylation	PPAKLARTDARGLFV CCHHHCCCCCCCCCC	28.53	26074081
978	Phosphorylation	LFVQALPSS------ CCCEECCCC------	100.00	25159151
979	Phosphorylation	FVQALPSS------- CCEECCCC-------	100.00	25159151

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
120	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
124	T	Phosphorylation	Kinase	GSK3B	P49841	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RFX1_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 RFX1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NFIX_HUMAN	NFIX	physical	12624117
NFIB_HUMAN	NFIB	physical	12624117
NFIC_HUMAN	NFIC	physical	12624117
HDAC1_HUMAN	HDAC1	physical	16464847
CHIP_HUMAN	STUB1	physical	27283392
HSP7C_HUMAN	HSPA8	physical	27283392
RFX3_HUMAN	RFX3	physical	27173435
HDAC1_HUMAN	HDAC1	physical	27173435
XYLT2_HUMAN	XYLT2	physical	27173435

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 RFX1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND MASSSPECTROMETRY.	15302935 [Abstract]