dbPTM

RADI_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RADI_HUMAN
UniProt AC	P35241
Protein Name	Radixin
Gene Name	RDX
Organism	Homo sapiens (Human).
Sequence Length	583
Subcellular Localization	Cell membrane Peripheral membrane protein Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cell projection, microvillus . Highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphas
Protein Description	Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane..
Protein Sequence	MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERAQLENEKKKREIAEKEKERIEREKEELMERLKQIEEQTIKAQKELEEQTRKALELDQERKRAKEEAERLEKERRAAEEAKSAIAKQAADQMKNQEQLAAELAEFTAKIALLEEAKKKKEEEATEWQHKAFAAQEDLEKTKEELKTVMSAPPPPPPPPVIPPTENEHDEHDENNAEASAELSNEGVMNHRSEEERVTETQKNERVKKQLQALSSELAQARDETKKTQNDVLHAENVKAGRDKYKTLRQIRQGNTKQRIDEFEAM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Ubiquitination	-----MPKPINVRVT -----CCCCEEEEEE	58.17	21890473
3	Ubiquitination	-----MPKPINVRVT -----CCCCEEEEEE	58.17	-
3	Ubiquitination	-----MPKPINVRVT -----CCCCEEEEEE	58.17	21890473
3	Ubiquitination	-----MPKPINVRVT -----CCCCEEEEEE	58.17	21890473
3	Ubiquitination	-----MPKPINVRVT -----CCCCEEEEEE	58.17	21890473
35	Ubiquitination	QLFDQVVKTVGLREV HHHHHHHHHHCHHHE	38.34	21890473
35	Ubiquitination	QLFDQVVKTVGLREV HHHHHHHHHHCHHHE	38.34	21906983
35	Ubiquitination	QLFDQVVKTVGLREV HHHHHHHHHHCHHHE	38.34	21890473
35	Ubiquitination	QLFDQVVKTVGLREV HHHHHHHHHHCHHHE	38.34	21890473
47	Ubiquitination	REVWFFGLQYVDSKG HHEEEEEEEEECCCC	2.54	19608861
47	Acetylation	REVWFFGLQYVDSKG HHEEEEEEEEECCCC	2.54	19608861
47	Ubiquitination	REVWFFGLQYVDSKG HHEEEEEEEEECCCC	2.54	21890473
51	Ubiquitination	FFGLQYVDSKGYSTW EEEEEEECCCCCHHH	39.43	21890473
55	Phosphorylation	QYVDSKGYSTWLKLN EEECCCCCHHHHHHC	13.48	-
66	Phosphorylation	LKLNKKVTQQDVKKE HHHCCCCCHHHHHHH	29.41	20068231
71	Malonylation	KVTQQDVKKENPLQF CCCHHHHHHHCCCCE	63.76	26320211
72	Ubiquitination	VTQQDVKKENPLQFK CCHHHHHHHCCCCEE	63.67	21890473
72	Malonylation	VTQQDVKKENPLQFK CCHHHHHHHCCCCEE	63.67	26320211
79	Ubiquitination	KENPLQFKFRAKFFP HHCCCCEEEEECCCC	22.45	21890473
79	Ubiquitination	KENPLQFKFRAKFFP HHCCCCEEEEECCCC	22.45	21890473
79	Ubiquitination	KENPLQFKFRAKFFP HHCCCCEEEEECCCC	22.45	21890473
79	Malonylation	KENPLQFKFRAKFFP HHCCCCEEEEECCCC	22.45	26320211
79	Acetylation	KENPLQFKFRAKFFP HHCCCCEEEEECCCC	22.45	19608861
79	Ubiquitination	KENPLQFKFRAKFFP HHCCCCEEEEECCCC	22.45	21890473
83	Succinylation	LQFKFRAKFFPEDVS CCEEEEECCCCCCCC	43.19	-
83	Ubiquitination	LQFKFRAKFFPEDVS CCEEEEECCCCCCCC	43.19	21890473
83	Ubiquitination	LQFKFRAKFFPEDVS CCEEEEECCCCCCCC	43.19	-
83	Ubiquitination	LQFKFRAKFFPEDVS CCEEEEECCCCCCCC	43.19	21890473
83	Succinylation	LQFKFRAKFFPEDVS CCEEEEECCCCCCCC	43.19	21890473
83	Ubiquitination	LQFKFRAKFFPEDVS CCEEEEECCCCCCCC	43.19	21890473
117	Glutathionylation	ILNDEIYCPPETAVL HHCCCCCCCHHHHHH	5.79	22555962
128	Phosphorylation	TAVLLASYAVQAKYG HHHHHHHHHHHHHHC	12.75	-
134	Phosphorylation	SYAVQAKYGDYNKEI HHHHHHHHCCCCCCC	20.46	19658100
137	Phosphorylation	VQAKYGDYNKEIHKP HHHHHCCCCCCCCCC	24.62	-
139	Ubiquitination	AKYGDYNKEIHKPGY HHHCCCCCCCCCCCC	52.39	21906983
143	Ubiquitination	DYNKEIHKPGYLAND CCCCCCCCCCCCCCC	45.88	-
146	Phosphorylation	KEIHKPGYLANDRLL CCCCCCCCCCCCCCC	15.92	28152594
151	Methylation	PGYLANDRLLPQRVL CCCCCCCCCCCHHHH	37.62	115490155
162	Ubiquitination	QRVLEQHKLTKEQWE HHHHHHHCCCHHHHH	58.51	21890473
162	Ubiquitination	QRVLEQHKLTKEQWE HHHHHHHCCCHHHHH	58.51	21890473
162	Ubiquitination	QRVLEQHKLTKEQWE HHHHHHHCCCHHHHH	58.51	21890473
162	Ubiquitination	QRVLEQHKLTKEQWE HHHHHHHCCCHHHHH	58.51	21906983
165	Ubiquitination	LEQHKLTKEQWEERI HHHHCCCHHHHHHHH	59.34	-
191	Phosphorylation	REDSMMEYLKIAQDL CHHHHHHHHHHHHHH	8.73	29759185
209	Ubiquitination	GVNYFEIKNKKGTEL CCEEEEEECCCCCEE	56.36	20639865
233	Ubiquitination	NIYEHDDKLTPKIGF CCEECCCCCCCCCCC	61.39	-
237	Ubiquitination	HDDKLTPKIGFPWSE CCCCCCCCCCCCHHH	50.67	21906983
243	Phosphorylation	PKIGFPWSEIRNISF CCCCCCHHHHCCCCC	24.31	27050516
249	Phosphorylation	WSEIRNISFNDKKFV HHHHCCCCCCCCEEE	22.88	30108239
253	Acetylation	RNISFNDKKFVIKPI CCCCCCCCEEEEEEC	49.57	129479
253	Ubiquitination	RNISFNDKKFVIKPI CCCCCCCCEEEEEEC	49.57	21890473
253	Ubiquitination	RNISFNDKKFVIKPI CCCCCCCCEEEEEEC	49.57	21890473
253	Ubiquitination	RNISFNDKKFVIKPI CCCCCCCCEEEEEEC	49.57	21906983
253	Ubiquitination	RNISFNDKKFVIKPI CCCCCCCCEEEEEEC	49.57	21890473
254	Ubiquitination	NISFNDKKFVIKPID CCCCCCCEEEEEECC	47.96	-
258	Ubiquitination	NDKKFVIKPIDKKAP CCCEEEEEECCCCCC	30.53	-
258	Acetylation	NDKKFVIKPIDKKAP CCCEEEEEECCCCCC	30.53	22636219
262	Acetylation	FVIKPIDKKAPDFVF EEEEECCCCCCCCEE	52.10	1221629485
262	Sumoylation	FVIKPIDKKAPDFVF EEEEECCCCCCCCEE	52.10	-
262	Ubiquitination	FVIKPIDKKAPDFVF EEEEECCCCCCCCEE	52.10	21890473
263	Acetylation	VIKPIDKKAPDFVFY EEEECCCCCCCCEEE	62.49	24222085
263	Ubiquitination	VIKPIDKKAPDFVFY EEEECCCCCCCCEEE	62.49	21906983
270	Phosphorylation	KAPDFVFYAPRLRIN CCCCCEEEECCHHCC	15.47	27273156
273	Methylation	DFVFYAPRLRINKRI CCEEEECCHHCCHHH	28.55	-
291	Phosphorylation	CMGNHELYMRRRKPD HCCCHHHHHCCCCCC	5.89	28258704
296	Ubiquitination	ELYMRRRKPDTIEVQ HHHHCCCCCCCHHHH	45.49	21890473
299	Phosphorylation	MRRRKPDTIEVQQMK HCCCCCCCHHHHHHH	27.80	28985074
305	Sulfoxidation	DTIEVQQMKAQAREE CCHHHHHHHHHHHHH	1.86	28183972
306	Methylation	TIEVQQMKAQAREEK CHHHHHHHHHHHHHH	32.77	24212849
306	Ubiquitination	TIEVQQMKAQAREEK CHHHHHHHHHHHHHH	32.77	21906983
335	Ubiquitination	KKREIAEKEKERIER HHHHHHHHHHHHHHH	66.13	-
344	Acetylation	KERIEREKEELMERL HHHHHHHHHHHHHHH	63.81	-
344	Ubiquitination	KERIEREKEELMERL HHHHHHHHHHHHHHH	63.81	-
352	Ubiquitination	EELMERLKQIEEQTI HHHHHHHHHHHHHHH	56.29	-
360	Ubiquitination	QIEEQTIKAQKELEE HHHHHHHHHHHHHHH	48.42	21906983
369	Phosphorylation	QKELEEQTRKALELD HHHHHHHHHHHHHHH	37.10	20068231
400	Ubiquitination	RRAAEEAKSAIAKQA HHHHHHHHHHHHHHH	43.64	-
405	Ubiquitination	EAKSAIAKQAADQMK HHHHHHHHHHHHHHC	34.06	-
427	Ubiquitination	ELAEFTAKIALLEEA HHHHHHHHHHHHHHH	26.00	-
435	Ubiquitination	IALLEEAKKKKEEEA HHHHHHHHHHHHHHH	69.29	-
448	Ubiquitination	EATEWQHKAFAAQED HHHHHHHHHHHHHHH	30.05	-
518	Phosphorylation	EEERVTETQKNERVK HHHHHCHHHHHHHHH	35.16	27470641
526	Ubiquitination	QKNERVKKQLQALSS HHHHHHHHHHHHHHH	54.08	21890473
526	Ubiquitination	QKNERVKKQLQALSS HHHHHHHHHHHHHHH	54.08	20639865
526	Ubiquitination	QKNERVKKQLQALSS HHHHHHHHHHHHHHH	54.08	21890473
526	Ubiquitination	QKNERVKKQLQALSS HHHHHHHHHHHHHHH	54.08	21890473
532	Phosphorylation	KKQLQALSSELAQAR HHHHHHHHHHHHHHH	25.45	25849741
533	Phosphorylation	KQLQALSSELAQARD HHHHHHHHHHHHHHH	37.16	25159151
542	Phosphorylation	LAQARDETKKTQNDV HHHHHHHHHCHHHHH	41.97	18452278
544	Ubiquitination	QARDETKKTQNDVLH HHHHHHHCHHHHHCH	63.86	-
545	Phosphorylation	ARDETKKTQNDVLHA HHHHHHCHHHHHCHH	33.87	20068231
556	Ubiquitination	VLHAENVKAGRDKYK HCHHHHHHCCHHHHH	57.62	2190698
556	Acetylation	VLHAENVKAGRDKYK HCHHHHHHCCHHHHH	57.62	7825077
562	Phosphorylation	VKAGRDKYKTLRQIR HHCCHHHHHHHHHHH	17.31	28796482
564	Phosphorylation	AGRDKYKTLRQIRQG CCHHHHHHHHHHHCC	24.88	22167270
573	Phosphorylation	RQIRQGNTKQRIDEF HHHHCCCHHHCCHHH	35.06	9456324
583	Sulfoxidation	RIDEFEAM------- CCHHHHCC-------	4.43	21406390

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
564	T	Phosphorylation	Kinase	GRK2	P25098	PSP
564	T	Phosphorylation	Kinase	PRKCQ	Q04759	GPS
564	T	Phosphorylation	Kinase	LRRK2	Q5S007	PSP
564	T	Phosphorylation	Kinase	MAP3K8	P41279	GPS
564	T	Phosphorylation	Kinase	HGK	O95819	PSP
564	T	Phosphorylation	Kinase	ROCK1	Q13464	PSP
564	T	Phosphorylation	Kinase	ROCK2	O75116	Uniprot
564	T	Phosphorylation	Kinase	STK10	O94804	GPS
564	T	Phosphorylation	Kinase	ROCK-SUBFAMILY	-	GPS
564	T	Phosphorylation	Kinase	ROCK_GROUP	-	PhosphoELM
573	T	Phosphorylation	Kinase	ROCK-SUBFAMILY	-	GPS
573	T	Phosphorylation	Kinase	ROCK_GROUP	-	PhosphoELM

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ICAM2_HUMAN	ICAM2	physical	11375520
TPC10_HUMAN	TRAPPC10	physical	22939629
AN32E_HUMAN	ANP32E	physical	22863883
SRC8_HUMAN	CTTN	physical	22863883
ERF3A_HUMAN	GSPT1	physical	22863883
ERF3B_HUMAN	GSPT2	physical	22863883
SNX2_HUMAN	SNX2	physical	22863883
VPS11_HUMAN	VPS11	physical	21148287
THIM_HUMAN	ACAA2	physical	26344197
ALDR_HUMAN	AKR1B1	physical	26344197
GDIR1_HUMAN	ARHGDIA	physical	26344197
GDIR3_HUMAN	ARHGDIG	physical	26344197
BAP31_HUMAN	BCAP31	physical	26344197
BRWD1_HUMAN	BRWD1	physical	26344197
CALR_HUMAN	CALR	physical	26344197
CALU_HUMAN	CALU	physical	26344197
CLIC1_HUMAN	CLIC1	physical	26344197
ENOA_HUMAN	ENO1	physical	26344197
FABP5_HUMAN	FABP5	physical	26344197
HCD2_HUMAN	HSD17B10	physical	26344197
HSP74_HUMAN	HSPA4	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
HS105_HUMAN	HSPH1	physical	26344197
INO1_HUMAN	ISYNA1	physical	26344197
PLSL_HUMAN	LCP1	physical	26344197
NOTC2_HUMAN	NOTCH2	physical	26344197
PDIA1_HUMAN	P4HB	physical	26344197
6PGD_HUMAN	PGD	physical	26344197
PLSI_HUMAN	PLS1	physical	26344197
PLST_HUMAN	PLS3	physical	26344197
IPYR_HUMAN	PPA1	physical	26344197
PSB5_HUMAN	PSMB5	physical	26344197
RCN1_HUMAN	RCN1	physical	26344197
STIP1_HUMAN	STIP1	physical	26344197
TAGL2_HUMAN	TAGLN2	physical	26344197
TKT_HUMAN	TKT	physical	26344197
TKTL2_HUMAN	TKTL2	physical	26344197
TRXR2_HUMAN	TXNRD2	physical	26344197
UCHL3_HUMAN	UCHL3	physical	26344197
TERA_HUMAN	VCP	physical	26344197
ERBB2_HUMAN	ERBB2	physical	27029001
MRP2_HUMAN	ABCC2	physical	25163515

Drug and Disease Associations

Kegg Disease
H00605	Deafness, autosomal recessive
OMIM Disease
611022	Deafness, autosomal recessive, 24 (DFNB24)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RADI_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79; LYS-258; LYS-263 ANDLYS-344, AND MASS SPECTROMETRY.	19608861 [Abstract]