dbPTM

RS25_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS25_HUMAN
UniProt AC	P62851
Protein Name	40S ribosomal protein S25
Gene Name	RPS25
Organism	Homo sapiens (Human).
Sequence Length	125
Subcellular Localization
Protein Description
Protein Sequence	MPPKDDKKKKDAGKSAKKDKDPVNKSGGKAKKKKWSKGKVRDKLNNLVLFDKATYDKLCKEVPNYKLITPAVVSERLKIRGSLARAALQELLSKGLIKLVSKHRAQVIYTRNTKGGDAPAAGEDA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
20	2-Hydroxyisobutyrylation	GKSAKKDKDPVNKSG CHHCCCCCCCCCCCC	73.19	-
25	Ubiquitination	KDKDPVNKSGGKAKK CCCCCCCCCCCHHCC	51.19	33845483
26	Phosphorylation	DKDPVNKSGGKAKKK CCCCCCCCCCHHCCC	47.80	28258704
29	Ubiquitination	PVNKSGGKAKKKKWS CCCCCCCHHCCCCCC	61.63	-
37	Ubiquitination	AKKKKWSKGKVRDKL HCCCCCCCCCHHHHH	62.73	23000965
39	Ubiquitination	KKKWSKGKVRDKLNN CCCCCCCCHHHHHHC	37.52	23000965
43	Acetylation	SKGKVRDKLNNLVLF CCCCHHHHHHCEEEE	42.42	23236377
43	Sumoylation	SKGKVRDKLNNLVLF CCCCHHHHHHCEEEE	42.42	-
43	Ubiquitination	SKGKVRDKLNNLVLF CCCCHHHHHHCEEEE	42.42	23000965
52	Succinylation	NNLVLFDKATYDKLC HCEEEEEHHHHHHHH	34.98	-
52	Succinylation	NNLVLFDKATYDKLC HCEEEEEHHHHHHHH	34.98	-
52	2-Hydroxyisobutyrylation	NNLVLFDKATYDKLC HCEEEEEHHHHHHHH	34.98	-
52	Ubiquitination	NNLVLFDKATYDKLC HCEEEEEHHHHHHHH	34.98	23000965
52	Malonylation	NNLVLFDKATYDKLC HCEEEEEHHHHHHHH	34.98	26320211
52	Acetylation	NNLVLFDKATYDKLC HCEEEEEHHHHHHHH	34.98	19608861
54	Phosphorylation	LVLFDKATYDKLCKE EEEEEHHHHHHHHHH	37.68	28152594
55	Phosphorylation	VLFDKATYDKLCKEV EEEEHHHHHHHHHHC	18.88	28152594
57	Malonylation	FDKATYDKLCKEVPN EEHHHHHHHHHHCCC	45.42	26320211
57	Ubiquitination	FDKATYDKLCKEVPN EEHHHHHHHHHHCCC	45.42	23000965
57	Acetylation	FDKATYDKLCKEVPN EEHHHHHHHHHHCCC	45.42	25953088
60	Malonylation	ATYDKLCKEVPNYKL HHHHHHHHHCCCCEE	72.66	26320211
60	Ubiquitination	ATYDKLCKEVPNYKL HHHHHHHHHCCCCEE	72.66	23000965
60	Acetylation	ATYDKLCKEVPNYKL HHHHHHHHHCCCCEE	72.66	19608861
65	Phosphorylation	LCKEVPNYKLITPAV HHHHCCCCEECCHHH	10.91	-
66	Acetylation	CKEVPNYKLITPAVV HHHCCCCEECCHHHH	39.80	19608861
66	2-Hydroxyisobutyrylation	CKEVPNYKLITPAVV HHHCCCCEECCHHHH	39.80	-
66	Ubiquitination	CKEVPNYKLITPAVV HHHCCCCEECCHHHH	39.80	23000965
66	Methylation	CKEVPNYKLITPAVV HHHCCCCEECCHHHH	39.80	22635435
66	Malonylation	CKEVPNYKLITPAVV HHHCCCCEECCHHHH	39.80	26320211
69	Phosphorylation	VPNYKLITPAVVSER CCCCEECCHHHHCHH	18.68	-
74	Phosphorylation	LITPAVVSERLKIRG ECCHHHHCHHHHHCH	15.48	26074081
82	Phosphorylation	ERLKIRGSLARAALQ HHHHHCHHHHHHHHH	14.70	29514088
93	Phosphorylation	AALQELLSKGLIKLV HHHHHHHHCCHHHHH	36.98	30266825
94	Succinylation	ALQELLSKGLIKLVS HHHHHHHCCHHHHHH	58.67	-
94	Succinylation	ALQELLSKGLIKLVS HHHHHHHCCHHHHHH	58.67	23954790
94	2-Hydroxyisobutyrylation	ALQELLSKGLIKLVS HHHHHHHCCHHHHHH	58.67	-
94	Ubiquitination	ALQELLSKGLIKLVS HHHHHHHCCHHHHHH	58.67	23000965
94	Acetylation	ALQELLSKGLIKLVS HHHHHHHCCHHHHHH	58.67	19608861
98	2-Hydroxyisobutyrylation	LLSKGLIKLVSKHRA HHHCCHHHHHHHHCC	48.13	-
98	Malonylation	LLSKGLIKLVSKHRA HHHCCHHHHHHHHCC	48.13	26320211
98	Acetylation	LLSKGLIKLVSKHRA HHHCCHHHHHHHHCC	48.13	25953088
98	Ubiquitination	LLSKGLIKLVSKHRA HHHCCHHHHHHHHCC	48.13	23000965
102	Ubiquitination	GLIKLVSKHRAQVIY CHHHHHHHHCCEEEE	29.63	-
109	Phosphorylation	KHRAQVIYTRNTKGG HHCCEEEEECCCCCC	10.78	28152594
110	Phosphorylation	HRAQVIYTRNTKGGD HCCEEEEECCCCCCC	13.30	28152594
114	Ubiquitination	VIYTRNTKGGDAPAA EEEECCCCCCCCCCC	65.53	22817900
114	Acetylation	VIYTRNTKGGDAPAA EEEECCCCCCCCCCC	65.53	25953088

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 RS25_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RS25_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 RS25_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HAP1_HUMAN	HAP1	physical	16169070
MDM2_HUMAN	MDM2	physical	22777350
A4_HUMAN	APP	physical	21832049
RS2_HUMAN	RPS2	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS9_HUMAN	RPS9	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
RS10_HUMAN	RPS10	physical	22863883
RS12_HUMAN	RPS12	physical	22863883
RS13_HUMAN	RPS13	physical	22863883
RS14_HUMAN	RPS14	physical	22863883
RS15A_HUMAN	RPS15A	physical	22863883
RS17_HUMAN	RPS17	physical	22863883
RS20_HUMAN	RPS20	physical	22863883
RS24_HUMAN	RPS24	physical	22863883
RS3A_HUMAN	RPS3A	physical	22863883
RS3_HUMAN	RPS3	physical	22863883
RS6_HUMAN	RPS6	physical	22863883
RS7_HUMAN	RPS7	physical	22863883
RS8_HUMAN	RPS8	physical	22863883
PAIRB_HUMAN	SERBP1	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
THAP1_HUMAN	THAP1	physical	25416956
UBIM_HUMAN	FAU	physical	26344197
HNRPU_HUMAN	HNRNPU	physical	26344197
RL10_HUMAN	RPL10	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13_HUMAN	RPL13	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL21_HUMAN	RPL21	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL28_HUMAN	RPL28	physical	26344197
RL29_HUMAN	RPL29	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL3L_HUMAN	RPL3L	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS10_HUMAN	RPS10	physical	26344197
RS11_HUMAN	RPS11	physical	26344197
RS15A_HUMAN	RPS15A	physical	26344197
RS16_HUMAN	RPS16	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS20_HUMAN	RPS20	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RS9_HUMAN	RPS9	physical	26344197
RL40_HUMAN	UBA52	physical	26344197

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 RS25_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-52; LYS-60; LYS-66 ANDLYS-94, AND MASS SPECTROMETRY.	19608861 [Abstract]