dbPTM

RSSA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RSSA_HUMAN
UniProt AC	P08865
Protein Name	40S ribosomal protein SA {ECO:0000255\|HAMAP-Rule:MF_03016}
Gene Name	RPSA {ECO:0000255\|HAMAP-Rule:MF_03016}
Organism	Homo sapiens (Human).
Sequence Length	295
Subcellular Localization	Cell membrane. Cytoplasm. Nucleus . 67LR is found at the surface of the plasma membrane, with its C-terminal laminin-binding domain accessible to extracellular ligands. 37LRP is found at the cell surface, in the cytoplasm and in the nucleus (By simil
Protein Description	Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Acts as a PPP1R16B-dependent substrate of PPP1CA.; (Microbial infection) Acts as a receptor for the Adeno-associated viruses 2,3,8 and 9.; (Microbial infection) Acts as a receptor for the Dengue virus.; (Microbial infection) Acts as a receptor for the Sindbis virus.; (Microbial infection) Acts as a receptor for the Venezuelan equine encephalitis virus.; (Microbial infection) Acts as a receptor for the pathogenic prion protein.; (Microbial infection) Acts as a receptor for bacteria..
Protein Sequence	MSGALDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVISSRNTGQRAVLKFAAATGATPIAGRFTPGTFTNQIQAAFREPRLLVVTDPRADHQPLTEASYVNLPTIALCNTDSPLRYVDIAIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKAVTKEEFQGEWTAPAPEFTATQPEVADWSEGVQVPSVPIQQFPTEDWSAQPATEDWSAAPTAQATEWVGATTDWS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSGALDVLQ ------CCCCCCHHH	32.54	22199227
2	Acetylation	------MSGALDVLQ ------CCCCCCHHH	32.54	19413330
11	Sumoylation	ALDVLQMKEEDVLKF CCCHHHCCHHHHHHH	45.02	-
11	2-Hydroxyisobutyrylation	ALDVLQMKEEDVLKF CCCHHHCCHHHHHHH	45.02	-
11	Acetylation	ALDVLQMKEEDVLKF CCCHHHCCHHHHHHH	45.02	26822725
11	Ubiquitination	ALDVLQMKEEDVLKF CCCHHHCCHHHHHHH	45.02	-
28	Phosphorylation	AGTHLGGTNLDFQME HCCCCCCCCCCHHHH	30.70	-
34	Sulfoxidation	GTNLDFQMEQYIYKR CCCCCHHHHHHEEEE	3.32	30846556
37	Phosphorylation	LDFQMEQYIYKRKSD CCHHHHHHEEEECCC	7.91	-
39	Phosphorylation	FQMEQYIYKRKSDGI HHHHHHEEEECCCCE	10.37	20090780
40	2-Hydroxyisobutyrylation	QMEQYIYKRKSDGIY HHHHHEEEECCCCEE	43.73	-
40	Methylation	QMEQYIYKRKSDGIY HHHHHEEEECCCCEE	43.73	11923885
40	Acetylation	QMEQYIYKRKSDGIY HHHHHEEEECCCCEE	43.73	26051181
40	Ubiquitination	QMEQYIYKRKSDGIY HHHHHEEEECCCCEE	43.73	-
42	Malonylation	EQYIYKRKSDGIYII HHHEEEECCCCEEEE	49.07	26320211
42	Acetylation	EQYIYKRKSDGIYII HHHEEEECCCCEEEE	49.07	26051181
42	2-Hydroxyisobutyrylation	EQYIYKRKSDGIYII HHHEEEECCCCEEEE	49.07	-
42	Ubiquitination	EQYIYKRKSDGIYII HHHEEEECCCCEEEE	49.07	-
43	Phosphorylation	QYIYKRKSDGIYIIN HHEEEECCCCEEEEE	45.14	19664994
47	Phosphorylation	KRKSDGIYIINLKRT EECCCCEEEEECCCH	10.98	30266825
52	Acetylation	GIYIINLKRTWEKLL CEEEEECCCHHHHHH	43.21	19608861
52	2-Hydroxyisobutyrylation	GIYIINLKRTWEKLL CEEEEECCCHHHHHH	43.21	-
52	Ubiquitination	GIYIINLKRTWEKLL CEEEEECCCHHHHHH	43.21	21906983
57	Ubiquitination	NLKRTWEKLLLAARA ECCCHHHHHHHHHHH	35.68	21890473
57	Acetylation	NLKRTWEKLLLAARA ECCCHHHHHHHHHHH	35.68	25825284
57	2-Hydroxyisobutyrylation	NLKRTWEKLLLAARA ECCCHHHHHHHHHHH	35.68	-
75	Phosphorylation	IENPADVSVISSRNT ECCCCCEEEEECCCC	17.80	28348404
78	Phosphorylation	PADVSVISSRNTGQR CCCEEEEECCCCCHH	22.53	24719451
79	Phosphorylation	ADVSVISSRNTGQRA CCEEEEECCCCCHHH	20.58	21712546
82	Phosphorylation	SVISSRNTGQRAVLK EEEECCCCCHHHHHH	33.31	27251275
89	Sumoylation	TGQRAVLKFAAATGA CCHHHHHHHHHHCCC	26.76	28112733
89	2-Hydroxyisobutyrylation	TGQRAVLKFAAATGA CCHHHHHHHHHHCCC	26.76	-
89	Malonylation	TGQRAVLKFAAATGA CCHHHHHHHHHHCCC	26.76	26320211
89	Ubiquitination	TGQRAVLKFAAATGA CCHHHHHHHHHHCCC	26.76	21890473
89	Acetylation	TGQRAVLKFAAATGA CCHHHHHHHHHHCCC	26.76	23954790
89	Methylation	TGQRAVLKFAAATGA CCHHHHHHHHHHCCC	26.76	87841
94	Phosphorylation	VLKFAAATGATPIAG HHHHHHHCCCCCCCC	23.71	23312004
97	Phosphorylation	FAAATGATPIAGRFT HHHHCCCCCCCCCCC	19.30	28112733
102	Phosphorylation	GATPIAGRFTPGTFT CCCCCCCCCCCCCHH	24.20	-
104	Phosphorylation	TPIAGRFTPGTFTNQ CCCCCCCCCCCHHHH	21.32	25850435
107	Phosphorylation	AGRFTPGTFTNQIQA CCCCCCCCHHHHHHH	28.61	25850435
109	Phosphorylation	RFTPGTFTNQIQAAF CCCCCCHHHHHHHHH	26.50	28348404
125	Phosphorylation	EPRLLVVTDPRADHQ CCCEEEECCCCCCCC	32.57	20068231
130	Phosphorylation	VVTDPRADHQPLTEA EECCCCCCCCCCCCC	42.08	20068231
135	Phosphorylation	RADHQPLTEASYVNL CCCCCCCCCCCCCCC	35.87	28152594
138	Phosphorylation	HQPLTEASYVNLPTI CCCCCCCCCCCCCEE	24.31	25693802
139	Phosphorylation	QPLTEASYVNLPTIA CCCCCCCCCCCCEEE	10.62	27155012
144	Phosphorylation	ASYVNLPTIALCNTD CCCCCCCEEEEECCC	23.27	28152594
148	S-palmitoylation	NLPTIALCNTDSPLR CCCEEEEECCCCCCE	3.68	29575903
148	Glutathionylation	NLPTIALCNTDSPLR CCCEEEEECCCCCCE	3.68	22555962
150	Phosphorylation	PTIALCNTDSPLRYV CEEEEECCCCCCEEE	36.54	26356563
155	Phosphorylation	CNTDSPLRYVDIAIP ECCCCCCEEEEEEEE	32.58	-
156	Phosphorylation	NTDSPLRYVDIAIPC CCCCCCEEEEEEEEC	15.34	28152594
163	Glutathionylation	YVDIAIPCNNKGAHS EEEEEEECCCCCHHH	7.77	22555962
163	S-palmitoylation	YVDIAIPCNNKGAHS EEEEEEECCCCCHHH	7.77	29575903
170	Phosphorylation	CNNKGAHSVGLMWWM CCCCCHHHHHHHHHH	19.83	-
175	Phosphorylation	AHSVGLMWWMLAREV HHHHHHHHHHHHHHH	5.16	-
180	Methylation	LMWWMLAREVLRMRG HHHHHHHHHHHHHHC	30.51	115492831
185	Methylation	LAREVLRMRGTISRE HHHHHHHHHCCCCCC	3.97	-
198	Sulfoxidation	REHPWEVMPDLYFYR CCCCCCCCCCEEEEC	1.13	30846556
204	Phosphorylation	VMPDLYFYRDPEEIE CCCCEEEECCHHHHH	10.68	-
212	Acetylation	RDPEEIEKEEQAAAE CCHHHHHHHHHHHHH	72.68	26051181
217	Sumoylation	IEKEEQAAAEKAVTK HHHHHHHHHHHCCCH	18.82	-
220	Acetylation	EEQAAAEKAVTKEEF HHHHHHHHCCCHHHH	43.35	23236377
220	Ubiquitination	EEQAAAEKAVTKEEF HHHHHHHHCCCHHHH	43.35	21890473
220	2-Hydroxyisobutyrylation	EEQAAAEKAVTKEEF HHHHHHHHCCCHHHH	43.35	-
225	Ubiquitination	AEKAVTKEEFQGEWT HHHCCCHHHHCCCCC	55.46	-
229	Sumoylation	VTKEEFQGEWTAPAP CCHHHHCCCCCCCCC	37.42	-
239	Phosphorylation	TAPAPEFTATQPEVA CCCCCCCCCCCCCCC	27.42	26074081
241	Phosphorylation	PAPEFTATQPEVADW CCCCCCCCCCCCCCC	41.41	26074081
244	Phosphorylation	EFTATQPEVADWSEG CCCCCCCCCCCCCCC	40.29	-
246	Phosphorylation	TATQPEVADWSEGVQ CCCCCCCCCCCCCCC	15.76	19007248
249	Phosphorylation	QPEVADWSEGVQVPS CCCCCCCCCCCCCCC	25.64	24275569
254	Phosphorylation	DWSEGVQVPSVPIQQ CCCCCCCCCCCCCCC	3.38	-
268	Phosphorylation	QFPTEDWSAQPATED CCCCCCCCCCCCCCC	29.37	24275569
273	Phosphorylation	DWSAQPATEDWSAAP CCCCCCCCCCCCCCC	40.95	-

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 RSSA_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CBX5_HUMAN	CBX5	physical	14730304
RS21_HUMAN	RPS21	physical	10079194
NEDD4_HUMAN	NEDD4	physical	22751010
SSRD_HUMAN	SSR4	physical	22939629
VDAC2_HUMAN	VDAC2	physical	22939629
TCPA_HUMAN	TCP1	physical	22939629
TCPD_HUMAN	CCT4	physical	22939629
TCPZ_HUMAN	CCT6A	physical	22939629
IL7RA_HUMAN	IL7R	physical	23151878
RNF8_HUMAN	RNF8	physical	22814251
BRCA1_HUMAN	BRCA1	physical	22814251
GTR5_HUMAN	SLC2A5	physical	21988832
HNRPQ_HUMAN	SYNCRIP	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
XRCC6_HUMAN	XRCC6	physical	22863883
ERF3_YEAST	SUP35	physical	24416454
LARP7_HUMAN	LARP7	physical	26186194
RL26L_HUMAN	RPL26L1	physical	26186194
RS21_HUMAN	RPS21	physical	26186194
RS27A_HUMAN	RPS27A	physical	26186194
SR140_HUMAN	U2SURP	physical	26186194
SF3B1_HUMAN	SF3B1	physical	26186194
SF3B2_HUMAN	SF3B2	physical	26186194
ZN768_HUMAN	ZNF768	physical	26186194
ZN574_HUMAN	ZNF574	physical	26186194
ZN121_HUMAN	ZNF121	physical	26186194
ZN358_HUMAN	ZNF358	physical	26186194
OZF_HUMAN	ZNF146	physical	26186194
ZN629_HUMAN	ZNF629	physical	26186194
KRI1_HUMAN	KRI1	physical	26186194
LTV1_HUMAN	LTV1	physical	26186194
UTP23_HUMAN	UTP23	physical	26186194
DHX57_HUMAN	DHX57	physical	26186194
TSR1_HUMAN	TSR1	physical	26186194
BMS1_HUMAN	BMS1	physical	26186194
ZN777_HUMAN	ZNF777	physical	26186194
CDR2L_HUMAN	CDR2L	physical	26186194
CHERP_HUMAN	CHERP	physical	26186194
KRR1_HUMAN	KRR1	physical	26186194
ZBT11_HUMAN	ZBTB11	physical	26186194
RS17_HUMAN	RPS17	physical	26186194
ZCRB1_HUMAN	ZCRB1	physical	26186194
CDR2_HUMAN	CDR2	physical	26186194
IMP3_HUMAN	IMP3	physical	26186194
GZF1_HUMAN	GZF1	physical	26186194
SRS10_HUMAN	SRSF10	physical	26186194
PURB_HUMAN	PURB	physical	26186194
ZN335_HUMAN	ZNF335	physical	26186194
IF4A2_HUMAN	EIF4A2	physical	26344197
LAGE3_HUMAN	LAGE3	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL23A_HUMAN	RPL23A	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL31_HUMAN	RPL31	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RL6_HUMAN	RPL6	physical	26344197
RLA0_HUMAN	RPLP0	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS10_HUMAN	RPS10	physical	26344197
RS12_HUMAN	RPS12	physical	26344197
RS15_HUMAN	RPS15	physical	26344197
RS15A_HUMAN	RPS15A	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RS8_HUMAN	RPS8	physical	26344197
RS9_HUMAN	RPS9	physical	26344197
QCR2_HUMAN	UQCRC2	physical	26344197
CDR2L_HUMAN	CDR2L	physical	28514442
RS27A_HUMAN	RPS27A	physical	28514442
CDR2_HUMAN	CDR2	physical	28514442
ZN335_HUMAN	ZNF335	physical	28514442
ZN358_HUMAN	ZNF358	physical	28514442
RS21_HUMAN	RPS21	physical	28514442
BMS1_HUMAN	BMS1	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
RS17_HUMAN	RPS17	physical	28514442
PURB_HUMAN	PURB	physical	28514442
ZN121_HUMAN	ZNF121	physical	28514442
ZN574_HUMAN	ZNF574	physical	28514442
UTP23_HUMAN	UTP23	physical	28514442
KRR1_HUMAN	KRR1	physical	28514442
RS3_HUMAN	RPS3	physical	28514442
ZN777_HUMAN	ZNF777	physical	28514442
YBOX1_HUMAN	YBX1	physical	28514442
DKC1_HUMAN	DKC1	physical	28514442

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RSSA_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, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-241, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-139, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-139, AND MASSSPECTROMETRY.	15592455 [Abstract]