dbPTM

RS27A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS27A_HUMAN
UniProt AC	P62979
Protein Name	Ubiquitin-40S ribosomal protein S27a
Gene Name	RPS27A
Organism	Homo sapiens (Human).
Sequence Length	156
Subcellular Localization	Ubiquitin: Cytoplasm. Nucleus.
Protein Description	Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.; 40S Ribosomal protein S27a: Component of the 40S subunit of the ribosome..
Protein Sequence	MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGAKKRKKKSYTTPKKNKHKRKKVKLAVLKYYKVDENGKISRLRRECPSDECGAGVFMASHFDRHYCGKCCLTYCFNKPEDK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Sumoylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	19608861
6	2-Hydroxyisobutyrylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	-
6	Sumoylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	-
6	Methylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	19608861
6	Malonylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	26320211
6	Acetylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	19608861
6	Ubiquitination	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	21906983
7	Phosphorylation	-MQIFVKTLTGKTIT -CEEEEEECCCCEEE	25.01	24043423
9	Phosphorylation	QIFVKTLTGKTITLE EEEEEECCCCEEEEE	41.69	23401153
11	Sumoylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
11	Sumoylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
11	Malonylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	26320211
11	Ubiquitination	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	21906983
11	Acetylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
12	Phosphorylation	VKTLTGKTITLEVEP EEECCCCEEEEEECC	22.12	25159151
14	Phosphorylation	TLTGKTITLEVEPSD ECCCCEEEEEECCCC	23.30	25159151
20	Phosphorylation	ITLEVEPSDTIENVK EEEEECCCCHHHHHH	33.60	21712546
22	Phosphorylation	LEVEPSDTIENVKAK EEECCCCHHHHHHHH	34.23	25159151
27	Ubiquitination	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	21906983
27	Acetylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
27	Sumoylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
27	Sumoylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
29	Ubiquitination	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	21906983
29	Acetylation	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	-
29	Sumoylation	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	-
33	Acetylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
33	Sumoylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
33	Ubiquitination	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	21906983
33	Malonylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	26320211
48	Sumoylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
48	Sumoylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	19608861
48	2-Hydroxyisobutyrylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
48	Malonylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	26320211
48	Acetylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	19608861
48	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	21906983
55	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC	35.82	25159151
57	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	23401153
59	Phosphorylation	DGRTLSDYNIQKEST CCCCCCCCCCCCHHH	15.70	23911959
63	2-Hydroxyisobutyrylation	LSDYNIQKESTLHLV CCCCCCCCHHHHHHH	50.24	-
63	Sumoylation	LSDYNIQKESTLHLV CCCCCCCCHHHHHHH	50.24	-
63	Sumoylation	LSDYNIQKESTLHLV CCCCCCCCHHHHHHH	50.24	-
63	Methylation	LSDYNIQKESTLHLV CCCCCCCCHHHHHHH	50.24	-
63	Ubiquitination	LSDYNIQKESTLHLV CCCCCCCCHHHHHHH	50.24	21906983
63	Malonylation	LSDYNIQKESTLHLV CCCCCCCCHHHHHHH	50.24	26320211
63	Acetylation	LSDYNIQKESTLHLV CCCCCCCCHHHHHHH	50.24	-
65	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHHHHHHHH	43.22	28355574
66	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHHHHHHHHH	21.20	22617229
72	Methylation	STLHLVLRLRGGAKK HHHHHHHHHCCCCHH	18.17	-
76	ADP-ribosylation	LVLRLRGGAKKRKKK HHHHHCCCCHHCCCC	27.99	28525742
84	Phosphorylation	AKKRKKKSYTTPKKN CHHCCCCCCCCCCCC	36.27	-
86	Phosphorylation	KRKKKSYTTPKKNKH HCCCCCCCCCCCCHH	43.65	29396449
87	Phosphorylation	RKKKSYTTPKKNKHK CCCCCCCCCCCCHHH	25.52	30576142
89	Ubiquitination	KKSYTTPKKNKHKRK CCCCCCCCCCHHHHH	67.87	-
99	Ubiquitination	KHKRKKVKLAVLKYY HHHHHHEEEEEEEEE	39.34	-
99	Acetylation	KHKRKKVKLAVLKYY HHHHHHEEEEEEEEE	39.34	25953088
104	2-Hydroxyisobutyrylation	KVKLAVLKYYKVDEN HEEEEEEEEEEECCC	39.68	-
104	Ubiquitination	KVKLAVLKYYKVDEN HEEEEEEEEEEECCC	39.68	21890473
104	Acetylation	KVKLAVLKYYKVDEN HEEEEEEEEEEECCC	39.68	19608861
104	Malonylation	KVKLAVLKYYKVDEN HEEEEEEEEEEECCC	39.68	26320211
105	Phosphorylation	VKLAVLKYYKVDENG EEEEEEEEEEECCCC	12.35	28152594
106	Phosphorylation	KLAVLKYYKVDENGK EEEEEEEEEECCCCC	11.71	28152594
107	Ubiquitination	LAVLKYYKVDENGKI EEEEEEEEECCCCCE	39.87	21890473
107	Succinylation	LAVLKYYKVDENGKI EEEEEEEEECCCCCE	39.87	27452117
107	Acetylation	LAVLKYYKVDENGKI EEEEEEEEECCCCCE	39.87	23749302
113	Ubiquitination	YKVDENGKISRLRRE EEECCCCCEEEHHHH	49.44	21906983
113	Acetylation	YKVDENGKISRLRRE EEECCCCCEEEHHHH	49.44	19608861
115	Phosphorylation	VDENGKISRLRRECP ECCCCCEEEHHHHCC	28.84	28348404
119	Methylation	GKISRLRRECPSDEC CCEEEHHHHCCCCCC	55.23	-
123	Phosphorylation	RLRRECPSDECGAGV EHHHHCCCCCCCCCC	58.67	29214152
123	O-linked_Glycosylation	RLRRECPSDECGAGV EHHHHCCCCCCCCCC	58.67	29351928
126	Glutathionylation	RECPSDECGAGVFMA HHCCCCCCCCCCCHH	5.63	22555962
132	Sulfoxidation	ECGAGVFMASHFDRH CCCCCCCHHCCCCCC	3.30	21406390
138	Methylation	FMASHFDRHYCGKCC CHHCCCCCCCCCCEE	23.02	-
143	2-Hydroxyisobutyrylation	FDRHYCGKCCLTYCF CCCCCCCCEEHHHHC	20.43	-
143	Ubiquitination	FDRHYCGKCCLTYCF CCCCCCCCEEHHHHC	20.43	21906983
143	Acetylation	FDRHYCGKCCLTYCF CCCCCCCCEEHHHHC	20.43	23749302
144	S-nitrosylation	DRHYCGKCCLTYCFN CCCCCCCEEHHHHCC	1.08	22178444
145	S-nitrosylation	RHYCGKCCLTYCFNK CCCCCCEEHHHHCCC	3.47	22178444
147	Phosphorylation	YCGKCCLTYCFNKPE CCCCEEHHHHCCCCC	12.34	27273156
148	Phosphorylation	CGKCCLTYCFNKPED CCCEEHHHHCCCCCC	5.10	28152594
149	S-nitrosylation	GKCCLTYCFNKPEDK CCEEHHHHCCCCCCC	2.27	22178444
152	Acetylation	CLTYCFNKPEDK--- EHHHHCCCCCCC---	29.54	21466224
152	Ubiquitination	CLTYCFNKPEDK--- EHHHHCCCCCCC---	29.54	19608861
152	Malonylation	CLTYCFNKPEDK--- EHHHHCCCCCCC---	29.54	26320211
156	Ubiquitination	CFNKPEDK------- HCCCCCCC-------	61.65	-
156	Acetylation	CFNKPEDK------- HCCCCCCC-------	61.65	-

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
65	S	Phosphorylation	Kinase	PINK1	Q9BXM7	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:21561866

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
65	S	Phosphorylation	24660806
[Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy.
65	S	ubiquitylation	24660806
[Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy.

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 RS27A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MDM2_HUMAN	MDM2	physical	21561866
A4_HUMAN	APP	physical	21832049
RS2_HUMAN	RPS2	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
TEBP_HUMAN	PTGES3	physical	22939629
SERA_HUMAN	PHGDH	physical	22939629
STRAP_HUMAN	STRAP	physical	22939629
SYTC_HUMAN	TARS	physical	22939629
TAF10_HUMAN	TAF10	physical	22939629
P53_HUMAN	TP53	physical	21561866
DAZP2_HUMAN	DAZAP2	physical	25416956
CACO2_HUMAN	CALCOCO2	physical	25416956
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 RS27A_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-6; LYS-48; LYS-104; LYS-107AND LYS-113, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASSSPECTROMETRY.	17081983 [Abstract]
Ubiquitylation
Reference	PubMed
"Polyubiquitination of proliferating cell nuclear antigen by HLTF andSHPRH prevents genomic instability from stalled replication forks."; Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X.,Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.; Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008). Cited for: UBIQUITINATION AT LYS-63, AND MUTAGENESIS OF LYS-48 AND LYS-63.	18719106 [Abstract]
"The proteomic reactor facilitates the analysis of affinity-purifiedproteins by mass spectrometry: application for identifyingubiquitinated proteins in human cells."; Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,Haines D.S., Figeys D.; J. Proteome Res. 6:298-305(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48, AND MASSSPECTROMETRY.	17203973 [Abstract]
"Mass spectrometric characterization of the affinity-purified human26S proteasome complex."; Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.; Biochemistry 46:3553-3565(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48, AND MASSSPECTROMETRY.	17323924 [Abstract]
"Differential regulation of EGF receptor internalization anddegradation by multiubiquitination within the kinase domain."; Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.; Mol. Cell 21:737-748(2006). Cited for: FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, ANDMASS SPECTROMETRY.	16543144 [Abstract]
"Alzheimer disease-specific conformation of hyperphosphorylated pairedhelical filament-tau is polyubiquitinated through Lys-48, Lys-11, andLys-6 ubiquitin conjugation."; Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.; J. Biol. Chem. 281:10825-10838(2006). Cited for: PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11AND LYS-48, AND MASS SPECTROMETRY.	16443603 [Abstract]

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