RT27_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RT27_HUMAN
• UniProt AC: Q92552
• Protein Name: 28S ribosomal protein S27, mitochondrial {ECO:0000305}
• Gene Name: MRPS27 {ECO:0000312|HGNC:HGNC:14512}
• Organism: Homo sapiens (Human).
• Sequence Length: 414
• Subcellular Localization: Cytoplasm . Mitochondrion .
• Protein Description: RNA-binding component of the mitochondrial small ribosomal subunit (mt-SSU) that plays a role in mitochondrial protein synthesis. [PubMed: 22841715 Stimulates mitochondrial mRNA translation of subunit components of the mitochondrial electron transport chain]
• Protein Sequence: MAASIVRRGMLLARQVVLPQLSPAGKRYLLSSAYVDSHKWEAREKEHYCLADLASLMDKTFERKLPVSSLTISRLIDNISSREEIDHAEYYLYKFRHSPNCWYLRNWTIHTWIRQCLKYDAQDKALYTLVNKVQYGIFPDNFTFNLLMDSFIKKENYKDALSVVFEVMMQEAFEVPSTQLLSLYVLFHCLAKKTDFSWEEERNFGASLLLPGLKQKNSVGFSSQLYGYALLGKVELQQGLRAVYHNMPLIWKPGYLDRALQVMEKVAASPEDIKLCREALDVLGAVLKALTSADGASEEQSQNDEDNQGSEKLVEQLDIEETEQSKLPQYLERFKALHSKLQALGKIESEGLLSLTTQLVKEKLSTCEAEDIATYEQNLQQWHLDLVQLIQREQQQREQAKQEYQAQKAAKASA

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
22	Phosphorylation	QVVLPQLSPAGKRYL HHHHHCCCCCHHHHH	13.88	-
45	Acetylation	HKWEAREKEHYCLAD HHCHHHHHHHCHHHH	44.21	25953088
49	Glutathionylation	AREKEHYCLADLASL HHHHHHCHHHHHHHH	2.45	22555962
59	Ubiquitination	DLASLMDKTFERKLP HHHHHHCHHHHCCCC	40.94	-
59	Ubiquitination	DLASLMDKTFERKLP HHHHHHCHHHHCCCC	40.94	-
68	Phosphorylation	FERKLPVSSLTISRL HHCCCCCCHHHHHHH	20.07	21406692
69	Phosphorylation	ERKLPVSSLTISRLI HCCCCCCHHHHHHHH	29.75	21406692
71	Phosphorylation	KLPVSSLTISRLIDN CCCCCHHHHHHHHHC	20.89	21406692
73	Phosphorylation	PVSSLTISRLIDNIS CCCHHHHHHHHHCCC	18.79	21406692
80	Phosphorylation	SRLIDNISSREEIDH HHHHHCCCCHHHHCH	29.60	22985185
81	Phosphorylation	RLIDNISSREEIDHA HHHHCCCCHHHHCHH	39.66	30243723
90	Phosphorylation	EEIDHAEYYLYKFRH HHHCHHHHHHHHCCC	10.27	25147952
91	Phosphorylation	EIDHAEYYLYKFRHS HHCHHHHHHHHCCCC	8.61	-
94	Acetylation	HAEYYLYKFRHSPNC HHHHHHHHCCCCCCC	33.07	26822725
118	Acetylation	TWIRQCLKYDAQDKA HHHHHHHCCCCCCHH	49.03	27452117
127	Phosphorylation	DAQDKALYTLVNKVQ CCCCHHHHHHHHHHH	11.68	21406692
128	Phosphorylation	AQDKALYTLVNKVQY CCCHHHHHHHHHHHC	25.69	21406692
150	Phosphorylation	TFNLLMDSFIKKENY HHHHHHHHHHCCCCH	18.20	24719451
194	Phosphorylation	FHCLAKKTDFSWEEE HHHHHHCCCCCHHHH	41.38	-
207	Phosphorylation	EERNFGASLLLPGLK HHHCCCCCCCCCCCC	21.67	21712546
218	Phosphorylation	PGLKQKNSVGFSSQL CCCCCCCCCCCHHHH	30.56	25072903
222	Phosphorylation	QKNSVGFSSQLYGYA CCCCCCCHHHHHHHH	15.96	25072903
223	Phosphorylation	KNSVGFSSQLYGYAL CCCCCCHHHHHHHHH	23.19	25072903
226	Phosphorylation	VGFSSQLYGYALLGK CCCHHHHHHHHHHHH	10.64	25072903
228	Phosphorylation	FSSQLYGYALLGKVE CHHHHHHHHHHHHHH	4.78	25072903
265	Malonylation	RALQVMEKVAASPED HHHHHHHHHCCCHHH	21.05	26320211
265	Ubiquitination	RALQVMEKVAASPED HHHHHHHHHCCCHHH	21.05	-
274	Acetylation	AASPEDIKLCREALD CCCHHHHHHHHHHHH	54.58	26051181
274	2-Hydroxyisobutyrylation	AASPEDIKLCREALD CCCHHHHHHHHHHHH	54.58	-
279	Ubiquitination	DIKLCREALDVLGAV HHHHHHHHHHHHHHH	6.96	-
292	Phosphorylation	AVLKALTSADGASEE HHHHHHHCCCCCCHH	25.80	21815630
297	Phosphorylation	LTSADGASEEQSQND HHCCCCCCHHHHCCC	47.39	27251275
301	Phosphorylation	DGASEEQSQNDEDNQ CCCCHHHHCCCCCCC	33.94	25159151
325	Phosphorylation	DIEETEQSKLPQYLE CHHHHHHHCHHHHHH	29.90	30631047
326	Ubiquitination	IEETEQSKLPQYLER HHHHHHHCHHHHHHH	64.97	-
326	Acetylation	IEETEQSKLPQYLER HHHHHHHCHHHHHHH	64.97	26051181
335	Succinylation	PQYLERFKALHSKLQ HHHHHHHHHHHHHHH	57.15	27452117
340	Ubiquitination	RFKALHSKLQALGKI HHHHHHHHHHHHCCC	33.59	-
340	2-Hydroxyisobutyrylation	RFKALHSKLQALGKI HHHHHHHHHHHHCCC	33.59	-
340	Acetylation	RFKALHSKLQALGKI HHHHHHHHHHHHCCC	33.59	25953088
340	Ubiquitination	RFKALHSKLQALGKI HHHHHHHHHHHHCCC	33.59	-
349	O-linked_Glycosylation	QALGKIESEGLLSLT HHHCCCCHHCHHHHH	40.20	28510447
349	Phosphorylation	QALGKIESEGLLSLT HHHCCCCHHCHHHHH	40.20	23403867
354	Ubiquitination	IESEGLLSLTTQLVK CCHHCHHHHHHHHHH	28.81	-
354	Phosphorylation	IESEGLLSLTTQLVK CCHHCHHHHHHHHHH	28.81	23403867
356	Phosphorylation	SEGLLSLTTQLVKEK HHCHHHHHHHHHHHH	14.77	23403867
357	Phosphorylation	EGLLSLTTQLVKEKL HCHHHHHHHHHHHHH	25.79	23403867
361	Ubiquitination	SLTTQLVKEKLSTCE HHHHHHHHHHHHCCC	58.69	2190698
375	Ubiquitination	EAEDIATYEQNLQQW CHHHHHHHHHHHHHH	13.39	21906983
375	Ubiquitination	EAEDIATYEQNLQQW CHHHHHHHHHHHHHH	13.39	-
413	Phosphorylation	AQKAAKASA------ HHHHHHHCC------	33.53	21601212

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RT27_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RT27_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RT27_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RT29_HUMAN	DAP3	physical	22939629
ICT1_HUMAN	ICT1	physical	20186120
RT29_HUMAN	DAP3	physical	20186120
RM03_HUMAN	MRPL3	physical	20186120
RM12_HUMAN	MRPL12	physical	20186120
NECA2_HUMAN	NECAB2	physical	25416956
RS8_HUMAN	RPS8	physical	26186194
DNJC1_HUMAN	DNAJC1	physical	26186194
LRC15_HUMAN	LRRC15	physical	26186194
RT22_HUMAN	MRPS22	physical	26344197
CH082_HUMAN	C8orf82	physical	28514442
NOA1_HUMAN	NOA1	physical	28514442
RT09_HUMAN	MRPS9	physical	28514442
RT33_HUMAN	MRPS33	physical	28514442
RT26_HUMAN	MRPS26	physical	28514442
RT23_HUMAN	MRPS23	physical	28514442
PTCD3_HUMAN	PTCD3	physical	28514442
RT35_HUMAN	MRPS35	physical	28514442
RT28_HUMAN	MRPS28	physical	28514442
RT21_HUMAN	MRPS21	physical	28514442
RT10_HUMAN	MRPS10	physical	28514442
RT14_HUMAN	MRPS14	physical	28514442
RT22_HUMAN	MRPS22	physical	28514442
RT18C_HUMAN	MRPS18C	physical	28514442
RT25_HUMAN	MRPS25	physical	28514442
RT16_HUMAN	MRPS16	physical	28514442
RT18B_HUMAN	MRPS18B	physical	28514442
MET17_HUMAN	METTL17	physical	28514442

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.