AiPD: Autoinhibited Protein Database

P23396

Gene name	RPS3
Protein name	40S ribosomal protein S3
Names	Small ribosomal subunit protein uS3
Species	Homo sapiens (Human)
KEGG Pathway	hsa:6188
EC number	4.2.99.18: Other carbon-oxygen lyases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

177-243 (Predicted disordered autoinhibitory region) PR

Target domain
Relief mechanism
Assay	cis-regPred

AID

177-243 (Predicted disordered autoinhibitory region)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Yeon JH et al. (2016) "Systems-wide Identification of cis-Regulatory Elements in Proteins", Cell Systems, 2, 89-100

Autoinhibited structure

Activated structure

83 structures for P23396

Entry ID	Method	Resolution	Chain	Position	Source
1WH9	NMR	-	A	17-95	PDB
4UG0	EM	-	SD	1-243	PDB
4V6X	EM	500 A	AD	1-243	PDB
5A2Q	EM	390 A	D	1-243	PDB
5AJ0	EM	350 A	BD	1-243	PDB
5FLX	EM	390 A	D	1-243	PDB
5LKS	EM	360 A	SD	1-243	PDB
5OA3	EM	430 A	D	1-243	PDB
5T2C	EM	360 A	Aq	1-243	PDB
5VYC	X-ray	600 A	D1/D2/D3/D4/D5/D6	1-243	PDB
6FEC	EM	630 A	g	1-227	PDB
6G51	EM	410 A	D	1-243	PDB
6G53	EM	450 A	D	1-243	PDB
6G5H	EM	360 A	D	1-243	PDB
6G5I	EM	350 A	D	1-243	PDB
6IP5	EM	390 A	2p	1-243	PDB
6IP6	EM	450 A	2p	1-243	PDB
6IP8	EM	390 A	2p	1-243	PDB
6OLE	EM	310 A	SD	2-227	PDB
6OLF	EM	390 A	SD	2-227	PDB
6OLG	EM	340 A	BD	2-221	PDB
6OLI	EM	350 A	SD	2-227	PDB
6OLZ	EM	390 A	BD	2-221	PDB
6OM0	EM	310 A	SD	2-227	PDB
6OM7	EM	370 A	SD	2-227	PDB
6QZP	EM	290 A	SD	1-227	PDB
6XA1	EM	280 A	SD	4-227	PDB
6Y0G	EM	320 A	SD	1-243	PDB
6Y2L	EM	300 A	SD	1-243	PDB
6Y57	EM	350 A	SD	1-243	PDB
6YBS	EM	310 A	Z	1-243	PDB
6Z6L	EM	300 A	SD	1-243	PDB
6Z6M	EM	310 A	SD	1-243	PDB
6Z6N	EM	290 A	SD	1-243	PDB
6ZLW	EM	260 A	F	1-243	PDB
6ZM7	EM	270 A	SD	1-243	PDB
6ZME	EM	300 A	SD	1-243	PDB
6ZMI	EM	260 A	SD	1-243	PDB
6ZMO	EM	310 A	SD	1-243	PDB
6ZMT	EM	300 A	F	1-243	PDB
6ZMW	EM	370 A	Z	1-243	PDB
6ZN5	EM	320 A	F	3-227	PDB
6ZOJ	EM	280 A	D	1-243	PDB
6ZOL	EM	280 A	D	1-243	PDB
6ZON	EM	300 A	b	1-243	PDB
6ZP4	EM	290 A	b	1-243	PDB
6ZUO	EM	310 A	D	1-243	PDB
6ZV6	EM	290 A	D	1-243	PDB
6ZVH	EM	290 A	D	1-227	PDB
6ZVJ	EM	380 A	b	4-227	PDB
6ZXD	EM	320 A	D	1-243	PDB
6ZXE	EM	300 A	D	1-243	PDB
6ZXF	EM	370 A	D	1-243	PDB
6ZXG	EM	260 A	D	1-243	PDB
6ZXH	EM	270 A	D	1-243	PDB
7A09	EM	350 A	b	1-243	PDB
7K5I	EM	290 A	D	1-243	PDB
7QP6	EM	470 A	Z	1-243	PDB
7QP7	EM	370 A	Z	1-243	PDB
7QVP	EM	300 A	RD/SD	1-243	PDB
7R4X	EM	215 A	D	1-243	PDB
7TQL	EM	340 A	F	3-227	PDB
7XNX	EM	270 A	SD	1-243	PDB
7XNY	EM	250 A	SD	1-243	PDB
8G5Y	EM	229 A	SD	1-243	PDB
8G5Z	EM	264 A	SD	1-226	PDB
8G60	EM	254 A	SD	1-243	PDB
8G61	EM	294 A	SD	1-243	PDB
8G6J	EM	280 A	SD	1-243	PDB
8GLP	EM	167 A	SD	1-243	PDB
8IFD	EM	259 A	2p	1-243	PDB
8IFE	EM	257 A	2p	1-243	PDB
8JDJ	EM	250 A	0	1-243	PDB
8JDK	EM	226 A	0	1-243	PDB
8JDL	EM	242 A	0	1-243	PDB
8JDM	EM	267 A	0	1-243	PDB
8OZ0	EM	350 A	h	1-243	PDB
8PPK	EM	298 A	D	1-243	PDB
8PPL	EM	265 A	AD	1-243	PDB
8T4S	EM	260 A	D	1-243	PDB
8Y0W	EM	340 A	SD	1-243	PDB
8Y0X	EM	330 A	SD	1-243	PDB
AF-P23396-F1	Predicted				AlphaFoldDB

113 variants for P23396

Variant ID(s)	Position	Change	Description	Diseaes Association	Provenance
rs939710830 CA224657313	2	A>T		No	ClinGen TOPMed
rs1046077337 CA224657315	2	A>V		No	ClinGen gnomAD
CA381877033 rs1381673730	3	V>A		No	ClinGen gnomAD
CA224657325 rs1001912436	3	V>L		No	ClinGen TOPMed gnomAD
TCGA novel	4	Q>*	Variant assessed as Somatic; impact. [NCI-TCGA]	No	NCI-TCGA
rs772964979 CA6189272	4	Q>R	Variant assessed as Somatic; 0.0 impact. [NCI-TCGA]	No	ClinGen ExAC NCI-TCGA TOPMed gnomAD
rs1033354284 CA224657350	5	I>M		No	ClinGen gnomAD
CA381877064 rs1415968412	5	I>V		No	ClinGen gnomAD
CA381877087 rs1399258948	6	S>C		No	ClinGen TOPMed gnomAD
CA381877083 rs1327928698	6	S>P		No	ClinGen TOPMed
rs1327928698 CA381877081	6	S>T		No	ClinGen TOPMed
CA381877131 rs1565162329	9	R>K		No	ClinGen Ensembl
CA381877158 rs1463071170	10	K>N		No	ClinGen TOPMed
rs748523553 CA6189358	11	F>I		No	ClinGen ExAC gnomAD
CA6189360 rs773847813	14	D>E		No	ClinGen ExAC gnomAD
TCGA novel	15	G>D	Variant assessed as Somatic; impact. [NCI-TCGA]	No	NCI-TCGA
CA224658577 rs1002914063	17	F>V		No	ClinGen Ensembl
CA381878196 rs1282731545	20	E>*		No	ClinGen TOPMed
CA6189363 rs776774578	23	E>A		No	ClinGen ExAC gnomAD
TCGA novel	25	L>F	Variant assessed as Somatic; impact. [NCI-TCGA]	No	NCI-TCGA
TCGA novel	28	E>K	Variant assessed as Somatic; impact. [NCI-TCGA]	No	NCI-TCGA
CA6189365 rs765478023	34	Y>H		No	ClinGen ExAC gnomAD
CA6189367 rs762736053	36	G>R		No	ClinGen ExAC gnomAD
rs766895283 CA6189371	44	T>N		No	ClinGen ExAC gnomAD
CA381878534 rs1345824468	48	I>V		No	ClinGen gnomAD
rs755628828 CA6189373	49	I>V		No	ClinGen ExAC TOPMed gnomAD
CA224658719 rs3206671	51	L>*		No	ClinGen Ensembl
rs1276122131 CA381878578	52	A>T		No	ClinGen gnomAD
CA224658725 rs11546210	52	A>V		No	ClinGen TOPMed
CA6189399 rs778241086	56	Q>E		No	ClinGen ExAC gnomAD
CA6189401 rs757739842	64	R>Q		No	ClinGen ExAC gnomAD
rs1366756752 CA381878836	65	R>Q		No	ClinGen gnomAD
CA381878861 rs1400923703	67	R>W		No	ClinGen gnomAD
rs781721862 CA381878923	72	V>I		No	ClinGen ExAC gnomAD
CA6189402 rs781721862	72	V>L		No	ClinGen ExAC gnomAD
rs1403609388 CA381878938	73	V>I		No	ClinGen gnomAD
rs11546235 CA224659562	74	Q>R		No	ClinGen gnomAD
rs11546227 CA224659564	76	R>G		No	ClinGen Ensembl
rs1229279903 CA381878998	77	F>I		No	ClinGen TOPMed
CA224659570 rs11546209	78	G>R		No	ClinGen Ensembl
CA381879042 rs1376284272	79	F>V		No	ClinGen gnomAD
rs377566662 CA224659597	80	P>L		No	ClinGen ESP TOPMed
CA224659584 rs11546212	80	P>S		No	ClinGen TOPMed
CA381879078 rs1281497092	81	E>Q		No	ClinGen gnomAD
rs959967422 CA224659608	83	S>N		No	ClinGen Ensembl
CA381880109 rs11546215	86	L>H		No	ClinGen gnomAD
CA224660321 rs11546215	86	L>P		No	ClinGen gnomAD
CA381880106 rs1460438636	86	L>V		No	ClinGen gnomAD
CA381880129 rs1565163571	88	A>P		No	ClinGen Ensembl
rs11546234 CA224660328	91	V>L		No	ClinGen Ensembl
rs1301527696 CA381880213	95	G>D		No	ClinGen gnomAD
CA381880245 rs1278023527	97	C>S		No	ClinGen gnomAD
CA381880272 rs1230305698	99	I>F		No	ClinGen gnomAD
rs528039603 COSM467420 CA6189431	106	R>C	kidney Variant assessed as Somatic; 0.0 impact. [Cosmic, NCI-TCGA]	No	ClinGen cosmic curated 1000Genomes ExAC NCI-TCGA gnomAD
COSM1356991 CA224660361 rs1802703	110	L>I	large_intestine Variant assessed as Somatic; impact. [Cosmic, NCI-TCGA]	No	ClinGen cosmic curated Ensembl NCI-TCGA
TCGA novel	112	G>missing	Variant assessed as Somatic; impact. [NCI-TCGA]	No	NCI-TCGA
CA6189433 rs776751854	114	A>P		No	ClinGen ExAC gnomAD
CA224661918 rs1019933958	127	M>L		No	ClinGen Ensembl
TCGA novel	131	A>V	Variant assessed as Somatic; impact. [NCI-TCGA]	No	NCI-TCGA
rs11546221 CA224661924	132	K>Q		No	ClinGen Ensembl
rs11546219 CA224661956	140	G>R		No	ClinGen Ensembl
CA224661962 rs1802701	142	L>I		No	ClinGen Ensembl
rs1424228633 CA381881220	147	A>T		No	ClinGen gnomAD
CA6189459 rs760942337	153	V>A		No	ClinGen ExAC gnomAD
rs1261132427 CA381881294	157	M>K		No	ClinGen gnomAD
TCGA novel	162	D>Y	Variant assessed as Somatic; impact. [NCI-TCGA]	No	NCI-TCGA
CA381881383 rs1244837718	164	V>I		No	ClinGen gnomAD
CA6189463 rs765258151	165	N>I		No	ClinGen ExAC gnomAD
rs752738974 CA6189464	165	N>K		No	ClinGen ExAC TOPMed gnomAD
CA381881436 rs1232968412	167	Y>F		No	ClinGen TOPMed
rs747317928 CA6189467 COSM931985	173	R>C	Variant assessed as Somatic; 0.0 impact. endometrium [NCI-TCGA, Cosmic]	No	ClinGen cosmic curated ExAC NCI-TCGA TOPMed gnomAD
rs201666763 CA224662041	173	R>H		No	ClinGen TOPMed
CA381881530 rs1360641558	174	H>R		No	ClinGen gnomAD
TCGA novel	177	L>F	Variant assessed as Somatic; impact. [NCI-TCGA]	No	NCI-TCGA
rs1802702 CA224662740	181	V>M		No	ClinGen Ensembl
rs1236091952 CA381881757	185	K>M		No	ClinGen TOPMed
rs780760239 CA6189537	185	K>N		No	ClinGen ExAC gnomAD
CA381881806 rs1592024620	189	M>L		No	ClinGen Ensembl
CA381881913 rs1592024642	196	G>D		No	ClinGen Ensembl
rs774988250 CA381881941	198	I>S		No	ClinGen ExAC TOPMed gnomAD
rs774988250 CA6189540	198	I>T		No	ClinGen ExAC TOPMed gnomAD
rs748676206 CA6189541	201	K>N		No	ClinGen ExAC gnomAD
CA381882057 rs1326337008	207	H>Y		No	ClinGen gnomAD
rs1242865269 CA381882067	208	V>M		No	ClinGen Ensembl
TCGA novel	210	I>T	Variant assessed as Somatic; impact. [NCI-TCGA]	No	NCI-TCGA
CA224662809 rs11546223	219	P>A		No	ClinGen Ensembl
rs11266773 CA224662861	220	T>A		No	ClinGen Ensembl
CA381882237 rs1464846112	220	T>I		No	ClinGen TOPMed
CA224662818 rs11266773	220	T>P		No	ClinGen Ensembl
rs1592024733 CA381882240	221	T>P		No	ClinGen Ensembl
rs1481403035 CA381882269	223	I>M		No	ClinGen gnomAD
rs759369058 CA6189547	223	I>T		No	ClinGen ExAC gnomAD
CA6189546 rs776757218	223	I>V		No	ClinGen ExAC gnomAD
rs878935892 CA224662894	225	E>Q		No	ClinGen Ensembl
TCGA novel	227	K>N	Variant assessed as Somatic; impact. [NCI-TCGA]	No	NCI-TCGA
rs1174164337 CA381882303	227	K>Q		No	ClinGen TOPMed
rs11546195 CA224662896	228	G>V		No	ClinGen Ensembl
rs1395895163 CA381882326	230	K>R		No	ClinGen gnomAD
CA381882330 rs1193061325	231	P>S		No	ClinGen TOPMed
rs73006114 CA6189550	233	P>L		No	ClinGen 1000Genomes ESP ExAC TOPMed gnomAD
CA6189549 rs73006114	233	P>Q		No	ClinGen 1000Genomes ESP ExAC TOPMed gnomAD
rs73006114 CA224662929	233	P>R		No	ClinGen 1000Genomes ESP ExAC TOPMed gnomAD
rs1404540682 CA381882365	236	M>I		No	ClinGen gnomAD
rs780895530 CA6189554	236	M>V		No	ClinGen ExAC gnomAD
CA6189555 rs374046719	237	P>S		No	ClinGen ESP ExAC TOPMed gnomAD
rs11546224 CA6189556	239	P>Q		No	ClinGen 1000Genomes ESP ExAC TOPMed gnomAD
rs11546224 CA224662979	239	P>R		No	ClinGen 1000Genomes ESP ExAC TOPMed gnomAD
rs936723303 CA224662967	239	P>S		No	ClinGen Ensembl
TCGA novel	240	V>I	Variant assessed as Somatic; impact. [NCI-TCGA]	No	NCI-TCGA
CA381882384 rs1343457825	240	V>L		No	ClinGen TOPMed
CA381882400 rs1303382753	242	T>I		No	ClinGen TOPMed
CA6189557 rs779421649	243	A>T		No	ClinGen ExAC gnomAD
rs748621426 CA6189558	243	A>V		No	ClinGen ExAC gnomAD

No associated diseases with P23396

3 regional properties for P23396

Type	Name	Position	InterPro Accession
domain	Ribosomal protein S3, C-terminal	106 - 188	IPR001351
domain	K Homology domain, type 2	20 - 93	IPR004044
conserved_site	Ribosomal protein S3, conserved site	147 - 183	IPR018280

Functions

		Description
EC Number	4.2.99.18	Other carbon-oxygen lyases
Subcellular Localization	Cytoplasm Nucleus Nucleus, nucleolus Mitochondrion inner membrane ; Peripheral membrane protein Cytoplasm, cytoskeleton, spindle	In normal cells, located mainly in the cytoplasm with small amounts in the nucleus but translocates to the nucleus in cells undergoing apoptosis (By similarity) Nuclear translocation is induced by DNA damaging agents such as hydrogen peroxide (PubMed:17560175) Accumulates in the mitochondrion in response to increased ROS levels (PubMed:23911537) Localizes to the spindle during mitosis (PubMed:23131551) Localized in cytoplasmic mRNP granules containing untranslated mRNAs (PubMed:17289661)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category	No pathway information available

21 GO annotations of cellular component

Name	Definition
cytoplasm	The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol	The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
cytosolic ribosome	A ribosome located in the cytosol.
cytosolic small ribosomal subunit	The small subunit of a ribosome located in the cytosol.
endoplasmic reticulum	The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
extracellular exosome	A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
focal adhesion	A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ).
membrane	A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
mitochondrial inner membrane	The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
mitochondrial matrix	The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
mitotic spindle	A spindle that forms as part of mitosis. Mitotic and meiotic spindles contain distinctive complements of proteins associated with microtubules.
NF-kappaB complex	A protein complex that consists of a homo- or heterodimer of members of a family of structurally related proteins that contain a conserved N-terminal region called the Rel homology domain (RHD). In the nucleus, NF-kappaB complexes act as transcription factors. In unstimulated cells, NF-kappaB dimers are sequestered in the cytoplasm by IkappaB monomers; signals that induce NF-kappaB activity cause degradation of IkappaB, allowing NF-kappaB dimers to translocate to the nucleus and induce gene expression.
nucleolus	A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
nucleoplasm	That part of the nuclear content other than the chromosomes or the nucleolus.
nucleus	A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
plasma membrane	The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
polysome	A multiribosomal structure representing a linear array of ribosomes held together by messenger RNA. They represent the active complexes in cellular protein synthesis and are able to incorporate amino acids into polypeptides both in vivo and in vitro.
postsynaptic density	An electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.
ribonucleoprotein complex	A macromolecular complex that contains both RNA and protein molecules.
ribosome	An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins.
ruffle membrane	The portion of the plasma membrane surrounding a ruffle.

24 GO annotations of molecular function

Name	Definition
class I DNA-(apurinic or apyrimidinic site) endonuclease activity	Catalysis of the cleavage of an AP site 3' of the baseless site by a beta-lyase mechanism, leaving an unsaturated aldehyde, termed a 3'-(4-hydroxy-5-phospho-2-pentenal) residue, and a 5'-phosphate.
damaged DNA binding	Binding to damaged DNA.
DNA binding	Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA-(apurinic or apyrimidinic site) endonuclease activity	Catalysis of the cleavage of the C-O-P bond in the AP site created when DNA glycosylase removes a damaged base, involved in the DNA base excision repair pathway (BER).
DNA-binding transcription factor binding	Binding to a DNA-binding transcription factor, a protein that interacts with a specific DNA sequence (sometimes referred to as a motif) within the regulatory region of a gene to modulate transcription.
endodeoxyribonuclease activity	Catalysis of the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks.
enzyme binding	Binding to an enzyme, a protein with catalytic activity.
Hsp70 protein binding	Binding to a Hsp70 protein, heat shock proteins around 70kDa in size.
Hsp90 protein binding	Binding to Hsp90 proteins, any of a group of heat shock proteins around 90kDa in size.
iron-sulfur cluster binding	Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
kinase binding	Binding to a kinase, any enzyme that catalyzes the transfer of a phosphate group.
microtubule binding	Binding to a microtubule, a filament composed of tubulin monomers.
mRNA binding	Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.
oxidized purine DNA binding	Binding to a DNA region containing an oxidized purine residue.
oxidized pyrimidine DNA binding	Binding to a DNA region containing an oxidized pyrimidine residue.
protein kinase A binding	Binding to a protein kinase A.
protein kinase binding	Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
protein-containing complex binding	Binding to a macromolecular complex.
RNA binding	Binding to an RNA molecule or a portion thereof.
small ribosomal subunit rRNA binding	Binding to small ribosomal subunit RNA (SSU rRNA), a constituent of the small ribosomal subunit. In S. cerevisiae, this is the 18S rRNA.
structural constituent of ribosome	The action of a molecule that contributes to the structural integrity of the ribosome.
supercoiled DNA binding	Binding to supercoiled DNA. For example, during replication and transcription, template DNA is negatively supercoiled in the receding downstream DNA and positively supercoiled in the approaching downstream DNA.
tubulin binding	Binding to monomeric or multimeric forms of tubulin, including microtubules.
ubiquitin-like protein conjugating enzyme binding	Binding to a ubiquitin-like protein conjugating enzyme such as ubiquitin conjugating enzyme.

33 GO annotations of biological process

Name	Definition
apoptotic process	A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
cell division	The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
cellular response to DNA damage stimulus	Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
cellular response to hydrogen peroxide	Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydrogen peroxide (H2O2) stimulus.
cellular response to reactive oxygen species	Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.
cellular response to tumor necrosis factor	Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a tumor necrosis factor stimulus.
chromosome segregation	The process in which genetic material, in the form of chromosomes, is organized into specific structures and then physically separated and apportioned to two or more sets. In eukaryotes, chromosome segregation begins with the condensation of chromosomes, includes chromosome separation, and ends when chromosomes have completed movement to the spindle poles.
cytoplasmic translation	The chemical reactions and pathways resulting in the formation of a protein in the cytoplasm. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein.
DNA repair	The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
negative regulation of DNA repair	Any process that stops, prevents, or reduces the frequency, rate or extent of DNA repair.
negative regulation of protein ubiquitination	Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of ubiquitin groups to a protein.
negative regulation of translation	Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.
positive regulation of activated T cell proliferation	Any process that activates or increases the rate or extent of activated T cell proliferation.
positive regulation of apoptotic signaling pathway	Any process that activates or increases the frequency, rate or extent of apoptotic signaling pathway.
positive regulation of base-excision repair	Any process that activates or increases the frequency, rate or extent of base-excision repair.
positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis	Any process that activates or increases the frequency, rate or extent of cysteine-type endopeptidase activity involved in execution phase of apoptosis.
positive regulation of DNA N-glycosylase activity	Any process that activates or increases the frequency, rate or extent of DNA N-glycosylase activity.
positive regulation of DNA repair	Any process that activates or increases the frequency, rate or extent of DNA repair.
positive regulation of endodeoxyribonuclease activity	Any process that activates or increases the frequency, rate or extent of endodeoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks.
positive regulation of gene expression	Any process that increases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA).
positive regulation of interleukin-2 production	Any process that activates or increases the frequency, rate, or extent of interleukin-2 production.
positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage	Any process that activates or increases the frequency, rate or extent of intrinsic apoptotic signaling pathway in response to DNA damage.
positive regulation of JUN kinase activity	Any process that activates or increases the frequency, rate or extent of JUN kinase activity.
positive regulation of microtubule polymerization	Any process that activates or increases the frequency, rate or extent of microtubule polymerization.
positive regulation of NF-kappaB transcription factor activity	Any process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB.
positive regulation of NIK/NF-kappaB signaling	Any process that activates or increases the frequency, rate or extent of NIK/NF-kappaB signaling.
positive regulation of protein-containing complex assembly	Any process that activates or increases the frequency, rate or extent of protein complex assembly.
positive regulation of T cell receptor signaling pathway	Any process that activates or increases the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
regulation of apoptotic process	Any process that modulates the occurrence or rate of cell death by apoptotic process.
response to TNF agonist	Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a TNF agonist stimulus.
spindle assembly	The aggregation, arrangement and bonding together of a set of components to form the spindle, the array of microtubules and associated molecules that serves to move duplicated chromosomes apart.
translation	The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
translational initiation	The process preceding formation of the peptide bond between the first two amino acids of a protein. This includes the formation of a complex of the ribosome, mRNA or circRNA, and an initiation complex that contains the first aminoacyl-tRNA.

7 homologous proteins in AiPD

UniProt AC	Gene Name	Protein Name	Species	Evidence Code
P05750	RPS3	40S ribosomal protein S3	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)	PR
Q06559	RpS3	40S ribosomal protein S3	Drosophila melanogaster (Fruit fly)	PR
P62908	Rps3	40S ribosomal protein S3	Mus musculus (Mouse)	PR
P48152	rps-3	40S ribosomal protein S3	Caenorhabditis elegans	PR
Q9FJA6	RPS3C	40S ribosomal protein S3-3	Arabidopsis thaliana (Mouse-ear cress)	PR
Q9SIP7	RPS3A	40S ribosomal protein S3-1	Arabidopsis thaliana (Mouse-ear cress)	PR
Q9M339	RPS3B	40S ribosomal protein S3-2	Arabidopsis thaliana (Mouse-ear cress)	PR

10	20	30	40	50	60
MAVQISKKRK	FVADGIFKAE	LNEFLTRELA	EDGYSGVEVR	VTPTRTEIII	LATRTQNVLG
70	80	90	100	110	120
EKGRRIRELT	AVVQKRFGFP	EGSVELYAEK	VATRGLCAIA	QAESLRYKLL	GGLAVRRACY
130	140	150	160	170	180
GVLRFIMESG	AKGCEVVVSG	KLRGQRAKSM	KFVDGLMIHS	GDPVNYYVDT	AVRHVLLRQG
190	200	210	220	230	240
VLGIKVKIML	PWDPTGKIGP	KKPLPDHVSI	VEPKDEILPT	TPISEQKGGK	PEPPAMPQPV

PTA