RPSA
entrez
3921
canonical
uniprot
P08865
canonical
ensembl
ENSG00000168028
resolver
ensp
ENSP00000346067
resolver
ensp
ENSP00000389351
resolver
ensp
ENSP00000410848
resolver
ensp
ENSP00000513423
resolver
ensp
ENSP00000513424
resolver
ensp
ENSP00000513425
resolver
ensp
ENSP00000539152
resolver
ensp
ENSP00000539153
resolver
ensp
ENSP00000592592
resolver
ensp
ENSP00000592595
resolver
ensp
ENSP00000592598
resolver
ensp
ENSP00000592601
resolver
ensp
ENSP00000592602
resolver
ensp
ENSP00000592603
resolver
enst
ENST00000301821
resolver
enst
ENST00000443003
resolver
enst
ENST00000458478
resolver
enst
ENST00000697729
resolver
enst
ENST00000697730
resolver
enst
ENST00000697731
resolver
enst
ENST00000869093
resolver
enst
ENST00000869094
resolver
enst
ENST00000922533
resolver
enst
ENST00000922536
resolver
enst
ENST00000922539
resolver
enst
ENST00000922542
resolver
enst
ENST00000922543
resolver
enst
ENST00000922544
resolver
genesymbol
RPSA
resolver
genesymbol_syn
LAMBR
resolver
genesymbol_syn
LAMR1
resolver
hgnc
HGNC:6502
resolver
uniprot
A0A0C4DG17
resolver
uniprot
P11085
resolver
uniprot
P12030
resolver
uniprot
Q16471
resolver
uniprot
Q6IPD1
resolver
uniprot
Q6IPD2
resolver
uniprot
Q6NSD1
resolver
uniprot
Q6NXQ8
resolver
uniprot
Q86VC0
resolver
uniprot_entry
A0A0C4DG17_HUMAN
resolver
uniprot_entry
RSSA_HUMAN
resolver
uniprot_sec
P11085
resolver
uniprot_sec
P12030
resolver
uniprot_sec
Q16471
resolver
uniprot_sec
Q6IPD1
resolver
uniprot_sec
Q6IPD2
resolver
uniprot_sec
Q6NSD1
resolver
uniprot_sec
Q6NXQ8
resolver
uniprot_sec
Q86VC0
resolver
amino_acid_sequence
MSGALDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVISSRNTGQRAVLKFAAATGATPIAGRFTPGTFTNQIQAAFREPRLLVVTDPRADHQPLTEASYVNLPTIALCNTDSPLRYVDIAIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKAVTKEEFQGEWTAPAPEFTATQPEVADWSEGVQVPSVPIQQFPTEDWSAQPATEDWSAAPTAQATEWVGATTDWS
uniprot
proteins
disease_involvement
DISEASE: Asplenia, isolated congenital (ICAS) [MIM:271400]: A rare primary immunodeficiency and life-threatening condition, often presenting with pneumococcal sepsis. Most affected individuals die of severe bacterial infections in early childhood. Isolated asplenia is distinct from asplenia associated with other complex visceral defects, notably heterotaxy syndromes such as Ivemark syndrome. {ECO:0000269|PubMed:23579497}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: 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. {ECO:0000255|HAMAP-Rule:MF_03016, ECO:0000269|PubMed:16263087, ECO:0000269|PubMed:6300843}.; FUNCTION: (Microbial infection) Acts as a receptor for the Adeno-associated viruses 2,3,8 and 9. {ECO:0000269|PubMed:16973587}.; FUNCTION: (Microbial infection) Acts as a receptor for the Dengue virus. {ECO:0000269|PubMed:15507651}.; FUNCTION: (Microbial infection) Acts as a receptor for the Sindbis virus. {ECO:0000269|PubMed:1385835}.; FUNCTION: (Microbial infection) Acts as a receptor for the Venezuelan equine encephalitis virus. {ECO:0000269|PubMed:1385835}.; FUNCTION: (Microbial infection) Acts as a receptor for the pathogenic prion protein. {ECO:0000269|PubMed:11689427, ECO:0000269|PubMed:9396609}.; FUNCTION: (Microbial infection) Acts as a receptor for bacteria. {ECO:0000269|PubMed:15516338}.
uniprot
proteins
mass_dalton
32854
uniprot
proteins
post_translational_modification
PTM: Acylated. Acylation may be a prerequisite for conversion of the monomeric 37 kDa laminin receptor precursor (37LRP) to the mature dimeric 67 kDa laminin receptor (67LR), and may provide a mechanism for membrane association (PubMed:9581863). {ECO:0000255|HAMAP-Rule:MF_03016, ECO:0000269|PubMed:9581863}.; PTM: Cleaved by stromelysin-3 (ST3) at the cell surface. Cleavage by stromelysin-3 may be a mechanism to alter cell-extracellular matrix interactions. {ECO:0000255|HAMAP-Rule:MF_03016}.
uniprot
proteins
protein_family
Universal ribosomal protein uS2 family
uniprot
proteins
pubmed
10079194
uniprot
proteins
pubmed
10772861
uniprot
proteins
pubmed
11689427
uniprot
proteins
pubmed
1385835
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
1534510
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15507651
uniprot
proteins
pubmed
15516338
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
16263087
uniprot
proteins
pubmed
16973587
uniprot
proteins
pubmed
18063583
uniprot
proteins
pubmed
1834645
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23579497
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2429301
uniprot
proteins
pubmed
24524803
uniprot
proteins
pubmed
2543954
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
2970639
uniprot
proteins
pubmed
6300843
uniprot
proteins
pubmed
8433567
uniprot
proteins
pubmed
8586453
uniprot
proteins
pubmed
8706699
uniprot
proteins
pubmed
8760291
uniprot
proteins
pubmed
8764073
uniprot
proteins
pubmed
9396609
uniprot
proteins
pubmed
9581863
uniprot
proteins
pubmed
9582194
uniprot
proteins
pubmed
9718729
uniprot
proteins
sequence_length
295
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane. Cytoplasm. Nucleus {ECO:0000255|HAMAP-Rule:MF_03016}. Note=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 similarity). Colocalizes with PPP1R16B in the cell membrane. {ECO:0000255|HAMAP-Rule:MF_03016}.
uniprot
proteins