P08865 (RSSA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
40S ribosomal protein SA

Alternative name(s):
37 kDa laminin receptor precursor
Short name=37LRP
37/67 kDa laminin receptor
Short name=LRP/LR
67 kDa laminin receptor
Short name=67LR
Colon carcinoma laminin-binding protein
Laminin receptor 1
Short name=LamR
Laminin-binding protein precursor p40
Short name=LBP/p40
Multidrug resistance-associated protein MGr1-Ag
NEM/1CHD4

Gene names

Name:	RPSA
Synonyms:	LAMBR, LAMR1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	295 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. Ref.15 Ref.24 Ref.25
Subunit structure	Monomer (37LRP) and homodimer (67LR). Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (28S, 5.8S and 5S). Interacts with RPS21. Interacts with several laminins including at least LAMB1. Interacts with MDK By similarity. Interacts with PRNP. The mature dimeric form interacts with PPP1R16B (via its fourth ankyrin repeat). Interacts with PPP1CA only in the presence of PPP1R16B. Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24
Subcellular location	Cell membrane. Cytoplasm. Nucleus By similarity. 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. Co-localizes with PPP1R16B in the cell membrane. Ref.23 Ref.24
Post-translational modification	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. Cleaved by stromelysin-3 (ST3) at the cell surface. Cleavage by stromelysin-3 may be a mechanism to alter cell-extracellular matrix interactions By similarity.
Miscellaneous	This protein appears to have acquired a second function as a laminin receptor specifically in the vertebrate lineage. It is thought that in vertebrates 37/67 kDa laminin receptor acquired a dual function during evolution. It developed from the ribosomal protein SA, playing an essential role in the protein biosynthesis lacking any laminin binding activity, to a cell surface receptor with laminin binding activity.
Sequence similarities	Belongs to the ribosomal protein S2P family.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat
Molecular function	Receptor Ribonucleoprotein Ribosomal protein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell adhesion Non-traceable author statement. Source: ProtInc endocrine pancreas development Traceable author statement. Source: Reactome endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Inferred from Biological aspect of Ancestor. Source: RefGenome endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Inferred from Biological aspect of Ancestor. Source: RefGenome mRNA metabolic process Traceable author statement. Source: Reactome rRNA export from nucleus Inferred from Biological aspect of Ancestor. Source: RefGenome ribosomal small subunit assembly Inferred from Biological aspect of Ancestor. Source: RefGenome translational elongation Traceable author statement. Source: Reactome translational termination Traceable author statement. Source: Reactome viral transcription Traceable author statement. Source: Reactome
Cellular component	90S preribosome Inferred from Biological aspect of Ancestor. Source: RefGenome cytosolic small ribosomal subunit Inferred from direct assay Ref.10. Source: UniProtKB nucleus Traceable author statement. Source: UniProtKB plasma membrane Inferred from direct assay Ref.24. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction Ref.24. Source: UniProtKB receptor activity Inferred from electronic annotation. Source: UniProtKB-KW ribosome binding Inferred from physical interaction Ref.21. Source: UniProtKB structural constituent of ribosome Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 295

294

40S ribosomal protein SA

PRO_0000134358

Regions

Repeat

230 – 232

3

[DE]-W-[ST] 1

Repeat

247 – 249

3

[DE]-W-[ST] 2

Repeat

266 – 268

3

[DE]-W-[ST] 3

Repeat

275 – 277

3

[DE]-W-[ST] 4

Repeat

293 – 295

3

[DE]-W-[ST] 5

Region

54 – 113

60

Interaction with PPP1R16B

Region

161 – 180

20

Laminin-binding

Region

205 – 229

25

Laminin-binding

Region

242 – 295

54

Laminin-binding

Sites

Site

115 – 116

2

Cleavage; by ST3; site 1 By similarity

Site

133 – 134

2

Cleavage; by ST3; site 2 By similarity

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.8

Modified residue

43

1

Phosphoserine By similarity

Modified residue

52

1

N6-acetyllysine Ref.29

Modified residue

139

1

Phosphotyrosine Ref.26 Ref.27

Modified residue

241

1

Phosphothreonine Ref.28

Natural variations

Natural variant

117

1

R → W. Ref.7
Corresponds to variant rs17856150 [ dbSNP | Ensembl ].

VAR_025522

Experimental info

Sequence conflict

60

1

L → V in CAA43469. Ref.9

Sequence conflict

84

1

Q → QVCGTV in CAA33112. Ref.2

Sequence conflict

115

1

A → T in AAH50688. Ref.7

Sequence conflict

135

1

T → S in AAH70263. Ref.7

Sequence conflict

211

1

E → G in AAB22299. Ref.3

Sequence conflict

214

1

E → G in AAH66941. Ref.7

Sequence conflict

228

1

Q → L in AAB22299. Ref.3

Secondary structure

1

.

.

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.

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.

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.

.

.

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.

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.

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295

Helix Strand Turn

Details...

Helix

12 – 21

10

Turn

22 – 24

3

Helix

32 – 37

6

Beta strand

38 – 41

4

Beta strand

47 – 49

3

Helix

51 – 66

16

Helix

71 – 73

3

Beta strand

74 – 78

5

Helix

81 – 94

14

Beta strand

97 – 101

5

Turn

105 – 109

5

Beta strand

120 – 125

6

Turn

127 – 130

4

Helix

131 – 139

9

Beta strand

144 – 148

5

Beta strand

158 – 163

6

Helix

168 – 185

18

Beta strand

191 – 193

3

Helix

199 – 202

4

Sequences

	Sequence		Length	Mass (Da)
	P08865 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: C68DDB16B759E79E	FASTA	295	32,854
	10 20 30 40 50 60 MSGALDVLQM KEEDVLKFLA AGTHLGGTNL DFQMEQYIYK RKSDGIYIIN LKRTWEKLLL 70 80 90 100 110 120 AARAIVAIEN PADVSVISSR NTGQRAVLKF AAATGATPIA GRFTPGTFTN QIQAAFREPR 130 140 150 160 170 180 LLVVTDPRAD HQPLTEASYV NLPTIALCNT DSPLRYVDIA IPCNNKGAHS VGLMWWMLAR 190 200 210 220 230 240 EVLRMRGTIS REHPWEVMPD LYFYRDPEEI EKEEQAAAEK AVTKEEFQGE WTAPAPEFTA 250 260 270 280 290 TQPEVADWSE GVQVPSVPIQ QFPTEDWSAQ PATEDWSAAP TAQATEWVGA TTDWS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Increased mRNA expression of a laminin-binding protein in human colon carcinoma: complete sequence of a full-length cDNA encoding the protein." Yow H., Wong J.M., Chen H.S., Lee C., Steele G.D. Jr., Chen L.B. Proc. Natl. Acad. Sci. U.S.A. 85:6394-6398(1988) [PubMed: 2970639] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Characteristics of a multicopy gene family predominantly consisting of processed pseudogenes." van den Ouweland A.M.W., van Duijnhoven H.L.P., Deichmann K.A., van Groningen J.J.M., de Leij L., van de Ven W.J.M. Nucleic Acids Res. 17:3829-3843(1989) [PubMed: 2543954] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Cloning of 67-kDa laminin receptor cDNA and gene expression in normal and malignant cell lines of the human lung." Satoh K., Narumi K., Sakai T., Abe T., Kikuchi T., Matsushima K., Sindoh S., Motomiya M. Cancer Lett. 62:199-203(1992) [PubMed: 1534510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[4]	"Isolation from a multigene family of the active human gene of the metastasis-associated multifunctional protein 37LRP/p40 at chromosome 3p21.3." Jackers P., Minoletti F., Belotti D., Clausse N., Sozzi G., Sobel M.E., Castronovo V. Oncogene 13:495-503(1996) [PubMed: 8760291] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Multidrug resistance associated protein MGr1-Ag is identical to human 67-KDa laminin receptor precursor." Shi Y., Zhai H., Wang X., Wu H., Ning X., Han Y., Zhang D., Xiao B., Wu K., Fan D. Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TRP-117. Tissue: Bone marrow, Brain, Cervix, Hippocampus, Liver, Lung, Lymph, Placenta, Prostate, Skin and Urinary bladder.
[8]	Bienvenut W.V., Potts A., Barblan J., Quadroni M. Submitted (JUL-2004) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-17, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[9]	"Determination and analysis of the primary sequence of human laminin-binding protein." Siyanova E.Y., Lukashev V.A., Blinov V.M., Troyanovskii S.M. Dokl. Biochem. 313:227-231(1990) Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-295.
[10]	"Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry." Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A. Eur. J. Biochem. 239:144-149(1996) [PubMed: 8706699] [Abstract] Cited for: PROTEIN SEQUENCE OF 16-26 AND 90-99.
[11]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 43-52; 64-80; 103-117; 129-155 AND 192-205, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[12]	"The gene for human E2 small nucleolar RNA resides in an intron of a laminin-binding protein gene." Selvamurugan N., Eliceiri G.L. Genomics 30:400-401(1995) [PubMed: 8586453] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-209. Tissue: Blood.
[13]	"Altered levels of laminin receptor mRNA in various human carcinoma cells that have different abilities to bind laminin." Wewer U.M., Liotta L.A., Jaye M., Ricca G.A., Drohan W.N., Claysmith A.P., Rao C.N., Wirth P., Coligan J.E., Albrechtsen R., Mudryj M., Sobel M.E. Proc. Natl. Acad. Sci. U.S.A. 83:7137-7141(1986) [PubMed: 2429301] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 161-295, PROTEIN SEQUENCE OF 177-184.
[14]	"A map of 75 human ribosomal protein genes." Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C. Genome Res. 8:509-523(1998) [PubMed: 9582194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 225-295.
[15]	"Laminin receptor on human breast carcinoma cells." Terranova V.P., Rao C.N., Kalebic T., Margulies I.M., Liotta L.A. Proc. Natl. Acad. Sci. U.S.A. 80:444-448(1983) [PubMed: 6300843] [Abstract] Cited for: FUNCTION, INTERACTION WITH LAMININ-1.
[16]	"Functional domains of the 67-kDa laminin receptor precursor." Castronovo V., Taraboletti G., Sobel M.E. J. Biol. Chem. 266:20440-20446(1991) [PubMed: 1834645] [Abstract] Cited for: DOMAINS, INTERACTION WITH LAMININ-1.
[17]	"Interaction between the 67 kilodalton metastasis-associated laminin receptor and laminin." Cioce V., Margulies I.M.K., Sobel M.E., Castronovo V. Kidney Int. 43:30-37(1993) [PubMed: 8433567] [Abstract] Cited for: INTERACTION WITH LAMININ-1.
[18]	"The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells." Rieger R., Edenhofer F., Lasmezas C.I., Weiss S. Nat. Med. 3:1383-1388(1997) [PubMed: 9396609] [Abstract] Cited for: INTERACTION WITH PRNP.
[19]	"Formation of the 67-kDa laminin receptor by acylation of the precursor." Buto S., Tagliabue E., Ardini E., Magnifico A., Ghirelli C., van den Brule F., Castronovo V., Colnaghi M.I., Sobel M.E., Menard S. J. Cell. Biochem. 69:244-251(1998) [PubMed: 9581863] [Abstract] Cited for: ACYLATION.
[20]	"The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution." Ardini E., Pesole G., Tagliabue E., Magnifico A., Castronovo V., Sobel M.E., Colnaghi M.I., Menard S. Mol. Biol. Evol. 15:1017-1025(1998) [PubMed: 9718729] [Abstract] Cited for: INTERACTION WITH LAMININ-5.
[21]	"Ribosome-associated protein LBP/p40 binds to S21 protein of 40S ribosome: analysis using a yeast two-hybrid system." Sato M., Saeki Y., Tanaka K., Kaneda Y. Biochem. Biophys. Res. Commun. 256:385-390(1999) [PubMed: 10079194] [Abstract] Cited for: INTERACTION WITH RPS21.
[22]	"Phage display mapping for peptide 11 sensitive sequences binding to laminin-1." Kazmin D.A., Hoyt T.R., Taubner L., Teintze M., Starkey J.R. J. Mol. Biol. 298:431-445(2000) [PubMed: 10772861] [Abstract] Cited for: INTERACTION WITH LAMB1.
[23]	"The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein." Gauczynski S., Peyrin J.-M., Haik S., Leucht C., Hundt C., Rieger R., Krasemann S., Deslys J.-P., Dormont D., Lasmezas C.I., Weiss S. EMBO J. 20:5863-5875(2001) [PubMed: 11689427] [Abstract] Cited for: PRION-BINDING, SUBCELLULAR LOCATION, SUBUNIT.
[24]	"The protein phosphatase-1 targeting subunit TIMAP regulates LAMR1 phosphorylation." Kim K., Li L., Kozlowski K., Suh H.S., Cao W., Ballermann B.J. Biochem. Biophys. Res. Commun. 338:1327-1334(2005) [PubMed: 16263087] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH PPP1R16B AND PPP1CA.
[25]	"67-kDa laminin receptor promotes internalization of cytotoxic necrotizing factor 1-expressing Escherichia coli K1 into human brain microvascular endothelial cells." Kim K.J., Chung J.W., Kim K.S. J. Biol. Chem. 280:1360-1368(2005) [PubMed: 15516338] [Abstract] Cited for: FUNCTION AS A RECEPTOR FOR BACTERIA.
[26]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." 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) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-139, MASS SPECTROMETRY.
[27]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases 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) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-139, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[28]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-241, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52, MASS SPECTROMETRY.
[30]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]	"Crystal structure of the human laminin receptor precursor." Jamieson K.V., Wu J., Hubbard S.R., Meruelo D. J. Biol. Chem. 283:3002-3005(2008) [PubMed: 18063583] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 9-205.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03799 mRNA. Translation: AAA36161.1.
X15005 mRNA. Translation: CAA33112.1.
S37431 mRNA. Translation: AAB22299.1.
U43901 Genomic DNA. Translation: AAC50652.1.
AF503367 mRNA. Translation: AAM33304.1.
BT007219 mRNA. Translation: AAP35883.1.
BC005391 mRNA. Translation: AAH05391.1.
BC008867 mRNA. Translation: AAH08867.1.
BC010418 mRNA. Translation: AAH10418.1.
BC013827 mRNA. Translation: AAH13827.1.
BC034537 mRNA. Translation: AAH34537.1.
BC050688 mRNA. Translation: AAH50688.1.
BC053370 mRNA. Translation: AAH53370.1.
BC062714 mRNA. Translation: AAH62714.1.
BC066941 mRNA. Translation: AAH66941.1.
BC068062 mRNA. Translation: AAH68062.1.
BC070263 mRNA. Translation: AAH70263.1.
BC071693 mRNA. Translation: AAH71693.1.
BC071968 mRNA. Translation: AAH71968.1.
BC071969 mRNA. Translation: AAH71969.1.
BC071970 mRNA. Translation: AAH71970.1.
BC073863 mRNA. Translation: AAH73863.1.
BC107567 mRNA. Translation: AAI07568.1.
X61156 mRNA. Translation: CAA43469.1.
U36484 Genomic DNA. Translation: AAC50313.1.
M14199 mRNA. Translation: AAA36165.1.
AB007146 Genomic DNA. Translation: BAA25812.1.

IPI

IPI00553164.

PIR

A31233.

RefSeq

NP_001012321.1. NM_001012321.1.
NP_002286.2. NM_002295.4.

UniGene

Hs.449909.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BCH	X-ray	2.15	A	2-220	[»]

ProteinModelPortal

P08865.

SMR

P08865. Positions 9-205.

ModBase

Search...

Protein-protein interaction databases

IntAct

P08865. 18 interactions.

MINT

MINT-1402850.

STRING

P08865.

PTM databases

PhosphoSite

P08865.

Polymorphism databases

DMDM

125969.

Proteomic databases

PRIDE

P08865.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000301821; ENSP00000346067; ENSG00000168028.
ENST00000415859; ENSP00000415465; ENSG00000168028.

GeneID

3921.

KEGG

hsa:3921.

NMPDR

fig|9606.3.peg.22328.

UCSC

uc003cjp.1. human.

Organism-specific databases

CTD

3921.

GeneCards

GC03P039448.

H-InvDB

HIX0003190.

HGNC

HGNC:6502. RPSA.

HPA

CAB009561.

MIM

150370. gene.

neXtProt

NX_P08865.

PharmGKB

PA30287.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG08346.

HOVERGEN

HBG054466.

InParanoid

P08865.

OrthoDB

EOG40ZQZ6.

PhylomeDB

P08865.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_111217. Metabolism.
REACT_15380. Diabetes pathways.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_6167. Influenza Infection.
REACT_71. Gene Expression.

Gene expression databases

Bgee

P08865.

Genevestigator

P08865.

GermOnline

ENSG00000168028. Homo sapiens.

Family and domain databases

InterPro

IPR001865. Ribosomal_S2.
IPR018130. Ribosomal_S2_CS.
IPR005707. Ribosomal_S2_euk/arc.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]

KO

K02998.

PANTHER

PTHR11489. Ribosomal_S2_e/a. 1 hit.

Pfam

PF00318. Ribosomal_S2. 1 hit.
[Graphical view]

PRINTS

PR00395. RIBOSOMALS2.

SUPFAM

SSF52313. Ribosomal_S2. 1 hit.

TIGRFAMs

TIGR01012. Sa_S2_E_A. 1 hit.

PROSITE

PS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

15405.

SOURCE

Search...

Entry information

Entry name

RSSA_HUMAN

Accession

Primary (citable) accession number: P08865
Secondary accession number(s): P11085 , P12030, Q16471, Q6IPD1, Q6IPD2, Q6NSD1, Q6NXQ8, Q86VC0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 143 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.