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P14206 (RSSA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein SA
Alternative name(s):
37 kDa laminin receptor precursor
Short name=37LRP
37 kDa oncofetal antigen
37/67 kDa laminin receptor
Short name=LRP/LR
67 kDa laminin receptor
Short name=67LR
Laminin receptor 1
Short name=LamR
Laminin-binding protein precursor p40
Short name=LBP/p40
OFA/iLRP
Gene names
Name:Rpsa
Synonyms:Lamr1, P40-8
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. Acts as a PPP1R16B-dependent substrate of PPP1CA By similarity. Enables malignant tumor cells to penetrate laminin tissue and vessel barriers. Activates precursor thymic anti-OFA/iLRP specific cytotoxic T-cell. May induce CD8 T-suppressor cells secreting IL-10. Ref.3 Ref.10 Ref.11 Ref.12 Ref.13

Subunit structure

Monomer (37LRP) and homodimer (67LR) By similarity. 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 By similarity. Interacts with several laminins including at least LAMB1. Interacts with MDK. Interacts with PRNP. The mature dimeric form interacts with PPP1R16B (via its fourth ankyrin repeat). Interacts with PPP1CA only in the presence of PPP1R16B By similarity. Ref.11 Ref.12 Ref.14 Ref.15

Subcellular location

Cell membrane. Cytoplasm. Nucleus. 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. Colocalizes with PPP1R16B in the cell membrane By similarity. 37LRP shuttles to the nucleus upon midkine (MDK) binding. Ref.8 Ref.10 Ref.13 Ref.14 Ref.15 Ref.17

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 By similarity. HAMAP-Rule MF_03016

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. HAMAP-Rule MF_03016

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 componentCell membrane
Cytoplasm
Membrane
Nucleus
   DomainRepeat
   Molecular functionReceptor
Ribonucleoprotein
Ribosomal protein
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-HAMAP

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

rRNA export from nucleus

Inferred from Biological aspect of Ancestor. Source: RefGenome

ribosomal small subunit assembly

Inferred from Biological aspect of Ancestor. Source: RefGenome

translation

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_component90S preribosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosolic small ribosomal subunit

Inferred from Biological aspect of Ancestor. Source: RefGenome

membrane

Inferred from sequence orthology PubMed 9588904. Source: MGI

nucleus

Inferred from direct assay PubMed 2146686. Source: MGI

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

small ribosomal subunit

Inferred from direct assay PubMed 2146686. Source: MGI

   Molecular_functionlaminin binding

Inferred from direct assay PubMed 8452943. Source: MGI

laminin receptor activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

structural constituent of ribosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 29529440S ribosomal protein SA HAMAP-Rule MF_03016
PRO_0000134359

Regions

Repeat230 – 2323[DE]-W-[ST] 1 HAMAP-Rule MF_03016
Repeat247 – 2493[DE]-W-[ST] 2 HAMAP-Rule MF_03016
Repeat266 – 2683[DE]-W-[ST] 3 HAMAP-Rule MF_03016
Repeat275 – 2773[DE]-W-[ST] 4 HAMAP-Rule MF_03016
Repeat293 – 2953[DE]-W-[ST] 5 HAMAP-Rule MF_03016
Region54 – 11360Interaction with PPP1R16B By similarity
Region161 – 18020Laminin-binding By similarity
Region205 – 22925Laminin-binding By similarity
Region242 – 29554Laminin-binding By similarity

Sites

Site115 – 1162Cleavage; by ST3; site 1 By similarity
Site133 – 1342Cleavage; by ST3; site 2 By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.7
Modified residue891N6-acetyllysine Ref.18
Modified residue1391Phosphotyrosine By similarity

Experimental info

Sequence conflict181F → L in AAA39413. Ref.1
Sequence conflict291N → H in BAB27355. Ref.5
Sequence conflict1551R → A in AAA39413. Ref.1
Sequence conflict2431P → T in AAH92041. Ref.6
Sequence conflict2491S → Y in BAC38701. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P14206 [UniParc].

Last modified May 1, 2007. Version 4.
Checksum: C698CFA6B759FD2E

FASTA29532,838
        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 
AQPEVADWSE GVQVPSVPIQ QFPTEDWSAQ PATEDWSAAP TAQATEWVGA TTEWS 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for a precursor of the high-affinity metastasis-associated murine laminin receptor."
Rao C.N., Castronovo V., Schmitt M.C., Wewer U.M., Claysmith A.P., Liotta L.A., Sobel M.E.
Biochemistry 28:7476-7486(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequence for a major messenger RNA for a 40 kilodalton polypeptide that is under translational control in mouse tumor cells."
Makrides S., Chitpatima S.T., Bandyopadhyay R., Brawerman G.
Nucleic Acids Res. 16:2349-2349(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"37 kilodalton oncofetal antigen protein and immature laminin receptor protein are identical, universal T-cell inducing immunogens on primary rodent and human cancers."
Coggin J.H. Jr., Barsoum A.L., Rohrer J.W.
Anticancer Res. 19:5535-5542(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Strain: BALB/c.
Tissue: Fibrosarcoma.
[4]"Genomic sequence analysis of laminin receptor loci in mice."
Lee I.Y., Baxter D.H., Qin S., Hood L.E.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CAST/Ei and SJL/J.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Liver, Muellerian duct, Pancreas, Spleen and Thymus.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6, Czech II and FVB/N.
Tissue: Brain, Colon, Eye, Kidney, Mammary gland, Mammary tumor and Pancreas.
[7]Kanor S., Quadroni M., Bienvenut W.V.
Submitted (MAR-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-10, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6J.
Tissue: Skeletal muscle.
[8]"Analysis of nuclear localization of laminin binding protein precursor p40 (LBP/p40)."
Sato M., Kinoshita K., Kaneda Y., Saeki Y., Iwamatsu A., Tanaka K.
Biochem. Biophys. Res. Commun. 229:896-901(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-40; 43-50; 90-100 AND 155-163, SUBCELLULAR LOCATION.
[9]Lubec G., Klug S., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 64-80; 90-117 AND 129-155, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Hippocampus.
[10]"Isolation of a tumor cell laminin receptor."
Rao N.C., Barsky S.H., Terranova V.P., Liotta L.A.
Biochem. Biophys. Res. Commun. 111:804-808(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS LAMININ RECEPTOR, SUBCELLULAR LOCATION.
[11]"Isolation of a laminin-binding protein from muscle cell membranes."
Lesot H., Kuehl U., von der Mark K.
EMBO J. 2:861-865(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LAMININ-1.
[12]"Isolation of a cell surface receptor protein for laminin from murine fibrosarcoma cells."
Malinoff H.L., Wicha M.S.
J. Cell Biol. 96:1475-1479(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LAMININ-1.
[13]"A 33-kDa polypeptide with homology to the laminin receptor: component of translation machinery."
Auth D., Brawerman G.
Proc. Natl. Acad. Sci. U.S.A. 89:4368-4372(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RIBOSOME, SUBCELLULAR LOCATION.
[14]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRNP, SUBCELLULAR LOCATION.
[15]"Midkine binds to 37-kDa laminin binding protein precursor, leading to nuclear transport of the complex."
Salama R.H.M., Muramatsu H., Zou K., Inui T., Kimura T., Muramatsu T.
Exp. Cell Res. 270:13-20(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MDK, SUBCELLULAR LOCATION.
[16]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Subcellular localization of prion proteins and the 37 kDa/67 kDa laminin receptor fused to fluorescent proteins."
Nikles D., Vana K., Gauczynski S., Knetsch H., Ludewigs H., Weiss S.
Biochim. Biophys. Acta 1782:335-340(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[18]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02870 mRNA. Translation: AAA39413.1.
X06406 mRNA. Translation: CAA29696.1.
AF140348 mRNA. Translation: AAD26866.1.
DQ360291 Genomic DNA. Translation: ABC95972.1.
DQ360292 Genomic DNA. Translation: ABC95977.1.
AK010423 mRNA. Translation: BAB26926.1.
AK010985 mRNA. Translation: BAB27306.1.
AK011041 mRNA. Translation: BAB27353.1.
AK011043 mRNA. Translation: BAB27355.1.
AK075778 mRNA. Translation: BAC35952.1.
AK075790 mRNA. Translation: BAC35960.1.
AK082935 mRNA. Translation: BAC38701.1.
AK088954 mRNA. Translation: BAC40671.1.
AK134224 mRNA. Translation: BAE22057.1.
AK135488 mRNA. Translation: BAE22550.1.
AK160551 mRNA. Translation: BAE35867.1.
AK160625 mRNA. Translation: BAE35924.1.
AK165219 mRNA. Translation: BAE38083.1.
AK166697 mRNA. Translation: BAE38953.1.
AK166874 mRNA. Translation: BAE39085.1.
AK167132 mRNA. Translation: BAE39278.1.
BC003829 mRNA. Translation: AAH03829.1.
BC037195 mRNA. Translation: AAH37195.1.
BC055886 mRNA. Translation: AAH55886.1.
BC081461 mRNA. Translation: AAH81461.1.
BC084677 mRNA. Translation: AAH84677.1.
BC092041 mRNA. Translation: AAH92041.1.
BC094902 mRNA. Translation: AAH94902.1.
BC099601 mRNA. Translation: AAH99601.1.
BC110285 mRNA. Translation: AAI10286.1.
CCDSCCDS23623.1.
PIRA29395.
RefSeqNP_035159.3. NM_011029.4.
XP_006543536.1. XM_006543473.1.
UniGeneMm.311972.
Mm.391708.
Mm.4071.

3D structure databases

ProteinModelPortalP14206.
SMRP14206. Positions 9-205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201107. 4 interactions.
DIPDIP-38089N.
IntActP14206. 9 interactions.
MINTMINT-1862996.

Chemistry

ChEMBLCHEMBL1075301.

PTM databases

PhosphoSiteP14206.

2D gel databases

REPRODUCTION-2DPAGEIPI00123604.
P14206.
SWISS-2DPAGEP14206.

Proteomic databases

MaxQBP14206.
PaxDbP14206.
PRIDEP14206.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035105; ENSMUSP00000035105; ENSMUSG00000032518.
GeneID102642689.
16785.
KEGGmmu:102642689.
mmu:16785.
UCSCuc009scd.2. mouse.

Organism-specific databases

CTD3921.
MGIMGI:105381. Rpsa.

Phylogenomic databases

eggNOGCOG0052.
GeneTreeENSGT00390000015036.
HOGENOMHOG000232073.
HOVERGENHBG054466.
InParanoidP14206.
KOK02998.
OMATEWDVVV.
OrthoDBEOG73NG4F.
PhylomeDBP14206.
TreeFamTF300100.

Gene expression databases

BgeeP14206.
CleanExMM_RPSA.
GenevestigatorP14206.

Family and domain databases

HAMAPMF_03015. Ribosomal_S2_euk.
MF_03016. Ribosomal_S2_laminin_receptor.
InterProIPR027504. 40S_ribosomal_SA.
IPR001865. Ribosomal_S2.
IPR018130. Ribosomal_S2_CS.
IPR027498. Ribosomal_S2_euk.
IPR005707. Ribosomal_S2_euk/arc.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERPTHR11489. PTHR11489. 1 hit.
PfamPF00318. Ribosomal_S2. 1 hit.
[Graphical view]
PRINTSPR00395. RIBOSOMALS2.
SUPFAMSSF52313. SSF52313. 1 hit.
TIGRFAMsTIGR01012. Sa_S2_E_A. 1 hit.
PROSITEPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPSA. mouse.
NextBio290650.
PROP14206.
SOURCESearch...

Entry information

Entry nameRSSA_MOUSE
AccessionPrimary (citable) accession number: P14206
Secondary accession number(s): Q58E74 expand/collapse secondary AC list , Q8BHL0, Q8BNL2, Q91V31, Q9CY13
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: May 1, 2007
Last modified: July 9, 2014
This is version 138 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot