P27635 (RL10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
60S ribosomal protein L10

Alternative name(s):
Laminin receptor homolog
Protein QM
Tumor suppressor QM

Gene names

Name:	RPL10
Synonyms:	DXS648E, QM

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	214 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)

Subunit structure	Component of the large 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).
Developmental stage	Down-regulated during adipocyte, kidney, and heart differentiation.
Involvement in disease	Defects in RPL10 are a cause of susceptibility to autism X-linked type 5 (AUTSX5) [MIM:300847]. A complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation. Note=RPL10 is involved in autism only in rare cases. Two hypomorphic variants affecting the translation process have been found in families with autism spectrum disorders, suggesting that aberrant translation may play a role in disease mechanisms. Ref.20 Ref.21
Sequence similarities	Belongs to the ribosomal protein L10e family.
Sequence caution	The sequence AAB22173.1 differs from that shown. Reason: Frameshift at position 124. The sequence CAM45852.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAM45853.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	endocrine pancreas development Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome translational elongation Traceable author statement. Source: Reactome translational termination Traceable author statement. Source: Reactome viral transcription Traceable author statement. Source: Reactome
Cellular component	cytosolic large ribosomal subunit Inferred from direct assay Ref.15. Source: UniProtKB endoplasmic reticulum Inferred from direct assay. Source: LIFEdb
Molecular function	structural constituent of ribosome Non-traceable author statement Ref.15. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.15

Chain

2 – 214

213

60S ribosomal protein L10

PRO_0000147105

Amino acid modifications

Modified residue

121

1

N6-acetyllysine Ref.17

Modified residue

208

1

N6-acetyllysine Ref.17

Cross-link

188

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.16

Natural variations

Natural variant

202

1

N → S. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Ref.7 Ref.8 Ref.10 Ref.12 Ref.14
Corresponds to variants rs4909 [ dbSNP | Ensembl ] and rs12012747 [ dbSNP | Ensembl ].

VAR_006922

Natural variant

206

1

L → M in AUTSX5. Ref.20

VAR_027795

Natural variant

213

1

H → Q in AUTSX5. Ref.20 Ref.21

VAR_027796

Experimental info

Sequence conflict

23

1

Missing in AAL88713. Ref.5

Sequence conflict

157

1

F → L in BAD97029. Ref.8

Secondary structure

1

.

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.

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.

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214

Helix Strand Turn

Details...

Turn

43 – 45

3

Beta strand

48 – 54

7

Beta strand

58 – 61

4

Helix

62 – 80

19

Beta strand

84 – 89

6

Beta strand

126 – 129

4

Beta strand

133 – 140

8

Helix

142 – 144

3

Helix

145 – 155

11

Helix

156 – 158

3

Beta strand

159 – 161

3

Beta strand

163 – 169

7

Sequences

	Sequence		Length	Mass (Da)
	P27635 [UniParc]. Last modified June 12, 2007. Version 4. Checksum: 0860CECC91DF74FE	FASTA	214	24,604
	10 20 30 40 50 60 MGRRPARCYR YCKNKPYPKS RFCRGVPDAK IRIFDLGRKK AKVDEFPLCG HMVSDEYEQL 70 80 90 100 110 120 SSEALEAARI CANKYMVKSC GKDGFHIRVR LHPFHVIRIN KMLSCAGADR LQTGMRGAFG 130 140 150 160 170 180 KPQGTVARVH IGQVIMSIRT KLQNKEHVIE ALRRAKFKFP GRQKIHISKK WGFTKFNADE 190 200 210 FEDMVAEKRL IPDGCGVKYI PNRGPLDKWR ALHS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The isolation and characterization of a novel cDNA demonstrating an altered mRNA level in nontumorigenic Wilms' microcell hybrid cells." Dowdy S.F., Lai K.M., Weissman B.E., Matsui Y., Hogan B.L.M., Stanbridge E.S. Nucleic Acids Res. 19:5763-5769(1991) [PubMed: 1658743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-202.
[2]	"Identification and characterization of a new gene in the human Xq28 region." van den Ouweland A.M.W., Kioschis P., Verdijk M., Tamanini F., Toniolo D., Poustka A., van Oost B.A. Hum. Mol. Genet. 1:269-273(1992) [PubMed: 1303197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-202.
[3]	"Sequence analysis of a novel gene expressed in normal and in tumor-derived tissue." Kroepelin M. Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-202. Tissue: Mammary gland.
[4]	"Genomic organization of a cDNA (QM) demonstrating an altered mRNA level in nontumorigenic Wilms' microcell hybrid cells and its localization to Xq28." Kaneko K., Kobayashi H., Onodera O., Miyatake T., Tsuji S. Hum. Mol. Genet. 1:529-533(1992) [PubMed: 1339145] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-202.
[5]	"QM, a putative tumor suppressor, regulates proto-oncogene c-Yes." Oh H.S., Kwon H., Sun S.K., Yang C.-H. J. Biol. Chem. 277:36489-36498(2002) [PubMed: 12138090] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Loss of heterozygosity and microsatellite instability at the Xq28 and the A/G heterozygosity of the QM gene are associated with ovarian cancer." Shen X.J., Ali-Fehmi R., Weng C.R., Sarkar F.H., Grignon D., Liao D.J. Cancer Biol. Ther. 5:523-528(2006) [PubMed: 16627977] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-202. Tissue: Mammary cancer, Ovarian carcinoma, Pancreatic cancer and Prostatic carcinoma.
[7]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-202.
[8]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-202. Tissue: Thymus.
[9]	"Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci." Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M. Hum. Mol. Genet. 5:659-668(1996) [PubMed: 8733135] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-202.
[11]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	"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 SER-202. Tissue: Brain, Mammary gland and Placenta.
[13]	"cDNA cloning and genomic analysis of a new multigene family sharing common phylogenetic and expression profiles with the laminin receptor gene." Bignon C., Roux-Dosseto M., Zeigler M.E., Wicha M.S., Martin P.M. Biochem. Biophys. Res. Commun. 184:1165-1172(1992) [PubMed: 1534224] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-147.
[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 135-214, VARIANT SER-202.
[15]	"Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing." Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R., Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G. J. Protein Chem. 22:249-258(2003) [PubMed: 12962325] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11, MASS SPECTROMETRY.
[16]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed: 18781797] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-188, MASS SPECTROMETRY.
[17]	"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-121 AND LYS-208, MASS SPECTROMETRY.
[18]	"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].
[19]	"Crystal structure of human ribosomal protein L10 core domain reveals eukaryote-specific motifs in addition to the conserved fold." Nishimura M., Kaminishi T., Takemoto C., Kawazoe M., Yoshida T., Tanaka A., Sugano S., Shirouzu M., Ohkubo T., Yokoyama S., Kobayashi Y. J. Mol. Biol. 377:421-430(2008) [PubMed: 18258260] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 34-182.
[20]	"Mutations in the ribosomal protein gene RPL10 suggest a novel modulating disease mechanism for autism." Klauck S.M., Felder B., Kolb-Kokocinski A., Schuster C., Chiocchetti A., Schupp I., Wellenreuther R., Schmoetzer G., Poustka F., Breitenbach-Koller L., Poustka A. Mol. Psychiatry 11:1073-1084(2006) [PubMed: 16940977] [Abstract] Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO AUTISM, VARIANTS AUTSX5 MET-206 AND GLN-213.
[21]	"Mutation and expression analyses of the ribosomal protein gene RPL10 in an extended German sample of patients with autism spectrum disorder." Chiocchetti A., Pakalapati G., Duketis E., Wiemann S., Poustka A., Poustka F., Klauck S.M. Am. J. Med. Genet. A 155:1472-1475(2011) [PubMed: 21567917] [Abstract] Cited for: VARIANT AUTSX5 GLN-213.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M64241 mRNA. Translation: AAA63253.1.
M81806 Genomic DNA. Translation: AAA36021.1.
M73791 mRNA. Translation: AAA36378.1.
S64169, S64168 Genomic DNA. Translation: AAB27665.1.
AF486812 mRNA. Translation: AAL88713.1.
DQ369703 mRNA. Translation: ABC88559.1.
DQ369704 mRNA. Translation: ABC88560.1.
DQ369705 mRNA. Translation: ABC88561.1.
DQ369706 mRNA. Translation: ABC88562.1.
DQ369707 mRNA. Translation: ABC88563.1.
DQ369708 mRNA. Translation: ABC88564.1.
DQ369709 mRNA. Translation: ABC88565.1.
DQ369710 mRNA. Translation: ABC88566.1.
DQ369711 mRNA. Translation: ABC88567.1.
DQ369712 mRNA. Translation: ABC88568.1.
DQ369713 mRNA. Translation: ABC88569.1.
DQ369714 mRNA. Translation: ABC88570.1.
DQ369715 mRNA. Translation: ABC88571.1.
DQ369716 mRNA. Translation: ABC88572.1.
CR456797 mRNA. Translation: CAG33078.1.
CR542069 mRNA. Translation: CAG46866.1.
AK223309 mRNA. Translation: BAD97029.1.
L44140 Genomic DNA. Translation: AAA92646.1.
BX936347, BX936346 Genomic DNA. Translation: CAI43214.1.
BX936346, BX936347 Genomic DNA. Translation: CAI43230.1.
BX936347, BX936346 Genomic DNA. Translation: CAM45852.1. Sequence problems.
BX936346, BX936347 Genomic DNA. Translation: CAM45853.1. Sequence problems.
CH471172 Genomic DNA. Translation: EAW72737.1.
CH471172 Genomic DNA. Translation: EAW72739.1.
BC003358 mRNA. Translation: AAH03358.1.
BC026276 mRNA. Translation: AAH26276.1.
BC071918 mRNA. Translation: AAH71918.1.
S35960 mRNA. Translation: AAB22173.1. Frameshift.
AB007170 Genomic DNA. Translation: BAA28595.1.

IPI

IPI00554723.

PIR

A42735.

RefSeq

NP_006004.2. NM_006013.3.

UniGene

Hs.401929.
Hs.534404.
Hs.657751.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PA2	X-ray	2.50	A/B	34-182	[»]

ProteinModelPortal

P27635.

SMR

P27635. Positions 3-207.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1133N.

IntAct

P27635. 6 interactions.

MINT

MINT-1153266.

STRING

P27635.

PTM databases

PhosphoSite

P27635.

Polymorphism databases

DMDM

148887414.

Proteomic databases

PRIDE

P27635.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000344746; ENSP00000341730; ENSG00000147403.
ENST00000369817; ENSP00000358832; ENSG00000147403.
ENST00000424325; ENSP00000413436; ENSG00000147403.

GeneID

6134.

KEGG

hsa:6134.

UCSC

uc004fkm.1. human.

Organism-specific databases

CTD

6134.

GeneCards

GC0XP153618.

H-InvDB

HIX0017152.

HGNC

HGNC:10298. RPL10.

HPA

CAB010339.
HPA011311.

MIM

300847. phenotype.
312173. gene.

neXtProt

NX_P27635.

Orphanet

106. Autism.

PharmGKB

PA34660.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG19820.

HOVERGEN

HBG002287.

OrthoDB

EOG4X6C95.

PhylomeDB

P27635.

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

ArrayExpress

P27635.

Bgee

P27635.

CleanEx

HS_RPL10.

Genevestigator

P27635.

GermOnline

ENSG00000147403. Homo sapiens.

Family and domain databases

InterPro

IPR001197. Ribosomal_L10e.
IPR016180. Ribosomal_L10e/L16.
IPR018255. Ribosomal_L10e_CS.
[Graphical view]

KO

K02866.

Pfam

PF00252. Ribosomal_L16. 1 hit.
[Graphical view]

PIRSF

PIRSF005590. Ribosomal_L10. 1 hit.

SUPFAM

SSF54686. Ribosomal_L10e/L16. 1 hit.

TIGRFAMs

TIGR00279. L10e. 1 hit.

PROSITE

PS01257. RIBOSOMAL_L10E. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

23827.

PMAP-CutDB

P27635.

SOURCE

Search...

Entry information

Entry name

RL10_HUMAN

Accession

Primary (citable) accession number: P27635
Secondary accession number(s): A3KQT0 , D3DWW6, Q16470, Q2HXT7, Q53FH7, Q6FGN8, Q8TDA5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	June 12, 2007
Last modified:	January 25, 2012
This is version 124 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.