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P02753 (RET4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinol-binding protein 4
Alternative name(s):
Plasma retinol-binding protein
Short name=PRBP
Short name=RBP
Gene names
Name:RBP4
ORF Names:PRO2222
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli.

Subcellular location

Secreted.

Involvement in disease

Retinal dystrophy, iris coloboma, and comedogenic acne syndrome (RDCCAS) [MIM:615147]: A disease characterized by retinal degeneration, ocular colobomas involving both the anterior and posterior segment, impaired night vision and loss of visual acuity. Additional characteristic features include developmental abnormalities and severe acne.
Note: The disease is caused by mutations affecting the gene represented in this entry. Loss of functional RBP4 protein results in serum retinol deficiency. Lack of normal levels of retinol impairs the visual cycle leading to night blindness at early stages; prolonged deficiency may lead to retinal degeneration. Additionally, retinol deficiency may result in dry skin, increased susceptibility to infection and acne (Ref.14). Ref.14 Ref.19 Ref.20

Sequence similarities

Belongs to the calycin superfamily. Lipocalin family.

Mass spectrometry

Molecular mass is 21063.46±1.88 Da from positions 17 - 199. Determined by ESI. Ref.10

Molecular mass is 20534 Da from positions 19 - 197. Determined by MALDI. Ref.11

Molecular mass is 20162 Da from positions 19 - 194. Determined by MALDI. Ref.11

Sequence caution

The sequence AAF69622.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processSensory transduction
Transport
Vision
   Cellular componentSecreted
   DiseaseDisease mutation
   DomainSignal
   LigandRetinol-binding
Vitamin A
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle tissue development

Inferred from sequence or structural similarity. Source: BHF-UCL

detection of light stimulus involved in visual perception

Inferred from electronic annotation. Source: Ensembl

embryonic organ morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

embryonic retina morphogenesis in camera-type eye

Inferred from sequence or structural similarity. Source: BHF-UCL

embryonic skeletal system development

Inferred from sequence or structural similarity. Source: BHF-UCL

eye development

Inferred from mutant phenotype Ref.20. Source: BHF-UCL

female genitalia morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

gluconeogenesis

Inferred from mutant phenotype PubMed 18466349. Source: BHF-UCL

glucose homeostasis

Inferred from direct assay PubMed 17003346. Source: BHF-UCL

heart development

Inferred from sequence or structural similarity. Source: BHF-UCL

heart trabecula formation

Inferred from sequence or structural similarity. Source: BHF-UCL

lung development

Inferred from sequence or structural similarity. Source: BHF-UCL

maintenance of gastrointestinal epithelium

Inferred from direct assay PubMed 10944490. Source: BHF-UCL

male gonad development

Inferred from electronic annotation. Source: Ensembl

negative regulation of cardiac muscle cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

phototransduction, visible light

Traceable author statement. Source: Reactome

positive regulation of immunoglobulin secretion

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of insulin secretion

Inferred from mutant phenotype PubMed 16034410. Source: BHF-UCL

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

response to retinoic acid

Inferred from direct assay PubMed 571335. Source: BHF-UCL

retinal metabolic process

Inferred from electronic annotation. Source: Ensembl

retinoid metabolic process

Traceable author statement. Source: Reactome

retinol metabolic process

Inferred from mutant phenotype Ref.20. Source: BHF-UCL

retinol transport

Inferred by curator PubMed 571335. Source: BHF-UCL

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

urinary bladder development

Inferred from sequence or structural similarity. Source: BHF-UCL

uterus development

Inferred from sequence or structural similarity. Source: BHF-UCL

vagina development

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 17003346PubMed 5132677. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 12228058. Source: UniProtKB

retinal binding

Inferred from electronic annotation. Source: UniProtKB-KW

retinol binding

Inferred from direct assay PubMed 571335. Source: BHF-UCL

retinol transporter activity

Inferred by curator PubMed 571335. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TTRO552452EBI-2116134,EBI-7038226From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.6 Ref.7 Ref.8
Chain19 – 201183Retinol-binding protein 4
PRO_0000017961
Chain19 – 200182Plasma retinol-binding protein(1-182)
PRO_0000017962
Chain19 – 199181Plasma retinol-binding protein(1-181)
PRO_0000017963
Chain19 – 197179Plasma retinol-binding protein(1-179)
PRO_0000017964
Chain19 – 194176Plasma retinol-binding protein(1-176)
PRO_0000017965

Amino acid modifications

Disulfide bond22 ↔ 178 Ref.6
Disulfide bond88 ↔ 192 Ref.6
Disulfide bond138 ↔ 147 Ref.6

Natural variations

Natural variant591I → N in RDCCAS. Ref.19 Ref.20
Corresponds to variant rs121918584 [ dbSNP | Ensembl ].
VAR_009276
Natural variant931G → D in RDCCAS. Ref.19 Ref.20
Corresponds to variant rs121918585 [ dbSNP | Ensembl ].
VAR_009277

Experimental info

Sequence conflict81L → F in AAH20633. Ref.4
Sequence conflict13 – 175LGSGR → WAA Ref.1
Sequence conflict13 – 175LGSGR → WAA Ref.5

Secondary structure

............................. 201
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02753 [UniParc].

Last modified March 29, 2005. Version 3.
Checksum: 660C6DD8CC9B811A

FASTA20123,010
        10         20         30         40         50         60 
MKWVWALLLL AALGSGRAER DCRVSSFRVK ENFDKARFSG TWYAMAKKDP EGLFLQDNIV 

        70         80         90        100        110        120 
AEFSVDETGQ MSATAKGRVR LLNNWDVCAD MVGTFTDTED PAKFKMKYWG VASFLQKGND 

       130        140        150        160        170        180 
DHWIVDTDYD TYAVQYSCRL LNLDGTCADS YSFVFSRDPN GLPPEAQKIV RQRQEELCLA 

       190        200 
RQYRLIVHNG YCDGRSERNL L 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of a full length cDNA coding for human retinol-binding protein."
Colantuoni V., Romano V., Bensi G., Santoro C., Costanzo F., Raugei G., Cortese R.
Nucleic Acids Res. 11:7769-7776(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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. expand/collapse author list , 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].
[4]"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].
Tissue: Liver.
[5]"Structure and cell-specific expression of a cloned human retinol binding protein gene: the 5'-flanking region contains hepatoma specific transcriptional signals."
D'Onofrio C., Colantuoni V., Cortese R.
EMBO J. 4:1981-1989(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-189.
[6]"The complete amino acid sequence of human serum retinol-binding protein."
Rask L., Anundi H., Fohlman J., Peterson P.A.
Ups. J. Med. Sci. 92:115-146(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-201, DISULFIDE BONDS.
[7]"Structural and functional studies of vitamin A-binding proteins."
Rask L., Anundi H., Boehme J., Eriksson U., Ronne H., Sege K., Peterson P.A.
Ann. N. Y. Acad. Sci. 359:79-90(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-201.
[8]"The primary structure of the human retinol-binding protein."
Rask L., Anundi H., Peterson P.A.
FEBS Lett. 104:55-58(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-183.
[9]"Functional prediction of the coding sequences of 79 new genes deduced by analysis of cDNA clones from human fetal liver."
Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M., He F.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-201.
Tissue: Fetal liver.
[10]"Characterization of two post-translationally processed forms of human serum retinol-binding protein: altered ratios in chronic renal failure."
Jaconi S., Rose K., Hughes G.J., Saurat J.-H., Siegenthaler G.
J. Lipid Res. 36:1247-1253(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY.
[11]"Comparative phenotypic analyses of human plasma and urinary retinol binding protein using mass spectrometric immunoassay."
Kiernan U.A., Tubbs K.A., Nedelkov D., Niederkofler E.E., Nelson R.W.
Biochem. Biophys. Res. Commun. 297:401-405(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
[12]"Comparative urine protein phenotyping using mass spectrometric immunoassay."
Kiernan U.A., Tubbs K.A., Nedelkov D., Niederkofler E.E., McConnell E., Nelson R.W.
J. Proteome Res. 2:191-197(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[13]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Exome analysis identified a novel mutation in the RBP4 gene in a consanguineous pedigree with retinal dystrophy and developmental abnormalities."
Cukras C., Gaasterland T., Lee P., Gudiseva H.V., Chavali V.R., Pullakhandam R., Maranhao B., Edsall L., Soares S., Reddy G.B., Sieving P.A., Ayyagari R.
PLoS ONE 7:E50205-E50205(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN RDCCAS.
[15]"The three-dimensional structure of retinol-binding protein."
Newcomer M.E., Jones T.A., Aqvist J., Sundelin J., Eriksson U., Rask L., Peterson P.A.
EMBO J. 3:1451-1454(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
[16]"Crystallographic refinement of human serum retinol binding protein at 2-A resolution."
Cowan S.W., Newcomer M.E., Jones T.A.
Proteins 8:44-61(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[17]"Three-dimensional structure and active site of three hydrophobic molecule-binding proteins with significant amino acid sequence similarity."
Monaco H.L., Zanotti G.
Biopolymers 32:457-465(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPARISON OF X-RAY STRUCTURES.
[18]"The structure of human retinol-binding protein (RBP) with its carrier protein transthyretin reveals an interaction with the carboxy terminus of RBP."
Naylor H.M., Newcomer M.E.
Biochemistry 38:2647-2653(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH TTR.
[19]"Phenotype in retinol deficiency due to a hereditary defect in retinol binding protein synthesis."
Seeliger M.W., Biesalski H.K., Wissinger B., Gollnick H., Gielen S., Frank J., Beck S.C., Zrenner E.
Invest. Ophthalmol. Vis. Sci. 40:3-11(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RDCCAS ASN-59 AND ASP-93.
[20]"Biochemical but not clinical vitamin A deficiency results from mutations in the gene for retinol binding protein."
Biesalski H.K., Frank J., Beck S.C., Heinrich F., Illek B., Reifen R., Gollnick H., Seeliger M.W., Wissinger B., Zrenner E.
Am. J. Clin. Nutr. 69:931-936(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS RDCCAS ASN-59 AND ASP-93.
+Additional computationally mapped references.

Web resources

Mutations of the RBP4 gene

Retina International's Scientific Newsletter

Wikipedia

Retinol-binding protein 4 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00129 mRNA. Translation: CAA24959.1.
AL356214 Genomic DNA. Translation: CAH72328.1.
CH471066 Genomic DNA. Translation: EAW50065.1.
CH471066 Genomic DNA. Translation: EAW50066.1.
CH471066 Genomic DNA. Translation: EAW50067.1.
BC020633 mRNA. Translation: AAH20633.1.
X02775 Genomic DNA. Translation: CAA26553.1.
X02824 Genomic DNA. Translation: CAB46489.1.
AF119868 mRNA. Translation: AAF69622.1. Different initiation.
AF025334 Genomic DNA. Translation: AAC02945.1.
AF025335 Genomic DNA. Translation: AAC02946.1.
CCDSCCDS31249.1.
PIRVAHU. A93494.
RefSeqNP_006735.2. NM_006744.3.
UniGeneHs.50223.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BRPX-ray2.50A19-200[»]
1BRQX-ray2.50A19-200[»]
1JYDX-ray1.70A19-200[»]
1JYJX-ray2.00A19-200[»]
1QABX-ray3.20E/F22-201[»]
1RBPX-ray2.00A19-200[»]
1RLBX-ray3.10E/F19-192[»]
2WQ9X-ray1.65A19-192[»]
2WQAX-ray2.85E/F19-194[»]
2WR6X-ray1.80A19-192[»]
3BSZX-ray3.38E/F19-194[»]
3FMZX-ray2.90A/B19-201[»]
ProteinModelPortalP02753.
SMRP02753. Positions 19-192.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111884. 5 interactions.
IntActP02753. 4 interactions.
STRING9606.ENSP00000360519.

Chemistry

BindingDBP02753.
ChEMBLCHEMBL3100.
DrugBankDB00162. Vitamin A.

PTM databases

PhosphoSiteP02753.

Polymorphism databases

DMDM62298174.

2D gel databases

SWISS-2DPAGEP02753.

Proteomic databases

MaxQBP02753.
PaxDbP02753.
PRIDEP02753.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371464; ENSP00000360519; ENSG00000138207.
ENST00000371467; ENSP00000360522; ENSG00000138207.
GeneID5950.
KEGGhsa:5950.
UCSCuc001kit.3. human.

Organism-specific databases

CTD5950.
GeneCardsGC10M095341.
H-InvDBHIX0009047.
HGNCHGNC:9922. RBP4.
HPACAB004555.
HPA001641.
MIM180250. gene.
615147. phenotype.
neXtProtNX_P02753.
Orphanet352718. Progressive retinal dystrophy due to retinol transport defect.
PharmGKBPA34289.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40507.
HOVERGENHBG004493.
InParanoidP02753.
KOK18271.
OMARYSGTWY.
OrthoDBEOG747PK3.
PhylomeDBP02753.
TreeFamTF331445.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000138207-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

BgeeP02753.
CleanExHS_RBP4.
GenevestigatorP02753.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022271. Lipocalin_ApoD.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002449. Retinol-bd/Purpurin.
[Graphical view]
PANTHERPTHR11873. PTHR11873. 1 hit.
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PIRSFPIRSF036893. Lipocalin_ApoD. 1 hit.
PIRSF500204. RBP_purpurin. 1 hit.
PRINTSPR00179. LIPOCALIN.
PR01174. RETINOLBNDNG.
SUPFAMSSF50814. SSF50814. 1 hit.
PROSITEPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRBP4. human.
EvolutionaryTraceP02753.
GeneWikiRetinol_binding_protein_4.
GenomeRNAi5950.
NextBio23182.
PROP02753.
SOURCESearch...

Entry information

Entry nameRET4_HUMAN
AccessionPrimary (citable) accession number: P02753
Secondary accession number(s): D3DR38 expand/collapse secondary AC list , O43478, O43479, Q5VY24, Q8WWA3, Q9P178
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 29, 2005
Last modified: July 9, 2014
This is version 174 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM