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P56704 (WNT3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein Wnt-3a
Gene names
Name:WNT3A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ligand for members of the frizzled family of seven transmembrane receptors. Wnt-3 and Wnt-3a play distinct roles in cell-cell signaling during morphogenesis of the developing neural tube.

Subunit structure

Homooligomer; disulfide-linked, leading to inactivation By similarity. Interacts with PORCN. Interacts with APCDD1 and WLS. Component of the Wnt-Fzd-LRP5-LRP6 signaling complex that contains a WNT protein, a FZD protein and LRP5 or LRP6. Interacts directly in the complex with LRP6. Ref.6 Ref.7 Ref.9

Subcellular location

Secretedextracellular spaceextracellular matrix.

Tissue specificity

Moderately expressed in placenta and at low levels in adult lung, spleen, and prostate.

Post-translational modification

Palmitoylation at Ser-209 is required for efficient binding to frizzled receptors. It is also required for subsequent palmitoylation at Cys-77. Palmitoylation is required for proper trafficking to cell surface, vacuolar acidification is critical to release palmitoylated WNT3A from WLS in secretory vesicles. Ref.8 Ref.10

Proteolytic processing by TIKI1 and TIKI2 promotes oxidation and formation of large disulfide-bond oligomers, leading to inactivation of WNT3A.

Sequence similarities

Belongs to the Wnt family.

Ontologies

Keywords
   Biological processWnt signaling pathway
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCOP9 signalosome assembly

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

Wnt signaling pathway involved in forebrain neuroblast division

Inferred from electronic annotation. Source: Ensembl

axis elongation involved in somitogenesis

Inferred from electronic annotation. Source: Ensembl

axon guidance

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway

Inferred from direct assay PubMed 19101069PubMed 20137080PubMed 20723538. Source: BHF-UCL

canonical Wnt signaling pathway involved in cardiac muscle cell fate commitment

Inferred from direct assay PubMed 20559569. Source: BHF-UCL

cell proliferation in forebrain

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

cellular protein localization

Inferred from electronic annotation. Source: Ensembl

cellular response to retinoic acid

Inferred from sequence or structural similarity. Source: UniProtKB

dorsal/ventral neural tube patterning

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Inferred from electronic annotation. Source: Ensembl

heart looping

Inferred from electronic annotation. Source: Ensembl

hemopoiesis

Inferred from electronic annotation. Source: Ensembl

hippocampus development

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

inner ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

mammary gland development

Inferred from electronic annotation. Source: Ensembl

negative regulation of axon extension involved in axon guidance

Inferred from electronic annotation. Source: Ensembl

negative regulation of fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of heart induction by canonical Wnt signaling pathway

Inferred from direct assay PubMed 19736317. Source: BHF-UCL

negative regulation of neurogenesis

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

negative regulation of neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

neuron differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

palate development

Inferred from mutant phenotype PubMed 18413325. Source: BHF-UCL

paraxial mesodermal cell fate commitment

Inferred from electronic annotation. Source: Ensembl

platelet aggregation

Inferred from electronic annotation. Source: Ensembl

positive regulation of B cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of canonical Wnt signaling pathway

Inferred from direct assay PubMed 17976063PubMed 18941195. Source: UniProtKB

positive regulation of canonical Wnt signaling pathway involved in controlling type B pancreatic cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cardiac muscle cell differentiation

Inferred from direct assay PubMed 20559569. Source: BHF-UCL

positive regulation of catenin import into nucleus

Inferred from direct assay PubMed 20137080PubMed 20723538. Source: BHF-UCL

positive regulation of cell proliferation

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

positive regulation of cell-cell adhesion mediated by cadherin

Inferred from electronic annotation. Source: Ensembl

positive regulation of collateral sprouting in absence of injury

Inferred from electronic annotation. Source: Ensembl

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of dermatome development

Inferred from direct assay PubMed 10654605. Source: BHF-UCL

positive regulation of mesodermal cell fate specification

Inferred from direct assay PubMed 20559569. Source: BHF-UCL

positive regulation of peptidyl-serine phosphorylation

Inferred from direct assay PubMed 20723538. Source: BHF-UCL

positive regulation of protein binding

Inferred from direct assay PubMed 16890161. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from direct assay PubMed 20137080PubMed 20412773. Source: BHF-UCL

positive regulation of protein tyrosine kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of receptor internalization

Inferred from direct assay PubMed 16890161. Source: BHF-UCL

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 20723538. Source: BHF-UCL

positive regulation of transcription, DNA-templated

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

post-anal tail morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of microtubule cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

skeletal muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

spinal cord association neuron differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

cell surface

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

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

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

plasma membrane

Traceable author statement. Source: Reactome

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionfrizzled binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction PubMed 19072540. Source: UniProtKB

receptor agonist activity

Inferred from direct assay PubMed 20723538. Source: BHF-UCL

transcription coactivator activity

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

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FZD8Q9H4612EBI-6173037,EBI-6254212

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P56704-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P56704-2)

The sequence of this isoform differs from the canonical sequence as follows:
     352-352: K → KNPGSRAGNSAHQPPHPQPPVRFHPPLRRAGKVP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 352334Protein Wnt-3a
PRO_0000041418

Sites

Site26 – 272Cleavage; by TIKI1 and TIKI2 By similarity

Amino acid modifications

Lipidation771S-palmitoyl cysteine Ref.10
Lipidation2091O-palmitoyl serine Ref.8 Ref.10
Lipidation2091O-palmitoyl serine; by PORCN Ref.8 Ref.10
Glycosylation871N-linked (GlcNAc...) Potential
Glycosylation2981N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence3521K → KNPGSRAGNSAHQPPHPQPP VRFHPPLRRAGKVP in isoform 2.
VSP_046558

Experimental info

Mutagenesis2091S → A: Abrogates WLS binding. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 10, 2002. Version 2.
Checksum: A317BD6D4A73920B

FASTA35239,365
        10         20         30         40         50         60 
MAPLGYFLLL CSLKQALGSY PIWWSLAVGP QYSSLGSQPI LCASIPGLVP KQLRFCRNYV 

        70         80         90        100        110        120 
EIMPSVAEGI KIGIQECQHQ FRGRRWNCTT VHDSLAIFGP VLDKATRESA FVHAIASAGV 

       130        140        150        160        170        180 
AFAVTRSCAE GTAAICGCSS RHQGSPGKGW KWGGCSEDIE FGGMVSREFA DARENRPDAR 

       190        200        210        220        230        240 
SAMNRHNNEA GRQAIASHMH LKCKCHGLSG SCEVKTCWWS QPDFRAIGDF LKDKYDSASE 

       250        260        270        280        290        300 
MVVEKHRESR GWVETLRPRY TYFKVPTERD LVYYEASPNF CEPNPETGSF GTRDRTCNVS 

       310        320        330        340        350 
SHGIDGCDLL CCGRGHNARA ERRREKCRCV FHWCCYVSCQ ECTRVYDVHT CK 

« Hide

Isoform 2 [UniParc].

Checksum: B2BBBFD1C7CA7E56
Show »

FASTA38542,905

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of WNT3a and WNT14 clustered in human chromosome 1q42 region."
Saitoh T., Hirai M., Katoh M.
Biochem. Biophys. Res. Commun. 284:1168-1175(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORMS 1 AND 2).
[5]"Differential expression of human Wnt genes 2, 3, 4, and 7B in human breast cell lines and normal and disease states of human breast tissue."
Huguet E.L., McMahon J.A., McMahon A.P., Bicknell R., Harris A.L.
Cancer Res. 54:2615-2621(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 207-330.
Tissue: Mammary gland.
[6]"Wntless, a conserved membrane protein dedicated to the secretion of Wnt proteins from signaling cells."
Baenziger C., Soldini D., Schuett C., Zipperlen P., Hausmann G., Basler K.
Cell 125:509-522(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WLS.
[7]"Reconstitution of a frizzled8.Wnt3a.LRP6 signaling complex reveals multiple Wnt and Dkk1 binding sites on LRP6."
Bourhis E., Tam C., Franke Y., Bazan J.F., Ernst J., Hwang J., Costa M., Cochran A.G., Hannoush R.N.
J. Biol. Chem. 285:9172-9179(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRP6 IN THE WNT/FZD/LRP6 COMPLEX.
[8]"WLS-dependent secretion of WNT3A requires Ser209 acylation and vacuolar acidification."
Coombs G.S., Yu J., Canning C.A., Veltri C.A., Covey T.M., Cheong J.K., Utomo V., Banerjee N., Zhang Z.H., Jadulco R.C., Concepcion G.P., Bugni T.S., Harper M.K., Mihalek I., Jones C.M., Ireland C.M., Virshup D.M.
J. Cell Sci. 123:3357-3367(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT SER-209 BY PORCN, MUTAGENESIS OF SER-209.
[9]"APCDD1 is a novel Wnt inhibitor mutated in hereditary hypotrichosis simplex."
Shimomura Y., Agalliu D., Vonica A., Luria V., Wajid M., Baumer A., Belli S., Petukhova L., Schinzel A., Brivanlou A.H., Barres B.A., Christiano A.M.
Nature 464:1043-1047(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APCDD1.
[10]"Fatty acid modification of Wnt1 and Wnt3a at serine is prerequisite for lipidation at cysteine and is essential for Wnt signalling."
Doubravska L., Krausova M., Gradl D., Vojtechova M., Tumova L., Lukas J., Valenta T., Pospichalova V., Fafilek B., Plachy J., Sebesta O., Korinek V.
Cell. Signal. 23:837-848(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-77 AND SER-209.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB060284 mRNA. Translation: BAB61052.1.
AK056278 mRNA. Translation: BAB71136.1.
AL136379 Genomic DNA. Translation: CAI23122.1.
BC103921 mRNA. Translation: AAI03922.1.
BC103922 mRNA. Translation: AAI03923.1.
BC103923 mRNA. Translation: AAI03924.1.
CCDSCCDS1564.1. [P56704-1]
RefSeqNP_149122.1. NM_033131.3. [P56704-1]
UniGeneHs.336930.

3D structure databases

ProteinModelPortalP56704.
SMRP56704. Positions 57-351.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124599. 3 interactions.
DIPDIP-58592N.
IntActP56704. 3 interactions.
STRING9606.ENSP00000284523.

Chemistry

BindingDBP56704.
ChEMBLCHEMBL1255137.

PTM databases

PhosphoSiteP56704.

Polymorphism databases

DMDM20532424.

Proteomic databases

PaxDbP56704.
PRIDEP56704.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000284523; ENSP00000284523; ENSG00000154342. [P56704-1]
ENST00000366753; ENSP00000355715; ENSG00000154342. [P56704-2]
GeneID89780.
KEGGhsa:89780.
UCSCuc001hrp.2. human.
uc001hrq.2. human. [P56704-1]

Organism-specific databases

CTD89780.
GeneCardsGC01P228194.
HGNCHGNC:15983. WNT3A.
HPAHPA050514.
MIM606359. gene.
neXtProtNX_P56704.
Orphanet85193. Idiopathic juvenile osteoporosis.
PharmGKBPA38074.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG284879.
HOGENOMHOG000039529.
HOVERGENHBG001595.
InParanoidP56704.
KOK00312.
OMACTTVNDS.
OrthoDBEOG7C8GJ8.
PhylomeDBP56704.
TreeFamTF105310.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkP56704.

Gene expression databases

BgeeP56704.
CleanExHS_WNT3A.
GenevestigatorP56704.

Family and domain databases

InterProIPR005817. Wnt.
IPR009141. Wnt3.
IPR018161. Wnt_CS.
[Graphical view]
PANTHERPTHR12027. PTHR12027. 1 hit.
PfamPF00110. wnt. 1 hit.
[Graphical view]
PRINTSPR01843. WNT3PROTEIN.
PR01349. WNTPROTEIN.
SMARTSM00097. WNT1. 1 hit.
[Graphical view]
PROSITEPS00246. WNT1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiWNT3A.
GenomeRNAi89780.
NextBio76263.
PROP56704.
SOURCESearch...

Entry information

Entry nameWNT3A_HUMAN
AccessionPrimary (citable) accession number: P56704
Secondary accession number(s): Q3SY79, Q3SY80, Q969P2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 10, 2002
Last modified: July 9, 2014
This is version 128 of the entry and version 2 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

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM