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P43026 (GDF5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. 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:
Growth/differentiation factor 5

Short name=GDF-5
Alternative name(s):
Bone morphogenetic protein 14
Short name=BMP-14
Cartilage-derived morphogenetic protein 1
Short name=CDMP-1
Lipopolysaccharide-associated protein 4
Short name=LAP-4
Short name=LPS-associated protein 4
Radotermin
Gene names
Name:GDF5
Synonyms:BMP14, CDMP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required to prevent excessive muscle loss upon denervation. This function requires SMAD4 and is mediated by phosphorylated SMAD1/5/8 By similarity. Could be involved in bone and cartilage formation. Chondrogenic signaling is mediated by the high-affinity receptor BMPR1B. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes.

Subunit structure

Homodimer; disulfide-linked By similarity. Interacts with serine proteases, HTRA1 and HTRA3 By similarity. Following LPS binding, may form a complex with CXCR4, HSP90AA1 and HSPA8. Ref.9

Subcellular location

Secreted. Cell membrane.

Tissue specificity

Predominantly expressed in long bones during embryonic development. Expressed in monocytes (at protein level).

Involvement in disease

Acromesomelic chondrodysplasia, Grebe type (AMDG) [MIM:200700]: An autosomal recessive acromesomelic chondrodysplasia. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers). AMDG is characterized by normal axial skeletons and missing or fused skeletal elements within the hands and feet.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

Acromesomelic chondrodysplasia, Hunter-Thompson type (AMDH) [MIM:201250]: An autosomal recessive form of dwarfism. Patients have limb abnormalities, with the middle and distal segments being most affected and the lower limbs more affected than the upper. AMDH is characterized by normal axial skeletons and missing or fused skeletal elements within the hands and feet.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Brachydactyly C (BDC) [MIM:113100]: A form of brachydactyly. Brachydactyly defines a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. Brachydactyly type C is characterized by deformity of the middle and proximal phalanges of the second and third fingers, sometimes with hypersegmentation of the proximal phalanx. The ring finger may be essentially normal and project beyond the others.
Note: The disease is caused by mutations affecting the gene represented in this entry. Some BDC patients with GDF5 mutations also manifest clinical features of ASPED angel-shaped phalango-epiphyseal dysplasia (ASPED), an autosomal dominant skeletal abnormality characterized by a typical angel-shaped phalanx, brachydactyly, specific radiological findings, abnormal dentition, hip dysplasia, and delayed bone age. This suggests that BDC and ASPED are part of the same clinical spectrum (Ref.8). Ref.8 Ref.13

Du Pan syndrome (DPS) [MIM:228900]: Rare autosomal recessive condition characterized by absence of the fibulae and severe acromesomelic limb shortening with small, non-functional toes. Although milder, the phenotype resembles the autosomal recessive Hunter-Thompson and Grebe types of acromesomelic chondrodysplasia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.14 Ref.19

Symphalangism, proximal 1B (SYM1B) [MIM:615298]: A disease characterized by the hereditary absence of the proximal interphalangeal joints. Distal interphalangeal joints are less frequently involved and metacarpophalangeal joints are rarely affected whereas carpal bone malformation and fusion are common. In the lower extremities, tarsal bone coalition is common. Conductive hearing loss is seen and is due to fusion of the stapes to the petrous part of the temporal bone.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.17 Ref.21

Multiple synostoses syndrome 2 (SYNS2) [MIM:610017]: A bone disease characterized by multiple progressive joint fusions that commonly involve proximal interphalangeal, tarsal-carpal, humeroradial and cervical spine joints. Additional features can include progressive conductive deafness and facial dysmorphism.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.16

Brachydactyly A2 (BDA2) [MIM:112600]: A form of brachydactyly. Brachydactyly defines a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. In brachydactyly type A2 shortening of the middle phalanges is confined to the index finger and the second toe, all other digits being more or less normal. Because of a rhomboid or triangular shape of the affected middle phalanx, the end of the second finger usually deviates radially.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.20

Osteoarthritis 5 (OS5) [MIM:612400]: A degenerative disease of the joints characterized by degradation of the hyaline articular cartilage and remodeling of the subchondral bone with sclerosis. Clinical symptoms include pain and joint stiffness often leading to significant disability and joint replacement.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Brachydactyly A1, C (BDA1C) [MIM:615072]: A form of brachydactyly type A1. Brachydactyly defines a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. Brachydactyly type A1 is characterized by middle phalanges of all the digits rudimentary or fused with the terminal phalanges. The proximal phalanges of the thumbs and big toes are short.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22

Sequence similarities

Belongs to the TGF-beta family.

Ontologies

Keywords
   Biological processChondrogenesis
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Dwarfism
   DomainSignal
   Molecular functionCytokine
Growth factor
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell-cell signaling

Traceable author statement PubMed 8589725. Source: ProtInc

chondrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

embryonic limb morphogenesis

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Traceable author statement. Source: Reactome

forelimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

growth

Inferred from electronic annotation. Source: InterPro

hindlimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of epithelial cell proliferation

Inferred from direct assay PubMed 9950587. Source: BHF-UCL

negative regulation of mesenchymal cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of chondrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta receptor signaling pathway

Traceable author statement Ref.2. Source: ProtInc

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiongrowth factor activity

Traceable author statement PubMed 8589725. Source: ProtInc

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Propeptide28 – 381354 Potential
PRO_0000033912
Chain382 – 501120Growth/differentiation factor 5
PRO_0000033913

Amino acid modifications

Glycosylation1891N-linked (GlcNAc...) Potential
Disulfide bond400 ↔ 466 Ref.9
Disulfide bond429 ↔ 498 Ref.9
Disulfide bond433 ↔ 500 Ref.9
Disulfide bond465Interchain By similarity

Natural variations

Natural variant1631R → G.
Corresponds to variant rs34534075 [ dbSNP | Ensembl ].
VAR_037977
Natural variant1731M → V in BDC. Ref.13
Corresponds to variant rs28936397 [ dbSNP | Ensembl ].
VAR_037978
Natural variant2761S → A. Ref.2 Ref.4
Corresponds to variant rs224331 [ dbSNP | Ensembl ].
VAR_026120
Natural variant3731L → R in SYM1B; the mature GDF5 protein is detected as the wild-type in the supernatant derived from the mutant transfected cells. Ref.21
VAR_054909
Natural variant3781R → Q in DPS. Ref.19
VAR_054910
Natural variant3801R → Q in BDA2; reduces activity; impairs processing. Ref.20
VAR_046743
Natural variant3991R → C in BDA1C; less effective than wild-type in stimulating chondrogenesis. Ref.22
VAR_064416
Natural variant4001C → Y in AMDG. Ref.10
VAR_017407
Natural variant4361P → T in DPS. Ref.19
VAR_054911
Natural variant4371Missing in DPS; located on the same allele as T-439 and L-440. Ref.14
VAR_037979
Natural variant4381R → L in SYNS2 and SYM1B; increased biological activity when compared to wild-type; normal binding to BMPR1B ectodomain but increased binding to that of BMPR1A. Ref.15 Ref.16
VAR_026545
Natural variant4391S → T in DPS; located on the same allele as L-437 del and L-440. Ref.14
VAR_037980
Natural variant4401H → L in DPS; located on the same allele as L-437 del and T-439. Ref.14
VAR_037981
Natural variant4411L → P in DPS and BDA2; the mutant is almost inactive; loss of binding to BMPR1A and BMPR1B ectodomains. Ref.12 Ref.15
Corresponds to variant rs28936683 [ dbSNP | Ensembl ].
VAR_017408
Natural variant4751S → N in SYNS2. Ref.10
VAR_037982
Natural variant4911E → K in SYM1B. Ref.17
VAR_037983

Experimental info

Sequence conflict381T → S in AAA57007. Ref.2
Sequence conflict254 – 2585APGGG → VPRSR in AAA57007. Ref.2
Sequence conflict3211A → T in AAA57007. Ref.2
Sequence conflict3841L → S in AAA57007. Ref.2

Secondary structure

........................... 501
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P43026 [UniParc].

Last modified January 23, 2002. Version 3.
Checksum: 37985F2D15C4F5EF

FASTA50155,411
        10         20         30         40         50         60 
MRLPKLLTFL LWYLAWLDLE FICTVLGAPD LGQRPQGTRP GLAKAEAKER PPLARNVFRP 

        70         80         90        100        110        120 
GGHSYGGGAT NANARAKGGT GQTGGLTQPK KDEPKKLPPR PGGPEPKPGH PPQTRQATAR 

       130        140        150        160        170        180 
TVTPKGQLPG GKAPPKAGSV PSSFLLKKAR EPGPPREPKE PFRPPPITPH EYMLSLYRTL 

       190        200        210        220        230        240 
SDADRKGGNS SVKLEAGLAN TITSFIDKGQ DDRGPVVRKQ RYVFDISALE KDGLLGAELR 

       250        260        270        280        290        300 
ILRKKPSDTA KPAAPGGGRA AQLKLSSCPS GRQPASLLDV RSVPGLDGSG WEVFDIWKLF 

       310        320        330        340        350        360 
RNFKNSAQLC LELEAWERGR AVDLRGLGFD RAARQVHEKA LFLVFGRTKK RDLFFNEIKA 

       370        380        390        400        410        420 
RSGQDDKTVY EYLFSQRRKR RAPLATRQGK RPSKNLKARC SRKALHVNFK DMGWDDWIIA 

       430        440        450        460        470        480 
PLEYEAFHCE GLCEFPLRSH LEPTNHAVIQ TLMNSMDPES TPPTCCVPTR LSPISILFID 

       490        500 
SANNVVYKQY EDMVVESCGC R 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of recombinant human growth/differentiation factor 5."
Hoetten G., Neidhardt H., Jacobowsky B., Pohl J.
Biochem. Biophys. Res. Commun. 204:646-652(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[2]"Cartilage-derived morphogenetic proteins. New members of the transforming growth factor-beta superfamily predominantly expressed in long bones during human embryonic development."
Chang S., Hoang B., Thomas J.T., Vukicevic S., Luyten F.P., Ryba N.J.P., Kozak C.A., Reddi A.H., Moos M.
J. Biol. Chem. 269:28227-28234(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-276.
Tissue: Articular cartilage.
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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], VARIANT ALA-276.
[5]"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: Brain.
[6]"A CD14-independent LPS receptor cluster."
Triantafilou K., Triantafilou M., Dedrick R.L.
Nat. Immunol. 2:338-345(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION AS LPS RECEPTOR, INTERACTION WITH CXCR4; HSP90AA1 AND HSPA8, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[7]"Cartilage-derived morphogenetic protein-1 promotes the differentiation of mesenchymal stem cells into chondrocytes."
Bai X., Xiao Z., Pan Y., Hu J., Pohl J., Wen J., Li L.
Biochem. Biophys. Res. Commun. 325:453-460(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"A novel mutation in CDMP1 causes brachydactyly type C with 'angel-shaped phalanx'. A genotype-phenotype correlation in the mutational spectrum."
Gutierrez-Amavizca B.E., Brambila-Tapia A.J., Juarez-Vazquez C.I., Holder-Espinasse M., Manouvrier-Hanu S., Escande F., Barros-Nunez P.
Eur. J. Med. Genet. 55:611-614(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN BDC.
[9]"Crystal structure analysis reveals a spring-loaded latch as molecular mechanism for GDF-5-type I receptor specificity."
Kotzsch A., Nickel J., Seher A., Sebald W., Muller T.D.
EMBO J. 28:937-947(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 387-501 IN COMPLEX WITH MOUSE BMPR1B, FUNCTION, DISULFIDE BONDS.
[10]"Disruption of human limb morphogenesis by a dominant negative mutation in CDMP1."
Thomas J.T., Kilpatrick M.W., Lin K., Erlacher L., Lembessis P., Costa T., Tsipouras P., Luyten F.P.
Nat. Genet. 17:58-64(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMDG TYR-400.
[11]"Multiple synostosis type 2 (SYNS2) maps to 20q11.2 and caused by a missense mutation in the growth/differentiation factor 5 (GDF5)."
Akarsu A.N., Rezaie T., Demirtas M., Farhud D.D., Sarfarazi M.
Am. J. Hum. Genet. 65:A281-A281(1999)
Cited for: VARIANT SYNS2 ASN-475.
[12]"Mutation in the cartilage-derived morphogenetic protein-1 (CDMP1) gene in a kindred affected with fibular hypoplasia and complex brachydactyly (DuPan syndrome)."
Faiyaz-Ul-Haque M., Ahmad W., Zaidi S.H.E., Haque S., Teebi A.S., Ahmad M., Cohn D.H., Tsui L.-C.
Clin. Genet. 61:454-458(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DPS PRO-441.
[13]"Brachydactyly type C caused by a homozygous missense mutation in the prodomain of CDMP1."
Schwabe G.C., Tuerkmen S., Leschik G., Palanduz S., Stoever B., Goecke T.O., Mundlos S.
Am. J. Med. Genet. A 124:356-363(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BDC VAL-173.
[14]"Du Pan syndrome phenotype caused by heterozygous pathogenic mutations in CDMP1 gene."
Szczaluba K., Hilbert K., Obersztyn E., Zabel B., Mazurczak T., Kozlowski K.
Am. J. Med. Genet. A 138:379-383(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DPS LEU-437 DEL; THR-439 AND LEU-440.
[15]"Activating and deactivating mutations in the receptor interaction site of GDF5 cause symphalangism or brachydactyly type A2."
Seemann P., Schwappacher R., Kjaer K.W., Krakow D., Lehmann K., Dawson K., Stricker S., Pohl J., Ploeger F., Staub E., Nickel J., Sebald W., Knaus P., Mundlos S.
J. Clin. Invest. 115:2373-2381(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SYM1B LEU-438, VARIANT BDA2 PRO-441, CHARACTERIZATION OF VARIANT SYM1B LEU-438, CHARACTERIZATION OF VARIANT BDA2 PRO-441.
[16]"GDF5 is a second locus for multiple-synostosis syndrome."
Dawson K., Seeman P., Sebald E., King L., Edwards M., Williams J. III, Mundlos S., Krakow D.
Am. J. Hum. Genet. 78:708-712(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SYNS2 LEU-438.
[17]"A novel mutation in GDF5 causes autosomal dominant symphalangism in two Chinese families."
Wang X., Xiao F., Yang Q., Liang B., Tang Z., Jiang L., Zhu Q., Chang W., Jiang J., Jiang C., Ren X., Liu J.-Y., Wang Q.K., Liu M.
Am. J. Med. Genet. A 140:1846-1853(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SYM1B LYS-491.
[18]"A functional polymorphism in the 5' UTR of GDF5 is associated with susceptibility to osteoarthritis."
Miyamoto Y., Mabuchi A., Shi D., Kubo T., Takatori Y., Saito S., Fujioka M., Sudo A., Uchida A., Yamamoto S., Ozaki K., Takigawa M., Tanaka T., Nakamura Y., Jiang Q., Ikegawa S.
Nat. Genet. 39:529-533(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO OSTEOARTHRITIS TYPE 5.
[19]"Compound heterozygosity for GDF5 in Du Pan type chondrodysplasia."
Douzgou S., Lehmann K., Mingarelli R., Mundlos S., Dallapiccola B.
Am. J. Med. Genet. A 146:2116-2121(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DPS GLN-378 AND THR-436.
[20]"Brachydactyly type A2 associated with a defect in proGDF5 processing."
Ploeger F., Seemann P., Schmidt-von Kegler M., Lehmann K., Seidel J., Kjaer K.W., Pohl J., Mundlos S.
Hum. Mol. Genet. 17:1222-1233(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BDA2 GLN-380, CHARACTERIZATION OF VARIANT BDA2 GLN-380.
[21]"Novel point mutations in GDF5 associated with two distinct limb malformations in Chinese: brachydactyly type C and proximal symphalangism."
Yang W., Cao L., Liu W., Jiang L., Sun M., Zhang D., Wang S., Lo W.H., Luo Y., Zhang X.
J. Hum. Genet. 53:368-374(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SYM1B ARG-373, CHARACTERIZATION OF VARIANT SYM1B ARG-373.
[22]"Mutations in GDF5 presenting as semidominant brachydactyly A1."
Byrnes A.M., Racacho L., Nikkel S.M., Xiao F., MacDonald H., Underhill T.M., Bulman D.E.
Hum. Mutat. 31:1155-1162(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BDA1C CYS-399, CHARACTERIZATION OF VARIANT BDA1C CYS-399.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X80915 Genomic DNA. Translation: CAA56874.1.
U13660 mRNA. Translation: AAA57007.1.
AL121586 Genomic DNA. Translation: CAB89416.1.
CH471077 Genomic DNA. Translation: EAW76208.1.
CH471077 Genomic DNA. Translation: EAW76209.1.
BC032495 mRNA. Translation: AAH32495.1.
PIRA55452.
JC2347.
RefSeqNP_000548.1. NM_000557.3.
UniGeneHs.1573.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WAQX-ray2.28A387-501[»]
2BHKX-ray2.40A382-501[»]
3EVSX-ray2.10B387-501[»]
3QB4X-ray2.28A/C387-501[»]
ProteinModelPortalP43026.
SMRP43026. Positions 398-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113839. 6 interactions.
DIPDIP-5823N.
IntActP43026. 3 interactions.
MINTMINT-7264433.
STRING9606.ENSP00000363489.

PTM databases

PhosphoSiteP43026.

Polymorphism databases

DMDM20141384.

Proteomic databases

PaxDbP43026.
PRIDEP43026.

Protocols and materials databases

DNASU8200.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374369; ENSP00000363489; ENSG00000125965.
ENST00000374372; ENSP00000363492; ENSG00000125965.
GeneID8200.
KEGGhsa:8200.
UCSCuc002xck.1. human.

Organism-specific databases

CTD8200.
GeneCardsGC20M034021.
HGNCHGNC:4220. GDF5.
HPAHPA015648.
MIM112600. phenotype.
113100. phenotype.
200700. phenotype.
201250. phenotype.
228900. phenotype.
601146. gene.
610017. phenotype.
612400. phenotype.
615072. phenotype.
615298. phenotype.
neXtProtNX_P43026.
Orphanet2098. Acromesomelic dysplasia, Grebe type.
968. Acromesomelic dysplasia, Hunter-Thomson type.
63442. Angel-shaped phalango-epiphyseal dysplasia.
93388. Brachydactyly type A1.
93396. Brachydactyly type A2.
93384. Brachydactyly type C.
2639. Fibular aplasia - complex brachydactyly.
3237. Multiple synostoses syndrome.
3250. Proximal symphalangism.
PharmGKBPA28635.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG317866.
HOGENOMHOG000231514.
HOVERGENHBG107938.
InParanoidP43026.
KOK04664.
OMADKGQDDR.
OrthoDBEOG7WMCK0.
PhylomeDBP43026.
TreeFamTF316134.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
SignaLinkP43026.

Gene expression databases

ArrayExpressP43026.
BgeeP43026.
CleanExHS_GDF5.
GenevestigatorP43026.

Family and domain databases

InterProIPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERPTHR11848. PTHR11848. 1 hit.
PfamPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
SMARTSM00204. TGFB. 1 hit.
[Graphical view]
PROSITEPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP43026.
GeneWikiGDF5.
GenomeRNAi8200.
NextBio30902.
PROP43026.
SOURCESearch...

Entry information

Entry nameGDF5_HUMAN
AccessionPrimary (citable) accession number: P43026
Secondary accession number(s): E1P5Q2, Q96SB1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2002
Last modified: April 16, 2014
This is version 153 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 20

Human chromosome 20: entries, gene names and cross-references to MIM