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P43026

- GDF5_HUMAN

UniProt

P43026 - GDF5_HUMAN

Protein

Growth/differentiation factor 5

Gene

GDF5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 3 (23 Jan 2002)
      Previous versions | rss
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    Functioni

    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.By similarity3 Publications

    GO - Molecular functioni

    1. growth factor activity Source: ProtInc
    2. protein binding Source: IntAct

    GO - Biological processi

    1. cell-cell signaling Source: ProtInc
    2. chondrocyte differentiation Source: Ensembl
    3. embryonic limb morphogenesis Source: Ensembl
    4. extracellular matrix organization Source: Reactome
    5. forelimb morphogenesis Source: Ensembl
    6. growth Source: InterPro
    7. hindlimb morphogenesis Source: Ensembl
    8. negative regulation of epithelial cell proliferation Source: BHF-UCL
    9. negative regulation of mesenchymal cell apoptotic process Source: Ensembl
    10. negative regulation of neuron apoptotic process Source: Ensembl
    11. positive regulation of chondrocyte differentiation Source: Ensembl
    12. positive regulation of neuron differentiation Source: Ensembl
    13. regulation of multicellular organism growth Source: Ensembl
    14. transforming growth factor beta receptor signaling pathway Source: ProtInc

    Keywords - Molecular functioni

    Cytokine, Growth factor

    Keywords - Biological processi

    Chondrogenesis

    Enzyme and pathway databases

    ReactomeiREACT_150331. Molecules associated with elastic fibres.
    SignaLinkiP43026.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:GDF5
    Synonyms:BMP14, CDMP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:4220. GDF5.

    Subcellular locationi

    Secreted 1 Publication. Cell membrane 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti400 – 4001C → Y in AMDG. 1 Publication
    VAR_017407
    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.2 Publications
    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 (PubMed:22828468).1 Publication
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti173 – 1731M → V in BDC. 1 Publication
    Corresponds to variant rs28936397 [ dbSNP | Ensembl ].
    VAR_037978
    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti378 – 3781R → Q in DPS. 1 Publication
    VAR_054910
    Natural varianti436 – 4361P → T in DPS. 1 Publication
    VAR_054911
    Natural varianti437 – 4371Missing in DPS; located on the same allele as T-439 and L-440. 1 Publication
    VAR_037979
    Natural varianti439 – 4391S → T in DPS; located on the same allele as L-437 del and L-440. 1 Publication
    VAR_037980
    Natural varianti440 – 4401H → L in DPS; located on the same allele as L-437 del and T-439. 1 Publication
    VAR_037981
    Natural varianti441 – 4411L → P in DPS and BDA2; the mutant is almost inactive; loss of binding to BMPR1A and BMPR1B ectodomains. 2 Publications
    Corresponds to variant rs28936683 [ dbSNP | Ensembl ].
    VAR_017408
    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti373 – 3731L → R in SYM1B; the mature GDF5 protein is detected as the wild-type in the supernatant derived from the mutant transfected cells. 1 Publication
    VAR_054909
    Natural varianti438 – 4381R → 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. 2 Publications
    VAR_026545
    Natural varianti491 – 4911E → K in SYM1B. 1 Publication
    VAR_037983
    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti438 – 4381R → 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. 2 Publications
    VAR_026545
    Natural varianti475 – 4751S → N in SYNS2. 1 Publication
    VAR_037982
    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti380 – 3801R → Q in BDA2; reduces activity; impairs processing. 1 Publication
    VAR_046743
    Natural varianti441 – 4411L → P in DPS and BDA2; the mutant is almost inactive; loss of binding to BMPR1A and BMPR1B ectodomains. 2 Publications
    Corresponds to variant rs28936683 [ dbSNP | Ensembl ].
    VAR_017408
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti399 – 3991R → C in BDA1C; less effective than wild-type in stimulating chondrogenesis. 1 Publication
    VAR_064416

    Keywords - Diseasei

    Disease mutation, Dwarfism

    Organism-specific databases

    MIMi112600. phenotype.
    113100. phenotype.
    200700. phenotype.
    201250. phenotype.
    228900. phenotype.
    610017. phenotype.
    612400. phenotype.
    615072. phenotype.
    615298. phenotype.
    Orphaneti2098. 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.
    PharmGKBiPA28635.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Propeptidei28 – 381354Sequence AnalysisPRO_0000033912Add
    BLAST
    Chaini382 – 501120Growth/differentiation factor 5PRO_0000033913Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi189 – 1891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi400 ↔ 4661 Publication
    Disulfide bondi429 ↔ 4981 Publication
    Disulfide bondi433 ↔ 5001 Publication
    Disulfide bondi465 – 465InterchainBy similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP43026.
    PRIDEiP43026.

    PTM databases

    PhosphoSiteiP43026.

    Expressioni

    Tissue specificityi

    Predominantly expressed in long bones during embryonic development. Expressed in monocytes (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP43026.
    BgeeiP43026.
    CleanExiHS_GDF5.
    GenevestigatoriP43026.

    Organism-specific databases

    HPAiHPA015648.

    Interactioni

    Subunit structurei

    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.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BMPR1AP368942EBI-8571476,EBI-1029237
    BMPR1BO002386EBI-8571476,EBI-7527193
    BMPR2Q138734EBI-8571476,EBI-527196

    Protein-protein interaction databases

    BioGridi113839. 6 interactions.
    DIPiDIP-5823N.
    IntActiP43026. 3 interactions.
    MINTiMINT-7264433.
    STRINGi9606.ENSP00000363489.

    Structurei

    Secondary structure

    1
    501
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi399 – 4035
    Beta strandi406 – 4083
    Helixi410 – 4123
    Helixi414 – 4163
    Beta strandi418 – 4203
    Beta strandi422 – 4254
    Beta strandi428 – 4325
    Helixi439 – 4413
    Helixi445 – 45612
    Turni458 – 4603
    Beta strandi466 – 47914
    Beta strandi481 – 4833
    Beta strandi485 – 50016

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WAQX-ray2.28A387-501[»]
    2BHKX-ray2.40A382-501[»]
    3EVSX-ray2.10B387-501[»]
    3QB4X-ray2.28A/C387-501[»]
    ProteinModelPortaliP43026.
    SMRiP43026. Positions 398-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP43026.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TGF-beta family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG317866.
    HOGENOMiHOG000231514.
    HOVERGENiHBG107938.
    InParanoidiP43026.
    KOiK04664.
    OMAiPITPHEY.
    OrthoDBiEOG7WMCK0.
    PhylomeDBiP43026.
    TreeFamiTF316134.

    Family and domain databases

    Gene3Di2.10.90.10. 1 hit.
    InterProiIPR029034. Cystine-knot_cytokine.
    IPR001839. TGF-b_C.
    IPR001111. TGF-b_N.
    IPR015615. TGF-beta-rel.
    IPR017948. TGFb_CS.
    [Graphical view]
    PANTHERiPTHR11848. PTHR11848. 1 hit.
    PfamiPF00019. TGF_beta. 1 hit.
    PF00688. TGFb_propeptide. 1 hit.
    [Graphical view]
    SMARTiSM00204. TGFB. 1 hit.
    [Graphical view]
    SUPFAMiSSF57501. SSF57501. 1 hit.
    PROSITEiPS00250. TGF_BETA_1. 1 hit.
    PS51362. TGF_BETA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P43026-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRLPKLLTFL LWYLAWLDLE FICTVLGAPD LGQRPQGTRP GLAKAEAKER    50
    PPLARNVFRP GGHSYGGGAT NANARAKGGT GQTGGLTQPK KDEPKKLPPR 100
    PGGPEPKPGH PPQTRQATAR TVTPKGQLPG GKAPPKAGSV PSSFLLKKAR 150
    EPGPPREPKE PFRPPPITPH EYMLSLYRTL SDADRKGGNS SVKLEAGLAN 200
    TITSFIDKGQ DDRGPVVRKQ RYVFDISALE KDGLLGAELR ILRKKPSDTA 250
    KPAAPGGGRA AQLKLSSCPS GRQPASLLDV RSVPGLDGSG WEVFDIWKLF 300
    RNFKNSAQLC LELEAWERGR AVDLRGLGFD RAARQVHEKA LFLVFGRTKK 350
    RDLFFNEIKA RSGQDDKTVY EYLFSQRRKR RAPLATRQGK RPSKNLKARC 400
    SRKALHVNFK DMGWDDWIIA PLEYEAFHCE GLCEFPLRSH LEPTNHAVIQ 450
    TLMNSMDPES TPPTCCVPTR LSPISILFID SANNVVYKQY EDMVVESCGC 500
    R 501
    Length:501
    Mass (Da):55,411
    Last modified:January 23, 2002 - v3
    Checksum:i37985F2D15C4F5EF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 381T → S in AAA57007. (PubMed:7961761)Curated
    Sequence conflicti254 – 2585APGGG → VPRSR in AAA57007. (PubMed:7961761)Curated
    Sequence conflicti321 – 3211A → T in AAA57007. (PubMed:7961761)Curated
    Sequence conflicti384 – 3841L → S in AAA57007. (PubMed:7961761)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti163 – 1631R → G.
    Corresponds to variant rs34534075 [ dbSNP | Ensembl ].
    VAR_037977
    Natural varianti173 – 1731M → V in BDC. 1 Publication
    Corresponds to variant rs28936397 [ dbSNP | Ensembl ].
    VAR_037978
    Natural varianti276 – 2761S → A.2 Publications
    Corresponds to variant rs224331 [ dbSNP | Ensembl ].
    VAR_026120
    Natural varianti373 – 3731L → R in SYM1B; the mature GDF5 protein is detected as the wild-type in the supernatant derived from the mutant transfected cells. 1 Publication
    VAR_054909
    Natural varianti378 – 3781R → Q in DPS. 1 Publication
    VAR_054910
    Natural varianti380 – 3801R → Q in BDA2; reduces activity; impairs processing. 1 Publication
    VAR_046743
    Natural varianti399 – 3991R → C in BDA1C; less effective than wild-type in stimulating chondrogenesis. 1 Publication
    VAR_064416
    Natural varianti400 – 4001C → Y in AMDG. 1 Publication
    VAR_017407
    Natural varianti436 – 4361P → T in DPS. 1 Publication
    VAR_054911
    Natural varianti437 – 4371Missing in DPS; located on the same allele as T-439 and L-440. 1 Publication
    VAR_037979
    Natural varianti438 – 4381R → 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. 2 Publications
    VAR_026545
    Natural varianti439 – 4391S → T in DPS; located on the same allele as L-437 del and L-440. 1 Publication
    VAR_037980
    Natural varianti440 – 4401H → L in DPS; located on the same allele as L-437 del and T-439. 1 Publication
    VAR_037981
    Natural varianti441 – 4411L → P in DPS and BDA2; the mutant is almost inactive; loss of binding to BMPR1A and BMPR1B ectodomains. 2 Publications
    Corresponds to variant rs28936683 [ dbSNP | Ensembl ].
    VAR_017408
    Natural varianti475 – 4751S → N in SYNS2. 1 Publication
    VAR_037982
    Natural varianti491 – 4911E → K in SYM1B. 1 Publication
    VAR_037983

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS13254.1.
    PIRiA55452.
    JC2347.
    RefSeqiNP_000548.2. NM_000557.4.
    UniGeneiHs.1573.

    Genome annotation databases

    EnsembliENST00000374369; ENSP00000363489; ENSG00000125965.
    ENST00000374372; ENSP00000363492; ENSG00000125965.
    GeneIDi8200.
    KEGGihsa:8200.
    UCSCiuc002xck.1. human.

    Polymorphism databases

    DMDMi20141384.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    GDF5 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS13254.1.
    PIRi A55452.
    JC2347.
    RefSeqi NP_000548.2. NM_000557.4.
    UniGenei Hs.1573.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WAQ X-ray 2.28 A 387-501 [» ]
    2BHK X-ray 2.40 A 382-501 [» ]
    3EVS X-ray 2.10 B 387-501 [» ]
    3QB4 X-ray 2.28 A/C 387-501 [» ]
    ProteinModelPortali P43026.
    SMRi P43026. Positions 398-501.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113839. 6 interactions.
    DIPi DIP-5823N.
    IntActi P43026. 3 interactions.
    MINTi MINT-7264433.
    STRINGi 9606.ENSP00000363489.

    PTM databases

    PhosphoSitei P43026.

    Polymorphism databases

    DMDMi 20141384.

    Proteomic databases

    PaxDbi P43026.
    PRIDEi P43026.

    Protocols and materials databases

    DNASUi 8200.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374369 ; ENSP00000363489 ; ENSG00000125965 .
    ENST00000374372 ; ENSP00000363492 ; ENSG00000125965 .
    GeneIDi 8200.
    KEGGi hsa:8200.
    UCSCi uc002xck.1. human.

    Organism-specific databases

    CTDi 8200.
    GeneCardsi GC20M034021.
    HGNCi HGNC:4220. GDF5.
    HPAi HPA015648.
    MIMi 112600. phenotype.
    113100. phenotype.
    200700. phenotype.
    201250. phenotype.
    228900. phenotype.
    601146. gene.
    610017. phenotype.
    612400. phenotype.
    615072. phenotype.
    615298. phenotype.
    neXtProti NX_P43026.
    Orphaneti 2098. 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.
    PharmGKBi PA28635.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG317866.
    HOGENOMi HOG000231514.
    HOVERGENi HBG107938.
    InParanoidi P43026.
    KOi K04664.
    OMAi PITPHEY.
    OrthoDBi EOG7WMCK0.
    PhylomeDBi P43026.
    TreeFami TF316134.

    Enzyme and pathway databases

    Reactomei REACT_150331. Molecules associated with elastic fibres.
    SignaLinki P43026.

    Miscellaneous databases

    EvolutionaryTracei P43026.
    GeneWikii GDF5.
    GenomeRNAii 8200.
    NextBioi 30902.
    PROi P43026.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P43026.
    Bgeei P43026.
    CleanExi HS_GDF5.
    Genevestigatori P43026.

    Family and domain databases

    Gene3Di 2.10.90.10. 1 hit.
    InterProi IPR029034. Cystine-knot_cytokine.
    IPR001839. TGF-b_C.
    IPR001111. TGF-b_N.
    IPR015615. TGF-beta-rel.
    IPR017948. TGFb_CS.
    [Graphical view ]
    PANTHERi PTHR11848. PTHR11848. 1 hit.
    Pfami PF00019. TGF_beta. 1 hit.
    PF00688. TGFb_propeptide. 1 hit.
    [Graphical view ]
    SMARTi SM00204. TGFB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57501. SSF57501. 1 hit.
    PROSITEi PS00250. TGF_BETA_1. 1 hit.
    PS51362. TGF_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. 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. 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. Cited for: VARIANT BDA1C CYS-399, CHARACTERIZATION OF VARIANT BDA1C CYS-399.

    Entry informationi

    Entry nameiGDF5_HUMAN
    AccessioniPrimary (citable) accession number: P43026
    Secondary accession number(s): E1P5Q2, Q96SB1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 157 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3