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P13497

- BMP1_HUMAN

UniProt

P13497 - BMP1_HUMAN

Protein

Bone morphogenetic protein 1

Gene

BMP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (21 Feb 2001)
      Previous versions | rss
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    Functioni

    Cleaves the C-terminal propeptides of procollagen I, II and III. Induces cartilage and bone formation. May participate in dorsoventral patterning during early development by cleaving chordin (CHRD). Responsible for the proteolytic activation of lysyl oxidase LOX.

    Catalytic activityi

    Cleavage of the C-terminal propeptide at Ala-|-Asp in type I and II procollagens and at Arg-|-Asp in type III.

    Cofactori

    Binds 1 zinc ion per subunit.1 Publication

    Enzyme regulationi

    Activity is increased by the procollagen C-endopeptidase enhancer protein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi213 – 2131Zinc; catalytic
    Active sitei214 – 21411 PublicationPROSITE-ProRule annotation
    Metal bindingi217 – 2171Zinc; catalytic
    Metal bindingi223 – 2231Zinc; catalytic

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. metalloendopeptidase activity Source: Reactome
    3. metallopeptidase activity Source: UniProtKB
    4. peptidase activity Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cartilage condensation Source: ProtInc
    2. cell differentiation Source: UniProtKB-KW
    3. extracellular matrix disassembly Source: Reactome
    4. extracellular matrix organization Source: Reactome
    5. lipoprotein metabolic process Source: Reactome
    6. multicellular organismal development Source: ProtInc
    7. ossification Source: UniProtKB-KW
    8. positive regulation of cartilage development Source: MGI
    9. proteolysis Source: UniProtKB
    10. skeletal system development Source: UniProtKB
    11. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Cytokine, Developmental protein, Growth factor, Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Chondrogenesis, Differentiation, Osteogenesis

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.4.24.19. 2681.
    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_13621. HDL-mediated lipid transport.
    REACT_150206. Crosslinking of collagen fibrils.
    REACT_150268. Anchoring fibril formation.

    Protein family/group databases

    MEROPSiM12.005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bone morphogenetic protein 1 (EC:3.4.24.19)
    Short name:
    BMP-1
    Alternative name(s):
    Mammalian tolloid protein
    Short name:
    mTld
    Procollagen C-proteinase
    Short name:
    PCP
    Gene namesi
    Name:BMP1
    Synonyms:PCOLC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:1067. BMP1.

    Subcellular locationi

    Golgi apparatustrans-Golgi network 1 Publication. Secretedextracellular spaceextracellular matrix 1 Publication
    Note: Co-localizes with POSTN in the Golgi.By similarity

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: UniProtKB-KW
    3. Golgi apparatus Source: UniProtKB-SubCell
    4. membrane-bounded vesicle Source: Ensembl
    5. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Golgi apparatus, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Osteogenesis imperfecta 13 (OI13) [MIM:614856]: An autosomal recessive form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI13 is characterized by normal teeth, faint blue sclerae, severe growth deficiency, borderline osteoporosis, severe bone deformity, and recurrent fractures affecting both upper and lower limbs.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121G → R in OI13; the mutation leads to severely reduced post-translational N-glycosylation of the protein and impairs protein secretion; leads to both reduced secretion and subsequent reduced processing of the substrates CHRD and COL1A1. 1 Publication
    Corresponds to variant rs318240762 [ dbSNP | Ensembl ].
    VAR_069096
    Natural varianti249 – 2491F → L in OI13; leads to a protein with deficient procollagen I C-terminal propeptide proteolytic activity. 1 Publication
    VAR_067224

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi119 – 1202RR → AA: Doesn't abolish secretion. 1 Publication

    Keywords - Diseasei

    Disease mutation, Osteogenesis imperfecta

    Organism-specific databases

    MIMi614856. phenotype.
    Orphaneti216812. Osteogenesis imperfecta type 3.
    PharmGKBiPA25377.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Propeptidei23 – 12098Sequence AnalysisPRO_0000028889Add
    BLAST
    Chaini121 – 986866Bone morphogenetic protein 1PRO_0000028890Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi91 – 911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi163 ↔ 319
    Disulfide bondi183 ↔ 205
    Disulfide bondi185 ↔ 186
    Disulfide bondi322 ↔ 348By similarity
    Glycosylationi332 – 3321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi375 ↔ 397By similarity
    Disulfide bondi435 ↔ 461By similarity
    Disulfide bondi488 ↔ 510By similarity
    Disulfide bondi551 ↔ 563By similarity
    Disulfide bondi559 ↔ 572By similarity
    Disulfide bondi574 ↔ 587By similarity
    Disulfide bondi591 ↔ 617By similarity
    Glycosylationi599 – 5991N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi644 ↔ 666By similarity
    Disulfide bondi707 ↔ 718By similarity
    Disulfide bondi714 ↔ 727By similarity
    Disulfide bondi729 ↔ 742By similarity
    Disulfide bondi747 ↔ 773By similarity
    Disulfide bondi800 ↔ 822By similarity
    Disulfide bondi860 ↔ 890By similarity
    Disulfide bondi917 ↔ 939By similarity

    Post-translational modificationi

    Proteolytically activated in the trans-Golgi network by furin-like/paired basic proprotein convertases, cleavage is not required for secretion.1 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP13497.
    PaxDbiP13497.
    PeptideAtlasiP13497.
    PRIDEiP13497.

    PTM databases

    PhosphoSiteiP13497.

    Miscellaneous databases

    PMAP-CutDBP13497.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiP13497.
    BgeeiP13497.
    CleanExiHS_BMP1.
    GenevestigatoriP13497.

    Organism-specific databases

    HPAiHPA014572.

    Interactioni

    Subunit structurei

    Interacts with POSTN, the interaction promotes deposition on the extracellular matrix.By similarity

    Protein-protein interaction databases

    BioGridi107117. 3 interactions.
    DIPiDIP-33403N.
    IntActiP13497. 6 interactions.
    MINTiMINT-1394084.
    STRINGi9606.ENSP00000305714.

    Structurei

    Secondary structure

    1
    986
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi126 – 1283
    Helixi131 – 1333
    Beta strandi134 – 1396
    Helixi145 – 16117
    Beta strandi165 – 1684
    Beta strandi173 – 1808
    Beta strandi194 – 2018
    Helixi203 – 2053
    Helixi208 – 21912
    Helixi224 – 2263
    Helixi230 – 2323
    Beta strandi234 – 2363
    Helixi238 – 2403
    Helixi246 – 2494
    Helixi254 – 2563
    Turni274 – 2774
    Beta strandi278 – 2803
    Beta strandi285 – 2906
    Helixi307 – 31610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EDGX-ray1.27A121-321[»]
    3EDHX-ray1.25A121-321[»]
    ProteinModelPortaliP13497.
    SMRiP13497. Positions 121-976.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13497.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini322 – 434113CUB 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini435 – 546112CUB 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini547 – 58842EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini591 – 703113CUB 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini704 – 74340EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini747 – 859113CUB 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini860 – 976117CUB 5PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni121 – 321201MetalloproteaseAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M12A family.Curated
    Contains 5 CUB domains.PROSITE-ProRule annotation
    Contains 2 EGF-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG70307.
    HOVERGENiHBG004859.
    InParanoidiP13497.
    KOiK05502.
    OMAiGRFCGGK.
    OrthoDBiEOG7N8ZTV.
    PhylomeDBiP13497.
    TreeFamiTF314351.

    Family and domain databases

    Gene3Di2.60.120.290. 5 hits.
    3.40.390.10. 1 hit.
    InterProiIPR015446. BMP_1/tolloid-like.
    IPR000859. CUB_dom.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR024079. MetalloPept_cat_dom.
    IPR001506. Peptidase_M12A.
    IPR006026. Peptidase_Metallo.
    [Graphical view]
    PfamiPF01400. Astacin. 1 hit.
    PF00431. CUB. 5 hits.
    PF07645. EGF_CA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001199. BMP_1/tolloid-like. 1 hit.
    PRINTSiPR00480. ASTACIN.
    SMARTiSM00042. CUB. 5 hits.
    SM00179. EGF_CA. 2 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49854. SSF49854. 5 hits.
    SSF57184. SSF57184. 2 hits.
    PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
    PS01180. CUB. 5 hits.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 2 hits.
    PS01187. EGF_CA. 2 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

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

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform BMP1-3 (identifier: P13497-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MPGVARLPLL LGLLLLPRPG RPLDLADYTY DLAEEDDSEP LNYKDPCKAA    50
    AFLGDIALDE EDLRAFQVQQ AVDLRRHTAR KSSIKAAVPG NTSTPSCQST 100
    NGQPQRGACG RWRGRSRSRR AATSRPERVW PDGVIPFVIG GNFTGSQRAV 150
    FRQAMRHWEK HTCVTFLERT DEDSYIVFTY RPCGCCSYVG RRGGGPQAIS 200
    IGKNCDKFGI VVHELGHVVG FWHEHTRPDR DRHVSIVREN IQPGQEYNFL 250
    KMEPQEVESL GETYDFDSIM HYARNTFSRG IFLDTIVPKY EVNGVKPPIG 300
    QRTRLSKGDI AQARKLYKCP ACGETLQDST GNFSSPEYPN GYSAHMHCVW 350
    RISVTPGEKI ILNFTSLDLY RSRLCWYDYV EVRDGFWRKA PLRGRFCGSK 400
    LPEPIVSTDS RLWVEFRSSS NWVGKGFFAV YEAICGGDVK KDYGHIQSPN 450
    YPDDYRPSKV CIWRIQVSEG FHVGLTFQSF EIERHDSCAY DYLEVRDGHS 500
    ESSTLIGRYC GYEKPDDIKS TSSRLWLKFV SDGSINKAGF AVNFFKEVDE 550
    CSRPNRGGCE QRCLNTLGSY KCSCDPGYEL APDKRRCEAA CGGFLTKLNG 600
    SITSPGWPKE YPPNKNCIWQ LVAPTQYRIS LQFDFFETEG NDVCKYDFVE 650
    VRSGLTADSK LHGKFCGSEK PEVITSQYNN MRVEFKSDNT VSKKGFKAHF 700
    FSDKDECSKD NGGCQQDCVN TFGSYECQCR SGFVLHDNKH DCKEAGCDHK 750
    VTSTSGTITS PNWPDKYPSK KECTWAISST PGHRVKLTFM EMDIESQPEC 800
    AYDHLEVFDG RDAKAPVLGR FCGSKKPEPV LATGSRMFLR FYSDNSVQRK 850
    GFQASHATEC GGQVRADVKT KDLYSHAQFG DNNYPGGVDC EWVIVAEEGY 900
    GVELVFQTFE VEEETDCGYD YMELFDGYDS TAPRLGRYCG SGPPEEVYSA 950
    GDSVLVKFHS DDTITKKGFH LRYTSTKFQD TLHSRK 986
    Length:986
    Mass (Da):111,249
    Last modified:February 21, 2001 - v2
    Checksum:iF89201913AC3CBEA
    GO
    Isoform BMP1-1 (identifier: P13497-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         703-730: DKDECSKDNGGCQQDCVNTFGSYECQCR → EKRPALQPPRGRPHQLKFRVQKRNRTPQ
         731-986: Missing.

    Show »
    Length:730
    Mass (Da):82,900
    Checksum:iE506D63729A9E86D
    GO
    Isoform BMP1-2 (identifier: P13497-7)

    Sequence is not available
    Length:
    Mass (Da):
    Isoform BMP1-4 (identifier: P13497-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         245-302: QEYNFLKMEP...NGVKPPIGQR → VLHSSLLLLS...AAPRTLRAGV
         303-986: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:302
    Mass (Da):33,424
    Checksum:i9FCDE92B1F884B15
    GO
    Isoform BMP1-5 (identifier: P13497-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         589-622: AACGGFLTKLNGSITSPGWPKEYPPNKNCIWQLV → GCYDLQVGKPLLWDRHCFRLSTHGPEMLGTALRG
         623-986: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:622
    Mass (Da):70,469
    Checksum:iA47CE9FD49D5A8D7
    GO
    Isoform BMP1-6 (identifier: P13497-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         703-717: DKDECSKDNGGCQQD → GGELFGLLGHPPRRP
         718-986: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:717
    Mass (Da):81,082
    Checksum:iAE07361E00A6A700
    GO
    Isoform BMP1-7 (identifier: P13497-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         703-823: DKDECSKDNG...KAPVLGRFCG → VLEGAGDRHS...PATFRGIWAL
         824-986: Missing.

    Show »
    Length:823
    Mass (Da):92,655
    Checksum:i09148B0724B5F1A8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti748 – 7481D → N in AAC41710. (PubMed:7798260)Curated
    Sequence conflicti934 – 9341R → S in AAC41710. (PubMed:7798260)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121G → R in OI13; the mutation leads to severely reduced post-translational N-glycosylation of the protein and impairs protein secretion; leads to both reduced secretion and subsequent reduced processing of the substrates CHRD and COL1A1. 1 Publication
    Corresponds to variant rs318240762 [ dbSNP | Ensembl ].
    VAR_069096
    Natural varianti45 – 451D → H in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036141
    Natural varianti249 – 2491F → L in OI13; leads to a protein with deficient procollagen I C-terminal propeptide proteolytic activity. 1 Publication
    VAR_067224
    Natural varianti719 – 7191V → I.
    Corresponds to variant rs11996036 [ dbSNP | Ensembl ].
    VAR_051584

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei245 – 30258QEYNF…PIGQR → VLHSSLLLLSCGSRNGASFP CSLESSTHQALCWTGLFLRP SPFPRLPLAAPRTLRAGV in isoform BMP1-4. 1 PublicationVSP_005463Add
    BLAST
    Alternative sequencei303 – 986684Missing in isoform BMP1-4. 1 PublicationVSP_005464Add
    BLAST
    Alternative sequencei589 – 62234AACGG…IWQLV → GCYDLQVGKPLLWDRHCFRL STHGPEMLGTALRG in isoform BMP1-5. 2 PublicationsVSP_005465Add
    BLAST
    Alternative sequencei623 – 986364Missing in isoform BMP1-5. 2 PublicationsVSP_005466Add
    BLAST
    Alternative sequencei703 – 823121DKDEC…GRFCG → VLEGAGDRHSHLSGLELLLC PHALVDTVPAPPSALHGDTH AHTHTHVHTHCPIAQETCRG PPLGASRLSPQGPGHLTLAP QEGSYLDFWDTHRGDPKPRR RRKSLKTFSLTPATFRGIWA L in isoform BMP1-7. CuratedVSP_005469Add
    BLAST
    Alternative sequencei703 – 73028DKDEC…ECQCR → EKRPALQPPRGRPHQLKFRV QKRNRTPQ in isoform BMP1-1. 1 PublicationVSP_005461Add
    BLAST
    Alternative sequencei703 – 71715DKDEC…GCQQD → GGELFGLLGHPPRRP in isoform BMP1-6. 1 PublicationVSP_005467Add
    BLAST
    Alternative sequencei718 – 986269Missing in isoform BMP1-6. 1 PublicationVSP_005468Add
    BLAST
    Alternative sequencei731 – 986256Missing in isoform BMP1-1. 1 PublicationVSP_005462Add
    BLAST
    Alternative sequencei824 – 986163Missing in isoform BMP1-7. CuratedVSP_005470Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50330 mRNA. Translation: AAA93462.1.
    M22488 mRNA. Translation: AAA51833.1.
    Y08723 mRNA. Translation: CAA69973.1.
    Y08724 mRNA. Translation: CAA69974.1.
    Y08725 mRNA. Translation: CAA69975.1.
    L35278 mRNA. Translation: AAC41703.1.
    L35279 mRNA. Translation: AAC41710.1.
    AK291620 mRNA. Translation: BAF84309.1.
    CH471080 Genomic DNA. Translation: EAW63698.1.
    CH471080 Genomic DNA. Translation: EAW63703.1.
    CH471080 Genomic DNA. Translation: EAW63704.1.
    BC136679 mRNA. Translation: AAI36680.1.
    CCDSiCCDS34856.1. [P13497-2]
    CCDS6026.1. [P13497-1]
    PIRiA37278. BMHU1.
    A58788.
    B58788.
    RefSeqiNP_001190.1. NM_001199.3. [P13497-2]
    NP_006120.1. NM_006129.4. [P13497-1]
    UniGeneiHs.1274.

    Genome annotation databases

    EnsembliENST00000306349; ENSP00000306121; ENSG00000168487. [P13497-2]
    ENST00000306385; ENSP00000305714; ENSG00000168487. [P13497-1]
    ENST00000397814; ENSP00000380915; ENSG00000168487. [P13497-4]
    ENST00000471755; ENSP00000428665; ENSG00000168487. [P13497-4]
    ENST00000520970; ENSP00000428332; ENSG00000168487. [P13497-2]
    ENST00000521385; ENSP00000430406; ENSG00000168487. [P13497-5]
    GeneIDi649.
    KEGGihsa:649.
    UCSCiuc003xbb.3. human. [P13497-2]
    uc003xbg.3. human. [P13497-1]

    Polymorphism databases

    DMDMi13124688.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50330 mRNA. Translation: AAA93462.1 .
    M22488 mRNA. Translation: AAA51833.1 .
    Y08723 mRNA. Translation: CAA69973.1 .
    Y08724 mRNA. Translation: CAA69974.1 .
    Y08725 mRNA. Translation: CAA69975.1 .
    L35278 mRNA. Translation: AAC41703.1 .
    L35279 mRNA. Translation: AAC41710.1 .
    AK291620 mRNA. Translation: BAF84309.1 .
    CH471080 Genomic DNA. Translation: EAW63698.1 .
    CH471080 Genomic DNA. Translation: EAW63703.1 .
    CH471080 Genomic DNA. Translation: EAW63704.1 .
    BC136679 mRNA. Translation: AAI36680.1 .
    CCDSi CCDS34856.1. [P13497-2 ]
    CCDS6026.1. [P13497-1 ]
    PIRi A37278. BMHU1.
    A58788.
    B58788.
    RefSeqi NP_001190.1. NM_001199.3. [P13497-2 ]
    NP_006120.1. NM_006129.4. [P13497-1 ]
    UniGenei Hs.1274.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EDG X-ray 1.27 A 121-321 [» ]
    3EDH X-ray 1.25 A 121-321 [» ]
    ProteinModelPortali P13497.
    SMRi P13497. Positions 121-976.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107117. 3 interactions.
    DIPi DIP-33403N.
    IntActi P13497. 6 interactions.
    MINTi MINT-1394084.
    STRINGi 9606.ENSP00000305714.

    Chemistry

    BindingDBi P13497.
    ChEMBLi CHEMBL3898.

    Protein family/group databases

    MEROPSi M12.005.

    PTM databases

    PhosphoSitei P13497.

    Polymorphism databases

    DMDMi 13124688.

    Proteomic databases

    MaxQBi P13497.
    PaxDbi P13497.
    PeptideAtlasi P13497.
    PRIDEi P13497.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000306349 ; ENSP00000306121 ; ENSG00000168487 . [P13497-2 ]
    ENST00000306385 ; ENSP00000305714 ; ENSG00000168487 . [P13497-1 ]
    ENST00000397814 ; ENSP00000380915 ; ENSG00000168487 . [P13497-4 ]
    ENST00000471755 ; ENSP00000428665 ; ENSG00000168487 . [P13497-4 ]
    ENST00000520970 ; ENSP00000428332 ; ENSG00000168487 . [P13497-2 ]
    ENST00000521385 ; ENSP00000430406 ; ENSG00000168487 . [P13497-5 ]
    GeneIDi 649.
    KEGGi hsa:649.
    UCSCi uc003xbb.3. human. [P13497-2 ]
    uc003xbg.3. human. [P13497-1 ]

    Organism-specific databases

    CTDi 649.
    GeneCardsi GC08P022022.
    HGNCi HGNC:1067. BMP1.
    HPAi HPA014572.
    MIMi 112264. gene.
    614856. phenotype.
    neXtProti NX_P13497.
    Orphaneti 216812. Osteogenesis imperfecta type 3.
    PharmGKBi PA25377.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG70307.
    HOVERGENi HBG004859.
    InParanoidi P13497.
    KOi K05502.
    OMAi GRFCGGK.
    OrthoDBi EOG7N8ZTV.
    PhylomeDBi P13497.
    TreeFami TF314351.

    Enzyme and pathway databases

    BRENDAi 3.4.24.19. 2681.
    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_13621. HDL-mediated lipid transport.
    REACT_150206. Crosslinking of collagen fibrils.
    REACT_150268. Anchoring fibril formation.

    Miscellaneous databases

    ChiTaRSi BMP1. human.
    EvolutionaryTracei P13497.
    GeneWikii Bone_morphogenetic_protein_1.
    GenomeRNAii 649.
    NextBioi 2632.
    PMAP-CutDB P13497.
    PROi P13497.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13497.
    Bgeei P13497.
    CleanExi HS_BMP1.
    Genevestigatori P13497.

    Family and domain databases

    Gene3Di 2.60.120.290. 5 hits.
    3.40.390.10. 1 hit.
    InterProi IPR015446. BMP_1/tolloid-like.
    IPR000859. CUB_dom.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR024079. MetalloPept_cat_dom.
    IPR001506. Peptidase_M12A.
    IPR006026. Peptidase_Metallo.
    [Graphical view ]
    Pfami PF01400. Astacin. 1 hit.
    PF00431. CUB. 5 hits.
    PF07645. EGF_CA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001199. BMP_1/tolloid-like. 1 hit.
    PRINTSi PR00480. ASTACIN.
    SMARTi SM00042. CUB. 5 hits.
    SM00179. EGF_CA. 2 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49854. SSF49854. 5 hits.
    SSF57184. SSF57184. 2 hits.
    PROSITEi PS00010. ASX_HYDROXYL. 2 hits.
    PS01180. CUB. 5 hits.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 2 hits.
    PS01187. EGF_CA. 2 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1."
      Li S.W., Sieron A.L., Fertala A., Hojima Y., Arnold W.V., Prockop D.J.
      Proc. Natl. Acad. Sci. U.S.A. 93:5127-5130(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BMP1-3).
      Tissue: Skin.
    2. "Novel regulators of bone formation: molecular clones and activities."
      Wozney J.M., Rosen V., Celeste A.J., Mitsock L.M., Whitters M.J., Kriz R.W., Hewick R.M., Wang E.A.
      Science 242:1528-1534(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BMP1-1).
    3. "Three alternatively spliced variants of the gene coding for the human bone morphogenetic protein-1."
      Janitz M., Heiser V., Boettcher U., Landt O., Lauster R.
      J. Mol. Med. 76:141-146(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BMP1-4; BMP1-5 AND BMP1-6).
      Tissue: Placenta.
    4. "Bone morphogenetic protein-1 and a mammalian tolloid homologue (mTld) are encoded by alternatively spliced transcripts which are differentially expressed in some tissues."
      Takahara K., Lyons G.E., Greenspan D.S.
      J. Biol. Chem. 269:32572-32578(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BMP1-3 AND BMP1-7).
      Tissue: Placenta.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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.
      , 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 BMP1-5).
      Tissue: Placenta.
    7. "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] (ISOFORM BMP1-3).
      Tissue: Brain.
    8. "Identification of amino acid residues in bone morphogenetic protein-1 important for procollagen C-proteinase activity."
      Garrigue-Antar L., Barker C., Kadler K.E.
      J. Biol. Chem. 276:26237-26242(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BOND AT 183-CYS--CYS-186.
    9. "Paired basic/Furin-like proprotein convertase cleavage of Pro-BMP-1 in the trans-Golgi network."
      Leighton M., Kadler K.E.
      J. Biol. Chem. 278:18478-18484(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, MUTAGENESIS OF 119-ARG--ARG-120.
    10. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    11. "Structural basis for the substrate specificity of bone morphogenetic protein 1/tolloid-like metalloproteases."
      Mac Sweeney A., Gil-Parrado S., Vinzenz D., Bernardi A., Hein A., Bodendorf U., Erbel P., Logel C., Gerhartz B.
      J. Mol. Biol. 384:228-239(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 121-321, ZINC-BINDING SITES, COFACTOR, ACTIVE SITE, DISULFIDE BONDS.
    12. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-45.
    13. Cited for: VARIANT OI13 ARG-12, CHARACTERIZATION OF VARIANT OI13 ARG-12.
    14. "Identification of a mutation causing deficient BMP1/mTLD proteolytic activity in autosomal recessive osteogenesis imperfecta."
      Martinez-Glez V., Valencia M., Caparros-Martin J.A., Aglan M., Temtamy S., Tenorio J., Pulido V., Lindert U., Rohrbach M., Eyre D., Giunta C., Lapunzina P., Ruiz-Perez V.L.
      Hum. Mutat. 33:343-350(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI13 LEU-249, CHARACTERIZATION OF VARIANT OI13 LEU-249.

    Entry informationi

    Entry nameiBMP1_HUMAN
    AccessioniPrimary (citable) accession number: P13497
    Secondary accession number(s): A8K6F5
    , B2RN46, D3DSR0, Q13292, Q13872, Q14874, Q99421, Q99422, Q99423, Q9UL38
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: February 21, 2001
    Last modified: October 1, 2014
    This is version 169 of the entry and version 2 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 8
      Human chromosome 8: 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. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3