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P13497

- BMP1_HUMAN

UniProt

P13497 - BMP1_HUMAN

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Protein

Bone morphogenetic protein 1

Gene

BMP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Zn2+1 PublicationNote: 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
Complete GO annotation...

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-KW
  4. membrane-bounded vesicle Source: Ensembl
  5. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

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 ↔ 3191 Publication
Disulfide bondi183 ↔ 2051 Publication
Disulfide bondi185 ↔ 1861 Publication
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

BgeeiP13497.
CleanExiHS_BMP1.
ExpressionAtlasiP13497. baseline and differential.
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 – 1283Combined sources
Helixi131 – 1333Combined sources
Beta strandi134 – 1396Combined sources
Helixi145 – 16117Combined sources
Beta strandi165 – 1684Combined sources
Beta strandi173 – 1808Combined sources
Beta strandi194 – 2018Combined sources
Helixi203 – 2053Combined sources
Helixi208 – 21912Combined sources
Helixi224 – 2263Combined sources
Helixi230 – 2323Combined sources
Beta strandi234 – 2363Combined sources
Helixi238 – 2403Combined sources
Helixi246 – 2494Combined sources
Helixi254 – 2563Combined sources
Turni274 – 2774Combined sources
Beta strandi278 – 2803Combined sources
Beta strandi285 – 2906Combined sources
Helixi307 – 31610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119018.
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

        10         20         30         40         50
MPGVARLPLL LGLLLLPRPG RPLDLADYTY DLAEEDDSEP LNYKDPCKAA
60 70 80 90 100
AFLGDIALDE EDLRAFQVQQ AVDLRRHTAR KSSIKAAVPG NTSTPSCQST
110 120 130 140 150
NGQPQRGACG RWRGRSRSRR AATSRPERVW PDGVIPFVIG GNFTGSQRAV
160 170 180 190 200
FRQAMRHWEK HTCVTFLERT DEDSYIVFTY RPCGCCSYVG RRGGGPQAIS
210 220 230 240 250
IGKNCDKFGI VVHELGHVVG FWHEHTRPDR DRHVSIVREN IQPGQEYNFL
260 270 280 290 300
KMEPQEVESL GETYDFDSIM HYARNTFSRG IFLDTIVPKY EVNGVKPPIG
310 320 330 340 350
QRTRLSKGDI AQARKLYKCP ACGETLQDST GNFSSPEYPN GYSAHMHCVW
360 370 380 390 400
RISVTPGEKI ILNFTSLDLY RSRLCWYDYV EVRDGFWRKA PLRGRFCGSK
410 420 430 440 450
LPEPIVSTDS RLWVEFRSSS NWVGKGFFAV YEAICGGDVK KDYGHIQSPN
460 470 480 490 500
YPDDYRPSKV CIWRIQVSEG FHVGLTFQSF EIERHDSCAY DYLEVRDGHS
510 520 530 540 550
ESSTLIGRYC GYEKPDDIKS TSSRLWLKFV SDGSINKAGF AVNFFKEVDE
560 570 580 590 600
CSRPNRGGCE QRCLNTLGSY KCSCDPGYEL APDKRRCEAA CGGFLTKLNG
610 620 630 640 650
SITSPGWPKE YPPNKNCIWQ LVAPTQYRIS LQFDFFETEG NDVCKYDFVE
660 670 680 690 700
VRSGLTADSK LHGKFCGSEK PEVITSQYNN MRVEFKSDNT VSKKGFKAHF
710 720 730 740 750
FSDKDECSKD NGGCQQDCVN TFGSYECQCR SGFVLHDNKH DCKEAGCDHK
760 770 780 790 800
VTSTSGTITS PNWPDKYPSK KECTWAISST PGHRVKLTFM EMDIESQPEC
810 820 830 840 850
AYDHLEVFDG RDAKAPVLGR FCGSKKPEPV LATGSRMFLR FYSDNSVQRK
860 870 880 890 900
GFQASHATEC GGQVRADVKT KDLYSHAQFG DNNYPGGVDC EWVIVAEEGY
910 920 930 940 950
GVELVFQTFE VEEETDCGYD YMELFDGYDS TAPRLGRYCG SGPPEEVYSA
960 970 980
GDSVLVKFHS DDTITKKGFH LRYTSTKFQD TLHSRK
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:
EMBLi
GenBanki
DDBJi
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]
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 ]
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.
GeneTreei ENSGT00760000119018.
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

Bgeei P13497.
CleanExi HS_BMP1.
ExpressionAtlasi P13497. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 171 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