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Protein

Bone morphogenetic protein 1

Gene

BMP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi213Zinc; catalytic1 Publication1
Active sitei214PROSITE-ProRule annotation1 Publication1
Metal bindingi217Zinc; catalytic1 Publication1
Metal bindingi223Zinc; catalytic1 Publication1

GO - Molecular functioni

GO - Biological processi

  • BMP signaling pathway Source: GO_Central
  • cartilage condensation Source: ProtInc
  • cell development Source: GO_Central
  • extracellular matrix disassembly Source: Reactome
  • lipoprotein metabolic process Source: Reactome
  • multicellular organism development Source: ProtInc
  • ossification Source: UniProtKB-KW
  • positive regulation of cartilage development Source: MGI
  • positive regulation of pathway-restricted SMAD protein phosphorylation Source: GO_Central
  • proteolysis Source: UniProtKB
  • regulation of apoptotic process Source: GO_Central
  • regulation of MAPK cascade Source: GO_Central
  • skeletal system development Source: UniProtKB
  • SMAD protein signal transduction Source: GO_Central
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

BioCyciZFISH:HS09771-MONOMER.
BRENDAi3.4.24.19. 2681.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-194223. HDL-mediated lipid transport.
R-HSA-2214320. Anchoring fibril formation.
R-HSA-2243919. Crosslinking of collagen fibrils.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:1067. BMP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Golgi apparatus, Secreted

Pathology & Biotechi

Involvement in diseasei

Osteogenesis imperfecta 13 (OI13)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:614856
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06909612G → 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 PublicationCorresponds to variant rs318240762dbSNPEnsembl.1
Natural variantiVAR_067224249F → L in OI13; leads to a protein with deficient procollagen I C-terminal propeptide proteolytic activity. 1 PublicationCorresponds to variant rs398122891dbSNPEnsembl.1
Natural variantiVAR_072248270M → V in OI13; partial loss of activity. 1 PublicationCorresponds to variant rs786205219dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi119 – 120RR → AA: Doesn't abolish secretion. 1 Publication2

Keywords - Diseasei

Disease mutation, Osteogenesis imperfecta

Organism-specific databases

DisGeNETi649.
MalaCardsiBMP1.
MIMi614856. phenotype.
OpenTargetsiENSG00000168487.
Orphaneti216812. Osteogenesis imperfecta type 3.
PharmGKBiPA25377.

Chemistry databases

ChEMBLiCHEMBL3898.
GuidetoPHARMACOLOGYi2333.

Polymorphism and mutation databases

BioMutaiBMP1.
DMDMi13124688.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
PropeptideiPRO_000002888923 – 120Sequence analysisAdd BLAST98
ChainiPRO_0000028890121 – 986Bone morphogenetic protein 1Add BLAST866

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi91N-linked (GlcNAc...)Sequence analysis1
Glycosylationi142N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi163 ↔ 3191 Publication
Disulfide bondi183 ↔ 2051 Publication
Disulfide bondi185 ↔ 1861 Publication
Disulfide bondi322 ↔ 348By similarity
Glycosylationi332N-linked (GlcNAc...)Sequence analysis1
Glycosylationi363N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi599N-linked (GlcNAc...)Sequence analysis1
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

EPDiP13497.
PaxDbiP13497.
PeptideAtlasiP13497.
PRIDEiP13497.

PTM databases

iPTMnetiP13497.
PhosphoSitePlusiP13497.

Miscellaneous databases

PMAP-CutDBP13497.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000168487.
CleanExiHS_BMP1.
ExpressionAtlasiP13497. baseline and differential.
GenevisibleiP13497. HS.

Organism-specific databases

HPAiHPA014572.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
DCNP075852EBI-12509497,EBI-9663608
MSTNO147932EBI-489827,EBI-8542977

GO - Molecular functioni

Protein-protein interaction databases

BioGridi107117. 39 interactors.
DIPiDIP-33403N.
IntActiP13497. 9 interactors.
MINTiMINT-1394084.
STRINGi9606.ENSP00000305714.

Chemistry databases

BindingDBiP13497.

Structurei

Secondary structure

1986
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi126 – 128Combined sources3
Helixi131 – 133Combined sources3
Beta strandi134 – 139Combined sources6
Helixi145 – 161Combined sources17
Beta strandi165 – 168Combined sources4
Beta strandi173 – 180Combined sources8
Beta strandi194 – 201Combined sources8
Helixi203 – 205Combined sources3
Helixi208 – 219Combined sources12
Helixi224 – 226Combined sources3
Helixi230 – 232Combined sources3
Beta strandi234 – 236Combined sources3
Helixi238 – 240Combined sources3
Helixi246 – 249Combined sources4
Helixi254 – 256Combined sources3
Turni274 – 277Combined sources4
Beta strandi278 – 280Combined sources3
Beta strandi285 – 290Combined sources6
Helixi307 – 316Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EDGX-ray1.27A121-321[»]
3EDHX-ray1.25A121-321[»]
ProteinModelPortaliP13497.
SMRiP13497.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13497.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini322 – 434CUB 1PROSITE-ProRule annotationAdd BLAST113
Domaini435 – 546CUB 2PROSITE-ProRule annotationAdd BLAST112
Domaini547 – 588EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini591 – 703CUB 3PROSITE-ProRule annotationAdd BLAST113
Domaini704 – 743EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini747 – 859CUB 4PROSITE-ProRule annotationAdd BLAST113
Domaini860 – 976CUB 5PROSITE-ProRule annotationAdd BLAST117

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni121 – 321MetalloproteaseAdd BLAST201

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

eggNOGiKOG3714. Eukaryota.
ENOG410ZPX7. LUCA.
GeneTreeiENSGT00760000119018.
HOVERGENiHBG004859.
InParanoidiP13497.
KOiK05502.
OMAiFCGGKLP.
OrthoDBiEOG091G009U.
PhylomeDBiP13497.
TreeFamiTF314351.

Family and domain databases

CDDicd00041. CUB. 5 hits.
Gene3Di2.60.120.290. 5 hits.
3.40.390.10. 1 hit.
InterProiIPR015446. BMP_1/tolloid-like.
IPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
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.
SM00181. EGF. 2 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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti748D → N in AAC41710 (PubMed:7798260).Curated1
Sequence conflicti934R → S in AAC41710 (PubMed:7798260).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06909612G → 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 PublicationCorresponds to variant rs318240762dbSNPEnsembl.1
Natural variantiVAR_03614145D → H in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_067224249F → L in OI13; leads to a protein with deficient procollagen I C-terminal propeptide proteolytic activity. 1 PublicationCorresponds to variant rs398122891dbSNPEnsembl.1
Natural variantiVAR_072248270M → V in OI13; partial loss of activity. 1 PublicationCorresponds to variant rs786205219dbSNPEnsembl.1
Natural variantiVAR_051584719V → I.Corresponds to variant rs11996036dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005463245 – 302QEYNF…PIGQR → VLHSSLLLLSCGSRNGASFP CSLESSTHQALCWTGLFLRP SPFPRLPLAAPRTLRAGV in isoform BMP1-4. 1 PublicationAdd BLAST58
Alternative sequenceiVSP_005464303 – 986Missing in isoform BMP1-4. 1 PublicationAdd BLAST684
Alternative sequenceiVSP_005465589 – 622AACGG…IWQLV → GCYDLQVGKPLLWDRHCFRL STHGPEMLGTALRG in isoform BMP1-5. 2 PublicationsAdd BLAST34
Alternative sequenceiVSP_005466623 – 986Missing in isoform BMP1-5. 2 PublicationsAdd BLAST364
Alternative sequenceiVSP_005469703 – 823DKDEC…GRFCG → VLEGAGDRHSHLSGLELLLC PHALVDTVPAPPSALHGDTH AHTHTHVHTHCPIAQETCRG PPLGASRLSPQGPGHLTLAP QEGSYLDFWDTHRGDPKPRR RRKSLKTFSLTPATFRGIWA L in isoform BMP1-7. CuratedAdd BLAST121
Alternative sequenceiVSP_005461703 – 730DKDEC…ECQCR → EKRPALQPPRGRPHQLKFRV QKRNRTPQ in isoform BMP1-1. 1 PublicationAdd BLAST28
Alternative sequenceiVSP_005467703 – 717DKDEC…GCQQD → GGELFGLLGHPPRRP in isoform BMP1-6. 1 PublicationAdd BLAST15
Alternative sequenceiVSP_005468718 – 986Missing in isoform BMP1-6. 1 PublicationAdd BLAST269
Alternative sequenceiVSP_005462731 – 986Missing in isoform BMP1-1. 1 PublicationAdd BLAST256
Alternative sequenceiVSP_005470824 – 986Missing in isoform BMP1-7. CuratedAdd BLAST163

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]
XP_011542919.1. XM_011544617.1. [P13497-4]
XP_016869227.1. XM_017013738.1. [P13497-5]
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.4. human. [P13497-1]

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.
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]
XP_011542919.1. XM_011544617.1. [P13497-4]
XP_016869227.1. XM_017013738.1. [P13497-5]
UniGeneiHs.1274.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EDGX-ray1.27A121-321[»]
3EDHX-ray1.25A121-321[»]
ProteinModelPortaliP13497.
SMRiP13497.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107117. 39 interactors.
DIPiDIP-33403N.
IntActiP13497. 9 interactors.
MINTiMINT-1394084.
STRINGi9606.ENSP00000305714.

Chemistry databases

BindingDBiP13497.
ChEMBLiCHEMBL3898.
GuidetoPHARMACOLOGYi2333.

Protein family/group databases

MEROPSiM12.005.

PTM databases

iPTMnetiP13497.
PhosphoSitePlusiP13497.

Polymorphism and mutation databases

BioMutaiBMP1.
DMDMi13124688.

Proteomic databases

EPDiP13497.
PaxDbiP13497.
PeptideAtlasiP13497.
PRIDEiP13497.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.4. human. [P13497-1]

Organism-specific databases

CTDi649.
DisGeNETi649.
GeneCardsiBMP1.
HGNCiHGNC:1067. BMP1.
HPAiHPA014572.
MalaCardsiBMP1.
MIMi112264. gene.
614856. phenotype.
neXtProtiNX_P13497.
OpenTargetsiENSG00000168487.
Orphaneti216812. Osteogenesis imperfecta type 3.
PharmGKBiPA25377.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3714. Eukaryota.
ENOG410ZPX7. LUCA.
GeneTreeiENSGT00760000119018.
HOVERGENiHBG004859.
InParanoidiP13497.
KOiK05502.
OMAiFCGGKLP.
OrthoDBiEOG091G009U.
PhylomeDBiP13497.
TreeFamiTF314351.

Enzyme and pathway databases

BioCyciZFISH:HS09771-MONOMER.
BRENDAi3.4.24.19. 2681.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-194223. HDL-mediated lipid transport.
R-HSA-2214320. Anchoring fibril formation.
R-HSA-2243919. Crosslinking of collagen fibrils.

Miscellaneous databases

ChiTaRSiBMP1. human.
EvolutionaryTraceiP13497.
GeneWikiiBone_morphogenetic_protein_1.
GenomeRNAii649.
PMAP-CutDBP13497.
PROiP13497.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000168487.
CleanExiHS_BMP1.
ExpressionAtlasiP13497. baseline and differential.
GenevisibleiP13497. HS.

Family and domain databases

CDDicd00041. CUB. 5 hits.
Gene3Di2.60.120.290. 5 hits.
3.40.390.10. 1 hit.
InterProiIPR015446. BMP_1/tolloid-like.
IPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
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.
SM00181. EGF. 2 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]
ProtoNetiSearch...

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 30, 2016
This is version 193 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.