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P13497 (BMP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bone morphogenetic protein 1

Short name=BMP-1
EC=3.4.24.19
Alternative name(s):
Mammalian tolloid protein
Short name=mTld
Procollagen C-proteinase
Short name=PCP
Gene names
Name:BMP1
Synonyms:PCOLC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length986 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Binds 1 zinc ion per subunit. Ref.11

Enzyme regulation

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

Subunit structure

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

Subcellular location

Golgi apparatustrans-Golgi network. Secretedextracellular spaceextracellular matrix. Note: Co-localizes with POSTN in the Golgi By similarity. Ref.9

Tissue specificity

Ubiquitous.

Post-translational modification

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.14

Sequence similarities

Belongs to the peptidase M12A family.

Contains 5 CUB domains.

Contains 2 EGF-like domains.

Ontologies

Keywords
   Biological processChondrogenesis
Differentiation
Osteogenesis
   Cellular componentExtracellular matrix
Golgi apparatus
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Osteogenesis imperfecta
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionCytokine
Developmental protein
Growth factor
Hydrolase
Metalloprotease
Protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcartilage condensation

Traceable author statement Ref.2. Source: ProtInc

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

lipoprotein metabolic process

Traceable author statement. Source: Reactome

multicellular organismal development

Traceable author statement Ref.4. Source: ProtInc

ossification

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cartilage development

Inferred from direct assay Ref.2. Source: MGI

proteolysis

Inferred from direct assay PubMed 16824737. Source: UniProtKB

skeletal system development

Non-traceable author statement Ref.4. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

membrane-bounded vesicle

Inferred from electronic annotation. Source: Ensembl

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

metalloendopeptidase activity

Traceable author statement. Source: Reactome

metallopeptidase activity

Non-traceable author statement Ref.4. Source: UniProtKB

peptidase activity

Inferred from direct assay PubMed 16824737. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform BMP1-3 (identifier: P13497-1)

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.
Isoform BMP1-1 (identifier: P13497-2)

The sequence of this isoform differs from the canonical sequence as follows:
     703-730: DKDECSKDNGGCQQDCVNTFGSYECQCR → EKRPALQPPRGRPHQLKFRVQKRNRTPQ
     731-986: Missing.
Isoform BMP1-2 (identifier: P13497-7)

The sequence of this isoform is not available.
Isoform BMP1-4 (identifier: P13497-3)

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.
Isoform BMP1-5 (identifier: P13497-4)

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.
Isoform BMP1-6 (identifier: P13497-5)

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.
Isoform BMP1-7 (identifier: P13497-6)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 12098 Potential
PRO_0000028889
Chain121 – 986866Bone morphogenetic protein 1
PRO_0000028890

Regions

Domain322 – 434113CUB 1
Domain435 – 546112CUB 2
Domain547 – 58842EGF-like 1; calcium-binding Potential
Domain591 – 703113CUB 3
Domain704 – 74340EGF-like 2; calcium-binding Potential
Domain747 – 859113CUB 4
Domain860 – 976117CUB 5
Region121 – 321201Metalloprotease

Sites

Active site2141 Ref.11
Metal binding2131Zinc; catalytic
Metal binding2171Zinc; catalytic
Metal binding2231Zinc; catalytic

Amino acid modifications

Glycosylation911N-linked (GlcNAc...) Potential
Glycosylation1421N-linked (GlcNAc...) Potential
Glycosylation3321N-linked (GlcNAc...) Potential
Glycosylation3631N-linked (GlcNAc...) Potential
Glycosylation5991N-linked (GlcNAc...) Potential
Disulfide bond163 ↔ 319 Ref.11
Disulfide bond183 ↔ 205 Ref.11
Disulfide bond185 ↔ 186 Ref.11
Disulfide bond322 ↔ 348 By similarity
Disulfide bond375 ↔ 397 By similarity
Disulfide bond435 ↔ 461 By similarity
Disulfide bond488 ↔ 510 By similarity
Disulfide bond551 ↔ 563 By similarity
Disulfide bond559 ↔ 572 By similarity
Disulfide bond574 ↔ 587 By similarity
Disulfide bond591 ↔ 617 By similarity
Disulfide bond644 ↔ 666 By similarity
Disulfide bond707 ↔ 718 By similarity
Disulfide bond714 ↔ 727 By similarity
Disulfide bond729 ↔ 742 By similarity
Disulfide bond747 ↔ 773 By similarity
Disulfide bond800 ↔ 822 By similarity
Disulfide bond860 ↔ 890 By similarity
Disulfide bond917 ↔ 939 By similarity

Natural variations

Alternative sequence245 – 30258QEYNF…PIGQR → VLHSSLLLLSCGSRNGASFP CSLESSTHQALCWTGLFLRP SPFPRLPLAAPRTLRAGV in isoform BMP1-4.
VSP_005463
Alternative sequence303 – 986684Missing in isoform BMP1-4.
VSP_005464
Alternative sequence589 – 62234AACGG…IWQLV → GCYDLQVGKPLLWDRHCFRL STHGPEMLGTALRG in isoform BMP1-5.
VSP_005465
Alternative sequence623 – 986364Missing in isoform BMP1-5.
VSP_005466
Alternative sequence703 – 823121DKDEC…GRFCG → VLEGAGDRHSHLSGLELLLC PHALVDTVPAPPSALHGDTH AHTHTHVHTHCPIAQETCRG PPLGASRLSPQGPGHLTLAP QEGSYLDFWDTHRGDPKPRR RRKSLKTFSLTPATFRGIWA L in isoform BMP1-7.
VSP_005469
Alternative sequence703 – 73028DKDEC…ECQCR → EKRPALQPPRGRPHQLKFRV QKRNRTPQ in isoform BMP1-1.
VSP_005461
Alternative sequence703 – 71715DKDEC…GCQQD → GGELFGLLGHPPRRP in isoform BMP1-6.
VSP_005467
Alternative sequence718 – 986269Missing in isoform BMP1-6.
VSP_005468
Alternative sequence731 – 986256Missing in isoform BMP1-1.
VSP_005462
Alternative sequence824 – 986163Missing in isoform BMP1-7.
VSP_005470
Natural variant121G → 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. Ref.13
Corresponds to variant rs318240762 [ dbSNP | Ensembl ].
VAR_069096
Natural variant451D → H in a breast cancer sample; somatic mutation. Ref.12
VAR_036141
Natural variant2491F → L in OI13; leads to a protein with deficient procollagen I C-terminal propeptide proteolytic activity. Ref.14
VAR_067224
Natural variant7191V → I.
Corresponds to variant rs11996036 [ dbSNP | Ensembl ].
VAR_051584

Experimental info

Mutagenesis119 – 1202RR → AA: Doesn't abolish secretion. Ref.9
Sequence conflict7481D → N in AAC41710. Ref.4
Sequence conflict9341R → S in AAC41710. Ref.4

Secondary structure

..................................... 986
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform BMP1-3 [UniParc].

Last modified February 21, 2001. Version 2.
Checksum: F89201913AC3CBEA

FASTA986111,249
        10         20         30         40         50         60 
MPGVARLPLL LGLLLLPRPG RPLDLADYTY DLAEEDDSEP LNYKDPCKAA AFLGDIALDE 

        70         80         90        100        110        120 
EDLRAFQVQQ AVDLRRHTAR KSSIKAAVPG NTSTPSCQST NGQPQRGACG RWRGRSRSRR 

       130        140        150        160        170        180 
AATSRPERVW PDGVIPFVIG GNFTGSQRAV FRQAMRHWEK HTCVTFLERT DEDSYIVFTY 

       190        200        210        220        230        240 
RPCGCCSYVG RRGGGPQAIS IGKNCDKFGI VVHELGHVVG FWHEHTRPDR DRHVSIVREN 

       250        260        270        280        290        300 
IQPGQEYNFL KMEPQEVESL GETYDFDSIM HYARNTFSRG IFLDTIVPKY EVNGVKPPIG 

       310        320        330        340        350        360 
QRTRLSKGDI AQARKLYKCP ACGETLQDST GNFSSPEYPN GYSAHMHCVW RISVTPGEKI 

       370        380        390        400        410        420 
ILNFTSLDLY RSRLCWYDYV EVRDGFWRKA PLRGRFCGSK LPEPIVSTDS RLWVEFRSSS 

       430        440        450        460        470        480 
NWVGKGFFAV YEAICGGDVK KDYGHIQSPN YPDDYRPSKV CIWRIQVSEG FHVGLTFQSF 

       490        500        510        520        530        540 
EIERHDSCAY DYLEVRDGHS ESSTLIGRYC GYEKPDDIKS TSSRLWLKFV SDGSINKAGF 

       550        560        570        580        590        600 
AVNFFKEVDE CSRPNRGGCE QRCLNTLGSY KCSCDPGYEL APDKRRCEAA CGGFLTKLNG 

       610        620        630        640        650        660 
SITSPGWPKE YPPNKNCIWQ LVAPTQYRIS LQFDFFETEG NDVCKYDFVE VRSGLTADSK 

       670        680        690        700        710        720 
LHGKFCGSEK PEVITSQYNN MRVEFKSDNT VSKKGFKAHF FSDKDECSKD NGGCQQDCVN 

       730        740        750        760        770        780 
TFGSYECQCR SGFVLHDNKH DCKEAGCDHK VTSTSGTITS PNWPDKYPSK KECTWAISST 

       790        800        810        820        830        840 
PGHRVKLTFM EMDIESQPEC AYDHLEVFDG RDAKAPVLGR FCGSKKPEPV LATGSRMFLR 

       850        860        870        880        890        900 
FYSDNSVQRK GFQASHATEC GGQVRADVKT KDLYSHAQFG DNNYPGGVDC EWVIVAEEGY 

       910        920        930        940        950        960 
GVELVFQTFE VEEETDCGYD YMELFDGYDS TAPRLGRYCG SGPPEEVYSA GDSVLVKFHS 

       970        980 
DDTITKKGFH LRYTSTKFQD TLHSRK 

« Hide

Isoform BMP1-1 [UniParc].

Checksum: E506D63729A9E86D
Show »

FASTA73082,900
Isoform BMP1-2 (Sequence not available).
Isoform BMP1-4 [UniParc].

Checksum: 9FCDE92B1F884B15
Show »

FASTA30233,424
Isoform BMP1-5 [UniParc].

Checksum: A47CE9FD49D5A8D7
Show »

FASTA62270,469
Isoform BMP1-6 [UniParc].

Checksum: AE07361E00A6A700
Show »

FASTA71781,082
Isoform BMP1-7 [UniParc].

Checksum: 09148B0724B5F1A8
Show »

FASTA82392,655

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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. expand/collapse author list , 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]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-45.
[13]"Attenuated BMP1 function compromises osteogenesis, leading to bone fragility in humans and zebrafish."
Asharani P.V., Keupp K., Semler O., Wang W., Li Y., Thiele H., Yigit G., Pohl E., Becker J., Frommolt P., Sonntag C., Altmuller J., Zimmermann K., Greenspan D.S., Akarsu N.A., Netzer C., Schonau E., Wirth R. expand/collapse author list , Hammerschmidt M., Nurnberg P., Wollnik B., Carney T.J.
Am. J. Hum. Genet. 90:661-674(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRBMHU1. A37278.
A58788.
B58788.
RefSeqNP_001190.1. NM_001199.3.
NP_006120.1. NM_006129.4.
UniGeneHs.1274.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EDGX-ray1.27A121-321[»]
3EDHX-ray1.25A121-321[»]
ProteinModelPortalP13497.
SMRP13497. Positions 121-976.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107117. 3 interactions.
DIPDIP-33403N.
IntActP13497. 6 interactions.
MINTMINT-1394084.
STRING9606.ENSP00000305714.

Chemistry

BindingDBP13497.
ChEMBLCHEMBL3898.

Protein family/group databases

MEROPSM12.005.

PTM databases

PhosphoSiteP13497.

Polymorphism databases

DMDM13124688.

Proteomic databases

PaxDbP13497.
PeptideAtlasP13497.
PRIDEP13497.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306349; ENSP00000306121; ENSG00000168487. [P13497-2]
ENST00000306385; ENSP00000305714; ENSG00000168487. [P13497-1]
ENST00000397814; ENSP00000380915; ENSG00000168487. [P13497-4]
ENST00000397816; ENSP00000380917; ENSG00000168487. [P13497-6]
ENST00000471755; ENSP00000428665; ENSG00000168487. [P13497-4]
ENST00000520970; ENSP00000428332; ENSG00000168487. [P13497-2]
ENST00000521385; ENSP00000430406; ENSG00000168487. [P13497-5]
GeneID649.
KEGGhsa:649.
UCSCuc003xbb.3. human. [P13497-2]
uc003xbg.3. human. [P13497-1]

Organism-specific databases

CTD649.
GeneCardsGC08P022022.
HGNCHGNC:1067. BMP1.
HPAHPA014572.
MIM112264. gene.
614856. phenotype.
neXtProtNX_P13497.
Orphanet216812. Osteogenesis imperfecta type 3.
PharmGKBPA25377.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG70307.
HOVERGENHBG004859.
InParanoidP13497.
KOK05502.
OMAGRFCGGK.
OrthoDBEOG7N8ZTV.
PhylomeDBP13497.
TreeFamTF314351.

Enzyme and pathway databases

BRENDA3.4.24.19. 2681.
ReactomeREACT_111217. Metabolism.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP13497.
BgeeP13497.
CleanExHS_BMP1.
GenevestigatorP13497.

Family and domain databases

Gene3D2.60.120.290. 5 hits.
3.40.390.10. 1 hit.
InterProIPR015446. 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]
PfamPF01400. Astacin. 1 hit.
PF00431. CUB. 5 hits.
PF07645. EGF_CA. 1 hit.
[Graphical view]
PIRSFPIRSF001199. BMP_1/tolloid-like. 1 hit.
PRINTSPR00480. ASTACIN.
SMARTSM00042. CUB. 5 hits.
SM00179. EGF_CA. 2 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF49854. SSF49854. 5 hits.
SSF57184. SSF57184. 2 hits.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

ChiTaRSBMP1. human.
EvolutionaryTraceP13497.
GeneWikiBone_morphogenetic_protein_1.
GenomeRNAi649.
NextBio2632.
PMAP-CutDBP13497.
PROP13497.
SOURCESearch...

Entry information

Entry nameBMP1_HUMAN
AccessionPrimary (citable) accession number: P13497
Secondary accession number(s): A8K6F5 expand/collapse secondary AC list , B2RN46, D3DSR0, Q13292, Q13872, Q14874, Q99421, Q99422, Q99423, Q9UL38
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 21, 2001
Last modified: April 16, 2014
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM