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Reviewed, UniProtKB/Swiss-Prot P13497 (BMP1_HUMAN)

Last modified June 16, 2009. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Bone morphogenetic protein 1
      Short name=BMP-1
    EC=3.4.24.19
Alternative name(s):
    Procollagen C-proteinase
      Short name=PCP
    Mammalian tolloid protein
      Short name=mTld
Gene names
Name: BMP1
Synonyms: PCOLC
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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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).

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 By similarity.

Enzyme regulation

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

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the peptidase M12A family.

Contains 5 CUB domains.

Contains 2 EGF-like domains.

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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.

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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 By similarity
Metal binding2131Zinc; catalytic By similarity
Metal binding2171Zinc; catalytic By similarity
Metal binding2231Zinc; catalytic By similarity

Amino acid modifications

Glycosylation911N-linked (GlcNAc...) Potential
Glycosylation1421N-linked (GlcNAc...) Potential
Glycosylation3321N-linked (GlcNAc...) Potential
Glycosylation3631N-linked (GlcNAc...) Potential
Glycosylation5991N-linked (GlcNAc...) Potential
Disulfide bond183 ↔ 186 Ref.5
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 variant451D → H in a breast cancer sample; somatic mutation. Ref.7
VAR_036141
Natural variant7191V → I: dbSNP rs11996036.
VAR_051584

Experimental info

Sequence conflict7481D → N Ref.4
Sequence conflict9341R → S Ref.4

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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

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Isoform BMP1-1.

Checksum: E506D63729A9E86D
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FASTA73082,900
Isoform BMP1-2 (Sequence not available). FASTA––
Isoform BMP1-4.

Checksum: 9FCDE92B1F884B15
Show »

FASTA30233,424
Isoform BMP1-5.

Checksum: A47CE9FD49D5A8D7
Show »

FASTA62270,469
Isoform BMP1-6.

Checksum: AE07361E00A6A700
Show »

FASTA71781,082
Isoform BMP1-7.

Checksum: 09148B0724B5F1A8
Show »

FASTA82392,655

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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: 8643539] [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: 3201241] [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: 9500680] [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: 7798260] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS BMP1-3 AND BMP1-7).
Tissue: Placenta.
[5]"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: 11283002] [Abstract]
Cited for: DISULFIDE BOND IN METALLOPROTEASE DOMAIN.
[6]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:RESEARCH008.1-RESEARCH008.16(2004) [PubMed: 14759258] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[7]"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: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-45.
+Additional computationally mapped references.

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Cross-references

Sequence databases

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.
IPIIPI00009054.
IPI00014021.
IPI00218040.
IPI00218042.
IPI00218044.
IPI00218045.
PIRBMHU1. A37278.
A58788.
B58788.
RefSeqNP_001190.1.
NP_006119.1.
NP_006120.1.
UniGeneHs.1274

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3EDGX-ray1.27A121-321[»]
3EDHX-ray1.25A121-321[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP13497. 4 interactions.

Protein family/group databases

MEROPSM12.005.

PTM databases

PhosphoSiteP13497.

Proteomic databases

PeptideAtlasP13497.
PRIDEP13497.

Genome annotation databases

EnsemblENSG00000168487. Homo sapiens. [Contig view]
GeneID649.
KEGGhsa:649.

Organism-specific databases

GeneCardsGC08P022078.
H-InvDBHIX0007366.
HGNCHGNC:1067. BMP1.
HPAHPA014572.
MIM112264. gene.
PharmGKBPA25377.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP13497.
OMAP13497. FRTIASS.

Enzyme and pathway databases

BRENDA3.4.24.19. 247.
ReactomeREACT_602. Lipid and lipoprotein metabolism.

Gene expression databases

ArrayExpressP13497.
BgeeP13497.
CleanExHS_BMP1.
GermOnlineENSG00000168487. Homo sapiens.

Family and domain databases

InterProIPR015446. BMP_1/tolloid-like.
IPR000859. CUB.
IPR006209. EGF.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_CS.
IPR000742. EGF_3.
IPR001881. EGF_Ca_bd.
IPR013091. EGF_Ca_bd_2.
IPR018097. EGF_Ca_bd_CS.
IPR006025. Pept_M_Zn_BS.
IPR006026. Peptidase_M.
IPR001506. Peptidase_M12A.
[Graphical view]
Gene3DG3DSA:2.60.120.290. CUB. 5 hits.
PANTHERPTHR10127:SF71. BMP_1. 1 hit.
PfamPF01400. Astacin. 1 hit.
PF00431. CUB. 5 hits.
PF00008. EGF. 1 hit.
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]
PROSITEPS00010. ASX_HYDROXYL. 2 hits.
PS01180. CUB. 5 hits.
PS00022. EGF_1. False negative.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 2 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio2632.
PMAP-CutDBP13497.
SOURCESearch...

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Entry information

Entry nameBMP1_HUMAN
AccessionPrimary (citable) accession number: P13497
Secondary accession number(s): Q13292 expand/collapse secondary AC list , Q13872, Q14874, Q99421, Q99422, Q99423, Q9UL38
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 21, 2001
Last modified: June 16, 2009
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 8

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents