Reviewed, UniProtKB/Swiss-Prot P13497 (BMP1_HUMAN)

Names and originHide

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributesHide

Sequence length	986 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)Hide

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.

OntologiesHide

Keywords
Biological process	Chondrogenesis Differentiation Osteogenesis
Coding sequence diversity	Alternative splicing Polymorphism
Domain	EGF-like domain Repeat Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Cytokine Developmental protein Growth factor Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cartilage condensation Traceable author statement. Source: ProtInc cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW ossification Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of cartilage development Ref.2 Inferred from direct assay. Source: MGI proteolysis Inferred from direct assay. Source: UniProtKB
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro cytokine activity Inferred from electronic annotation. Source: UniProtKB-KW growth factor activity Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative productsHide

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)Hide

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Potential

Propeptide

23 – 120

98

Potential

PRO_0000028889

Chain

121 – 986

866

Bone morphogenetic protein 1

PRO_0000028890

Regions

Domain

322 – 434

113

CUB 1

Domain

435 – 546

112

CUB 2

Domain

547 – 588

42

EGF-like 1; calcium-binding Potential

Domain

591 – 703

113

CUB 3

Domain

704 – 743

40

EGF-like 2; calcium-binding Potential

Domain

747 – 859

113

CUB 4

Domain

860 – 976

117

CUB 5

Region

121 – 321

201

Metalloprotease

Sites

Active site

214

1

By similarity

Metal binding

213

1

Zinc; catalytic By similarity

Metal binding

217

1

Zinc; catalytic By similarity

Metal binding

223

1

Zinc; catalytic By similarity

Amino acid modifications

Glycosylation

91

1

N-linked (GlcNAc...) Potential

Glycosylation

142

1

N-linked (GlcNAc...) Potential

Glycosylation

332

1

N-linked (GlcNAc...) Potential

Glycosylation

363

1

N-linked (GlcNAc...) Potential

Glycosylation

599

1

N-linked (GlcNAc...) Potential

Disulfide bond

183 ↔ 186

Disulfide bond

322 ↔ 348

By similarity

Disulfide bond

375 ↔ 397

By similarity

Disulfide bond

435 ↔ 461

By similarity

Disulfide bond

488 ↔ 510

By similarity

Disulfide bond

551 ↔ 563

By similarity

Disulfide bond

559 ↔ 572

By similarity

Disulfide bond

574 ↔ 587

By similarity

Disulfide bond

591 ↔ 617

By similarity

Disulfide bond

644 ↔ 666

By similarity

Disulfide bond

707 ↔ 718

By similarity

Disulfide bond

714 ↔ 727

By similarity

Disulfide bond

729 ↔ 742

By similarity

Disulfide bond

747 ↔ 773

By similarity

Disulfide bond

800 ↔ 822

By similarity

Disulfide bond

860 ↔ 890

By similarity

Disulfide bond

917 ↔ 939

By similarity

Natural variations

Alternative sequence

245 – 302

58

QEYNF…PIGQR → VLHSSLLLLSCGSRNGASFP CSLESSTHQALCWTGLFLRP SPFPRLPLAAPRTLRAGV in isoform BMP1-4.

VSP_005463

Alternative sequence

303 – 986

684

Missing in isoform BMP1-4.

VSP_005464

Alternative sequence

589 – 622

34

AACGG…IWQLV → GCYDLQVGKPLLWDRHCFRL STHGPEMLGTALRG in isoform BMP1-5.

VSP_005465

Alternative sequence

623 – 986

364

Missing in isoform BMP1-5.

VSP_005466

Alternative sequence

703 – 823

121

DKDEC…GRFCG → VLEGAGDRHSHLSGLELLLC PHALVDTVPAPPSALHGDTH AHTHTHVHTHCPIAQETCRG PPLGASRLSPQGPGHLTLAP QEGSYLDFWDTHRGDPKPRR RRKSLKTFSLTPATFRGIWA L in isoform BMP1-7.

VSP_005469

Alternative sequence

703 – 730

28

DKDEC…ECQCR → EKRPALQPPRGRPHQLKFRV QKRNRTPQ in isoform BMP1-1.

VSP_005461

Alternative sequence

703 – 717

15

DKDEC…GCQQD → GGELFGLLGHPPRRP in isoform BMP1-6.

VSP_005467

Alternative sequence

718 – 986

269

Missing in isoform BMP1-6.

VSP_005468

Alternative sequence

731 – 986

256

Missing in isoform BMP1-1.

VSP_005462

Alternative sequence

824 – 986

163

Missing in isoform BMP1-7.

VSP_005470

Natural variant

45

1

D → H in a breast cancer sample; somatic mutation. Ref.10

VAR_036141

Natural variant

719

1

V → I. [dbSNP:rs11996036]

VAR_051584

Experimental info

Sequence conflict

748

1

D → N Ref.4

Sequence conflict

934

1

R → S Ref.4

Secondary structure

1

.

.

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.

.

.

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.

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.

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986

Helix Strand Turn

Details...

Helix

126 – 128

3

Beta strand

135 – 138

4

Helix

147 – 161

15

Beta strand

166 – 168

3

Beta strand

176 – 180

5

Beta strand

197 – 201

5

Helix

211 – 214

4

Helix

224 – 226

3

Helix

230 – 232

3

Beta strand

234 – 236

3

Helix

238 – 240

3

Helix

246 – 249

4

Helix

254 – 256

3

Turn

274 – 277

4

Beta strand

285 – 290

6

Helix

310 – 316

7

SequencesHide

	Sequence		Length	Mass (Da)
	Isoform BMP1-3 [UniParc]. Last modified February 21, 2001. Version 2. Checksum: F89201913AC3CBEA	FASTA	986	111,249
	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
	Isoform BMP1-1. Checksum: E506D63729A9E86D	FASTA	730	82,900
	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 FSEKRPALQP PRGRPHQLKF 730 RVQKRNRTPQ
	Isoform BMP1-2 (Sequence not available).	FASTA	–	–
	Isoform BMP1-4. Checksum: 9FCDE92B1F884B15	FASTA	302	33,424
	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 IQPGVLHSSL LLLSCGSRNG ASFPCSLESS THQALCWTGL FLRPSPFPRL PLAAPRTLRA GV
	Isoform BMP1-5. Checksum: A47CE9FD49D5A8D7	FASTA	622	70,469
	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 APDKRRCEGC YDLQVGKPLL 610 620 WDRHCFRLST HGPEMLGTAL RG
	Isoform BMP1-6. Checksum: AE07361E00A6A700	FASTA	717	81,082
	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 LHGKFCGSEK PEVITSQYNN MRVEFKSDNT VSKKGFKAHF FSGGELFGLL GHPPRRP
	Isoform BMP1-7. Checksum: 09148B0724B5F1A8	FASTA	823	92,655
	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 FSVLEGAGDR HSHLSGLELL 730 740 750 760 770 780 LCPHALVDTV PAPPSALHGD THAHTHTHVH THCPIAQETC RGPPLGASRL SPQGPGHLTL 790 800 810 820 APQEGSYLDF WDTHRGDPKP RRRRKSLKTF SLTPATFRGI WAL

ReferencesHide

	« Hide 'large scale' referencesShow '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]	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. , 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. , 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: 14702039] [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: 15489334] [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: 11283002] [Abstract] Cited for: DISULFIDE BOND AT 183-CYS--CYS-186.
[9]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed: 14759258] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[10]	"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. , 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.

Cross-referencesHide

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.
BC136679 mRNA. Translation: AAI36680.1.

IPI

IPI00009054.
IPI00014021.
IPI00218040.
IPI00218042.
IPI00218044.
IPI00218045.

PIR

BMHU1. A37278.
A58788.
B58788.

RefSeq

NP_001190.1.
NP_006120.1.

UniGene

Hs.1274

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3EDG	X-ray	1.27	A	121-321	[»]
3EDH	X-ray	1.25	A	121-321	[»]

SMR

P13497. Positions 443-702, 546-745, 598-855.

ModBase

Search...

Protein-protein interaction databases

IntAct

P13497. 4 interactions.

MINT

MINT-1394084.

STRING

P13497.

Protein family/group databases

MEROPS

M12.005.

PTM databases

PhosphoSite

P13497.

Proteomic databases

PeptideAtlas

P13497.

PRIDE

P13497.

Genome annotation databases

Ensembl

ENST00000306385; ENSP00000305714; ENSG00000168487; Homo sapiens. [Genome view]

GeneID

649.

KEGG

hsa:649.

UCSC

uc003xba.1. human.
uc003xbb.1. human.
uc003xbg.1. human.

Organism-specific databases

CTD

649.

GeneCards

GC08P022078.

H-InvDB

HIX0007366.

HGNC

HGNC:1067. BMP1.

HPA

HPA014572.

MIM

112264. gene.

PharmGKB

PA25377.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14114.

HOVERGEN

HBG004859.

InParanoid

P13497.

OMA

RWRGRPR.

OrthoDB

EOG9WSZVQ.

PhylomeDB

P13497.

Enzyme and pathway databases

BRENDA

3.4.24.19. 247.

Reactome

REACT_602. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

P13497.

Bgee

P13497.

CleanEx

HS_BMP1.

Genevestigator

P13497.

GermOnline

ENSG00000168487. Homo sapiens.

Family and domain databases

InterPro

IPR015446. BMP_1/tolloid-like.
IPR000859. CUB.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR000742. EGF_3.
IPR001881. EGF_Ca-bd.
IPR013091. EGF_Ca-bd_2.
IPR018097. EGF_Ca-bd_CS.
IPR001506. Peptidase_M12A.
IPR006026. Peptidase_Metallo.
[Graphical view]

Gene3D

G3DSA:2.60.120.290. CUB. 5 hits.

PANTHER

PTHR10127:SF71. BMP_1. 1 hit.

Pfam

PF01400. Astacin. 1 hit.
PF00431. CUB. 5 hits.
PF07645. EGF_CA. 2 hits.
[Graphical view]

PIRSF

PIRSF001199. BMP_1/tolloid-like. 1 hit.

PRINTS

PR00480. ASTACIN.

SMART

SM00042. CUB. 5 hits.
SM00179. EGF_CA. 2 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]

SUPFAM

SSF49854. CUB. 5 hits.

PROSITE

PS00010. 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]

ProtoNet

Search...

Other Resources

NextBio

2632.

PMAP-CutDB

P13497.

SOURCE

Search...

Entry informationHide

Entry name

BMP1_HUMAN

Accession

Primary (citable) accession number: P13497
Secondary accession number(s): A8K6F5 , B2RN46, 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:	July 13, 2010
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.