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Reviewed, UniProtKB/Swiss-Prot P13497 (BMP1_HUMAN)

Last modified July 13, 2010. Version 129. 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 originHide

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) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
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Protein attributesHide

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)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.

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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.
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Sequence annotation (Features)Hide

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
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.10
VAR_036141
Natural variant7191V → I. [dbSNP:rs11996036]
VAR_051584

Experimental info

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

Secondary structure

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

Details...

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SequencesHide

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.

Checksum: E506D63729A9E86D
Show »

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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ReferencesHide

« 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]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: 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. 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-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.
IPIIPI00009054.
IPI00014021.
IPI00218040.
IPI00218042.
IPI00218044.
IPI00218045.
PIRBMHU1. A37278.
A58788.
B58788.
RefSeqNP_001190.1.
NP_006120.1.
UniGeneHs.1274

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EDGX-ray1.27A121-321[»]
3EDHX-ray1.25A121-321[»]
SMRP13497. Positions 443-702, 546-745, 598-855.
ModBaseSearch...

Protein-protein interaction databases

IntActP13497. 4 interactions.
MINTMINT-1394084.
STRINGP13497.

Protein family/group databases

MEROPSM12.005.

PTM databases

PhosphoSiteP13497.

Proteomic databases

PeptideAtlasP13497.
PRIDEP13497.

Genome annotation databases

EnsemblENST00000306385; ENSP00000305714; ENSG00000168487; Homo sapiens. [Genome view]
GeneID649.
KEGGhsa:649.
UCSCuc003xba.1. human.
uc003xbb.1. human.
uc003xbg.1. human.

Organism-specific databases

CTD649.
GeneCardsGC08P022078.
H-InvDBHIX0007366.
HGNCHGNC:1067. BMP1.
HPAHPA014572.
MIM112264. gene.
PharmGKBPA25377.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG14114.
HOVERGENHBG004859.
InParanoidP13497.
OMARWRGRPR.
OrthoDBEOG9WSZVQ.
PhylomeDBP13497.

Enzyme and pathway databases

BRENDA3.4.24.19. 247.
ReactomeREACT_602. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpressP13497.
BgeeP13497.
CleanExHS_BMP1.
GenevestigatorP13497.
GermOnlineENSG00000168487. Homo sapiens.

Family and domain databases

InterProIPR015446. 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]
Gene3DG3DSA:2.60.120.290. CUB. 5 hits.
PANTHERPTHR10127:SF71. BMP_1. 1 hit.
PfamPF01400. Astacin. 1 hit.
PF00431. CUB. 5 hits.
PF07645. EGF_CA. 2 hits.
[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. CUB. 5 hits.
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 informationHide

Entry nameBMP1_HUMAN
AccessionPrimary (citable) accession number: P13497
Secondary accession number(s): A8K6F5 expand/collapse secondary AC list , 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.
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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

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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