Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q13867 (BLMH_HUMAN)

Last modified June 16, 2009. Version 88. 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Bleomycin hydrolase
      Short name=BLM hydrolase
      Short name=BMH
      Short name=BH
    EC=3.4.22.40
Gene names
Name: BLMH
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length455 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B-aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity By similarity.

Catalytic activity

Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-aminoalanine, but also shows general aminopeptidase activity. The specificity varies somewhat with source, but amino acid arylamides of Met, Leu and Ala are preferred.

Subunit structure

Homohexamer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the peptidase C1 family.

Hide | Top

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm Ref.2

Traceable author statement. Source: ProtInc

nucleus Ref.2

Traceable author statement. Source: ProtInc

   Molecular functionaminopeptidase activity

Traceable author statement. Source: ProtInc

carboxypeptidase activity

Traceable author statement. Source: ProtInc

cysteine-type endopeptidase activity Ref.2

Traceable author statement. Source: ProtInc

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 455455Bleomycin hydrolase
PRO_0000050550

Sites

Active site731
Active site3721
Active site3961

Natural variations

Natural variant4431I → V Common polymorphism. dbSNP rs1050565. Ref.2 Ref.6
VAR_010896

Secondary structure

1 ....................................................................... 455
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q13867-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 577E86241EB0D460

FASTA45552,562
        10         20         30         40         50         60 
MSSSGLNSEK VAALIQKLNS DPQFVLAQNV GTTHDLLDIC LKRATVQRAQ HVFQHAVPQE 

        70         80         90        100        110        120 
GKPITNQKSS GRCWIFSCLN VMRLPFMKKL NIEEFEFSQS YLFFWDKVER CYFFLSAFVD 

       130        140        150        160        170        180 
TAQRKEPEDG RLVQFLLMNP ANDGGQWDML VNIVEKYGVI PKKCFPESYT TEATRRMNDI 

       190        200        210        220        230        240 
LNHKMREFCI RLRNLVHSGA TKGEISATQD VMMEEIFRVV CICLGNPPET FTWEYRDKDK 

       250        260        270        280        290        300 
NYQKIGPITP LEFYREHVKP LFNMEDKICL VNDPRPQHKY NKLYTVEYLS NMVGGRKTLY 

       310        320        330        340        350        360 
NNQPIDFLKK MVAASIKDGE AVWFGCDVGK HFNSKLGLSD MNLYDHELVF GVSLKNMNKA 

       370        380        390        400        410        420 
ERLTFGESLM THAMTFTAVS EKDDQDGAFT KWRVENSWGE DHGHKGYLCM TDEWFSEYVY 

       430        440        450 
EVVVDRKHVP EEVLAVLEQE PIILPAWDPM GALAE

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"Cloning and expression analysis of human bleomycin hydrolase, a cysteine proteinase involved in chemotherapy resistance."
Ferrando A.A., Velasco G., Campo E., Lopez-Otin C.
Cancer Res. 56:1746-1750(1996) [PubMed: 8620487] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Human bleomycin hydrolase: molecular cloning, sequencing, functional expression, and enzymatic characterization."
Broemme D., Rossi A.B., Smeekens S.P., Anderson D.C., Payan D.G.
Biochemistry 35:6706-6714(1996) [PubMed: 8639621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT VAL-443.
Tissue: Lung.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"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].
Tissue: Lymph.
[6]"Full-insert sequence of mapped XREF EST."
Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 292-455, VARIANT VAL-443.
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]"Crystal structure of human bleomycin hydrolase, a self-compartmentalizing cysteine protease."
O'Farrell P.A., Gonzalez F., Zheng W., Johnston S.A., Joshua-Tor L.
Structure 7:619-627(1999) [PubMed: 10404591] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

X92106 mRNA. Translation: CAA63078.1.
BT007018 mRNA. Translation: AAP35664.1.
AK223403 mRNA. Translation: BAD97123.1.
BC003616 mRNA. Translation: AAH03616.1.
AF091082 mRNA. Translation: AAC72951.1.
IPIIPI00219575.
RefSeqNP_000377.1.
UniGeneHs.371914

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1CB5X-ray2.59A/B/C2-454[»]
2CB5X-ray1.85A/B2-454[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ13867. 3 interactions.

Protein family/group databases

MEROPSC01.084.

PTM databases

PhosphoSiteQ13867.

Proteomic databases

PeptideAtlasQ13867.
PRIDEQ13867.

Genome annotation databases

EnsemblENSG00000108578. Homo sapiens. [Contig view]
GeneID642.
KEGGhsa:642.
NMPDRfig|9606.3.peg.13445.

Organism-specific databases

GeneCardsGC17M025599.
H-InvDBHIX0013682.
HGNCHGNC:1059. BLMH.
MIM602403. gene.
PharmGKBPA25370.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ13867.
HOVERGENQ13867.

Enzyme and pathway databases

BRENDA3.4.22.40. 247.

Gene expression databases

ArrayExpressQ13867.
BgeeQ13867.
CleanExHS_BLMH.
GermOnlineENSG00000108578. Homo sapiens.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR004134. Peptidase_C1B.
[Graphical view]
PANTHERPTHR10363. Peptidase_C1B. 1 hit.
PfamPF03051. Peptidase_C1_2. 1 hit.
[Graphical view]
PIRSFPIRSF005700. PepC. 1 hit.
PROSITEPS00640. THIOL_PROTEASE_ASN. False negative.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio2604.
SOURCESearch...

Hide | Top

Entry information

Entry nameBLMH_HUMAN
AccessionPrimary (citable) accession number: Q13867
Secondary accession number(s): Q53F86, Q9UER9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

Human chromosome 17

Human chromosome 17: 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents