Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q13867 (BLMH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bleomycin hydrolase

Short name=BH
Short name=BLM hydrolase
Short name=BMH
EC=3.4.22.40
Gene names
Name:BLMH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length455 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APPP05067-42EBI-718504,EBI-302641

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 455455Bleomycin hydrolase
PRO_0000050550

Sites

Active site731
Active site3721
Active site3961

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue3911N6-acetyllysine Ref.9

Natural variations

Natural variant4431I → V Common polymorphism. Ref.2 Ref.8
Corresponds to variant rs1050565 [ dbSNP | Ensembl ].
VAR_010896

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13867 [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

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] [Europe PMC] [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] [Europe PMC] [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]"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].
Tissue: Amygdala.
[5]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].
[6]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Lymph.
[8]"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.
[9]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X92106 mRNA. Translation: CAA63078.1.
BT007018 mRNA. Translation: AAP35664.1.
AK223403 mRNA. Translation: BAD97123.1.
AK312896 mRNA. Translation: BAG35743.1.
CH471159 Genomic DNA. Translation: EAW51224.1.
BC003616 mRNA. Translation: AAH03616.1.
AF091082 mRNA. Translation: AAC72951.1.
CCDSCCDS32604.1.
RefSeqNP_000377.1. NM_000386.3.
UniGeneHs.371914.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CB5X-ray2.59A/B/C2-454[»]
2CB5X-ray1.85A/B2-454[»]
ProteinModelPortalQ13867.
SMRQ13867. Positions 2-454.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107111. 25 interactions.
IntActQ13867. 11 interactions.
MINTMINT-1397729.
STRING9606.ENSP00000261714.

Protein family/group databases

MEROPSC01.084.

PTM databases

PhosphoSiteQ13867.

Proteomic databases

MaxQBQ13867.
PaxDbQ13867.
PeptideAtlasQ13867.
PRIDEQ13867.

Protocols and materials databases

DNASU642.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261714; ENSP00000261714; ENSG00000108578.
GeneID642.
KEGGhsa:642.
UCSCuc002hez.2. human.

Organism-specific databases

CTD642.
GeneCardsGC17M028575.
HGNCHGNC:1059. BLMH.
HPAHPA039548.
MIM602403. gene.
neXtProtNX_Q13867.
Orphanet364195. Resistance to bleomycine in the treatment of testicular cancer.
PharmGKBPA25370.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3579.
HOGENOMHOG000064089.
HOVERGENHBG002388.
InParanoidQ13867.
KOK01372.
OMAPVRWRVQ.
PhylomeDBQ13867.
TreeFamTF323372.

Enzyme and pathway databases

BRENDA3.4.22.40. 2681.
ReactomeREACT_6900. Immune System.
SABIO-RKQ13867.

Gene expression databases

BgeeQ13867.
CleanExHS_BLMH.
GenevestigatorQ13867.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR004134. Peptidase_C1B.
[Graphical view]
PANTHERPTHR10363. PTHR10363. 1 hit.
PfamPF03051. Peptidase_C1_2. 1 hit.
[Graphical view]
PIRSFPIRSF005700. PepC. 1 hit.
PROSITEPS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBLMH. human.
EvolutionaryTraceQ13867.
GeneWikiBleomycin_hydrolase.
BLMH.
GenomeRNAi642.
NextBio2604.
PROQ13867.
SOURCESearch...

Entry information

Entry nameBLMH_HUMAN
AccessionPrimary (citable) accession number: Q13867
Secondary accession number(s): B2R796, Q53F86, Q9UER9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 139 of the entry and version 1 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 17

Human chromosome 17: entries, gene names and cross-references to MIM