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Protein

Bleomycin hydrolase

Gene

BLMH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei73 – 731
Active sitei372 – 3721
Active sitei396 – 3961

GO - Molecular functioni

  • aminopeptidase activity Source: ProtInc
  • carboxypeptidase activity Source: ProtInc
  • cysteine-type endopeptidase activity Source: ProtInc
  • cysteine-type peptidase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.40. 2681.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SABIO-RKQ13867.

Protein family/group databases

MEROPSiC01.084.

Names & Taxonomyi

Protein namesi
Recommended name:
Bleomycin hydrolase (EC:3.4.22.40)
Short name:
BH
Short name:
BLM hydrolase
Short name:
BMH
Gene namesi
Name:BLMH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:1059. BLMH.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

Orphaneti364195. Resistance to bleomycine in the treatment of testicular cancer.
PharmGKBiPA25370.

Chemistry

DrugBankiDB00290. Bleomycin.

Polymorphism and mutation databases

BioMutaiBLMH.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 455455Bleomycin hydrolasePRO_0000050550Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei391 – 3911N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ13867.
PaxDbiQ13867.
PeptideAtlasiQ13867.
PRIDEiQ13867.

PTM databases

PhosphoSiteiQ13867.

Expressioni

Gene expression databases

BgeeiQ13867.
CleanExiHS_BLMH.
ExpressionAtlasiQ13867. baseline and differential.
GenevisibleiQ13867. HS.

Organism-specific databases

HPAiHPA039548.
HPA064307.

Interactioni

Subunit structurei

Homohexamer.

Binary interactionsi

WithEntry#Exp.IntActNotes
APPP05067-42EBI-718504,EBI-302641
NUDT12Q9BQG23EBI-718504,EBI-10230612
WDYHV1Q96HA83EBI-718504,EBI-741158

Protein-protein interaction databases

BioGridi107111. 26 interactions.
IntActiQ13867. 13 interactions.
MINTiMINT-1397729.
STRINGi9606.ENSP00000261714.

Structurei

Secondary structure

1
455
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Helixi8 – 1912Combined sources
Helixi22 – 3110Combined sources
Helixi36 – 405Combined sources
Helixi43 – 486Combined sources
Beta strandi54 – 563Combined sources
Beta strandi69 – 713Combined sources
Helixi73 – 8917Combined sources
Helixi99 – 12325Combined sources
Helixi131 – 1388Combined sources
Helixi147 – 15711Combined sources
Helixi162 – 1643Combined sources
Helixi170 – 1723Combined sources
Helixi175 – 19723Combined sources
Helixi202 – 22423Combined sources
Beta strandi229 – 2368Combined sources
Beta strandi242 – 2487Combined sources
Helixi250 – 2578Combined sources
Turni258 – 2614Combined sources
Helixi264 – 2663Combined sources
Beta strandi267 – 2715Combined sources
Beta strandi280 – 2867Combined sources
Beta strandi300 – 3023Combined sources
Helixi305 – 31713Combined sources
Beta strandi322 – 3265Combined sources
Turni328 – 3314Combined sources
Turni334 – 3374Combined sources
Helixi346 – 3505Combined sources
Helixi359 – 3646Combined sources
Beta strandi372 – 38110Combined sources
Beta strandi389 – 3957Combined sources
Beta strandi407 – 4115Combined sources
Helixi412 – 4187Combined sources
Beta strandi419 – 4257Combined sources
Helixi426 – 4283Combined sources
Helixi431 – 4344Combined sources
Helixi435 – 4384Combined sources
Beta strandi442 – 4443Combined sources
Helixi449 – 4513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CB5X-ray2.59A/B/C2-454[»]
2CB5X-ray1.85A/B2-454[»]
ProteinModelPortaliQ13867.
SMRiQ13867. Positions 2-454.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13867.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG3579.
GeneTreeiENSGT00390000001735.
HOGENOMiHOG000064089.
HOVERGENiHBG002388.
InParanoidiQ13867.
KOiK01372.
OMAiKLYTVDY.
PhylomeDBiQ13867.
TreeFamiTF323372.

Family and domain databases

InterProiIPR000169. Pept_cys_AS.
IPR004134. Peptidase_C1B.
[Graphical view]
PANTHERiPTHR10363. PTHR10363. 1 hit.
PfamiPF03051. Peptidase_C1_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005700. PepC. 1 hit.
PROSITEiPS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q13867-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSGLNSEK VAALIQKLNS DPQFVLAQNV GTTHDLLDIC LKRATVQRAQ
60 70 80 90 100
HVFQHAVPQE GKPITNQKSS GRCWIFSCLN VMRLPFMKKL NIEEFEFSQS
110 120 130 140 150
YLFFWDKVER CYFFLSAFVD TAQRKEPEDG RLVQFLLMNP ANDGGQWDML
160 170 180 190 200
VNIVEKYGVI PKKCFPESYT TEATRRMNDI LNHKMREFCI RLRNLVHSGA
210 220 230 240 250
TKGEISATQD VMMEEIFRVV CICLGNPPET FTWEYRDKDK NYQKIGPITP
260 270 280 290 300
LEFYREHVKP LFNMEDKICL VNDPRPQHKY NKLYTVEYLS NMVGGRKTLY
310 320 330 340 350
NNQPIDFLKK MVAASIKDGE AVWFGCDVGK HFNSKLGLSD MNLYDHELVF
360 370 380 390 400
GVSLKNMNKA ERLTFGESLM THAMTFTAVS EKDDQDGAFT KWRVENSWGE
410 420 430 440 450
DHGHKGYLCM TDEWFSEYVY EVVVDRKHVP EEVLAVLEQE PIILPAWDPM

GALAE
Length:455
Mass (Da):52,562
Last modified:November 1, 1996 - v1
Checksum:i577E86241EB0D460
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti443 – 4431I → V Common polymorphism. 2 Publications
Corresponds to variant rs1050565 [ dbSNP | Ensembl ].
VAR_010896

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32604.1.
RefSeqiNP_000377.1. NM_000386.3.
UniGeneiHs.371914.

Genome annotation databases

EnsembliENST00000261714; ENSP00000261714; ENSG00000108578.
GeneIDi642.
KEGGihsa:642.
UCSCiuc002hez.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32604.1.
RefSeqiNP_000377.1. NM_000386.3.
UniGeneiHs.371914.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CB5X-ray2.59A/B/C2-454[»]
2CB5X-ray1.85A/B2-454[»]
ProteinModelPortaliQ13867.
SMRiQ13867. Positions 2-454.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107111. 26 interactions.
IntActiQ13867. 13 interactions.
MINTiMINT-1397729.
STRINGi9606.ENSP00000261714.

Chemistry

DrugBankiDB00290. Bleomycin.

Protein family/group databases

MEROPSiC01.084.

PTM databases

PhosphoSiteiQ13867.

Polymorphism and mutation databases

BioMutaiBLMH.

Proteomic databases

MaxQBiQ13867.
PaxDbiQ13867.
PeptideAtlasiQ13867.
PRIDEiQ13867.

Protocols and materials databases

DNASUi642.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261714; ENSP00000261714; ENSG00000108578.
GeneIDi642.
KEGGihsa:642.
UCSCiuc002hez.2. human.

Organism-specific databases

CTDi642.
GeneCardsiGC17M028575.
HGNCiHGNC:1059. BLMH.
HPAiHPA039548.
HPA064307.
MIMi602403. gene.
neXtProtiNX_Q13867.
Orphaneti364195. Resistance to bleomycine in the treatment of testicular cancer.
PharmGKBiPA25370.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3579.
GeneTreeiENSGT00390000001735.
HOGENOMiHOG000064089.
HOVERGENiHBG002388.
InParanoidiQ13867.
KOiK01372.
OMAiKLYTVDY.
PhylomeDBiQ13867.
TreeFamiTF323372.

Enzyme and pathway databases

BRENDAi3.4.22.40. 2681.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SABIO-RKQ13867.

Miscellaneous databases

ChiTaRSiBLMH. human.
EvolutionaryTraceiQ13867.
GeneWikiiBleomycin_hydrolase.
BLMH.
GenomeRNAii642.
NextBioi2604.
PROiQ13867.
SOURCEiSearch...

Gene expression databases

BgeeiQ13867.
CleanExiHS_BLMH.
ExpressionAtlasiQ13867. baseline and differential.
GenevisibleiQ13867. HS.

Family and domain databases

InterProiIPR000169. Pept_cys_AS.
IPR004134. Peptidase_C1B.
[Graphical view]
PANTHERiPTHR10363. PTHR10363. 1 hit.
PfamiPF03051. Peptidase_C1_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005700. PepC. 1 hit.
PROSITEiPS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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).

Entry informationi

Entry nameiBLMH_HUMAN
AccessioniPrimary (citable) accession number: Q13867
Secondary accession number(s): B2R796, Q53F86, Q9UER9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.