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Q13867

- BLMH_HUMAN

UniProt

Q13867 - BLMH_HUMAN

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Protein

Bleomycin hydrolase

Gene
BLMH
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. aminopeptidase activity Source: ProtInc
  2. carboxypeptidase activity Source: ProtInc
  3. cysteine-type endopeptidase activity Source: ProtInc
  4. cysteine-type peptidase activity Source: ProtInc
  5. protein binding Source: IntAct

GO - Biological processi

  1. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  2. protein polyubiquitination Source: Reactome
  3. proteolysis Source: ProtInc
  4. response to drug Source: Ensembl
  5. response to toxic substance Source: Ensembl
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: Chromosome 17

Organism-specific databases

HGNCiHGNC:1059. BLMH.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

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

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-acetylmethionine By 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.
GenevestigatoriQ13867.

Organism-specific databases

HPAiHPA039548.

Interactioni

Subunit structurei

Homohexamer.

Binary interactionsi

WithEntry#Exp.IntActNotes
APPP05067-42EBI-718504,EBI-302641

Protein-protein interaction databases

BioGridi107111. 25 interactions.
IntActiQ13867. 11 interactions.
MINTiMINT-1397729.
STRINGi9606.ENSP00000261714.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ13867.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.

Phylogenomic databases

eggNOGiCOG3579.
HOGENOMiHOG000064089.
HOVERGENiHBG002388.
InParanoidiQ13867.
KOiK01372.
OMAiPVRWRVQ.
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

MSSSGLNSEK VAALIQKLNS DPQFVLAQNV GTTHDLLDIC LKRATVQRAQ    50
HVFQHAVPQE GKPITNQKSS GRCWIFSCLN VMRLPFMKKL NIEEFEFSQS 100
YLFFWDKVER CYFFLSAFVD TAQRKEPEDG RLVQFLLMNP ANDGGQWDML 150
VNIVEKYGVI PKKCFPESYT TEATRRMNDI LNHKMREFCI RLRNLVHSGA 200
TKGEISATQD VMMEEIFRVV CICLGNPPET FTWEYRDKDK NYQKIGPITP 250
LEFYREHVKP LFNMEDKICL VNDPRPQHKY NKLYTVEYLS NMVGGRKTLY 300
NNQPIDFLKK MVAASIKDGE AVWFGCDVGK HFNSKLGLSD MNLYDHELVF 350
GVSLKNMNKA ERLTFGESLM THAMTFTAVS EKDDQDGAFT KWRVENSWGE 400
DHGHKGYLCM TDEWFSEYVY EVVVDRKHVP EEVLAVLEQE PIILPAWDPM 450
GALAE 455
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS32604.1.
RefSeqi NP_000377.1. NM_000386.3.
UniGenei Hs.371914.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CB5 X-ray 2.59 A/B/C 2-454 [» ]
2CB5 X-ray 1.85 A/B 2-454 [» ]
ProteinModelPortali Q13867.
SMRi Q13867. Positions 2-454.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107111. 25 interactions.
IntActi Q13867. 11 interactions.
MINTi MINT-1397729.
STRINGi 9606.ENSP00000261714.

Protein family/group databases

MEROPSi C01.084.

PTM databases

PhosphoSitei Q13867.

Proteomic databases

MaxQBi Q13867.
PaxDbi Q13867.
PeptideAtlasi Q13867.
PRIDEi Q13867.

Protocols and materials databases

DNASUi 642.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261714 ; ENSP00000261714 ; ENSG00000108578 .
GeneIDi 642.
KEGGi hsa:642.
UCSCi uc002hez.2. human.

Organism-specific databases

CTDi 642.
GeneCardsi GC17M028575.
HGNCi HGNC:1059. BLMH.
HPAi HPA039548.
MIMi 602403. gene.
neXtProti NX_Q13867.
Orphaneti 364195. Resistance to bleomycine in the treatment of testicular cancer.
PharmGKBi PA25370.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3579.
HOGENOMi HOG000064089.
HOVERGENi HBG002388.
InParanoidi Q13867.
KOi K01372.
OMAi PVRWRVQ.
PhylomeDBi Q13867.
TreeFami TF323372.

Enzyme and pathway databases

BRENDAi 3.4.22.40. 2681.
Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SABIO-RK Q13867.

Miscellaneous databases

ChiTaRSi BLMH. human.
EvolutionaryTracei Q13867.
GeneWikii Bleomycin_hydrolase.
BLMH.
GenomeRNAii 642.
NextBioi 2604.
PROi Q13867.
SOURCEi Search...

Gene expression databases

Bgeei Q13867.
CleanExi HS_BLMH.
Genevestigatori Q13867.

Family and domain databases

InterProi IPR000169. Pept_cys_AS.
IPR004134. Peptidase_C1B.
[Graphical view ]
PANTHERi PTHR10363. PTHR10363. 1 hit.
Pfami PF03051. Peptidase_C1_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF005700. PepC. 1 hit.
PROSITEi PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 140 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

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