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Q13867

- BLMH_HUMAN

UniProt

Q13867 - BLMH_HUMAN

Protein

Bleomycin hydrolase

Gene

BLMH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    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

    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-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.
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13867.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    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

    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: October 1, 2014
    This is version 141 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