Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bleomycin hydrolase

Gene

Blmh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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 – 731PROSITE-ProRule annotation
Active sitei372 – 3721PROSITE-ProRule annotation
Active sitei396 – 3961PROSITE-ProRule annotation

GO - Molecular functioni

  • cysteine-type endopeptidase activity Source: InterPro
  • peptidase activity Source: MGI

GO - Biological processi

  • response to drug Source: MGI
  • response to toxic substance Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.40. 3474.
ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1345186. Blmh.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 455455Bleomycin hydrolasePRO_0000050551Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8R016.
MaxQBiQ8R016.
PaxDbiQ8R016.
PRIDEiQ8R016.

PTM databases

iPTMnetiQ8R016.
PhosphoSiteiQ8R016.
SwissPalmiQ8R016.

Expressioni

Gene expression databases

BgeeiQ8R016.
CleanExiMM_BLMH.
ExpressionAtlasiQ8R016. baseline and differential.
GenevisibleiQ8R016. MM.

Interactioni

Subunit structurei

Homohexamer.By similarity

Protein-protein interaction databases

IntActiQ8R016. 2 interactions.
MINTiMINT-2514591.
STRINGi10090.ENSMUSP00000021197.

Structurei

3D structure databases

ProteinModelPortaliQ8R016.
SMRiQ8R016. Positions 2-454.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4128. Eukaryota.
COG3579. LUCA.
GeneTreeiENSGT00390000001735.
HOGENOMiHOG000064089.
HOVERGENiHBG002388.
InParanoidiQ8R016.
KOiK01372.
OMAiKLYTVDY.
PhylomeDBiQ8R016.
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.

Q8R016-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNAGLNSEK VSALIQKLNS DPQFVLAQNV GTTHDLLDIC LRRATVQGAQ
60 70 80 90 100
HVFQHVVPQE GKPVTNQKSS GRCWIFSCLN VMRLPFMKKF NIEEFEFSQS
110 120 130 140 150
YLFFWDKVER CYFFLNAFVD TAQKKEPEDG RLVQYLLMNP TNDGGQWDML
160 170 180 190 200
VNIVEKYGVV PKKCFPESHT TEATRRMNDI LNHKMREFCI RLRNLVHSGA
210 220 230 240 250
TKGEISSTQD AMMEEIFRVV CICLGNPPET FTWEYRDKDK NYHKIGPITP
260 270 280 290 300
LQFYKEHVKP LFNMEDKICF VNDPRPQHKY NKLYTVDYLS NMVGGRKTLY
310 320 330 340 350
NNQPIDFLKK MVAASIKDGE AVWFGCDVGK HFNGKLGLSD MNVYDHELVF
360 370 380 390 400
GVSLKNMNKA ERLAFGESLM THAMTFTAVS EKDNQEGTFV KWRVENSWGE
410 420 430 440 450
DHGHKGYLCM TDEWFSEYVY EVVVDKKHVP EEVLAVLEQE PIVLPAWDPM

GALAE
Length:455
Mass (Da):52,511
Last modified:June 1, 2002 - v1
Checksum:i032F3B1DA1AD5063
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161Q → K in BAC28989 (PubMed:16141072).Curated
Sequence conflicti151 – 1511V → A in AAH24090 (PubMed:15489334).Curated
Sequence conflicti391 – 3911K → R in BAC30706 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK035228 mRNA. Translation: BAC28989.1.
AK040799 mRNA. Translation: BAC30706.1.
AK051441 mRNA. Translation: BAC34639.1.
AK053872 mRNA. Translation: BAC35568.1.
AK150438 mRNA. Translation: BAE29560.1.
AK167325 mRNA. Translation: BAE39427.1.
AL603842 Genomic DNA. Translation: CAI35070.1.
BC024090 mRNA. Translation: AAH24090.1.
BC027037 mRNA. Translation: AAH27037.1.
BC027362 mRNA. Translation: AAH27362.1.
BC027403 mRNA. Translation: AAH27403.1.
CCDSiCCDS25073.1.
RefSeqiNP_848760.1. NM_178645.4.
UniGeneiMm.399785.

Genome annotation databases

EnsembliENSMUST00000021197; ENSMUSP00000021197; ENSMUSG00000020840.
GeneIDi104184.
KEGGimmu:104184.
UCSCiuc007kge.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK035228 mRNA. Translation: BAC28989.1.
AK040799 mRNA. Translation: BAC30706.1.
AK051441 mRNA. Translation: BAC34639.1.
AK053872 mRNA. Translation: BAC35568.1.
AK150438 mRNA. Translation: BAE29560.1.
AK167325 mRNA. Translation: BAE39427.1.
AL603842 Genomic DNA. Translation: CAI35070.1.
BC024090 mRNA. Translation: AAH24090.1.
BC027037 mRNA. Translation: AAH27037.1.
BC027362 mRNA. Translation: AAH27362.1.
BC027403 mRNA. Translation: AAH27403.1.
CCDSiCCDS25073.1.
RefSeqiNP_848760.1. NM_178645.4.
UniGeneiMm.399785.

3D structure databases

ProteinModelPortaliQ8R016.
SMRiQ8R016. Positions 2-454.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R016. 2 interactions.
MINTiMINT-2514591.
STRINGi10090.ENSMUSP00000021197.

Protein family/group databases

MEROPSiC01.084.

PTM databases

iPTMnetiQ8R016.
PhosphoSiteiQ8R016.
SwissPalmiQ8R016.

Proteomic databases

EPDiQ8R016.
MaxQBiQ8R016.
PaxDbiQ8R016.
PRIDEiQ8R016.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021197; ENSMUSP00000021197; ENSMUSG00000020840.
GeneIDi104184.
KEGGimmu:104184.
UCSCiuc007kge.2. mouse.

Organism-specific databases

CTDi642.
MGIiMGI:1345186. Blmh.

Phylogenomic databases

eggNOGiKOG4128. Eukaryota.
COG3579. LUCA.
GeneTreeiENSGT00390000001735.
HOGENOMiHOG000064089.
HOVERGENiHBG002388.
InParanoidiQ8R016.
KOiK01372.
OMAiKLYTVDY.
PhylomeDBiQ8R016.
TreeFamiTF323372.

Enzyme and pathway databases

BRENDAi3.4.22.40. 3474.
ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiBlmh. mouse.
NextBioi356692.
PROiQ8R016.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R016.
CleanExiMM_BLMH.
ExpressionAtlasiQ8R016. baseline and differential.
GenevisibleiQ8R016. MM.

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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Aorta, Bone marrow, Embryonic spinal ganglion, Eye, Placenta and Urinary bladder.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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].
    Strain: C57BL/6J and FVB/N.
    Tissue: Liver, Mammary gland and Retina.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiBLMH_MOUSE
AccessioniPrimary (citable) accession number: Q8R016
Secondary accession number(s): Q3TJR8
, Q8BLZ4, Q8BZH9, Q8C111, Q8CID9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2002
Last modified: May 11, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.