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Q8R016 (BLMH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length455 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

response to drug

Inferred from mutant phenotype. Source: MGI

response to toxin

Inferred from mutant phenotype. Source: MGI

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

soluble fraction

Inferred from direct assay. Source: MGI

   Molecular functioncysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 455455Bleomycin hydrolase
PRO_0000050551

Sites

Active site731 By similarity
Active site3721 By similarity
Active site3961 By similarity

Amino acid modifications

Modified residue3911N6-acetyllysine By similarity

Experimental info

Sequence conflict161Q → K in BAC28989. Ref.1
Sequence conflict1511V → A in AAH24090. Ref.3
Sequence conflict3911K → R in BAC30706. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8R016 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 032F3B1DA1AD5063

FASTA45552,511
        10         20         30         40         50         60 
MNNAGLNSEK VSALIQKLNS DPQFVLAQNV GTTHDLLDIC LRRATVQGAQ HVFQHVVPQE 

        70         80         90        100        110        120 
GKPVTNQKSS GRCWIFSCLN VMRLPFMKKF NIEEFEFSQS YLFFWDKVER CYFFLNAFVD 

       130        140        150        160        170        180 
TAQKKEPEDG RLVQYLLMNP TNDGGQWDML VNIVEKYGVV PKKCFPESHT TEATRRMNDI 

       190        200        210        220        230        240 
LNHKMREFCI RLRNLVHSGA TKGEISSTQD AMMEEIFRVV CICLGNPPET FTWEYRDKDK 

       250        260        270        280        290        300 
NYHKIGPITP LQFYKEHVKP LFNMEDKICF VNDPRPQHKY NKLYTVDYLS NMVGGRKTLY 

       310        320        330        340        350        360 
NNQPIDFLKK MVAASIKDGE AVWFGCDVGK HFNGKLGLSD MNVYDHELVF GVSLKNMNKA 

       370        380        390        400        410        420 
ERLAFGESLM THAMTFTAVS EKDNQEGTFV KWRVENSWGE DHGHKGYLCM TDEWFSEYVY 

       430        440        450 
EVVVDKKHVP EEVLAVLEQE PIVLPAWDPM GALAE 

« Hide

References

[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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Aorta, Bone marrow, Embryonic spinal ganglion, Eye, Placenta and Urinary bladder.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6 and FVB/N.
Tissue: Liver, Mammary gland and Retina.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00153107.
RefSeqNP_848760.1. NM_178645.4.
UniGeneMm.399785.

3D structure databases

ProteinModelPortalQ8R016.
SMRQ8R016. Positions 2-454.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8R016.

Protein family/group databases

MEROPSC01.084.

PTM databases

PhosphoSiteQ8R016.

Proteomic databases

PRIDEQ8R016.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021197; ENSMUSP00000021197; ENSMUSG00000020840.
GeneID104184.
KEGGmmu:104184.
UCSCuc007kge.2. mouse.

Organism-specific databases

CTD642.
MGIMGI:1345186. Blmh.

Phylogenomic databases

eggNOGroNOG14490.
GeneTreeENSGT00390000001735.
HOGENOMHBG350935.
HOVERGENHBG002388.
InParanoidQ8R016.
OMAFVKWRVE.
OrthoDBEOG4J3WGT.
PhylomeDBQ8R016.

Enzyme and pathway databases

BRENDA3.4.22.40. 3474.

Gene expression databases

ArrayExpressQ8R016.
BgeeQ8R016.
CleanExMM_BLMH.
GenevestigatorQ8R016.
GermOnlineENSMUSG00000020840. Mus musculus.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR004134. Peptidase_C1B.
[Graphical view]
KOK01372.
PANTHERPTHR10363. Peptidase_C1B. 1 hit.
PfamPF03051. Peptidase_C1_2. 1 hit.
[Graphical view]
PIRSFPIRSF005700. PepC. 1 hit.
PROSITEPS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio356692.
SOURCESearch...

Entry information

Entry nameBLMH_MOUSE
AccessionPrimary (citable) accession number: Q8R016
Secondary accession number(s): Q3TJR8 expand/collapse secondary AC list , Q8BLZ4, Q8BZH9, Q8C111, Q8CID9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2002
Last modified: November 16, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families