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Reviewed, UniProtKB/Swiss-Prot Q9BSE5 (SPEB_HUMAN)

Last modified July 22, 2008. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Agmatinase, mitochondrial
    EC=3.5.3.11
Alternative name(s):
    Agmatine ureohydrolase
      Short name=AUH
Gene names
Name: AGMAT
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Agmatine + H(2)O = putrescine + urea.

Cofactor

Manganese Potential.

Pathway

Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine (ADC route): step 1/1.

Subcellular location

Mitochondrion.

Tissue specificity

Highly expressed in liver and kidney. Also found in skeletal muscle, fetal liver, brain, testis, skin and the gastrointestinal tract.

Sequence similarities

Belongs to the arginase family. Agmatinase subfamily.

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Ontologies

Keywords

   Biological processPutrescine biosynthesis
Spermidine biosynthesis
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandManganese
Metal-binding
   Molecular functionHydrolase

Gene Ontology (GO)

None. [Check GOA]

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 352Agmatinase, mitochondrial

Sites

Metal binding1621Manganese 1 By similarity
Metal binding1851Manganese 1 By similarity
Metal binding1851Manganese 2 By similarity
Metal binding1871Manganese 2 By similarity
Metal binding1891Manganese 1 By similarity
Metal binding2761Manganese 1 By similarity
Metal binding2761Manganese 2 By similarity
Metal binding2781Manganese 2 By similarity

Natural variations

Natural variant1051G → R: dbSNP rs6429757.

Experimental info

Sequence conflict1401R → Q in AAL24446. Ref.1
Sequence conflict1451Y → C in BAB15633. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q9BSE5-1 [UniParc].

Last modified February 20, 2007. Version 2.
Checksum: 394738202353314A

FASTA35237,660
        10         20         30         40         50         60 
MLRLLASGCA RGPGPGVGAR PAAGLFHPGR RQSRQASDAP RNQPPSPEFV ARPVGVCSMM 

        70         80         90        100        110        120 
RLPVQTSPEG LDAAFIGVPL DTGTSNRPGA RFGPRRIREE SVMLGTVNPS TGALPFQSLM 

       130        140        150        160        170        180 
VADLGDVNVN LYNLQDSCRR IQEAYEKIVA AGCIPLTLGG DHTITYPILQ AMAKKHGPVG 

       190        200        210        220        230        240 
LLHVDAHTDT TDKALGEKLY HGAPFRRCVD EGLLDCKRVV QIGIRGSSTT LDPYRYNRSQ 

       250        260        270        280        290        300 
GFRVVLAEDC WMKSLVPLMG EVRQQMGGKP IYISFDIDAL DPAYAPGTGT PEIAGLTPSQ 

       310        320        330        340        350 
ALEIIRGCQG LNVMGCDLVE VSPPYDLSGN TALLAANLLF EMLCALPKVT TV

« Hide

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References

« Hide 'large scale' references
[1]"Cloning of human agmatinase. An alternate path for polyamine synthesis induced in liver by hepatitis B virus."
Mistry S.K., Burwell T.J., Chambers R.M., Rudolph-Owen L., Spaltmann F., Cook W.J., Morris S.M. Jr.
Am. J. Physiol. 282:G375-G381(2002) [PubMed: 11804860] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-105, TISSUE SPECIFICITY.
Tissue: Kidney.
[2]"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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-105.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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], VARIANT ARG-105.
Tissue: Ovary.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AY057097 mRNA. Translation: AAL24446.1.
AK027037 mRNA. Translation: BAB15633.1.
AL121992 Genomic DNA. Translation: CAI22366.1.
BC005090 mRNA. Translation: AAH05090.1.
RefSeqNP_079034.3.
UniGeneHs.567583

3D structure databases

HSSPHSSP built from PDB template 1GQ6 based on UniProtKB P37819.
ModBaseSearch...

PTM databases

PhosphoSiteQ9BSE5.

Proteomic databases

PeptideAtlasQ9BSE5.

Genome annotation databases

EnsemblENSG00000116771. Homo sapiens. [Contig view]
GeneID79814.
KEGGhsa:79814.
NMPDRfig|9606.3.peg.360.

Organism-specific databases

H-InvDBHIX0000155.
HGNCHGNC:18407. AGMAT.
PharmGKBPA24619.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMQ9BSE5.
HOVERGENQ9BSE5.

Gene expression databases

ArrayExpressQ9BSE5.
CleanExHS_AGMAT.
GermOnlineENSG00000116771. Homo sapiens.

Family and domain databases

InterProIPR005925. Agmatinase.
IPR005924. Arginase.
IPR006035. Ureohydrolase.
[Graphical view]
Gene3DG3DSA:3.40.800.10. Ureohydrolase. 1 hit.
PANTHERPTHR11358. Ureohydrolase. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PRINTSPR00116. ARGINASE.
TIGRFAMsTIGR01230. agmatinase. 1 hit.
PROSITEPS00147. ARGINASE_1. 1 hit.
PS00148. ARGINASE_2. 1 hit.
PS01053. ARGINASE_3. 1 hit.
[Graphical view]
ProDomQ9BSE5.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

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Entry information

Entry nameSPEB_HUMAN
AccessionPrimary (citable) accession number: Q9BSE5
Secondary accession number(s): Q5TDH1, Q9H5J3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: February 20, 2007
Last modified: July 22, 2008
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

PATHWAY comments

Index of metabolic and biosynthesis pathways

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents