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Q9BSE5 (SPEB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Agmatinase, mitochondrial

EC=3.5.3.11
Alternative name(s):
Agmatine ureohydrolase
Short name=AUH
Gene names
Name:AGMAT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Catalytic activity

Agmatine + H2O = putrescine + urea. Ref.5

Cofactor

Manganese Potential.

Pathway

Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: 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. Within brain, expression is higher in the cerebral cortex with lower levels in the medulla and spinal cord. Ref.1 Ref.5

Sequence similarities

Belongs to the arginase family. Agmatinase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Mitochondrion Potential
Chain36 – 352317Agmatinase, mitochondrial
PRO_0000002089

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

Amino acid modifications

Modified residue1931N6-acetyllysine By similarity
Modified residue2171N6-acetyllysine; alternate By similarity
Modified residue2171N6-succinyllysine; alternate By similarity

Natural variations

Natural variant1051G → R. Ref.1 Ref.2 Ref.4
Corresponds to variant rs6429757 [ dbSNP | Ensembl ].
VAR_023485
Natural variant1401R → Q. Ref.1
Corresponds to variant rs11580170 [ dbSNP | Ensembl ].
VAR_048332

Experimental info

Sequence conflict1451Y → C in BAB15633. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9BSE5 [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

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS ARG-105 AND GLN-140.
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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-105.
Tissue: Ovary.
[5]"Cloning and characterization of human agmatinase."
Iyer R.K., Kim H.K., Tsoa R.W., Grody W.W., Cederbaum S.D.
Mol. Genet. Metab. 75:209-218(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY057097 mRNA. Translation: AAL24446.1.
AK027037 mRNA. Translation: BAB15633.1.
AL121992 Genomic DNA. Translation: CAI22366.1.
BC005090 mRNA. Translation: AAH05090.1.
CCDSCCDS160.1.
RefSeqNP_079034.3. NM_024758.4.
UniGeneHs.461532.

3D structure databases

ProteinModelPortalQ9BSE5.
SMRQ9BSE5. Positions 42-349.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122909. 10 interactions.
STRING9606.ENSP00000364986.

PTM databases

PhosphoSiteQ9BSE5.

Polymorphism databases

DMDM126302602.

Proteomic databases

MaxQBQ9BSE5.
PaxDbQ9BSE5.
PeptideAtlasQ9BSE5.
PRIDEQ9BSE5.

Protocols and materials databases

DNASU79814.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375826; ENSP00000364986; ENSG00000116771.
GeneID79814.
KEGGhsa:79814.
UCSCuc001awv.2. human.

Organism-specific databases

CTD79814.
GeneCardsGC01M015898.
H-InvDBHIX0000155.
HGNCHGNC:18407. AGMAT.
HPAHPA026443.
HPA028321.
neXtProtNX_Q9BSE5.
PharmGKBPA24619.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0010.
HOGENOMHOG000204320.
HOVERGENHBG023165.
InParanoidQ9BSE5.
KOK01480.
OMASPPYDPF.
OrthoDBEOG7M98GH.
PhylomeDBQ9BSE5.
TreeFamTF328612.

Enzyme and pathway databases

BioCycMetaCyc:HS04051-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00534; UER00287.

Gene expression databases

BgeeQ9BSE5.
CleanExHS_AGMAT.
GenevestigatorQ9BSE5.

Family and domain databases

Gene3D3.40.800.10. 1 hit.
InterProIPR005925. Agmatinase-rel.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERPTHR11358. PTHR11358. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFPIRSF036979. Arginase. 1 hit.
PRINTSPR00116. ARGINASE.
TIGRFAMsTIGR01230. agmatinase. 1 hit.
PROSITEPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiAgmatinase.
GenomeRNAi79814.
NextBio69414.
PROQ9BSE5.

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 9, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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