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Q9BSE5

- SPEB_HUMAN

UniProt

Q9BSE5 - SPEB_HUMAN

Protein

Agmatinase, mitochondrial

Gene

AGMAT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (20 Feb 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Agmatine + H2O = putrescine + urea.1 Publication

    Cofactori

    Manganese.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi162 – 1621Manganese 1PROSITE-ProRule annotation
    Metal bindingi185 – 1851Manganese 1PROSITE-ProRule annotation
    Metal bindingi185 – 1851Manganese 2PROSITE-ProRule annotation
    Metal bindingi187 – 1871Manganese 2PROSITE-ProRule annotation
    Metal bindingi189 – 1891Manganese 1PROSITE-ProRule annotation
    Metal bindingi276 – 2761Manganese 1PROSITE-ProRule annotation
    Metal bindingi276 – 2761Manganese 2PROSITE-ProRule annotation
    Metal bindingi278 – 2781Manganese 2PROSITE-ProRule annotation

    GO - Molecular functioni

    1. agmatinase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. agmatine biosynthetic process Source: Reactome
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. polyamine metabolic process Source: Reactome
    4. putrescine biosynthetic process from arginine Source: UniProtKB-UniPathway
    5. small molecule metabolic process Source: Reactome
    6. spermidine biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Putrescine biosynthesis, Spermidine biosynthesis

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04051-MONOMER.
    ReactomeiREACT_14800. Agmatine biosynthesis.
    UniPathwayiUPA00534; UER00287.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Agmatinase, mitochondrial (EC:3.5.3.11)
    Alternative name(s):
    Agmatine ureohydrolase
    Short name:
    AUH
    Gene namesi
    Name:AGMAT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:18407. AGMAT.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrion Source: Reactome

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24619.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3535MitochondrionSequence AnalysisAdd
    BLAST
    Chaini36 – 352317Agmatinase, mitochondrialPRO_0000002089Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei193 – 1931N6-acetyllysineBy similarity
    Modified residuei217 – 2171N6-acetyllysine; alternateBy similarity
    Modified residuei217 – 2171N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9BSE5.
    PaxDbiQ9BSE5.
    PeptideAtlasiQ9BSE5.
    PRIDEiQ9BSE5.

    PTM databases

    PhosphoSiteiQ9BSE5.

    Expressioni

    Tissue specificityi

    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.2 Publications

    Gene expression databases

    BgeeiQ9BSE5.
    CleanExiHS_AGMAT.
    GenevestigatoriQ9BSE5.

    Organism-specific databases

    HPAiHPA026443.
    HPA028321.

    Interactioni

    Protein-protein interaction databases

    BioGridi122909. 10 interactions.
    STRINGi9606.ENSP00000364986.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BSE5.
    SMRiQ9BSE5. Positions 42-349.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the arginase family. Agmatinase subfamily.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0010.
    HOGENOMiHOG000204320.
    HOVERGENiHBG023165.
    InParanoidiQ9BSE5.
    KOiK01480.
    OMAiSPPYDPF.
    OrthoDBiEOG7M98GH.
    PhylomeDBiQ9BSE5.
    TreeFamiTF328612.

    Family and domain databases

    Gene3Di3.40.800.10. 1 hit.
    InterProiIPR005925. Agmatinase-rel.
    IPR006035. Ureohydrolase.
    IPR023696. Ureohydrolase_domain.
    IPR020855. Ureohydrolase_Mn_BS.
    [Graphical view]
    PANTHERiPTHR11358. PTHR11358. 1 hit.
    PfamiPF00491. Arginase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036979. Arginase. 1 hit.
    PRINTSiPR00116. ARGINASE.
    TIGRFAMsiTIGR01230. agmatinase. 1 hit.
    PROSITEiPS01053. ARGINASE_1. 1 hit.
    PS51409. ARGINASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9BSE5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRLLASGCA RGPGPGVGAR PAAGLFHPGR RQSRQASDAP RNQPPSPEFV    50
    ARPVGVCSMM RLPVQTSPEG LDAAFIGVPL DTGTSNRPGA RFGPRRIREE 100
    SVMLGTVNPS TGALPFQSLM VADLGDVNVN LYNLQDSCRR IQEAYEKIVA 150
    AGCIPLTLGG DHTITYPILQ AMAKKHGPVG LLHVDAHTDT TDKALGEKLY 200
    HGAPFRRCVD EGLLDCKRVV QIGIRGSSTT LDPYRYNRSQ GFRVVLAEDC 250
    WMKSLVPLMG EVRQQMGGKP IYISFDIDAL DPAYAPGTGT PEIAGLTPSQ 300
    ALEIIRGCQG LNVMGCDLVE VSPPYDLSGN TALLAANLLF EMLCALPKVT 350
    TV 352
    Length:352
    Mass (Da):37,660
    Last modified:February 20, 2007 - v2
    Checksum:i394738202353314A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti145 – 1451Y → C in BAB15633. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti105 – 1051G → R.3 Publications
    Corresponds to variant rs6429757 [ dbSNP | Ensembl ].
    VAR_023485
    Natural varianti140 – 1401R → Q.1 Publication
    Corresponds to variant rs11580170 [ dbSNP | Ensembl ].
    VAR_048332

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY057097 mRNA. Translation: AAL24446.1.
    AK027037 mRNA. Translation: BAB15633.1.
    AL121992 Genomic DNA. Translation: CAI22366.1.
    BC005090 mRNA. Translation: AAH05090.1.
    CCDSiCCDS160.1.
    RefSeqiNP_079034.3. NM_024758.4.
    UniGeneiHs.461532.

    Genome annotation databases

    EnsembliENST00000375826; ENSP00000364986; ENSG00000116771.
    GeneIDi79814.
    KEGGihsa:79814.
    UCSCiuc001awv.2. human.

    Polymorphism databases

    DMDMi126302602.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY057097 mRNA. Translation: AAL24446.1 .
    AK027037 mRNA. Translation: BAB15633.1 .
    AL121992 Genomic DNA. Translation: CAI22366.1 .
    BC005090 mRNA. Translation: AAH05090.1 .
    CCDSi CCDS160.1.
    RefSeqi NP_079034.3. NM_024758.4.
    UniGenei Hs.461532.

    3D structure databases

    ProteinModelPortali Q9BSE5.
    SMRi Q9BSE5. Positions 42-349.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122909. 10 interactions.
    STRINGi 9606.ENSP00000364986.

    PTM databases

    PhosphoSitei Q9BSE5.

    Polymorphism databases

    DMDMi 126302602.

    Proteomic databases

    MaxQBi Q9BSE5.
    PaxDbi Q9BSE5.
    PeptideAtlasi Q9BSE5.
    PRIDEi Q9BSE5.

    Protocols and materials databases

    DNASUi 79814.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375826 ; ENSP00000364986 ; ENSG00000116771 .
    GeneIDi 79814.
    KEGGi hsa:79814.
    UCSCi uc001awv.2. human.

    Organism-specific databases

    CTDi 79814.
    GeneCardsi GC01M015898.
    H-InvDB HIX0000155.
    HGNCi HGNC:18407. AGMAT.
    HPAi HPA026443.
    HPA028321.
    neXtProti NX_Q9BSE5.
    PharmGKBi PA24619.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0010.
    HOGENOMi HOG000204320.
    HOVERGENi HBG023165.
    InParanoidi Q9BSE5.
    KOi K01480.
    OMAi SPPYDPF.
    OrthoDBi EOG7M98GH.
    PhylomeDBi Q9BSE5.
    TreeFami TF328612.

    Enzyme and pathway databases

    UniPathwayi UPA00534 ; UER00287 .
    BioCyci MetaCyc:HS04051-MONOMER.
    Reactomei REACT_14800. Agmatine biosynthesis.

    Miscellaneous databases

    GeneWikii Agmatinase.
    GenomeRNAii 79814.
    NextBioi 69414.
    PROi Q9BSE5.

    Gene expression databases

    Bgeei Q9BSE5.
    CleanExi HS_AGMAT.
    Genevestigatori Q9BSE5.

    Family and domain databases

    Gene3Di 3.40.800.10. 1 hit.
    InterProi IPR005925. Agmatinase-rel.
    IPR006035. Ureohydrolase.
    IPR023696. Ureohydrolase_domain.
    IPR020855. Ureohydrolase_Mn_BS.
    [Graphical view ]
    PANTHERi PTHR11358. PTHR11358. 1 hit.
    Pfami PF00491. Arginase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036979. Arginase. 1 hit.
    PRINTSi PR00116. ARGINASE.
    TIGRFAMsi TIGR01230. agmatinase. 1 hit.
    PROSITEi PS01053. ARGINASE_1. 1 hit.
    PS51409. ARGINASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSPEB_HUMAN
    AccessioniPrimary (citable) accession number: Q9BSE5
    Secondary accession number(s): Q5TDH1, Q9H5J3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: February 20, 2007
    Last modified: October 1, 2014
    This is version 121 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3