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Q9H4A4

- AMPB_HUMAN

UniProt

Q9H4A4 - AMPB_HUMAN

Protein

Aminopeptidase B

Gene

RNPEP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (27 Mar 2002)
      Previous versions | rss
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    Functioni

    Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) By similarity.By similarity

    Catalytic activityi

    Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi325 – 3251Zinc; catalyticPROSITE-ProRule annotation
    Active sitei326 – 3261Proton acceptorPROSITE-ProRule annotation
    Metal bindingi329 – 3291Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi348 – 3481Zinc; catalyticPROSITE-ProRule annotation
    Sitei414 – 4141Transition state stabilizerBy similarity

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB
    2. epoxide hydrolase activity Source: UniProtKB
    3. metalloexopeptidase activity Source: UniProtKB
    4. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. leukotriene biosynthetic process Source: InterPro
    2. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM01.014.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aminopeptidase B (EC:3.4.11.6)
    Short name:
    AP-B
    Alternative name(s):
    Arginine aminopeptidase
    Arginyl aminopeptidase
    Gene namesi
    Name:RNPEP
    Synonyms:APB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10078. RNPEP.

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB
    2. extracellular space Source: InterPro
    3. extracellular vesicular exosome Source: UniProt
    4. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34451.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 650649Aminopeptidase BPRO_0000095088Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei7 – 71Phosphoserine2 Publications
    Modified residuei446 – 4461N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H4A4.
    PaxDbiQ9H4A4.
    PRIDEiQ9H4A4.

    PTM databases

    PhosphoSiteiQ9H4A4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9H4A4.
    BgeeiQ9H4A4.
    CleanExiHS_RNPEP.
    GenevestigatoriQ9H4A4.

    Organism-specific databases

    HPAiHPA036074.
    HPA036075.

    Interactioni

    Protein-protein interaction databases

    BioGridi111978. 5 interactions.
    IntActiQ9H4A4. 1 interaction.
    MINTiMINT-1182309.
    STRINGi9606.ENSP00000295640.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H4A4.
    SMRiQ9H4A4. Positions 8-643.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni298 – 3025Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Phylogenomic databases

    eggNOGiCOG0308.
    HOVERGENiHBG001274.
    InParanoidiQ9H4A4.
    KOiK01260.
    OMAiPPGNVKK.
    OrthoDBiEOG7SJD42.
    PhylomeDBiQ9H4A4.
    TreeFamiTF300758.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR015571. Pept_M1_aminopeptidase-B.
    IPR001930. Peptidase_M1.
    IPR015211. Peptidase_M1_C.
    IPR014782. Peptidase_M1_N.
    [Graphical view]
    PANTHERiPTHR11533. PTHR11533. 1 hit.
    PTHR11533:SF153. PTHR11533:SF153. 1 hit.
    PfamiPF09127. Leuk-A4-hydro_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view]
    PRINTSiPR00756. ALADIPTASE.
    SUPFAMiSSF48371. SSF48371. 1 hit.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9H4A4-1 [UniParc]FASTAAdd to Basket

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    MASGEHSPGS GAARRPLHSA QAVDVASASN FRAFELLHLH LDLRAEFGPP    50
    GPGAGSRGLS GTAVLDLRCL EPEGAAELRL DSHPCLEVTA AALRRERPGS 100
    EEPPAEPVSF YTQPFSHYGQ ALCVSFPQPC RAAERLQVLL TYRVGEGPGV 150
    CWLAPEQTAG KKKPFVYTQG QAVLNRAFFP CFDTPAVKYK YSALIEVPDG 200
    FTAVMSASTW EKRGPNKFFF QMCQPIPSYL IALAIGDLVS AEVGPRSRVW 250
    AEPCLIDAAK EEYNGVIEEF LATGEKLFGP YVWGRYDLLF MPPSFPFGGM 300
    ENPCLTFVTP CLLAGDRSLA DVIIHEISHS WFGNLVTNAN WGEFWLNEGF 350
    TMYAQRRIST ILFGAAYTCL EAATGRALLR QHMDITGEEN PLNKLRVKIE 400
    PGVDPDDTYN ETPYEKGFCF VSYLAHLVGD QDQFDSFLKA YVHEFKFRSI 450
    LADDFLDFYL EYFPELKKKR VDIIPGFEFD RWLNTPGWPP YLPDLSPGDS 500
    LMKPAEELAQ LWAAEELDMK AIEAVAISPW KTYQLVYFLD KILQKSPLPP 550
    GNVKKLGDTY PSISNARNAE LRLRWGQIVL KNDHQEDFWK VKEFLHNQGK 600
    QKYTLPLYHA MMGGSEVAQT LAKETFASTA SQLHSNVVNY VQQIVAPKGS 650
    Length:650
    Mass (Da):72,596
    Last modified:March 27, 2002 - v2
    Checksum:i4C04FE09689F2487
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21A → V in CAC14047. 1 PublicationCurated
    Sequence conflicti11 – 144GAAR → ARPGGRCTPRRL in CAC12957. 1 PublicationCurated
    Sequence conflicti149 – 1491G → R in CAC12957. 1 PublicationCurated
    Sequence conflicti153 – 1531L → V in CAC12957. 1 PublicationCurated
    Sequence conflicti208 – 2103STW → RPG in CAC12957. 1 PublicationCurated
    Sequence conflicti262 – 2621Missing in CAC12957. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti579 – 5791V → I.
    Corresponds to variant rs3820439 [ dbSNP | Ensembl ].
    VAR_051566

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ242586 mRNA. Translation: CAC12957.1.
    AJ296161 mRNA. Translation: CAC14047.1.
    BC001064 mRNA. Translation: AAH01064.1.
    BC012166 mRNA. Translation: AAH12166.1.
    AL390139 mRNA. Translation: CAB99087.1.
    CCDSiCCDS1418.1.
    PIRiT51870.
    RefSeqiNP_064601.3. NM_020216.3.
    XP_005245477.1. XM_005245420.1.
    XP_005245478.1. XM_005245421.1.
    UniGeneiHs.497391.

    Genome annotation databases

    EnsembliENST00000295640; ENSP00000295640; ENSG00000176393.
    GeneIDi6051.
    KEGGihsa:6051.
    UCSCiuc001gxd.3. human.

    Polymorphism databases

    DMDMi20137480.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ242586 mRNA. Translation: CAC12957.1 .
    AJ296161 mRNA. Translation: CAC14047.1 .
    BC001064 mRNA. Translation: AAH01064.1 .
    BC012166 mRNA. Translation: AAH12166.1 .
    AL390139 mRNA. Translation: CAB99087.1 .
    CCDSi CCDS1418.1.
    PIRi T51870.
    RefSeqi NP_064601.3. NM_020216.3.
    XP_005245477.1. XM_005245420.1.
    XP_005245478.1. XM_005245421.1.
    UniGenei Hs.497391.

    3D structure databases

    ProteinModelPortali Q9H4A4.
    SMRi Q9H4A4. Positions 8-643.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111978. 5 interactions.
    IntActi Q9H4A4. 1 interaction.
    MINTi MINT-1182309.
    STRINGi 9606.ENSP00000295640.

    Chemistry

    BindingDBi Q9H4A4.
    ChEMBLi CHEMBL2432.

    Protein family/group databases

    MEROPSi M01.014.

    PTM databases

    PhosphoSitei Q9H4A4.

    Polymorphism databases

    DMDMi 20137480.

    Proteomic databases

    MaxQBi Q9H4A4.
    PaxDbi Q9H4A4.
    PRIDEi Q9H4A4.

    Protocols and materials databases

    DNASUi 6051.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295640 ; ENSP00000295640 ; ENSG00000176393 .
    GeneIDi 6051.
    KEGGi hsa:6051.
    UCSCi uc001gxd.3. human.

    Organism-specific databases

    CTDi 6051.
    GeneCardsi GC01P201951.
    H-InvDB HIX0023896.
    HGNCi HGNC:10078. RNPEP.
    HPAi HPA036074.
    HPA036075.
    MIMi 602675. gene.
    neXtProti NX_Q9H4A4.
    PharmGKBi PA34451.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0308.
    HOVERGENi HBG001274.
    InParanoidi Q9H4A4.
    KOi K01260.
    OMAi PPGNVKK.
    OrthoDBi EOG7SJD42.
    PhylomeDBi Q9H4A4.
    TreeFami TF300758.

    Miscellaneous databases

    ChiTaRSi RNPEP. human.
    GeneWikii RNPEP.
    GenomeRNAii 6051.
    NextBioi 23595.
    PROi Q9H4A4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H4A4.
    Bgeei Q9H4A4.
    CleanExi HS_RNPEP.
    Genevestigatori Q9H4A4.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR015571. Pept_M1_aminopeptidase-B.
    IPR001930. Peptidase_M1.
    IPR015211. Peptidase_M1_C.
    IPR014782. Peptidase_M1_N.
    [Graphical view ]
    PANTHERi PTHR11533. PTHR11533. 1 hit.
    PTHR11533:SF153. PTHR11533:SF153. 1 hit.
    Pfami PF09127. Leuk-A4-hydro_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view ]
    PRINTSi PR00756. ALADIPTASE.
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human aminopeptidase B on chromosome 1q32.2: cDNA, genomic structure and expression."
      Piesse C., Tymms M., Garrafa E., Gouzy C., Lacasa M., Cadel S., Foulon T., Cohen P.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Human aminopeptidase B cDNA cloning."
      Kristensen T.
      Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    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].
      Tissue: Lung.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 291-650.
      Tissue: Brain.
    5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAMPB_HUMAN
    AccessioniPrimary (citable) accession number: Q9H4A4
    Secondary accession number(s): Q9BVM9, Q9H1D4, Q9NPT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: March 27, 2002
    Last modified: October 1, 2014
    This is version 129 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3