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P53582

- MAP11_HUMAN

UniProt

P53582 - MAP11_HUMAN

Protein

Methionine aminopeptidase 1

Gene

METAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (25 Jul 2003)
      Previous versions | rss
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    Functioni

    Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle.2 PublicationsUniRule annotation

    Catalytic activityi

    Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.1 PublicationUniRule annotation

    Cofactori

    Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.UniRule annotation
    Binds 1 sodium ion per subunit. The sodium ion has a structural role.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei203 – 2031Substrate
    Metal bindingi220 – 2201Divalent metal cation 1
    Metal bindingi231 – 2311Divalent metal cation 1
    Metal bindingi231 – 2311Divalent metal cation 2; catalytic
    Metal bindingi294 – 2941Divalent metal cation 2; catalytic; via tele nitrogen
    Binding sitei301 – 3011Substrate
    Metal bindingi327 – 3271Divalent metal cation 2; catalytic
    Metal bindingi358 – 3581Divalent metal cation 1
    Metal bindingi358 – 3581Divalent metal cation 2; catalytic

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-HAMAP
    3. metalloaminopeptidase activity Source: UniProtKB-HAMAP
    4. metalloexopeptidase activity Source: UniProtKB

    GO - Biological processi

    1. N-terminal protein amino acid modification Source: HGNC
    2. peptidyl-methionine modification Source: HGNC
    3. phototransduction, visible light Source: Reactome
    4. protein initiator methionine removal Source: UniProtKB-HAMAP
    5. regulation of rhodopsin mediated signaling pathway Source: Reactome
    6. regulation of translation Source: HGNC
    7. rhodopsin mediated signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    BRENDAi3.4.11.18. 2681.
    ReactomeiREACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
    SABIO-RKP53582.

    Protein family/group databases

    MEROPSiM24.017.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 1UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 1UniRule annotation
    Short name:
    MetAP 1UniRule annotation
    Alternative name(s):
    Peptidase M 1UniRule annotation
    Gene namesi
    Name:METAP1
    Synonyms:KIAA0094
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:15789. METAP1.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. cytosol Source: Reactome
    3. cytosolic ribosome Source: UniProtKB-HAMAP

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30764.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 386385Methionine aminopeptidase 1PRO_0000148967Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP53582.
    PaxDbiP53582.
    PeptideAtlasiP53582.
    PRIDEiP53582.

    PTM databases

    PhosphoSiteiP53582.

    Expressioni

    Gene expression databases

    ArrayExpressiP53582.
    BgeeiP53582.
    CleanExiHS_METAP1.
    GenevestigatoriP53582.

    Organism-specific databases

    HPAiCAB025485.

    Interactioni

    Subunit structurei

    Associates with the 60S ribosomal subunit of the 80S translational complex.UniRule annotation

    Protein-protein interaction databases

    BioGridi116785. 5 interactions.
    IntActiP53582. 1 interaction.
    MINTiMINT-1191219.
    STRINGi9606.ENSP00000296411.

    Structurei

    Secondary structure

    1
    386
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi84 – 863
    Helixi107 – 1104
    Helixi117 – 1215
    Turni122 – 1243
    Helixi133 – 15523
    Helixi163 – 17614
    Turni182 – 1854
    Helixi186 – 1883
    Beta strandi191 – 1977
    Beta strandi200 – 2023
    Beta strandi216 – 22510
    Beta strandi228 – 23710
    Helixi243 – 26119
    Helixi271 – 28212
    Beta strandi293 – 2953
    Beta strandi297 – 30610
    Beta strandi309 – 3113
    Beta strandi323 – 3264
    Beta strandi329 – 3335
    Beta strandi337 – 3393
    Beta strandi346 – 3483
    Beta strandi354 – 3563
    Beta strandi358 – 3636
    Beta strandi365 – 3706
    Helixi381 – 3833

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B3HX-ray1.10A81-384[»]
    2B3KX-ray1.55A81-384[»]
    2B3LX-ray1.50A81-384[»]
    2G6PX-ray1.90A81-384[»]
    2GZ5X-ray1.10A81-384[»]
    2NQ6X-ray1.50A81-384[»]
    2NQ7X-ray1.60A81-384[»]
    4FLIX-ray1.55A81-386[»]
    4FLJX-ray1.74A81-386[»]
    4FLKX-ray1.47A81-386[»]
    4FLLX-ray1.50A81-386[»]
    4HXXX-ray2.09A81-384[»]
    4IKRX-ray1.78A81-384[»]
    4IKSX-ray1.70A81-384[»]
    4IKTX-ray1.60A81-384[»]
    4IKUX-ray1.30A81-384[»]
    4IU6X-ray1.90A1-384[»]
    ProteinModelPortaliP53582.
    SMRiP53582. Positions 81-384.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53582.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni9 – 5244Zinc finger-like; important for proper ribosome associationUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000030427.
    HOVERGENiHBG067178.
    InParanoidiP53582.
    KOiK01265.
    OMAiMPGDRPL.
    OrthoDBiEOG786H38.
    PhylomeDBiP53582.
    TreeFamiTF105753.

    Family and domain databases

    Gene3Di3.90.230.10. 1 hit.
    HAMAPiMF_01974. MetAP_1.
    InterProiIPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002467. Pept_M24A_MAP1.
    [Graphical view]
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    PRINTSiPR00599. MAPEPTIDASE.
    SUPFAMiSSF55920. SSF55920. 1 hit.
    TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
    PROSITEiPS00680. MAP_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P53582-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAVETRVCE TDGCSSEAKL QCPTCIKLGI QGSYFCSQEC FKGSWATHKL    50
    LHKKAKDEKA KREVSSWTVE GDINTDPWAG YRYTGKLRPH YPLMPTRPVP 100
    SYIQRPDYAD HPLGMSESEQ ALKGTSQIKL LSSEDIEGMR LVCRLAREVL 150
    DVAAGMIKPG VTTEEIDHAV HLACIARNCY PSPLNYYNFP KSCCTSVNEV 200
    ICHGIPDRRP LQEGDIVNVD ITLYRNGYHG DLNETFFVGE VDDGARKLVQ 250
    TTYECLMQAI DAVKPGVRYR ELGNIIQKHA QANGFSVVRS YCGHGIHKLF 300
    HTAPNVPHYA KNKAVGVMKS GHVFTIEPMI CEGGWQDETW PDGWTAVTRD 350
    GKRSAQFEHT LLVTDTGCEI LTRRLDSARP HFMSQF 386
    Length:386
    Mass (Da):43,215
    Last modified:July 25, 2003 - v2
    Checksum:i372879013C2BB01D
    GO

    Sequence cautioni

    The sequence AAH30054.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA07679.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D42084 mRNA. Translation: BAA07679.1. Different initiation.
    AK304239 mRNA. Translation: BAG65108.1.
    CH471057 Genomic DNA. Translation: EAX06083.1.
    BC030054 mRNA. Translation: AAH30054.1. Different initiation.
    CCDSiCCDS47110.1.
    RefSeqiNP_055958.2. NM_015143.2.
    UniGeneiHs.480364.

    Genome annotation databases

    EnsembliENST00000296411; ENSP00000296411; ENSG00000164024.
    GeneIDi23173.
    KEGGihsa:23173.
    UCSCiuc003huf.4. human.

    Polymorphism databases

    DMDMi33302602.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D42084 mRNA. Translation: BAA07679.1 . Different initiation.
    AK304239 mRNA. Translation: BAG65108.1 .
    CH471057 Genomic DNA. Translation: EAX06083.1 .
    BC030054 mRNA. Translation: AAH30054.1 . Different initiation.
    CCDSi CCDS47110.1.
    RefSeqi NP_055958.2. NM_015143.2.
    UniGenei Hs.480364.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2B3H X-ray 1.10 A 81-384 [» ]
    2B3K X-ray 1.55 A 81-384 [» ]
    2B3L X-ray 1.50 A 81-384 [» ]
    2G6P X-ray 1.90 A 81-384 [» ]
    2GZ5 X-ray 1.10 A 81-384 [» ]
    2NQ6 X-ray 1.50 A 81-384 [» ]
    2NQ7 X-ray 1.60 A 81-384 [» ]
    4FLI X-ray 1.55 A 81-386 [» ]
    4FLJ X-ray 1.74 A 81-386 [» ]
    4FLK X-ray 1.47 A 81-386 [» ]
    4FLL X-ray 1.50 A 81-386 [» ]
    4HXX X-ray 2.09 A 81-384 [» ]
    4IKR X-ray 1.78 A 81-384 [» ]
    4IKS X-ray 1.70 A 81-384 [» ]
    4IKT X-ray 1.60 A 81-384 [» ]
    4IKU X-ray 1.30 A 81-384 [» ]
    4IU6 X-ray 1.90 A 1-384 [» ]
    ProteinModelPortali P53582.
    SMRi P53582. Positions 81-384.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116785. 5 interactions.
    IntActi P53582. 1 interaction.
    MINTi MINT-1191219.
    STRINGi 9606.ENSP00000296411.

    Chemistry

    BindingDBi P53582.
    ChEMBLi CHEMBL2474.

    Protein family/group databases

    MEROPSi M24.017.

    PTM databases

    PhosphoSitei P53582.

    Polymorphism databases

    DMDMi 33302602.

    Proteomic databases

    MaxQBi P53582.
    PaxDbi P53582.
    PeptideAtlasi P53582.
    PRIDEi P53582.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296411 ; ENSP00000296411 ; ENSG00000164024 .
    GeneIDi 23173.
    KEGGi hsa:23173.
    UCSCi uc003huf.4. human.

    Organism-specific databases

    CTDi 23173.
    GeneCardsi GC04P099916.
    HGNCi HGNC:15789. METAP1.
    HPAi CAB025485.
    MIMi 610151. gene.
    neXtProti NX_P53582.
    PharmGKBi PA30764.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000030427.
    HOVERGENi HBG067178.
    InParanoidi P53582.
    KOi K01265.
    OMAi MPGDRPL.
    OrthoDBi EOG786H38.
    PhylomeDBi P53582.
    TreeFami TF105753.

    Enzyme and pathway databases

    BRENDAi 3.4.11.18. 2681.
    Reactomei REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
    SABIO-RK P53582.

    Miscellaneous databases

    EvolutionaryTracei P53582.
    GeneWikii METAP1.
    GenomeRNAii 23173.
    NextBioi 44587.
    PROi P53582.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P53582.
    Bgeei P53582.
    CleanExi HS_METAP1.
    Genevestigatori P53582.

    Family and domain databases

    Gene3Di 3.90.230.10. 1 hit.
    HAMAPi MF_01974. MetAP_1.
    InterProi IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002467. Pept_M24A_MAP1.
    [Graphical view ]
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    PRINTSi PR00599. MAPEPTIDASE.
    SUPFAMi SSF55920. SSF55920. 1 hit.
    TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
    PROSITEi PS00680. MAP_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
      DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrow.
    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].
      Tissue: Trachea.
    3. 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] OF 110-386.
      Tissue: Placenta.
    5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Structural basis for the functional differences between type I and type II human methionine aminopeptidases."
      Addlagatta A., Hu X., Liu J.O., Matthews B.W.
      Biochemistry 44:14741-14749(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT IONS, FUNCTION, COFACTOR.
    8. "Identification of pyridinylpyrimidines as inhibitors of human methionine aminopeptidases."
      Hu X., Addlagatta A., Matthews B.W., Liu J.O.
      Angew. Chem. Int. Ed. 45:3772-3775(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT IONS AND INHIBITORS.
    9. "Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression."
      Hu X., Addlagatta A., Lu J., Matthews B.W., Liu J.O.
      Proc. Natl. Acad. Sci. U.S.A. 103:18148-18153(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT IONS AND INHIBITORS, CATALYTIC ACTIVITY, FUNCTION.
    10. "Structure of the angiogenesis inhibitor ovalicin bound to its noncognate target, human Type 1 methionine aminopeptidase."
      Addlagatta A., Matthews B.W.
      Protein Sci. 15:1842-1848(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT IONS AND THE INHIBITOR OVALICIN.

    Entry informationi

    Entry nameiMAP11_HUMAN
    AccessioniPrimary (citable) accession number: P53582
    Secondary accession number(s): B4E2E6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 25, 2003
    Last modified: October 1, 2014
    This is version 150 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3