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P50579

- MAP2_HUMAN

UniProt

P50579 - MAP2_HUMAN

Protein

Methionine aminopeptidase 2

Gene

METAP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo.
    Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis.

    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 By similarity. Also manganese has been proposed to be the physiological cofactor for human METAP2.3 PublicationsUniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei231 – 2311Substrate
    Metal bindingi251 – 2511Divalent metal cation 1
    Metal bindingi262 – 2621Divalent metal cation 1
    Metal bindingi262 – 2621Divalent metal cation 2; catalytic
    Metal bindingi331 – 3311Divalent metal cation 2; catalytic; via tele nitrogen
    Binding sitei339 – 3391Substrate
    Metal bindingi364 – 3641Divalent metal cation 2; catalytic
    Metal bindingi459 – 4591Divalent metal cation 1
    Metal bindingi459 – 4591Divalent 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
    5. poly(A) RNA binding 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. protein processing Source: HGNC
    6. regulation of rhodopsin mediated signaling pathway Source: Reactome
    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.

    Protein family/group databases

    MEROPSiM24.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 2UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 2UniRule annotation
    Short name:
    MetAP 2UniRule annotation
    Alternative name(s):
    Initiation factor 2-associated 67 kDa glycoproteinUniRule annotation
    Short name:
    p67UniRule annotation
    Short name:
    p67eIF2UniRule annotation
    Peptidase MUniRule annotation
    Gene namesi
    Name:METAP2UniRule annotation
    Synonyms:MNPEP, P67EIF2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:16672. METAP2.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation
    Note: About 30% of expressed METAP2 associates with polysomes.

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. cytosol Source: Reactome
    3. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30765.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 478477Methionine aminopeptidase 2PRO_0000148982Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei45 – 451Phosphoserine2 Publications
    Modified residuei60 – 601Phosphoserine; alternate1 Publication
    Glycosylationi60 – 601O-linked (GlcNAc); alternateBy similarity
    Modified residuei63 – 631Phosphoserine; alternate1 Publication
    Glycosylationi63 – 631O-linked (GlcNAc); alternateBy similarity
    Modified residuei74 – 741Phosphoserine2 Publications

    Post-translational modificationi

    Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. O-glycosylation is required for EIF2S1 binding.1 PublicationUniRule annotation

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP50579.
    PaxDbiP50579.
    PeptideAtlasiP50579.
    PRIDEiP50579.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00033036.

    PTM databases

    PhosphoSiteiP50579.

    Expressioni

    Gene expression databases

    ArrayExpressiP50579.
    BgeeiP50579.
    CleanExiHS_METAP2.
    GenevestigatoriP50579.

    Organism-specific databases

    HPAiCAB013025.
    HPA019095.

    Interactioni

    Subunit structurei

    Interacts strongly with the eIF-2 gamma-subunit EIF2S3 By similarity. Binds EIF2S1 at low magnesium concentrations.By similarity6 Publications

    Protein-protein interaction databases

    BioGridi116184. 12 interactions.
    IntActiP50579. 2 interactions.
    MINTiMINT-2803706.
    STRINGi9606.ENSP00000325312.

    Structurei

    Secondary structure

    1
    478
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi120 – 1234
    Beta strandi133 – 1353
    Beta strandi141 – 1433
    Helixi149 – 1513
    Helixi154 – 1618
    Helixi163 – 18624
    Helixi193 – 20816
    Turni212 – 2143
    Beta strandi215 – 22511
    Beta strandi228 – 2303
    Beta strandi248 – 2569
    Beta strandi259 – 2679
    Helixi271 – 2733
    Helixi274 – 29017
    Helixi297 – 30913
    Beta strandi312 – 3154
    Beta strandi318 – 3214
    Beta strandi329 – 3346
    Beta strandi337 – 3393
    Beta strandi343 – 3497
    Beta strandi360 – 37011
    Beta strandi382 – 3854
    Helixi397 – 40913
    Turni410 – 4123
    Helixi417 – 4226
    Helixi429 – 4379
    Beta strandi440 – 4445
    Beta strandi455 – 46410
    Beta strandi469 – 4713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B59X-ray1.80A109-478[»]
    1B6AX-ray1.60A1-478[»]
    1BN5X-ray1.80A1-478[»]
    1BOAX-ray1.80A1-478[»]
    1KQ0X-ray2.00A1-478[»]
    1KQ9X-ray1.90A1-478[»]
    1QZYX-ray1.60A1-478[»]
    1R58X-ray1.90A110-478[»]
    1R5GX-ray2.00A110-478[»]
    1R5HX-ray2.40A110-478[»]
    1YW7X-ray1.85A110-478[»]
    1YW8X-ray2.65A110-478[»]
    1YW9X-ray1.64A110-478[»]
    2ADUX-ray1.90A110-478[»]
    2EA2X-ray2.50A110-478[»]
    2EA4X-ray2.35A110-478[»]
    2GA2X-ray1.95A110-478[»]
    2OAZX-ray1.90A110-478[»]
    ProteinModelPortaliP50579.
    SMRiP50579. Positions 110-478.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50579.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi41 – 466Poly-Lys
    Compositional biasi98 – 1069Poly-Lys

    Sequence similaritiesi

    Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000226278.
    HOVERGENiHBG050495.
    InParanoidiP50579.
    KOiK01265.
    OMAiIQICEEL.
    PhylomeDBiP50579.
    TreeFamiTF300426.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPiMF_03175. MetAP_2_euk.
    InterProiIPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002468. Pept_M24A_MAP2.
    IPR018349. Pept_M24A_MAP2_BS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    PRINTSiPR00599. MAPEPTIDASE.
    SUPFAMiSSF55920. SSF55920. 2 hits.
    TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
    PROSITEiPS01202. MAP_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P50579-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAGVEEVAAS GSHLNGDLDP DDREEGAAST AEEAAKKKRR KKKKSKGPSA    50
    AGEQEPDKES GASVDEVARQ LERSALEDKE RDEDDEDGDG DGDGATGKKK 100
    KKKKKKRGPK VQTDPPSVPI CDLYPNGVFP KGQECEYPPT QDGRTAAWRT 150
    TSEEKKALDQ ASEEIWNDFR EAAEAHRQVR KYVMSWIKPG MTMIEICEKL 200
    EDCSRKLIKE NGLNAGLAFP TGCSLNNCAA HYTPNAGDTT VLQYDDICKI 250
    DFGTHISGRI IDCAFTVTFN PKYDTLLKAV KDATNTGIKC AGIDVRLCDV 300
    GEAIQEVMES YEVEIDGKTY QVKPIRNLNG HSIGQYRIHA GKTVPIVKGG 350
    EATRMEEGEV YAIETFGSTG KGVVHDDMEC SHYMKNFDVG HVPIRLPRTK 400
    HLLNVINENF GTLAFCRRWL DRLGESKYLM ALKNLCDLGI VDPYPPLCDI 450
    KGSYTAQFEH TILLRPTCKE VVSRGDDY 478
    Length:478
    Mass (Da):52,892
    Last modified:October 1, 1996 - v1
    Checksum:i5788E4BB83E48F9A
    GO
    Isoform 2 (identifier: P50579-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         50-50: Missing.
         87-109: DGDGDGDGATGKKKKKKKKKRGP → A

    Note: No experimental confirmation available.

    Show »
    Length:455
    Mass (Da):50,510
    Checksum:i6B2C99F5B40B951F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti434 – 4341N → D in BAC03733. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei50 – 501Missing in isoform 2. 1 PublicationVSP_055467
    Alternative sequencei87 – 10923DGDGD…KKRGP → A in isoform 2. 1 PublicationVSP_055468Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29607 mRNA. Translation: AAA82930.1.
    U13261 mRNA. Translation: AAC63402.1.
    AK091730 mRNA. Translation: BAC03733.1.
    AK315559 mRNA. Translation: BAG37935.1.
    AC018475 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97537.1.
    CH471054 Genomic DNA. Translation: EAW97538.1.
    BC013782 mRNA. Translation: AAH13782.1.
    CCDSiCCDS9052.1.
    PIRiS52112. DPHUM2.
    RefSeqiNP_006829.1. NM_006838.3.
    UniGeneiHs.444986.

    Genome annotation databases

    EnsembliENST00000261220; ENSP00000261220; ENSG00000111142. [P50579-2]
    ENST00000323666; ENSP00000325312; ENSG00000111142. [P50579-1]
    GeneIDi10988.
    KEGGihsa:10988.
    UCSCiuc001tec.3. human.

    Polymorphism databases

    DMDMi1703273.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29607 mRNA. Translation: AAA82930.1 .
    U13261 mRNA. Translation: AAC63402.1 .
    AK091730 mRNA. Translation: BAC03733.1 .
    AK315559 mRNA. Translation: BAG37935.1 .
    AC018475 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97537.1 .
    CH471054 Genomic DNA. Translation: EAW97538.1 .
    BC013782 mRNA. Translation: AAH13782.1 .
    CCDSi CCDS9052.1.
    PIRi S52112. DPHUM2.
    RefSeqi NP_006829.1. NM_006838.3.
    UniGenei Hs.444986.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B59 X-ray 1.80 A 109-478 [» ]
    1B6A X-ray 1.60 A 1-478 [» ]
    1BN5 X-ray 1.80 A 1-478 [» ]
    1BOA X-ray 1.80 A 1-478 [» ]
    1KQ0 X-ray 2.00 A 1-478 [» ]
    1KQ9 X-ray 1.90 A 1-478 [» ]
    1QZY X-ray 1.60 A 1-478 [» ]
    1R58 X-ray 1.90 A 110-478 [» ]
    1R5G X-ray 2.00 A 110-478 [» ]
    1R5H X-ray 2.40 A 110-478 [» ]
    1YW7 X-ray 1.85 A 110-478 [» ]
    1YW8 X-ray 2.65 A 110-478 [» ]
    1YW9 X-ray 1.64 A 110-478 [» ]
    2ADU X-ray 1.90 A 110-478 [» ]
    2EA2 X-ray 2.50 A 110-478 [» ]
    2EA4 X-ray 2.35 A 110-478 [» ]
    2GA2 X-ray 1.95 A 110-478 [» ]
    2OAZ X-ray 1.90 A 110-478 [» ]
    ProteinModelPortali P50579.
    SMRi P50579. Positions 110-478.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116184. 12 interactions.
    IntActi P50579. 2 interactions.
    MINTi MINT-2803706.
    STRINGi 9606.ENSP00000325312.

    Chemistry

    BindingDBi P50579.
    ChEMBLi CHEMBL3922.
    DrugBanki DB00134. L-Methionine.
    GuidetoPHARMACOLOGYi 1573.

    Protein family/group databases

    MEROPSi M24.002.

    PTM databases

    PhosphoSitei P50579.

    Polymorphism databases

    DMDMi 1703273.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00033036.

    Proteomic databases

    MaxQBi P50579.
    PaxDbi P50579.
    PeptideAtlasi P50579.
    PRIDEi P50579.

    Protocols and materials databases

    DNASUi 10988.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261220 ; ENSP00000261220 ; ENSG00000111142 . [P50579-2 ]
    ENST00000323666 ; ENSP00000325312 ; ENSG00000111142 . [P50579-1 ]
    GeneIDi 10988.
    KEGGi hsa:10988.
    UCSCi uc001tec.3. human.

    Organism-specific databases

    CTDi 10988.
    GeneCardsi GC12P095800.
    HGNCi HGNC:16672. METAP2.
    HPAi CAB013025.
    HPA019095.
    MIMi 601870. gene.
    neXtProti NX_P50579.
    PharmGKBi PA30765.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226278.
    HOVERGENi HBG050495.
    InParanoidi P50579.
    KOi K01265.
    OMAi IQICEEL.
    PhylomeDBi P50579.
    TreeFami TF300426.

    Enzyme and pathway databases

    BRENDAi 3.4.11.18. 2681.
    Reactomei REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.

    Miscellaneous databases

    ChiTaRSi METAP2. human.
    EvolutionaryTracei P50579.
    GeneWikii METAP2.
    GenomeRNAii 10988.
    NextBioi 41747.
    PROi P50579.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P50579.
    Bgeei P50579.
    CleanExi HS_METAP2.
    Genevestigatori P50579.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPi MF_03175. MetAP_2_euk.
    InterProi IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002468. Pept_M24A_MAP2.
    IPR018349. Pept_M24A_MAP2_BS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    PRINTSi PR00599. MAPEPTIDASE.
    SUPFAMi SSF55920. SSF55920. 2 hits.
    TIGRFAMsi TIGR00501. met_pdase_II. 1 hit.
    PROSITEi PS01202. MAP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes."
      Arfin S.M., Kendall R.L., Hall L., Weaver L.H., Stewart A.E., Matthews B.W., Bradshaw R.A.
      Proc. Natl. Acad. Sci. U.S.A. 92:7714-7718(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Molecular cloning of a human complementary DNA encoding an initiation factor 2-associated protein (p67)."
      Li X., Chang Y.
      Biochim. Biophys. Acta 1260:333-336(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    3. "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] (ISOFORMS 1 AND 2).
      Tissue: Heart and Placenta.
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Lymph.
    7. "Glycosylation of eukaryotic peptide chain initiation factor 2 (eIF-2)-associated 67-kDa polypeptide (p67) and its possible role in the inhibition of eIF-2 kinase-catalyzed phosphorylation of the eIF-2 alpha-subunit."
      Datta B., Ray M.K., Chakrabarti D., Wylie D.E., Gupta N.K.
      J. Biol. Chem. 264:20620-20624(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN EIF2S1 PROTECTION, GLYCOSYLATION.
    8. "Physiologically relevant metal cofactor for methionine aminopeptidase-2 is manganese."
      Wang J., Sheppard G.S., Lou P., Kawai M., Park C., Egan D.A., Schneider A., Bouska J., Lesniewski R., Henkin J.
      Biochemistry 42:5035-5042(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-60; SER-63 AND SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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].
    11. "Protein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases."
      Xiao Q., Zhang F., Nacev B.A., Liu J.O., Pei D.
      Biochemistry 49:5588-5599(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Localization and function of a eukaryotic-initiation-factor-2-associated 67-kDa glycoprotein."
      Wu S.
      World J. Biol. Chem. 1:313-320(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Structure of human methionine aminopeptidase-2 complexed with fumagillin."
      Liu S., Widom J., Kemp C.W., Crews C.M., Clardy J.
      Science 282:1324-1327(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FUMAGILLIN, COFACTOR.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH COBALT IONS AND BENGAMIDE, FUNCTION.
    17. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 110-478 IN COMPLEX WITH INHIBITOR A-357300.
    18. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 110-478 IN COMPLEX WITH 4-ARYL-1,2,3-TRIAZOLE AND COBALT IONS.
    19. "Human methionine aminopeptidase type 2 in complex with L- and D-methionine."
      Nonato M.C., Widom J., Clardy J.
      Bioorg. Med. Chem. Lett. 16:2580-2583(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH ZINC IONS AND METHIONINE, PARTIAL PROTEIN SEQUENCE.
    20. "Lead optimization of methionine aminopeptidase-2 (MetAP2) inhibitors containing sulfonamides of 5,6-disubstituted anthranilic acids."
      Wang G.T., Mantei R.A., Kawai M., Tedrow J.S., Barnes D.M., Wang J., Zhang Q., Lou P., Garcia L.A., Bouska J., Yates M., Park C., Judge R.A., Lesniewski R., Sheppard G.S., Bell R.L.
      Bioorg. Med. Chem. Lett. 17:2817-2822(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 110-478 IN COMPLEX WITH MANGANESE AND INHIBITOR.
    21. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 110-478 IN COMPLEX WITH COBALT IONS AND INHIBITOR, COFACTOR, FUNCTION.

    Entry informationi

    Entry nameiMAP2_HUMAN
    AccessioniPrimary (citable) accession number: P50579
    Secondary accession number(s): B2RDI8, G3XA91, Q8NB11
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 149 of the entry and version 1 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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