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P53582

- MAP11_HUMAN

UniProt

P53582 - MAP11_HUMAN

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Protein

Methionine aminopeptidase 1

Gene
METAP1, KIAA0094
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 Publications

Catalytic activityi

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

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.1 Publication
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
Complete GO annotation...

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 1 (EC:3.4.11.18)
Short name:
MAP 1
Short name:
MetAP 1
Alternative name(s):
Peptidase M 1
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 By similarity UniRule annotation

GO - Cellular componenti

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

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 1UniRule annotationPRO_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 By similarity.

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.

Miscellaneous databases

EvolutionaryTraceiP53582.

Family & Domainsi

Region

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

Sequence similaritiesi

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 149 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

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