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P53582 (MAP11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionine aminopeptidase 1

Short name=MAP 1
Short name=MetAP 1
EC=3.4.11.18
Alternative name(s):
Peptidase M 1
Gene names
Name:METAP1
Synonyms:KIAA0094
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.9

Catalytic activity

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. Ref.9

Cofactor

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. Ref.7

Binds 1 sodium ion per subunit. The sodium ion has a structural role. Ref.7

Subunit structure

Associates with the 60S ribosomal subunit of the 80S translational complex By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03174.

Sequence similarities

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

Sequence caution

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 386385Methionine aminopeptidase 1 HAMAP-Rule MF_03174
PRO_0000148967

Regions

Region9 – 5244Zinc finger-like; important for proper ribosome association By similarity

Sites

Metal binding2201Divalent metal cation 1
Metal binding2311Divalent metal cation 1
Metal binding2311Divalent metal cation 2; catalytic
Metal binding2941Divalent metal cation 2; catalytic; via tele nitrogen
Metal binding3271Divalent metal cation 2; catalytic
Metal binding3581Divalent metal cation 1
Metal binding3581Divalent metal cation 2; catalytic
Binding site2031Substrate
Binding site3011Substrate

Amino acid modifications

Modified residue21N-acetylalanine Ref.5

Secondary structure

................................................. 386
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53582 [UniParc].

Last modified July 25, 2003. Version 2.
Checksum: 372879013C2BB01D

FASTA38643,215
        10         20         30         40         50         60 
MAAVETRVCE TDGCSSEAKL QCPTCIKLGI QGSYFCSQEC FKGSWATHKL LHKKAKDEKA 

        70         80         90        100        110        120 
KREVSSWTVE GDINTDPWAG YRYTGKLRPH YPLMPTRPVP SYIQRPDYAD HPLGMSESEQ 

       130        140        150        160        170        180 
ALKGTSQIKL LSSEDIEGMR LVCRLAREVL DVAAGMIKPG VTTEEIDHAV HLACIARNCY 

       190        200        210        220        230        240 
PSPLNYYNFP KSCCTSVNEV ICHGIPDRRP LQEGDIVNVD ITLYRNGYHG DLNETFFVGE 

       250        260        270        280        290        300 
VDDGARKLVQ TTYECLMQAI DAVKPGVRYR ELGNIIQKHA QANGFSVVRS YCGHGIHKLF 

       310        320        330        340        350        360 
HTAPNVPHYA KNKAVGVMKS GHVFTIEPMI CEGGWQDETW PDGWTAVTRD GKRSAQFEHT 

       370        380 
LLVTDTGCEI LTRRLDSARP HFMSQF 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS47110.1.
RefSeqNP_055958.2. NM_015143.2.
UniGeneHs.480364.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP53582.
SMRP53582. Positions 81-384.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116785. 3 interactions.
IntActP53582. 1 interaction.
MINTMINT-1191219.
STRING9606.ENSP00000296411.

Chemistry

BindingDBP53582.
ChEMBLCHEMBL2474.

Protein family/group databases

MEROPSM24.017.

PTM databases

PhosphoSiteP53582.

Polymorphism databases

DMDM33302602.

Proteomic databases

MaxQBP53582.
PaxDbP53582.
PeptideAtlasP53582.
PRIDEP53582.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296411; ENSP00000296411; ENSG00000164024.
GeneID23173.
KEGGhsa:23173.
UCSCuc003huf.4. human.

Organism-specific databases

CTD23173.
GeneCardsGC04P099916.
HGNCHGNC:15789. METAP1.
HPACAB025485.
MIM610151. gene.
neXtProtNX_P53582.
PharmGKBPA30764.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0024.
HOGENOMHOG000030427.
HOVERGENHBG067178.
InParanoidP53582.
KOK01265.
OMAMPGDRPL.
OrthoDBEOG786H38.
PhylomeDBP53582.
TreeFamTF105753.

Enzyme and pathway databases

BRENDA3.4.11.18. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
SABIO-RKP53582.

Gene expression databases

ArrayExpressP53582.
BgeeP53582.
CleanExHS_METAP1.
GenevestigatorP53582.

Family and domain databases

Gene3D3.90.230.10. 1 hit.
HAMAPMF_01974. MetAP_1.
InterProIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
PfamPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSPR00599. MAPEPTIDASE.
SUPFAMSSF55920. SSF55920. 1 hit.
TIGRFAMsTIGR00500. met_pdase_I. 1 hit.
PROSITEPS00680. MAP_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP53582.
GeneWikiMETAP1.
GenomeRNAi23173.
NextBio44587.
PROP53582.
SOURCESearch...

Entry information

Entry nameMAP11_HUMAN
AccessionPrimary (citable) accession number: P53582
Secondary accession number(s): B4E2E6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 25, 2003
Last modified: July 9, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM