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Reviewed, UniProtKB/Swiss-Prot P53582 (AMPM1_HUMAN)

Last modified November 3, 2009. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Removes the amino-terminal methionine from nascent proteins. 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 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions. Ref.7

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

Sequence similarities

Belongs to the peptidase M24A family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CBWD1Q9BRT81EBI-1051435,EBI-1054417

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 386386Methionine aminopeptidase 1
PRO_0000148967

Sites

Metal binding2201Cobalt 1
Metal binding2311Cobalt 1
Metal binding2311Cobalt 2
Metal binding2941Cobalt 2
Metal binding3271Cobalt 2
Metal binding3581Cobalt 1
Metal binding3581Cobalt 2
Binding site2031Substrate
Binding site3011Substrate

Amino acid modifications

Modified residue2531Phosphotyrosine Ref.5

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P53582-1 [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: 7788527] [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: 14702039] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 110-386.
Tissue: Placenta.
[5]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, MASS SPECTROMETRY.
[6]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 16274222] [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: 16724298] [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: 17114291] [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: 16823043] [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

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.
IPIIPI00022239.
RefSeqNP_055958.2.
UniGeneHs.480364

3D structure databases

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[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP53582. 1 interaction.
STRINGP53582.

Protein family/group databases

MEROPSM24.001.

PTM databases

PhosphoSiteP53582.

Proteomic databases

PeptideAtlasP53582.
PRIDEP53582.

Genome annotation databases

EnsemblENST00000296411; ENSP00000296411; ENSG00000164024; Homo sapiens. [Genome view]
GeneID23173.
KEGGhsa:23173.
UCSCuc003huf.2. human.

Organism-specific databases

CTD23173.
GeneCardsGC04P100162.
H-InvDBHIX0004393.
HGNCHGNC:15789. METAP1.
MIM610151. gene.
PharmGKBPA30764.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOGENOMP53582.
HOVERGENP53582.
OMAVIQKHAE.

Enzyme and pathway databases

BRENDA3.4.11.18. 247.

Gene expression databases

ArrayExpressP53582.
BgeeP53582.
CleanExHS_METAP1.
GenevestigatorP53582.
GermOnlineENSG00000164024. Homo sapiens.

Family and domain databases

InterProIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
Gene3DG3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
PANTHERPTHR10804:SF13. Pept_M24A_MAP1. 1 hit.
PTHR10804. Peptidase_M24_cat_core. 1 hit.
PfamPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSPR00599. MAPEPTIDASE.
TIGRFAMsTIGR00500. met_pdase_I. 1 hit.
PROSITEPS00680. MAP_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBP53582.
NextBio44587.
SOURCESearch...

Entry information

Entry nameAMPM1_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: November 3, 2009
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 4

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents