Methionine aminopeptidase 1 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P53582 (AMPM1_HUMAN)

Last modified June 16, 2009. Version 96. History...

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

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Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Removes the amino-terminal methionine from nascent proteins. Required for normal progression through the cell cycle. Ref.5 Ref.7
Catalytic activity	Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. Ref.7
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.5 Binds 1 sodium ion per subunit. The sodium ion has a structural role. Ref.5
Sequence similarities	Belongs to the peptidase M24A family.

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Ontologies

Keywords
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	N-terminal protein amino acid modification Traceable author statement. Source: HGNC peptidyl-methionine modification Traceable author statement. Source: HGNC proteolysis Inferred from electronic annotation. Source: InterPro regulation of translation Traceable author statement. Source: HGNC
Cellular component	cytoplasm Traceable author statement. Source: HGNC
Molecular function	aminopeptidase activity Traceable author statement. Source: UniProtKB cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Traceable author statement. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
CBWD1	Q9BRT8	1	EBI-1051435,EBI-1054417

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 386

386

Methionine aminopeptidase 1

PRO_0000148967

Sites

Metal binding

220

Cobalt 1

Metal binding

231

Cobalt 1

Metal binding

231

Cobalt 2

Metal binding

294

Cobalt 2

Metal binding

327

Cobalt 2

Metal binding

358

Cobalt 1

Metal binding

358

Cobalt 2

Binding site

203

Substrate

Binding site

301

Substrate

Amino acid modifications

Modified residue

253

Phosphotyrosine Ref.3

Secondary structure

386

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P53582-1 [UniParc].

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

386

43,215

        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

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References

	« Hide 'large scale' referencesShow '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]	"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.
[3]	"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.
[4]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.

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Cross-references

Sequence databases

D42084 mRNA. Translation: BAA07679.1. Different initiation.
BC030054 mRNA. Translation: AAH30054.1. Different initiation.

IPI

IPI00022239.

RefSeq

NP_055958.2.

UniGene

Hs.480364

3D structure databases

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P53582. 1 interaction.

Protein family/group databases

MEROPS

M24.001.

PTM databases

PhosphoSite

P53582.

Proteomic databases

PeptideAtlas

P53582.

PRIDE

P53582.

Genome annotation databases

Ensembl

ENSG00000164024. Homo sapiens. [Contig view]

GeneID

23173.

KEGG

hsa:23173.

Organism-specific databases

GeneCards

GC04P100162.

H-InvDB

HIX0004393.

HGNC

HGNC:15789. METAP1.

MIM

610151. gene.

PharmGKB

PA30764.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P53582.

HOVERGEN

P53582.

OMA

P53582. VIQKHAE.

Enzyme and pathway databases

BRENDA

3.4.11.18. 247.

Gene expression databases

ArrayExpress

P53582.

Bgee

P53582.

CleanEx

HS_METAP1.

GermOnline

ENSG00000164024. Homo sapiens.

Family and domain databases

InterPro

IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]

Gene3D

G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.

PANTHER

PTHR10804:SF13. Pept_M24A_MAP1. 1 hit.
PTHR10804. Peptidase_M24_cat_core. 1 hit.

Pfam

PF00557. Peptidase_M24. 1 hit.
[Graphical view]

PRINTS

PR00599. MAPEPTIDASE.

TIGRFAMs

TIGR00500. met_pdase_I. 1 hit.

PROSITE

PS00680. MAP_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

BindingDB

P53582.

NextBio

44587.

SOURCE

Search...

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Entry information

Entry name

AMPM1_HUMAN

Accession

Primary (citable) accession number: P53582

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 25, 2003
Last modified:	June 16, 2009
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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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

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents