Methionine aminopeptidase 2 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P50579 (AMPM2_HUMAN)

Last modified November 25, 2008. Version 87. History...

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

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Names and origin

Protein names

Recommended name:
    Methionine aminopeptidase 2
      Short name=MetAP 2
      Short name=MAP 2
    EC=3.4.11.18
Alternative name(s):
    Peptidase M 2
    Initiation factor 2-associated 67 kDa glycoprotein
    p67eIF2
      Short name=p67

Gene names

Name:	METAP2
Synonyms:	MNPEP, P67EIF2

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	478 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.
Catalytic activity	Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Cofactor	Binds 2 cobalt ions per subunit By similarity.
Sequence similarities	Belongs to the peptidase M24C 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 Inferred from direct assay. Source: HGNC peptidyl-methionine modification Inferred from direct assay. Source: HGNC protein processing Inferred from direct assay. Source: HGNC proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from direct assay. Source: HGNC
Molecular function	aminopeptidase activity Inferred from direct assay. Source: UniProtKB cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 478

478

Methionine aminopeptidase 2

PRO_0000148982

Regions

Compositional bias

36 – 46

Arg/Lys-rich (basic)

Compositional bias

82 – 93

Asp/Glu-rich (acidic)

Compositional bias

98 – 106

Poly-Lys

Sites

Active site

231

Metal binding

251

Cobalt 2 By similarity

Metal binding

262

Cobalt 1 By similarity

Metal binding

262

Cobalt 2 By similarity

Metal binding

331

Cobalt 1 By similarity

Metal binding

364

Cobalt 1 By similarity

Metal binding

459

Cobalt 1 By similarity

Metal binding

459

Cobalt 2 By similarity

Amino acid modifications

Modified residue

Phosphoserine

Modified residue

Phosphoserine

Modified residue

Phosphoserine

Modified residue

Phosphoserine

Secondary structure

478

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P50579-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 5788E4BB83E48F9A
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FASTA

478

52,892

        10         20         30         40         50         60 
MAGVEEVAAS GSHLNGDLDP DDREEGAAST AEEAAKKKRR KKKKSKGPSA AGEQEPDKES 

        70         80         90        100        110        120 
GASVDEVARQ LERSALEDKE RDEDDEDGDG DGDGATGKKK KKKKKKRGPK VQTDPPSVPI 

       130        140        150        160        170        180 
CDLYPNGVFP KGQECEYPPT QDGRTAAWRT TSEEKKALDQ ASEEIWNDFR EAAEAHRQVR 

       190        200        210        220        230        240 
KYVMSWIKPG MTMIEICEKL EDCSRKLIKE NGLNAGLAFP TGCSLNNCAA HYTPNAGDTT 

       250        260        270        280        290        300 
VLQYDDICKI DFGTHISGRI IDCAFTVTFN PKYDTLLKAV KDATNTGIKC AGIDVRLCDV 

       310        320        330        340        350        360 
GEAIQEVMES YEVEIDGKTY QVKPIRNLNG HSIGQYRIHA GKTVPIVKGG EATRMEEGEV 

       370        380        390        400        410        420 
YAIETFGSTG KGVVHDDMEC SHYMKNFDVG HVPIRLPRTK HLLNVINENF GTLAFCRRWL 

       430        440        450        460        470 
DRLGESKYLM ALKNLCDLGI VDPYPPLCDI KGSYTAQFEH TILLRPTCKE VVSRGDDY

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7644482] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 7873610] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"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]. Tissue: Lymph.
[4]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-60; SER-63 AND SER-74, MASS SPECTROMETRY.
[5]	"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: 9812898] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 109-478.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

U29607 mRNA. Translation: AAA82930.1.
U13261 mRNA. Translation: AAC63402.1.
BC013782 mRNA. Translation: AAH13782.1.

PIR

DPHUM2. S52112.

RefSeq

NP_006829.1.

UniGene

Hs.591005

3D structure databases

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	[»]

ModBase

Search...

Protein family/group databases

MEROPS

M24.002.

PTM databases

PhosphoSite

P50579.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00033036.

Proteomic databases

PeptideAtlas

P50579.

Genome annotation databases

Ensembl

ENSG00000111142. Homo sapiens. [Contig view]

GeneID

10988.

KEGG

hsa:10988.

Organism-specific databases

H-InvDB

HIX0010896.

HGNC

HGNC:16672. METAP2.

HPA

CAB013025.

MIM

601870. gene.

PharmGKB

PA30765.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P50579.

HOVERGEN

P50579.

Gene expression databases

ArrayExpress

P50579.

CleanEx

HS_METAP2.

GermOnline

ENSG00000111142. Homo sapiens.

Family and domain databases

InterPro

IPR001714. Pept_M24_MAP.
IPR002468. Pept_M24A_MAP2.
IPR000994. Peptidase_M24_cat_core.
[Graphical view]

Gene3D

G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.

PANTHER

PTHR10804:SF9. Pept_M24A_MAP2. 1 hit.
PTHR10804. Peptidase_M24_cat_core. 1 hit.

Pfam

PF00557. Peptidase_M24. 1 hit.
[Graphical view]

PRINTS

PR00599. MAPEPTIDASE.

TIGRFAMs

TIGR00501. met_pdase_II. 1 hit.

PROSITE

PS01202. MAP_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00134. L-Methionine.

LinkHub

P50579.

NextBio

41747.

SOURCE

Search...

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Entry information

Entry name

AMPM2_HUMAN

Accession

Primary (citable) accession number: P50579

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 25, 2008
This is version 87 of the entry and version 1 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 12

Human chromosome 12: 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

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents