Methionine aminopeptidase 2 - Mus musculus (Mouse)

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O08663 (AMPM2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Methionine aminopeptidase 2
Short name=MAP 2
Short name=MetAP 2
EC=3.4.11.18

Alternative name(s):
Initiation factor 2-associated 67 kDa glycoprotein
Peptidase M 2
p67eIF2
Short name=p67

Gene names

Name:	Metap2
Synonyms:	Mnpep, P67eif2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	478 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Removes the amino-terminal methionine from nascent proteins By similarity. Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis By similarity.
Catalytic activity	Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
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 By similarity.
Subunit structure	Binds EIF2S1 at low magnesium concentrations. Interacts strongly with the eIF-2 gamma-subunit EIF2S3 By similarity.
Subcellular location	Cytoplasm. Note: About 30% of expressed METAP2 associates with polysomes By similarity.
Post-translational modification	Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. O-glycosylation is required for EIF2S1 binding By similarity.
Sequence similarities	Belongs to the peptidase M24A family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	N-terminal protein amino acid modification Inferred from sequence or structural similarity. Source: HGNC peptidyl-methionine modification Inferred from sequence or structural similarity. Source: HGNC protein processing Inferred from sequence or structural similarity. Source: HGNC proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from sequence or structural similarity. Source: HGNC
Molecular function	aminopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB protein binding Inferred from physical interaction. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 478

477

Methionine aminopeptidase 2

PRO_0000148983

Regions

Compositional bias

36 – 46

Arg/Lys-rich (basic)

Compositional bias

82 – 93

Asp/Glu-rich (acidic)

Compositional bias

98 – 106

Poly-Lys

Sites

Metal binding

251

Cobalt 1 By similarity

Metal binding

262

Cobalt 1 By similarity

Metal binding

262

Cobalt 2 By similarity

Metal binding

331

Cobalt 2 By similarity

Metal binding

364

Cobalt 2 By similarity

Metal binding

459

Cobalt 1 By similarity

Metal binding

459

Cobalt 2 By similarity

Binding site

231

Substrate By similarity

Binding site

339

Substrate By similarity

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

427

N6-acetyllysine By similarity

Glycosylation

O-linked (GlcNAc) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O08663 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: BBB9A2AFC19952E8
Show »

FASTA

478

52,922

        10         20         30         40         50         60 
MAGVEQAASF GGHLNGDLDP DDREEGTSST AEEAAKKKRR KKKKGKGAVS AVQQELDKES 

        70         80         90        100        110        120 
GALVDEVAKQ LESQALEEKE RDDDDEDGDG DADGATGKKK 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 PKYDILLTAV KDATNTGIKC AGIDVRLCDV 

       310        320        330        340        350        360 
GEAIQEVMES YEVEIDGKTY QVKPIRNLNG HSIGPYRIHA 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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Sekiguchi S., Suzuki E. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6 X CBA. Tissue: Liver.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Testis.
[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]. Strain: C57BL/6J. Tissue: Mammary gland.
[4]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 260-281; 297-318; 355-371 AND 386-395, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB003144 mRNA. Translation: BAA19789.1. AK076804 mRNA. Translation: BAC36488.1. BC002213 mRNA. Translation: AAH02213.1.
IPI	IPI00272238.
RefSeq	NP_062622.1. NM_019648.3.
UniGene	Mm.289329.
3D structure databases
ProteinModelPortal	O08663.
SMR	O08663. Positions 110-478.
ModBase	Search...
Protein-protein interaction databases
STRING	O08663.
Protein family/group databases
MEROPS	M24.002.
PTM databases
PhosphoSite	O08663.
Proteomic databases
PRIDE	O08663.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000047910; ENSMUSP00000048285; ENSMUSG00000036112.
GeneID	56307.
KEGG	mmu:56307.
Organism-specific databases
CTD	10988.
MGI	MGI:1929701. Metap2.
Phylogenomic databases
eggNOG	roNOG14581.
HOVERGEN	HBG050495.
InParanoid	O08663.
OrthoDB	EOG46T31M.
PhylomeDB	O08663.
Enzyme and pathway databases
BRENDA	3.4.11.18. 3474.
Gene expression databases
ArrayExpress	O08663.
Bgee	O08663.
CleanEx	MM_METAP2.
Genevestigator	O08663.
GermOnline	ENSMUSG00000036112. Mus musculus.
Family and domain databases
InterPro	IPR001714. Pept_M24_MAP. IPR000994. Pept_M24_structural-domain. IPR002468. Pept_M24A_MAP2. IPR018349. Pept_M24A_MAP2_BS. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:3.90.230.10. Peptidase_M24_cat_core. 2 hits. G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KO	K01265.
PANTHER	PTHR10804:SF9. Pept_M24A_MAP2. 1 hit.
Pfam	PF00557. Peptidase_M24. 1 hit. [Graphical view]
PRINTS	PR00599. MAPEPTIDASE.
SUPFAM	SSF55920. Peptidase_M24_cat_core. 1 hit.
TIGRFAMs	TIGR00501. Met_pdase_II. 1 hit.
PROSITE	PS01202. MAP_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	312244.
SOURCE	Search...

Entry information

Entry name

AMPM2_MOUSE

Accession

Primary (citable) accession number: O08663

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 1, 1997
Last modified:	November 16, 2011
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents