Reviewed, UniProtKB/Swiss-Prot O08663 (AMPM2_MOUSE)

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

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

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 eIF-2 alpha-subunit from inhibitory phosphorylation by eIF-2 kinases. Plays a critical role in the regulation of protein synthesis. It also interacts with the eIF-2 gamma-subunit 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.
Sequence similarities	Belongs to the peptidase M24A family.

Ontologies

Keywords
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
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: InterPro
Cellular component	cytoplasm Inferred from sequence or structural similarity. Source: HGNC
Molecular function	aminopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB cobalt 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	1	1	Removed By similarity
	Chain	2 – 478	477	Methionine aminopeptidase 2		PRO_0000148983
Regions
	Compositional bias	36 – 46	11	Arg/Lys-rich (basic)
	Compositional bias	82 – 93	12	Asp/Glu-rich (acidic)
	Compositional bias	98 – 106	9	Poly-Lys
Sites
	Metal binding	251	1	Cobalt 1 By similarity
	Metal binding	262	1	Cobalt 1 By similarity
	Metal binding	262	1	Cobalt 2 By similarity
	Metal binding	331	1	Cobalt 2 By similarity
	Metal binding	364	1	Cobalt 2 By similarity
	Metal binding	459	1	Cobalt 1 By similarity
	Metal binding	459	1	Cobalt 2 By similarity
	Binding site	231	1	Substrate By similarity
	Binding site	339	1	Substrate By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	60	1	Phosphoserine By similarity
	Modified residue	427	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O08663-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: BBB9A2AFC19952E8	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

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. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai 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.
UniGene	Mm.289329
3D structure databases
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.
Genome annotation databases
Ensembl	ENSMUST00000047910; ENSMUSP00000048285; ENSMUSG00000036112; Mus musculus. [Genome view]
GeneID	56307.
KEGG	mmu:56307.
UCSC	uc007gve.1. mouse.
Organism-specific databases
CTD	56307.
MGI	MGI:1929701. Metap2.
Phylogenomic databases
eggNOG	roNOG14581.
HOVERGEN	O08663.
InParanoid	O08663.
OrthoDB	EOG9WM7DH.
PhylomeDB	O08663.
Enzyme and pathway databases
BRENDA	3.4.11.18. 244.
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. [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
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:	February 9, 2010
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)