Reviewed, UniProtKB/Swiss-Prot P38174 (AMPM2_YEAST)

Names and origin

Protein names

Recommended name:
    Methionine aminopeptidase 2
      Short name=MetAP 2
    EC=3.4.11.18
Alternative name(s):
    Peptidase M 2

Gene names

Name:	MAP2
Ordered Locus Names:	YBL091C
ORF Names:	YBL0701

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	421 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions By similarity.
Subcellular location	Cytoplasm. Ref.4
Miscellaneous	Present with 1080 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the peptidase M24A family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from direct assay. Source: SGD
Cellular component	cytoplasm Traceable author statement. Source: SGD
Molecular function	cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloaminopeptidase activity Ref.1 Inferred from genetic interaction. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 421	421	Methionine aminopeptidase 2		PRO_0000148988
Sites
	Metal binding	194	1	Cobalt 1 By similarity
	Metal binding	205	1	Cobalt 1 By similarity
	Metal binding	205	1	Cobalt 2 By similarity
	Metal binding	274	1	Cobalt 2 By similarity
	Metal binding	307	1	Cobalt 2 By similarity
	Metal binding	402	1	Cobalt 1 By similarity
	Metal binding	402	1	Cobalt 2 By similarity
	Binding site	174	1	Substrate By similarity
	Binding site	282	1	Substrate By similarity
Amino acid modifications
	Modified residue	9	1	Phosphoserine Ref.7
	Modified residue	12	1	Phosphoserine Ref.7
	Modified residue	35	1	Phosphoserine Ref.7 Ref.6
Experimental info
	Sequence conflict	86	1	V → D in AAC49142. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P38174-1 [UniParc]. Last modified August 31, 2004. Version 3. Checksum: 2B3AEFDD6D659A80	FASTA	421	47,502
	10 20 30 40 50 60 MTDAEIENSP ASDLKELNLE NEGVEQQDQA KADESDPVES KKKKNKKKKK KKSNVKKIEL 70 80 90 100 110 120 LFPDGKYPEG AWMDYHQDFN LQRTTVEESR YLKRDLERAE HWNDVRKGAE IHRRVRRAIK 130 140 150 160 170 180 DRIVPGMKLM DIADMIENTT RKYTGAENLL AMEDPKSQGI GFPTGLSLNH CAAHFTPNAG 190 200 210 220 230 240 DKTVLKYEDV MKVDYGVQVN GNIIDSAFTV SFDPQYDNLL AAVKDATYTG IKEAGIDVRL 250 260 270 280 290 300 TDIGEAIQEV MESYEVEING ETYQVKPCRN LCGHSIAPYR IHGGKSVPIV KNGDTTKMEE 310 320 330 340 350 360 GEHFAIETFG STGRGYVTAG GEVSHYARSA EDHQVMPTLD SAKNLLKTID RNFGTLPFCR 370 380 390 400 410 420 RYLDRLGQEK YLFALNNLVR HGLVQDYPPL NDIPGSYTAQ FEHTILLHAH KKEVVSKGDD Y

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases." Li X., Chang Y.-H. Proc. Natl. Acad. Sci. U.S.A. 92:12357-12361(1995) [PubMed: 8618900] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 76626 / YPH500.
[2]	"Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II." Obermaier B., Gassenhuber J., Piravandi E., Domdey H. Yeast 11:1103-1112(1995) [PubMed: 7502586] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, MASS SPECTROMETRY.
[7]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-12 AND SER-35, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U17437 Genomic DNA. Translation: AAC49142.1. X79489 Genomic DNA. Translation: CAA56011.1. Different initiation. Z35851 Genomic DNA. Translation: CAA84912.1. Z35852 Genomic DNA. Translation: CAA84913.1.
RefSeq	NP_009462.1.
3D structure databases
HSSP	HSSP built from PDB template 1B6A based on UniProtKB P50579.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6459N.
IntAct	P38174. 3 interactions.
STRING	P38174.
Protein family/group databases
MEROPS	M24.002.
Proteomic databases
PeptideAtlas	P38174.
Genome annotation databases
Ensembl	YBL091C; YBL091C; YBL091C; Saccharomyces cerevisiae. [Genome view]
GeneID	852187.
GenomeReviews	Gene locus YBL091C in contig Y13134_GR.
KEGG	sce:YBL091C.
NMPDR	fig|4932.3.peg.148.
Organism-specific databases
CYGD	YBL091c.
SGD	S000000187. MAP2.
Phylogenomic databases
HOGENOM	P38174.
OMA	TPNAGDK.
Enzyme and pathway databases
BRENDA	3.4.11.18. 250.
Gene expression databases
ArrayExpress	P38174.
Genevestigator	P38174.
GermOnline	YBL091C. Saccharomyces cerevisiae.
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	970658.

Entry information

Entry name

AMPM2_YEAST

Accession

Primary (citable) accession number: P38174
Secondary accession number(s): P89493

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	August 31, 2004
Last modified:	November 3, 2009
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)