P50579 (AMPM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	478 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Removes the N-terminal methionine from nascent proteins. The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo. Ref.6 Ref.8 Ref.13 Ref.18 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. Ref.6 Ref.8 Ref.13 Ref.18
Catalytic activity	Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. Ref.8
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.12 Ref.18
Subunit structure	Interacts strongly with the eIF-2 gamma-subunit EIF2S3 By similarity. Binds EIF2S1 at low magnesium concentrations.
Subcellular location	Cytoplasm. Note: About 30% of expressed METAP2 associates with polysomes. Ref.10
Post-translational modification	Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. O-glycosylation is required for EIF2A binding.
Sequence similarities	Belongs to the peptidase M24A family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	N-terminal protein amino acid modification Inferred from direct assay PubMed 8858118. Source: HGNC peptidyl-methionine modification Inferred from direct assay PubMed 8858118. Source: HGNC protein processing Inferred from direct assay PubMed 8858118. Source: HGNC proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay PubMed 15102683. Source: HGNC
Molecular_function	aminopeptidase activity Inferred from direct assay PubMed 8858118. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from direct assay PubMed 8858118. Source: UniProtKB
Complete GO annotation...

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

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

Metal binding

262

1

Cobalt 1

Metal binding

262

1

Cobalt 2

Metal binding

331

1

Cobalt 2

Metal binding

364

1

Cobalt 2

Metal binding

459

1

Cobalt 1

Metal binding

459

1

Cobalt 2

Binding site

231

1

Substrate

Binding site

339

1

Substrate

Amino acid modifications

Modified residue

45

1

Phosphoserine Ref.7 Ref.9

Modified residue

60

1

Phosphoserine; alternate Ref.7

Modified residue

63

1

Phosphoserine; alternate Ref.7

Modified residue

74

1

Phosphoserine Ref.7 Ref.9

Glycosylation

60

1

O-linked (GlcNAc); alternate By similarity

Glycosylation

63

1

O-linked (GlcNAc); alternate By similarity

Secondary structure

1

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478

Helix Strand Turn

Details...

Helix

120 – 123

4

Beta strand

133 – 135

3

Beta strand

141 – 143

3

Helix

149 – 151

3

Helix

154 – 161

8

Helix

163 – 186

24

Helix

193 – 208

16

Turn

212 – 214

3

Beta strand

215 – 225

11

Beta strand

228 – 230

3

Beta strand

248 – 256

9

Beta strand

259 – 267

9

Helix

271 – 273

3

Helix

274 – 290

17

Helix

297 – 309

13

Beta strand

312 – 315

4

Beta strand

318 – 321

4

Beta strand

329 – 334

6

Beta strand

337 – 339

3

Beta strand

343 – 349

7

Beta strand

360 – 370

11

Beta strand

382 – 385

4

Helix

397 – 409

13

Turn

410 – 412

3

Helix

417 – 422

6

Helix

429 – 437

9

Beta strand

440 – 444

5

Beta strand

455 – 464

10

Beta strand

469 – 471

3

Sequences

	Sequence		Length	Mass (Da)
	P50579 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 5788E4BB83E48F9A	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

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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph.
[6]	"Glycosylation of eukaryotic peptide chain initiation factor 2 (eIF-2)-associated 67-kDa polypeptide (p67) and its possible role in the inhibition of eIF-2 kinase-catalyzed phosphorylation of the eIF-2 alpha-subunit." Datta B., Ray M.K., Chakrabarti D., Wylie D.E., Gupta N.K. J. Biol. Chem. 264:20620-20624(1989) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN EIF2S1 PROTECTION, GLYCOSYLATION.
[7]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-60; SER-63 AND SER-74, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Protein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases." Xiao Q., Zhang F., Nacev B.A., Liu J.O., Pei D. Biochemistry 49:5588-5599(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[9]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-74, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Localization and function of a eukaryotic-initiation-factor-2-associated 67-kDa glycoprotein." Wu S. World J. Biol. Chem. 1:313-320(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FUMAGILLIN, COFACTOR.
[13]	"Proteomics-based target identification: bengamides as a new class of methionine aminopeptidase inhibitors." Towbin H., Bair K.W., DeCaprio J.A., Eck M.J., Kim S., Kinder F.R., Morollo A., Mueller D.R., Schindler P., Song H.K., van Oostrum J., Versace R.W., Voshol H., Wood J., Zabludoff S., Phillips P.E. J. Biol. Chem. 278:52964-52971(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH COBALT IONS AND BENGAMIDE, FUNCTION.
[14]	"3-amino-2-hydroxyamides and related compounds as inhibitors of methionine aminopeptidase-2." Sheppard G.S., Wang J., Kawai M., BaMaung N.Y., Craig R.A., Erickson S.A., Lynch L., Patel J., Yang F., Searle X.B., Lou P., Park C., Kim K.H., Henkin J., Lesniewski R. Bioorg. Med. Chem. Lett. 14:865-868(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 110-478 IN COMPLEX WITH INHIBITOR A-357300.
[15]	"4-aryl-1,2,3-triazole: a novel template for a reversible methionine aminopeptidase 2 inhibitor, optimized to inhibit angiogenesis in vivo." Kallander L.S., Lu Q., Chen W., Tomaszek T., Yang G., Tew D., Meek T.D., Hofmann G.A., Schulz-Pritchard C.K., Smith W.W., Janson C.A., Ryan M.D., Zhang G.-F., Johanson K.O., Kirkpatrick R.B., Ho T.F., Fisher P.W., Mattern M.R. , Johnson R.K., Hansbury M.J., Winkler J.D., Ward K.W., Veber D.F., Thompson S.K. J. Med. Chem. 48:5644-5647(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 110-478 IN COMPLEX WITH 4-ARYL-1,2,3-TRIAZOLE AND COBALT IONS.
[16]	"Human methionine aminopeptidase type 2 in complex with L- and D-methionine." Nonato M.C., Widom J., Clardy J. Bioorg. Med. Chem. Lett. 16:2580-2583(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH ZINC IONS AND METHIONINE, PARTIAL PROTEIN SEQUENCE.
[17]	"Lead optimization of methionine aminopeptidase-2 (MetAP2) inhibitors containing sulfonamides of 5,6-disubstituted anthranilic acids." Wang G.T., Mantei R.A., Kawai M., Tedrow J.S., Barnes D.M., Wang J., Zhang Q., Lou P., Garcia L.A., Bouska J., Yates M., Park C., Judge R.A., Lesniewski R., Sheppard G.S., Bell R.L. Bioorg. Med. Chem. Lett. 17:2817-2822(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 110-478 IN COMPLEX WITH MANGANESE AND INHIBITOR.
[18]	"Highly potent inhibitors of methionine aminopeptidase-2 based on a 1,2,4-triazole pharmacophore." Marino J.P. Jr., Fisher P.W., Hofmann G.A., Kirkpatrick R.B., Janson C.A., Johnson R.K., Ma C., Mattern M., Meek T.D., Ryan M.D., Schulz C., Smith W.W., Tew D.G., Tomazek T.A. Jr., Veber D.F., Xiong W.C., Yamamoto Y., Yamashita K., Yang G., Thompson S.K. J. Med. Chem. 50:3777-3785(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 110-478 IN COMPLEX WITH COBALT IONS AND INHIBITOR, COFACTOR, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U29607 mRNA. Translation: AAA82930.1.
U13261 mRNA. Translation: AAC63402.1.
AK315559 mRNA. Translation: BAG37935.1.
CH471054 Genomic DNA. Translation: EAW97537.1.
BC013782 mRNA. Translation: AAH13782.1.

IPI

IPI00033036.

PIR

DPHUM2. S52112.

RefSeq

NP_006829.1. NM_006838.3.

UniGene

Hs.444986.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P50579.

ModBase

Search...

Protein-protein interaction databases

IntAct

P50579. 1 interaction.

MINT

MINT-2803706.

STRING

9606.ENSP00000325312.

Protein family/group databases

MEROPS

M24.002.

PTM databases

PhosphoSite

P50579.

Polymorphism databases

DMDM

1703273.

2D gel databases

REPRODUCTION-2DPAGE

IPI00033036.

Proteomic databases

PaxDb

P50579.

PeptideAtlas

P50579.

PRIDE

P50579.

Protocols and materials databases

DNASU

10988.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000323666; ENSP00000325312; ENSG00000111142.

GeneID

10988.

KEGG

hsa:10988.

UCSC

uc001tec.3. human.

Organism-specific databases

CTD

10988.

GeneCards

GC12P095800.

HGNC

HGNC:16672. METAP2.

HPA

CAB013025.
HPA019095.

MIM

601870. gene.

neXtProt

NX_P50579.

PharmGKB

PA30765.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0024.

HOGENOM

HOG000226278.

HOVERGEN

HBG050495.

InParanoid

P50579.

KO

K01265.

OMA

NLNGHNI.

OrthoDB

EOG46T31M.

PhylomeDB

P50579.

Enzyme and pathway databases

BRENDA

3.4.11.18. 2681.

Gene expression databases

ArrayExpress

P50579.

Bgee

P50579.

CleanEx

HS_METAP2.

Genevestigator

P50579.

GermOnline

ENSG00000111142. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.
3.90.230.10. 2 hits.

InterPro

IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

PANTHER

PTHR10804:SF9. PTHR10804:SF9. 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

BindingDB

P50579.

ChEMBL

CHEMBL3922.

ChiTaRS

METAP2. human.

DrugBank

DB00134. L-Methionine.

EvolutionaryTrace

P50579.

GenomeRNAi

10988.

NextBio

41747.

SOURCE

Search...

Entry information

Entry name

AMPM2_HUMAN

Accession

Primary (citable) accession number: P50579
Secondary accession number(s): B2RDI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 134 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.