P53582 (AMPM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methionine aminopeptidase 1
Short name=MAP 1
Short name=MetAP 1
EC=3.4.11.18

Alternative name(s):
Peptidase M 1

Gene names

Name:	METAP1
Synonyms:	KIAA0094

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	386 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Removes the N-terminal methionine from nascent proteins. Required for normal progression through the cell cycle. Ref.6 Ref.8
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.6 Binds 1 sodium ion per subunit. The sodium ion has a structural role. Ref.6
Sequence similarities	Belongs to the peptidase M24A family.
Sequence caution	The sequence AAH30054.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA07679.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	N-terminal protein amino acid modification Traceable author statement PubMed 16386852. Source: HGNC peptidyl-methionine modification Traceable author statement PubMed 16386852. Source: HGNC proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of translation Traceable author statement PubMed 16386852. Source: HGNC
Cellular_component	cytoplasm Traceable author statement PubMed 14532271. Source: HGNC
Molecular_function	aminopeptidase activity Traceable author statement PubMed 16386852. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Traceable author statement PubMed 16386852. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 386

386

Methionine aminopeptidase 1

PRO_0000148967

Sites

Metal binding

220

1

Cobalt 1

Metal binding

231

1

Cobalt 1

Metal binding

231

1

Cobalt 2

Metal binding

294

1

Cobalt 2

Metal binding

327

1

Cobalt 2

Metal binding

358

1

Cobalt 1

Metal binding

358

1

Cobalt 2

Binding site

203

1

Substrate

Binding site

301

1

Substrate

Secondary structure

1

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386

Helix Strand Turn

Details...

Beta strand

84 – 86

3

Helix

107 – 110

4

Helix

117 – 121

5

Turn

122 – 124

3

Helix

133 – 155

23

Helix

163 – 176

14

Turn

182 – 185

4

Helix

186 – 188

3

Beta strand

191 – 197

7

Beta strand

200 – 202

3

Beta strand

216 – 225

10

Beta strand

228 – 237

10

Helix

243 – 261

19

Helix

271 – 282

12

Beta strand

293 – 295

3

Beta strand

297 – 306

10

Beta strand

309 – 311

3

Beta strand

323 – 326

4

Beta strand

329 – 333

5

Beta strand

337 – 339

3

Beta strand

346 – 348

3

Beta strand

354 – 356

3

Beta strand

358 – 363

6

Beta strand

365 – 370

6

Helix

381 – 383

3

Sequences

	Sequence		Length	Mass (Da)
	P53582 [UniParc]. Last modified July 25, 2003. Version 2. Checksum: 372879013C2BB01D	FASTA	386	43,215
	10 20 30 40 50 60 MAAVETRVCE TDGCSSEAKL QCPTCIKLGI QGSYFCSQEC FKGSWATHKL LHKKAKDEKA 70 80 90 100 110 120 KREVSSWTVE GDINTDPWAG YRYTGKLRPH YPLMPTRPVP SYIQRPDYAD HPLGMSESEQ 130 140 150 160 170 180 ALKGTSQIKL LSSEDIEGMR LVCRLAREVL DVAAGMIKPG VTTEEIDHAV HLACIARNCY 190 200 210 220 230 240 PSPLNYYNFP KSCCTSVNEV ICHGIPDRRP LQEGDIVNVD ITLYRNGYHG DLNETFFVGE 250 260 270 280 290 300 VDDGARKLVQ TTYECLMQAI DAVKPGVRYR ELGNIIQKHA QANGFSVVRS YCGHGIHKLF 310 320 330 340 350 360 HTAPNVPHYA KNKAVGVMKS GHVFTIEPMI CEGGWQDETW PDGWTAVTRD GKRSAQFEHT 370 380 LLVTDTGCEI LTRRLDSARP HFMSQF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N. DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[2]	"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: Trachea.
[3]	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].
[4]	"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] OF 110-386. Tissue: Placenta.
[5]	"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].
[6]	"Structural basis for the functional differences between type I and type II human methionine aminopeptidases." Addlagatta A., Hu X., Liu J.O., Matthews B.W. Biochemistry 44:14741-14749(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT IONS, FUNCTION, COFACTOR.
[7]	"Identification of pyridinylpyrimidines as inhibitors of human methionine aminopeptidases." Hu X., Addlagatta A., Matthews B.W., Liu J.O. Angew. Chem. Int. Ed. 45:3772-3775(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT IONS AND INHIBITORS.
[8]	"Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression." Hu X., Addlagatta A., Lu J., Matthews B.W., Liu J.O. Proc. Natl. Acad. Sci. U.S.A. 103:18148-18153(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT IONS AND INHIBITORS, CATALYTIC ACTIVITY, FUNCTION.
[9]	"Structure of the angiogenesis inhibitor ovalicin bound to its noncognate target, human Type 1 methionine aminopeptidase." Addlagatta A., Matthews B.W. Protein Sci. 15:1842-1848(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT IONS AND THE INHIBITOR OVALICIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D42084 mRNA. Translation: BAA07679.1. Different initiation.
AK304239 mRNA. Translation: BAG65108.1.
CH471057 Genomic DNA. Translation: EAX06083.1.
BC030054 mRNA. Translation: AAH30054.1. Different initiation.

IPI

IPI00022239.

RefSeq

NP_055958.2. NM_015143.2.

UniGene

Hs.480364.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2B3H	X-ray	1.10	A	81-384	[»]
2B3K	X-ray	1.55	A	81-384	[»]
2B3L	X-ray	1.50	A	81-384	[»]
2G6P	X-ray	1.90	A	81-384	[»]
2GZ5	X-ray	1.10	A	81-384	[»]
2NQ6	X-ray	1.50	A	81-384	[»]
2NQ7	X-ray	1.60	A	81-384	[»]
4FLI	X-ray	1.55	A	81-386	[»]
4FLJ	X-ray	1.74	A	81-386	[»]
4FLK	X-ray	1.47	A	81-386	[»]
4FLL	X-ray	1.50	A	81-386	[»]
4HXX	X-ray	2.09	A	81-384	[»]

ProteinModelPortal

P53582.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1191219.

STRING

9606.ENSP00000296411.

Protein family/group databases

MEROPS

M24.017.

PTM databases

PhosphoSite

P53582.

Polymorphism databases

DMDM

33302602.

Proteomic databases

PaxDb

P53582.

PeptideAtlas

P53582.

PRIDE

P53582.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000296411; ENSP00000296411; ENSG00000164024.

GeneID

23173.

KEGG

hsa:23173.

UCSC

uc003huf.4. human.

Organism-specific databases

CTD

23173.

GeneCards

GC04P099916.

HGNC

HGNC:15789. METAP1.

HPA

CAB025485.

MIM

610151. gene.

neXtProt

NX_P53582.

PharmGKB

PA30764.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0024.

HOGENOM

HOG000030427.

HOVERGEN

HBG067178.

InParanoid

P53582.

KO

K01265.

OMA

GEVIQKH.

OrthoDB

EOG40S0FP.

PhylomeDB

P53582.

Enzyme and pathway databases

BRENDA

3.4.11.18. 2681.

SABIO-RK

P53582.

Gene expression databases

ArrayExpress

P53582.

Bgee

P53582.

CleanEx

HS_METAP1.

Genevestigator

P53582.

GermOnline

ENSG00000164024. Homo sapiens.

Family and domain databases

Gene3D

3.90.230.10. 1 hit.

InterPro

IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]

Pfam

PF00557. Peptidase_M24. 1 hit.
[Graphical view]

PRINTS

PR00599. MAPEPTIDASE.

SUPFAM

SSF55920. Peptidase_M24_cat_core. 1 hit.

TIGRFAMs

TIGR00500. met_pdase_I. 1 hit.

PROSITE

PS00680. MAP_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P53582.

ChEMBL

CHEMBL2474.

EvolutionaryTrace

P53582.

GenomeRNAi

23173.

NextBio

44587.

SOURCE

Search...

Entry information

Entry name

AMPM1_HUMAN

Accession

Primary (citable) accession number: P53582
Secondary accession number(s): B4E2E6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 25, 2003
Last modified:	May 29, 2013
This is version 135 of the entry and version 2 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.