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Protein

Methionine aminopeptidase 1

Gene

METAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle.UniRule annotation2 Publications

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation1 Publication

Cofactori

Co2+UniRule annotation4 Publications, Zn2+UniRule annotation, Mn2+UniRule annotation, Fe2+UniRule annotationNote: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei203SubstrateUniRule annotation3 Publications1
Metal bindingi220Divalent metal cation 1UniRule annotation4 Publications1
Metal bindingi231Divalent metal cation 1UniRule annotation4 Publications1
Metal bindingi231Divalent metal cation 2; catalyticUniRule annotation4 Publications1
Metal bindingi294Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation4 Publications1
Binding sitei301SubstrateUniRule annotation3 Publications1
Metal bindingi327Divalent metal cation 2; catalyticUniRule annotation4 Publications1
Metal bindingi358Divalent metal cation 1UniRule annotation4 Publications1
Metal bindingi358Divalent metal cation 2; catalyticUniRule annotation4 Publications1

GO - Molecular functioni

  • aminopeptidase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • metalloexopeptidase activity Source: UniProtKB

GO - Biological processi

  • N-terminal protein amino acid modification Source: HGNC
  • peptidyl-methionine modification Source: HGNC
  • platelet aggregation Source: UniProtKB
  • regulation of rhodopsin mediated signaling pathway Source: Reactome
  • regulation of translation Source: HGNC

Keywordsi

Molecular functionAminopeptidase, Hydrolase, Protease
LigandMetal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS08982-MONOMER
BRENDAi3.4.11.18 2681
ReactomeiR-HSA-2514859 Inactivation, recovery and regulation of the phototransduction cascade
SABIO-RKiP53582

Protein family/group databases

MEROPSiM24.017

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 1UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 1UniRule annotation
Short name:
MetAP 1UniRule annotation
Alternative name(s):
Peptidase M 1UniRule annotation
Gene namesi
Name:METAP1
Synonyms:KIAA0094
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000164024.11
HGNCiHGNC:15789 METAP1
MIMi610151 gene
neXtProtiNX_P53582

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi23173
OpenTargetsiENSG00000164024
PharmGKBiPA30764

Chemistry databases

ChEMBLiCHEMBL2474
DrugBankiDB07901 5-CHLORO-6-METHYL-N-(2-PHENYLETHYL)-2-PYRIDIN-2-YLPYRIMIDIN-4-AMINE
DB04324 Ovalicin
GuidetoPHARMACOLOGYi1572

Polymorphism and mutation databases

BioMutaiMETAP1
DMDMi33302602

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001489672 – 386Methionine aminopeptidase 1Add BLAST385

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP53582
MaxQBiP53582
PaxDbiP53582
PeptideAtlasiP53582
PRIDEiP53582
ProteomicsDBi56586

PTM databases

iPTMnetiP53582
PhosphoSitePlusiP53582

Expressioni

Gene expression databases

BgeeiENSG00000164024
CleanExiHS_METAP1
ExpressionAtlasiP53582 baseline and differential
GenevisibleiP53582 HS

Organism-specific databases

HPAiCAB025485
HPA037997
HPA037998

Interactioni

Subunit structurei

Associates with the 60S ribosomal subunit of the 80S translational complex.UniRule annotation

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi116785, 17 interactors
IntActiP53582, 8 interactors
MINTiP53582
STRINGi9606.ENSP00000296411

Chemistry databases

BindingDBiP53582

Structurei

Secondary structure

1386
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi84 – 86Combined sources3
Helixi107 – 110Combined sources4
Helixi117 – 121Combined sources5
Turni122 – 124Combined sources3
Helixi133 – 155Combined sources23
Helixi163 – 176Combined sources14
Turni182 – 185Combined sources4
Helixi186 – 188Combined sources3
Beta strandi191 – 197Combined sources7
Beta strandi200 – 202Combined sources3
Beta strandi216 – 225Combined sources10
Beta strandi228 – 237Combined sources10
Helixi243 – 261Combined sources19
Helixi271 – 282Combined sources12
Beta strandi293 – 295Combined sources3
Beta strandi297 – 306Combined sources10
Beta strandi309 – 311Combined sources3
Beta strandi323 – 326Combined sources4
Beta strandi329 – 333Combined sources5
Beta strandi337 – 339Combined sources3
Beta strandi346 – 348Combined sources3
Beta strandi354 – 356Combined sources3
Beta strandi358 – 363Combined sources6
Beta strandi365 – 370Combined sources6
Helixi381 – 383Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B3HX-ray1.10A81-384[»]
2B3KX-ray1.55A81-384[»]
2B3LX-ray1.50A81-384[»]
2G6PX-ray1.90A81-384[»]
2GZ5X-ray1.10A81-384[»]
2NQ6X-ray1.50A81-384[»]
2NQ7X-ray1.60A81-384[»]
4FLIX-ray1.55A81-386[»]
4FLJX-ray1.74A81-386[»]
4FLKX-ray1.47A81-386[»]
4FLLX-ray1.50A81-386[»]
4HXXX-ray2.09A81-384[»]
4IKRX-ray1.78A81-384[»]
4IKSX-ray1.70A81-384[»]
4IKTX-ray1.60A81-384[»]
4IKUX-ray1.30A81-384[»]
4IU6X-ray1.90A1-384[»]
4U1BX-ray1.89A81-386[»]
4U69X-ray1.60A81-386[»]
4U6CX-ray1.91A81-386[»]
4U6EX-ray1.90A81-386[»]
4U6JX-ray1.56A81-386[»]
4U6WX-ray1.83A81-386[»]
4U6ZX-ray1.80A81-386[»]
4U70X-ray1.60A81-386[»]
4U71X-ray1.80A81-386[»]
4U73X-ray1.80A81-386[»]
4U75X-ray1.94A81-386[»]
4U76X-ray1.87A81-386[»]
ProteinModelPortaliP53582
SMRiP53582
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53582

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni9 – 52Zinc finger-like; important for proper ribosome associationUniRule annotationAdd BLAST44

Sequence similaritiesi

Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG2738 Eukaryota
COG0024 LUCA
GeneTreeiENSGT00390000002284
HOGENOMiHOG000030427
HOVERGENiHBG067178
InParanoidiP53582
KOiK01265
OMAiGDHAYTF
OrthoDBiEOG091G0F4A
PhylomeDBiP53582
TreeFamiTF105753

Family and domain databases

CDDicd01086 MetAP1, 1 hit
HAMAPiMF_01974 MetAP_1, 1 hit
InterProiView protein in InterPro
IPR036005 Creatinase/aminopeptidase-like
IPR000994 Pept_M24
IPR001714 Pept_M24_MAP
IPR002467 Pept_M24A_MAP1
IPR031615 Zfn-C6H2
PfamiView protein in Pfam
PF00557 Peptidase_M24, 1 hit
PF15801 zf-C6H2, 1 hit
PRINTSiPR00599 MAPEPTIDASE
SUPFAMiSSF55920 SSF55920, 1 hit
TIGRFAMsiTIGR00500 met_pdase_I, 1 hit
PROSITEiView protein in PROSITE
PS00680 MAP_1, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53582-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVETRVCE TDGCSSEAKL QCPTCIKLGI QGSYFCSQEC FKGSWATHKL
60 70 80 90 100
LHKKAKDEKA KREVSSWTVE GDINTDPWAG YRYTGKLRPH YPLMPTRPVP
110 120 130 140 150
SYIQRPDYAD HPLGMSESEQ ALKGTSQIKL LSSEDIEGMR LVCRLAREVL
160 170 180 190 200
DVAAGMIKPG VTTEEIDHAV HLACIARNCY PSPLNYYNFP KSCCTSVNEV
210 220 230 240 250
ICHGIPDRRP LQEGDIVNVD ITLYRNGYHG DLNETFFVGE VDDGARKLVQ
260 270 280 290 300
TTYECLMQAI DAVKPGVRYR ELGNIIQKHA QANGFSVVRS YCGHGIHKLF
310 320 330 340 350
HTAPNVPHYA KNKAVGVMKS GHVFTIEPMI CEGGWQDETW PDGWTAVTRD
360 370 380
GKRSAQFEHT LLVTDTGCEI LTRRLDSARP HFMSQF
Length:386
Mass (Da):43,215
Last modified:July 25, 2003 - v2
Checksum:i372879013C2BB01D
GO

Sequence cautioni

The sequence AAH30054 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA07679 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS47110.1
RefSeqiNP_055958.2, NM_015143.2
UniGeneiHs.480364

Genome annotation databases

EnsembliENST00000296411; ENSP00000296411; ENSG00000164024
GeneIDi23173
KEGGihsa:23173
UCSCiuc003huf.5 human

Similar proteinsi

Entry informationi

Entry nameiMAP11_HUMAN
AccessioniPrimary (citable) accession number: P53582
Secondary accession number(s): B4E2E6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 25, 2003
Last modified: June 20, 2018
This is version 184 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

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