Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Methionine aminopeptidase 1

Gene

METAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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-HAMAP
  • metalloaminopeptidase activity Source: UniProtKB-HAMAP
  • metalloexopeptidase activity Source: UniProtKB

GO - Biological processi

  • N-terminal protein amino acid modification Source: HGNC
  • peptidyl-methionine modification Source: HGNC
  • platelet aggregation Source: UniProtKB
  • protein initiator methionine removal Source: UniProtKB-HAMAP
  • regulation of rhodopsin mediated signaling pathway Source: Reactome
  • regulation of translation Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS08982-MONOMER.
BRENDAi3.4.11.18. 2681.
ReactomeiR-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
SABIO-RKP53582.

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

HGNCiHGNC:15789. METAP1.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytoplasm Source: HGNC
  • cytosol Source: Reactome
  • cytosolic ribosome Source: UniProtKB-HAMAP
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi23173.
OpenTargetsiENSG00000164024.
PharmGKBiPA30764.

Chemistry databases

ChEMBLiCHEMBL2474.
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.

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

Protein-protein interaction databases

BioGridi116785. 12 interactors.
IntActiP53582. 7 interactors.
MINTiMINT-1191219.
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.
OMAiKGQARTP.
OrthoDBiEOG091G0F4A.
PhylomeDBiP53582.
TreeFamiTF105753.

Family and domain databases

CDDicd01086. MetAP1. 1 hit.
Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1. 1 hit.
InterProiIPR000994. Pept_M24.
IPR001714. Pept_M24_MAP.
IPR002467. Pept_M24A_MAP1.
IPR031615. Zfn-C6H2.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
PF15801. zf-C6H2. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi116785. 12 interactors.
IntActiP53582. 7 interactors.
MINTiMINT-1191219.
STRINGi9606.ENSP00000296411.

Chemistry databases

BindingDBiP53582.
ChEMBLiCHEMBL2474.
GuidetoPHARMACOLOGYi1572.

Protein family/group databases

MEROPSiM24.017.

PTM databases

iPTMnetiP53582.
PhosphoSitePlusiP53582.

Polymorphism and mutation databases

BioMutaiMETAP1.
DMDMi33302602.

Proteomic databases

EPDiP53582.
MaxQBiP53582.
PaxDbiP53582.
PeptideAtlasiP53582.
PRIDEiP53582.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi23173.
DisGeNETi23173.
GeneCardsiMETAP1.
HGNCiHGNC:15789. METAP1.
HPAiCAB025485.
HPA037997.
HPA037998.
MIMi610151. gene.
neXtProtiNX_P53582.
OpenTargetsiENSG00000164024.
PharmGKBiPA30764.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:HS08982-MONOMER.
BRENDAi3.4.11.18. 2681.
ReactomeiR-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
SABIO-RKP53582.

Miscellaneous databases

ChiTaRSiMETAP1. human.
EvolutionaryTraceiP53582.
GeneWikiiMETAP1.
GenomeRNAii23173.
PROiP53582.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000164024.
CleanExiHS_METAP1.
ExpressionAtlasiP53582. baseline and differential.
GenevisibleiP53582. HS.

Family and domain databases

CDDicd01086. MetAP1. 1 hit.
Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1. 1 hit.
InterProiIPR000994. Pept_M24.
IPR001714. Pept_M24_MAP.
IPR002467. Pept_M24A_MAP1.
IPR031615. Zfn-C6H2.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
PF15801. zf-C6H2. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMAP11_HUMAN
AccessioniPrimary (citable) accession number: P53582
Secondary accession number(s): B4E2E6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 25, 2003
Last modified: November 30, 2016
This is version 173 of the entry and version 2 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.