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Protein

Methionine aminopeptidase 2

Gene

METAP2

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 4 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).UniRule annotationSAAS annotation
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.UniRule annotation
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).UniRule annotation

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Fe2+SAAS annotation
  • Mn2+SAAS annotation
  • Zn2+SAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei230 – 2301SubstrateUniRule annotation
Metal bindingi250 – 2501Divalent metal cation 1UniRule annotation
Metal bindingi261 – 2611Divalent metal cation 1UniRule annotation
Metal bindingi261 – 2611Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi330 – 3301Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei338 – 3381SubstrateUniRule annotation
Metal bindingi363 – 3631Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi458 – 4581Divalent metal cation 1UniRule annotation
Metal bindingi458 – 4581Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

AminopeptidaseUniRule annotationSAAS annotation, Hydrolase, Protease

Keywords - Ligandi

Metal-bindingUniRule annotationSAAS annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2UniRule annotation
Short name:
MetAP 2UniRule annotation
Alternative name(s):
Initiation factor 2-associated 67 kDa glycoproteinUniRule annotation
Peptidase MUniRule annotation
Gene namesi
Name:METAP2UniRule annotationImported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:16672. METAP2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

PTM / Processingi

Post-translational modificationi

Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. O-glycosylation is required for EIF2S1 binding.UniRule annotation

Keywords - PTMi

GlycoproteinUniRule annotation

Proteomic databases

EPDiF8VQZ7.
MaxQBiF8VQZ7.
PaxDbiF8VQZ7.
PeptideAtlasiF8VQZ7.

Expressioni

Gene expression databases

BgeeiENSG00000111142.
ExpressionAtlasiF8VQZ7. baseline and differential.

Interactioni

Subunit structurei

Binds EIF2S1 at low magnesium concentrations. Interacts strongly with the eIF-2 gamma-subunit EIF2S3.UniRule annotation

Protein-protein interaction databases

IntActiF8VQZ7. 1 interaction.
STRINGi9606.ENSP00000325312.

Structurei

3D structure databases

ProteinModelPortaliF8VQZ7.
SMRiF8VQZ7. Positions 109-477.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini167 – 464298Peptidase_M24InterPro annotationAdd
BLAST

Phylogenomic databases

eggNOGiKOG2775. Eukaryota.
COG0024. LUCA.
GeneTreeiENSGT00530000063220.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk. 1 hit.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

F8VQZ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGVEEVAAS GSHLNGDLDP DDREEGAAST AEEAAKKKRR KKKKSKGPSA
60 70 80 90 100
GEQEPDKESG ASVDEVARQL ERSALEDKER DEDDEDGDGD GDGATGKKKK
110 120 130 140 150
KKKKKRGPKV QTDPPSVPIC DLYPNGVFPK GQECEYPPTQ DGRTAAWRTT
160 170 180 190 200
SEEKKALDQA SEEIWNDFRE AAEAHRQVRK YVMSWIKPGM TMIEICEKLE
210 220 230 240 250
DCSRKLIKEN GLNAGLAFPT GCSLNNCAAH YTPNAGDTTV LQYDDICKID
260 270 280 290 300
FGTHISGRII DCAFTVTFNP KYDTLLKAVK DATNTGIKCA GIDVRLCDVG
310 320 330 340 350
EAIQEVMESY EVEIDGKTYQ VKPIRNLNGH SIGQYRIHAG KTVPIVKGGE
360 370 380 390 400
ATRMEEGEVY AIETFGSTGK GVVHDDMECS HYMKNFDVGH VPIRLPRTKH
410 420 430 440 450
LLNVINENFG TLAFCRRWLD RLGESKYLMA LKNLCDLGIV DPYPPLCDIK
460 470
GSYTAQFEHT ILLRPTCKEV VSRGDDY
Length:477
Mass (Da):52,820
Last modified:September 21, 2011 - v1
Checksum:i2ABB853D47E76249
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC018475 Genomic DNA. No translation available.
RefSeqiXP_005268640.1. XM_005268583.3.
UniGeneiHs.444986.

Genome annotation databases

EnsembliENST00000551840; ENSP00000450063; ENSG00000111142.
GeneIDi10988.
UCSCiuc058ryg.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC018475 Genomic DNA. No translation available.
RefSeqiXP_005268640.1. XM_005268583.3.
UniGeneiHs.444986.

3D structure databases

ProteinModelPortaliF8VQZ7.
SMRiF8VQZ7. Positions 109-477.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiF8VQZ7. 1 interaction.
STRINGi9606.ENSP00000325312.

Proteomic databases

EPDiF8VQZ7.
MaxQBiF8VQZ7.
PaxDbiF8VQZ7.
PeptideAtlasiF8VQZ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000551840; ENSP00000450063; ENSG00000111142.
GeneIDi10988.
UCSCiuc058ryg.1. human.

Organism-specific databases

CTDi10988.
HGNCiHGNC:16672. METAP2.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2775. Eukaryota.
COG0024. LUCA.
GeneTreeiENSGT00530000063220.

Miscellaneous databases

ChiTaRSiMETAP2. human.
GenomeRNAii10988.

Gene expression databases

BgeeiENSG00000111142.
ExpressionAtlasiF8VQZ7. baseline and differential.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk. 1 hit.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiF8VQZ7_HUMAN
AccessioniPrimary (citable) accession number: F8VQZ7
Entry historyi
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: September 7, 2016
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.