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 2

Gene

Metap2

Organism
Mus musculus (Mouse)
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).UniRule 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

Catalytic activityi

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

Cofactori

Co2+UniRule annotation, 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei231 – 2311SubstrateUniRule annotation
Metal bindingi251 – 2511Divalent metal cation 1UniRule annotation
Metal bindingi262 – 2621Divalent metal cation 1UniRule annotation
Metal bindingi262 – 2621Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi331 – 3311Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei339 – 3391SubstrateUniRule annotation
Metal bindingi364 – 3641Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi459 – 4591Divalent metal cation 1UniRule annotation
Metal bindingi459 – 4591Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-HAMAP
  3. metalloaminopeptidase activity Source: UniProtKB-HAMAP
  4. metalloexopeptidase activity Source: UniProtKB
  5. poly(A) RNA binding Source: MGI

GO - Biological processi

  1. N-terminal protein amino acid modification Source: HGNC
  2. peptidyl-methionine modification Source: HGNC
  3. protein initiator methionine removal Source: UniProtKB-HAMAP
  4. protein processing Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BRENDAi3.4.11.18. 3474.
ReactomeiREACT_311545. Inactivation, recovery and regulation of the phototransduction cascade.

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
Short name:
p67UniRule annotation
Short name:
p67eIF2UniRule annotation
Peptidase MUniRule annotation
Gene namesi
Name:Metap2
Synonyms:Mnpep, P67eif2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1929701. Metap2.

Subcellular locationi

Cytoplasm
Note: About 30% of expressed METAP2 associates with polysomes.UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: HGNC
  2. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 478477Methionine aminopeptidase 2PRO_0000148983Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei60 – 601Phosphoserine; alternateBy similarity
Glycosylationi60 – 601O-linked (GlcNAc); alternateBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO08663.
PaxDbiO08663.
PRIDEiO08663.

PTM databases

PhosphoSiteiO08663.

Expressioni

Gene expression databases

BgeeiO08663.
CleanExiMM_METAP2.
ExpressionAtlasiO08663. baseline and differential.
GenevestigatoriO08663.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi207891. 5 interactions.
IntActiO08663. 1 interaction.
MINTiMINT-1858053.

Structurei

3D structure databases

ProteinModelPortaliO08663.
SMRiO08663. Positions 110-478.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi41 – 466Poly-Lys
Compositional biasi98 – 1069Poly-Lys

Sequence similaritiesi

Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0024.
HOVERGENiHBG050495.
InParanoidiO08663.
KOiK01265.
OrthoDBiEOG7QRQVF.
PhylomeDBiO08663.
TreeFamiTF300426.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk.
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]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O08663-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGVEQAASF GGHLNGDLDP DDREEGTSST AEEAAKKKRR KKKKGKGAVS
60 70 80 90 100
AVQQELDKES GALVDEVAKQ LESQALEEKE RDDDDEDGDG DADGATGKKK
110 120 130 140 150
KKKKKKRGPK VQTDPPSVPI CDLYPNGVFP KGQECEYPPT QDGRTAAWRT
160 170 180 190 200
TSEEKKALDQ ASEEIWNDFR EAAEAHRQVR KYVMSWIKPG MTMIEICEKL
210 220 230 240 250
EDCSRKLIKE NGLNAGLAFP TGCSLNNCAA HYTPNAGDTT VLQYDDICKI
260 270 280 290 300
DFGTHISGRI IDCAFTVTFN PKYDILLTAV KDATNTGIKC AGIDVRLCDV
310 320 330 340 350
GEAIQEVMES YEVEIDGKTY QVKPIRNLNG HSIGPYRIHA GKTVPIVKGG
360 370 380 390 400
EATRMEEGEV YAIETFGSTG KGVVHDDMEC SHYMKNFDVG HVPIRLPRTK
410 420 430 440 450
HLLNVINENF GTLAFCRRWL DRLGESKYLM ALKNLCDLGI VDPYPPLCDI
460 470
KGSYTAQFEH TILLRPTCKE VVSRGDDY
Length:478
Mass (Da):52,922
Last modified:June 30, 1997 - v1
Checksum:iBBB9A2AFC19952E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB003144 mRNA. Translation: BAA19789.1.
AK076804 mRNA. Translation: BAC36488.1.
BC002213 mRNA. Translation: AAH02213.1.
CCDSiCCDS48673.1.
RefSeqiNP_062622.1. NM_019648.3.
XP_006513959.1. XM_006513896.2.
XP_006513960.1. XM_006513897.2.
UniGeneiMm.289329.

Genome annotation databases

EnsembliENSMUST00000047910; ENSMUSP00000048285; ENSMUSG00000036112.
ENSMUST00000180840; ENSMUSP00000138006; ENSMUSG00000036112.
GeneIDi56307.
KEGGimmu:56307.
UCSCiuc007gve.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB003144 mRNA. Translation: BAA19789.1.
AK076804 mRNA. Translation: BAC36488.1.
BC002213 mRNA. Translation: AAH02213.1.
CCDSiCCDS48673.1.
RefSeqiNP_062622.1. NM_019648.3.
XP_006513959.1. XM_006513896.2.
XP_006513960.1. XM_006513897.2.
UniGeneiMm.289329.

3D structure databases

ProteinModelPortaliO08663.
SMRiO08663. Positions 110-478.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207891. 5 interactions.
IntActiO08663. 1 interaction.
MINTiMINT-1858053.

Chemistry

BindingDBiO08663.
ChEMBLiCHEMBL1075272.

PTM databases

PhosphoSiteiO08663.

Proteomic databases

MaxQBiO08663.
PaxDbiO08663.
PRIDEiO08663.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000047910; ENSMUSP00000048285; ENSMUSG00000036112.
ENSMUST00000180840; ENSMUSP00000138006; ENSMUSG00000036112.
GeneIDi56307.
KEGGimmu:56307.
UCSCiuc007gve.1. mouse.

Organism-specific databases

CTDi10988.
MGIiMGI:1929701. Metap2.

Phylogenomic databases

eggNOGiCOG0024.
HOVERGENiHBG050495.
InParanoidiO08663.
KOiK01265.
OrthoDBiEOG7QRQVF.
PhylomeDBiO08663.
TreeFamiTF300426.

Enzyme and pathway databases

BRENDAi3.4.11.18. 3474.
ReactomeiREACT_311545. Inactivation, recovery and regulation of the phototransduction cascade.

Miscellaneous databases

ChiTaRSiMetap2. mouse.
NextBioi312244.
PROiO08663.
SOURCEiSearch...

Gene expression databases

BgeeiO08663.
CleanExiMM_METAP2.
ExpressionAtlasiO08663. baseline and differential.
GenevestigatoriO08663.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk.
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]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Sekiguchi S., Suzuki E.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X CBA.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 260-281; 297-318; 355-371 AND 386-395, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.

Entry informationi

Entry nameiMAP2_MOUSE
AccessioniPrimary (citable) accession number: O08663
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 14, 1998
Last sequence update: June 30, 1997
Last modified: March 31, 2015
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.