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P38062

- MAP2_RAT

UniProt

P38062 - MAP2_RAT

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Protein

Methionine aminopeptidase 2

Gene

Metap2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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).
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.

Catalytic activityi

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

Cofactori

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

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. 5301.

Protein family/group databases

MEROPSiM24.002.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi70995. Metap2.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: HGNC
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_0000148984Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei60 – 601Phosphoserine; alternateBy similarity
Glycosylationi60 – 601O-linked (GlcNAc); alternate1 Publication
Modified residuei63 – 631Phosphoserine; alternateBy similarity
Glycosylationi63 – 631O-linked (GlcNAc); alternate1 Publication

Post-translational modificationi

O-glycosylated; contains 12 O-linked GlcNAc.1 Publication
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

PaxDbiP38062.
PRIDEiP38062.

Expressioni

Inductioni

Heat shock increases expression by more than 36-fold.1 Publication

Gene expression databases

GenevestigatoriP38062.

Interactioni

Subunit structurei

Binds EIF2S1 at low magnesium concentrations (By similarity). Interacts strongly with the eIF-2 gamma-subunit EIF2S3.1 PublicationUniRule annotation

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000032680.

Structurei

3D structure databases

ProteinModelPortaliP38062.
SMRiP38062. Positions 110-478.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi36 – 10671Lys-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
HOVERGENiHBG050495.
InParanoidiP38062.
KOiK01265.
PhylomeDBiP38062.

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.

P38062-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGVEEASSF GGHLNRDLDP DDREEGTSST AEEAAKKKRR KKKKGKGAVS
60 70 80 90 100
AGQQELDKES GTSVDEVAKQ LERQALEEKE KDDDDEDGDG DGDGAAGKKK
110 120 130 140 150
KKKKKKRGPR 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 PKYDILLKAV 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):53,052
Last modified:October 1, 1996 - v2
Checksum:iBE1C0E91E0CB3D74
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti464 – 47815LRPTC…RGDDY → CAQPVKKLSAEEMTIKT in AAA41111. (PubMed:8496145)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L10652 mRNA. Translation: AAA41111.1.
PIRiA46702.
RefSeqiNP_071984.1. NM_022539.1.
UniGeneiRn.1984.

Genome annotation databases

GeneIDi64370.
KEGGirno:64370.
UCSCiRGD:70995. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L10652 mRNA. Translation: AAA41111.1 .
PIRi A46702.
RefSeqi NP_071984.1. NM_022539.1.
UniGenei Rn.1984.

3D structure databases

ProteinModelPortali P38062.
SMRi P38062. Positions 110-478.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000032680.

Protein family/group databases

MEROPSi M24.002.

Proteomic databases

PaxDbi P38062.
PRIDEi P38062.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 64370.
KEGGi rno:64370.
UCSCi RGD:70995. rat.

Organism-specific databases

CTDi 10988.
RGDi 70995. Metap2.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226278.
HOVERGENi HBG050495.
InParanoidi P38062.
KOi K01265.
PhylomeDBi P38062.

Enzyme and pathway databases

BRENDAi 3.4.11.18. 5301.

Miscellaneous databases

NextBioi 613106.
PROi P38062.

Gene expression databases

Genevestigatori P38062.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPi MF_03175. MetAP_2_euk.
InterProi IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 2 hits.
TIGRFAMsi TIGR00501. met_pdase_II. 1 hit.
PROSITEi PS01202. MAP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and characterization of complementary DNA encoding the eukaryotic initiation factor 2-associated 67-kDa protein (p67)."
    Wu S., Gupta S., Chatterjee N., Hileman R.E., Kinzy T.G., Denslow N.D., Merrick W.C., Chakrabarti D., Osterman J.C., Gupta N.K.
    J. Biol. Chem. 268:10796-10801(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Reuber H35.
    Tissue: Liver.
  2. "Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes."
    Arfin S.M., Kendall R.L., Hall L., Weaver L.H., Stewart A.E., Matthews B.W., Bradshaw R.A.
    Proc. Natl. Acad. Sci. U.S.A. 92:7714-7718(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO C-TERMINUS.
  3. Cited for: INDUCTION BY HEAT SHOCK.
  4. "A glycosylation site, 60SGTS63, of p67 is required for its ability to regulate the phosphorylation and activity of eukaryotic initiation factor 2alpha."
    Datta R., Choudhury P., Ghosh A., Datta B.
    Biochemistry 42:5453-5460(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-60 AND SER-63.
  5. "The N-terminal lysine residue-rich domain II and the 340-430 amino acid segment of eukaryotic initiation factor 2-associated glycoprotein p67 are the binding sites for the gamma-subunit of eIF2."
    Ghosh A., Datta R., Majumdar A., Bhattacharya M., Datta B.
    Exp. Cell Res. 312:3184-3203(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF2S3.

Entry informationi

Entry nameiMAP2_RAT
AccessioniPrimary (citable) accession number: P38062
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3