SubmitCancel

Skip Header

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

P38062

- MAP2_RAT

UniProt

P38062 - MAP2_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Methionine aminopeptidase 2
Gene
Metap2, Mnpep, P67eif2
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).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

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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei231 – 2311Substrate By similarity
Metal bindingi251 – 2511Divalent metal cation 1 By similarity
Metal bindingi262 – 2621Divalent metal cation 1 By similarity
Metal bindingi262 – 2621Divalent metal cation 2; catalytic By similarity
Metal bindingi331 – 3311Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei339 – 3391Substrate By similarity
Metal bindingi364 – 3641Divalent metal cation 2; catalytic By similarity
Metal bindingi459 – 4591Divalent metal cation 1 By similarity
Metal bindingi459 – 4591Divalent metal cation 2; catalytic By similarity

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
Complete GO annotation...

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 2 (EC:3.4.11.18)
Short name:
MAP 2
Short name:
MetAP 2
Alternative name(s):
Initiation factor 2-associated 67 kDa glycoprotein
Short name:
p67
Short name:
p67eIF2
Peptidase M
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 By similarity.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 – 11Removed By similarity
Chaini2 – 478477Methionine aminopeptidase 2UniRule annotation
PRO_0000148984Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei60 – 601Phosphoserine; alternate By similarity
Glycosylationi60 – 601O-linked (GlcNAc); alternate Inferred
Modified residuei63 – 631Phosphoserine; alternate By similarity
Glycosylationi63 – 631O-linked (GlcNAc); alternate Inferred

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 By similarity.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 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000032680.

Structurei

3D structure databases

ProteinModelPortaliP38062.
SMRiP38062. Positions 110-478.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi36 – 10671Lys-richUniRule annotation
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
HOVERGENiHBG050495.
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

MAGVEEASSF GGHLNRDLDP DDREEGTSST AEEAAKKKRR KKKKGKGAVS    50
AGQQELDKES GTSVDEVAKQ LERQALEEKE KDDDDEDGDG DGDGAAGKKK 100
KKKKKKRGPR VQTDPPSVPI CDLYPNGVFP KGQECEYPPT QDGRTAAWRT 150
TSEEKKALDQ ASEEIWNDFR EAAEAHRQVR KYVMSWIKPG MTMIEICEKL 200
EDCSRKLIKE NGLNAGLAFP TGCSLNNCAA HYTPNAGDTT VLQYDDICKI 250
DFGTHISGRI IDCAFTVTFN PKYDILLKAV KDATNTGIKC AGIDVRLCDV 300
GEAIQEVMES YEVEIDGKTY QVKPIRNLNG HSIGPYRIHA GKTVPIVKGG 350
EATRMEEGEV YAIETFGSTG KGVVHDDMEC SHYMKNFDVG HVPIRLPRTK 400
HLLNVINENF GTLAFCRRWL DRLGESKYLM ALKNLCDLGI VDPYPPLCDI 450
KGSYTAQFEH TILLRPTCKE VVSRGDDY 478
Length:478
Mass (Da):53,052
Last modified:October 1, 1996 - v2
Checksum:iBE1C0E91E0CB3D74
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti464 – 47815LRPTC…RGDDY → CAQPVKKLSAEEMTIKT in AAA41111. 1 Publication
Add
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...

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.
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: June 11, 2014
This is version 121 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

Similar proteinsi