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O08663

- MAP2_MOUSE

UniProt

O08663 - MAP2_MOUSE

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Protein
Methionine aminopeptidase 2
Gene
Metap2, Mnpep, P67eif2
Organism
Mus musculus (Mouse)
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) By similarity.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 By similarity.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
  5. protein 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_188266. Inactivation, recovery and regulation of the phototransduction cascade.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:1929701. 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_0000148983Add
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 By similarity

Post-translational modificationi

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

MaxQBiO08663.
PaxDbiO08663.
PRIDEiO08663.

PTM databases

PhosphoSiteiO08663.

Expressioni

Gene expression databases

ArrayExpressiO08663.
BgeeiO08663.
CleanExiMM_METAP2.
GenevestigatoriO08663.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliO08663.
SMRiO08663. Positions 110-478.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

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

MAGVEQAASF GGHLNGDLDP DDREEGTSST AEEAAKKKRR KKKKGKGAVS    50
AVQQELDKES GALVDEVAKQ LESQALEEKE RDDDDEDGDG DADGATGKKK 100
KKKKKKRGPK VQTDPPSVPI CDLYPNGVFP KGQECEYPPT QDGRTAAWRT 150
TSEEKKALDQ ASEEIWNDFR EAAEAHRQVR KYVMSWIKPG MTMIEICEKL 200
EDCSRKLIKE NGLNAGLAFP TGCSLNNCAA HYTPNAGDTT VLQYDDICKI 250
DFGTHISGRI IDCAFTVTFN PKYDILLTAV 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):52,922
Last modified:July 1, 1997 - v1
Checksum:iBBB9A2AFC19952E8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006513896.1.
XP_006513960.1. XM_006513897.1.
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:
EMBL
GenBank
DDBJ
Links Updated
AB003144 mRNA. Translation: BAA19789.1 .
AK076804 mRNA. Translation: BAC36488.1 .
BC002213 mRNA. Translation: AAH02213.1 .
CCDSi CCDS48673.1.
RefSeqi NP_062622.1. NM_019648.3.
XP_006513959.1. XM_006513896.1.
XP_006513960.1. XM_006513897.1.
UniGenei Mm.289329.

3D structure databases

ProteinModelPortali O08663.
SMRi O08663. Positions 110-478.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 207891. 5 interactions.
IntActi O08663. 1 interaction.
MINTi MINT-1858053.

Chemistry

BindingDBi O08663.
ChEMBLi CHEMBL1075272.

Protein family/group databases

MEROPSi M24.002.

PTM databases

PhosphoSitei O08663.

Proteomic databases

MaxQBi O08663.
PaxDbi O08663.
PRIDEi O08663.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000047910 ; ENSMUSP00000048285 ; ENSMUSG00000036112 .
ENSMUST00000180840 ; ENSMUSP00000138006 ; ENSMUSG00000036112 .
GeneIDi 56307.
KEGGi mmu:56307.
UCSCi uc007gve.1. mouse.

Organism-specific databases

CTDi 10988.
MGIi MGI:1929701. Metap2.

Phylogenomic databases

eggNOGi COG0024.
HOVERGENi HBG050495.
InParanoidi O08663.
KOi K01265.
OrthoDBi EOG7QRQVF.
PhylomeDBi O08663.
TreeFami TF300426.

Enzyme and pathway databases

BRENDAi 3.4.11.18. 3474.
Reactomei REACT_188266. Inactivation, recovery and regulation of the phototransduction cascade.

Miscellaneous databases

ChiTaRSi METAP2. mouse.
NextBioi 312244.
PROi O08663.
SOURCEi Search...

Gene expression databases

ArrayExpressi O08663.
Bgeei O08663.
CleanExi MM_METAP2.
Genevestigatori O08663.

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

« Hide 'large scale' publications
  1. Sekiguchi S., Suzuki E.
    Submitted (APR-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(2005) [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(2004) [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 (JAN-2009) 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 15, 1998
Last sequence update: July 1, 1997
Last modified: September 3, 2014
This is version 127 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

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