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P50579 (MAP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionine aminopeptidase 2

Short name=MAP 2
Short name=MetAP 2
EC=3.4.11.18
Alternative name(s):
Initiation factor 2-associated 67 kDa glycoprotein
Short name=p67
Short name=p67eIF2
Peptidase M
Gene names
Name:METAP2
Synonyms:MNPEP, P67EIF2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo. Ref.6 Ref.10 Ref.15 Ref.20

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. Ref.6 Ref.10 Ref.15 Ref.20

Catalytic activity

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. Ref.10

Cofactor

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. Also manganese has been proposed to be the physiological cofactor for human METAP2. Ref.7 Ref.14 Ref.20

Subunit structure

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

Subcellular location

Cytoplasm. Note: About 30% of expressed METAP2 associates with polysomes. Ref.12

Post-translational modification

Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. O-glycosylation is required for EIF2S1 binding. HAMAP-Rule MF_03175

Sequence similarities

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

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
   Molecular functionAminopeptidase
Hydrolase
Protease
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processN-terminal protein amino acid modification

Inferred from direct assay PubMed 8858118. Source: HGNC

peptidyl-methionine modification

Inferred from direct assay PubMed 8858118. Source: HGNC

phototransduction, visible light

Traceable author statement. Source: Reactome

protein initiator methionine removal

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protein processing

Inferred from direct assay PubMed 8858118. Source: HGNC

regulation of rhodopsin mediated signaling pathway

Traceable author statement. Source: Reactome

rhodopsin mediated signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15102683. Source: HGNC

cytosol

Traceable author statement. Source: Reactome

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionaminopeptidase activity

Inferred from direct assay PubMed 8858118. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metalloaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metalloexopeptidase activity

Inferred from direct assay PubMed 8858118. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 478477Methionine aminopeptidase 2 HAMAP-Rule MF_03175
PRO_0000148982

Regions

Compositional bias41 – 466Poly-Lys HAMAP-Rule MF_03175
Compositional bias98 – 1069Poly-Lys HAMAP-Rule MF_03175

Sites

Metal binding2511Divalent metal cation 1
Metal binding2621Divalent metal cation 1
Metal binding2621Divalent metal cation 2; catalytic
Metal binding3311Divalent metal cation 2; catalytic; via tele nitrogen
Metal binding3641Divalent metal cation 2; catalytic
Metal binding4591Divalent metal cation 1
Metal binding4591Divalent metal cation 2; catalytic
Binding site2311Substrate
Binding site3391Substrate

Amino acid modifications

Modified residue21N-acetylalanine Ref.9
Modified residue451Phosphoserine Ref.8 Ref.11
Modified residue601Phosphoserine; alternate Ref.8
Modified residue631Phosphoserine; alternate Ref.8
Modified residue741Phosphoserine Ref.8 Ref.11
Glycosylation601O-linked (GlcNAc); alternate By similarity
Glycosylation631O-linked (GlcNAc); alternate By similarity

Secondary structure

........................................................ 478
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50579 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 5788E4BB83E48F9A

FASTA47852,892
        10         20         30         40         50         60 
MAGVEEVAAS GSHLNGDLDP DDREEGAAST AEEAAKKKRR KKKKSKGPSA AGEQEPDKES 

        70         80         90        100        110        120 
GASVDEVARQ LERSALEDKE RDEDDEDGDG DGDGATGKKK KKKKKKRGPK VQTDPPSVPI 

       130        140        150        160        170        180 
CDLYPNGVFP KGQECEYPPT QDGRTAAWRT TSEEKKALDQ ASEEIWNDFR EAAEAHRQVR 

       190        200        210        220        230        240 
KYVMSWIKPG MTMIEICEKL EDCSRKLIKE NGLNAGLAFP TGCSLNNCAA HYTPNAGDTT 

       250        260        270        280        290        300 
VLQYDDICKI DFGTHISGRI IDCAFTVTFN PKYDTLLKAV KDATNTGIKC AGIDVRLCDV 

       310        320        330        340        350        360 
GEAIQEVMES YEVEIDGKTY QVKPIRNLNG HSIGQYRIHA GKTVPIVKGG EATRMEEGEV 

       370        380        390        400        410        420 
YAIETFGSTG KGVVHDDMEC SHYMKNFDVG HVPIRLPRTK HLLNVINENF GTLAFCRRWL 

       430        440        450        460        470 
DRLGESKYLM ALKNLCDLGI VDPYPPLCDI KGSYTAQFEH TILLRPTCKE VVSRGDDY 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Molecular cloning of a human complementary DNA encoding an initiation factor 2-associated protein (p67)."
Li X., Chang Y.
Biochim. Biophys. Acta 1260:333-336(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Lymph.
[6]"Glycosylation of eukaryotic peptide chain initiation factor 2 (eIF-2)-associated 67-kDa polypeptide (p67) and its possible role in the inhibition of eIF-2 kinase-catalyzed phosphorylation of the eIF-2 alpha-subunit."
Datta B., Ray M.K., Chakrabarti D., Wylie D.E., Gupta N.K.
J. Biol. Chem. 264:20620-20624(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN EIF2S1 PROTECTION, GLYCOSYLATION.
[7]"Physiologically relevant metal cofactor for methionine aminopeptidase-2 is manganese."
Wang J., Sheppard G.S., Lou P., Kawai M., Park C., Egan D.A., Schneider A., Bouska J., Lesniewski R., Henkin J.
Biochemistry 42:5035-5042(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-60; SER-63 AND SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"Protein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases."
Xiao Q., Zhang F., Nacev B.A., Liu J.O., Pei D.
Biochemistry 49:5588-5599(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Localization and function of a eukaryotic-initiation-factor-2-associated 67-kDa glycoprotein."
Wu S.
World J. Biol. Chem. 1:313-320(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Structure of human methionine aminopeptidase-2 complexed with fumagillin."
Liu S., Widom J., Kemp C.W., Crews C.M., Clardy J.
Science 282:1324-1327(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FUMAGILLIN, COFACTOR.
[15]"Proteomics-based target identification: bengamides as a new class of methionine aminopeptidase inhibitors."
Towbin H., Bair K.W., DeCaprio J.A., Eck M.J., Kim S., Kinder F.R., Morollo A., Mueller D.R., Schindler P., Song H.K., van Oostrum J., Versace R.W., Voshol H., Wood J., Zabludoff S., Phillips P.E.
J. Biol. Chem. 278:52964-52971(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH COBALT IONS AND BENGAMIDE, FUNCTION.
[16]"3-amino-2-hydroxyamides and related compounds as inhibitors of methionine aminopeptidase-2."
Sheppard G.S., Wang J., Kawai M., BaMaung N.Y., Craig R.A., Erickson S.A., Lynch L., Patel J., Yang F., Searle X.B., Lou P., Park C., Kim K.H., Henkin J., Lesniewski R.
Bioorg. Med. Chem. Lett. 14:865-868(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 110-478 IN COMPLEX WITH INHIBITOR A-357300.
[17]"4-aryl-1,2,3-triazole: a novel template for a reversible methionine aminopeptidase 2 inhibitor, optimized to inhibit angiogenesis in vivo."
Kallander L.S., Lu Q., Chen W., Tomaszek T., Yang G., Tew D., Meek T.D., Hofmann G.A., Schulz-Pritchard C.K., Smith W.W., Janson C.A., Ryan M.D., Zhang G.-F., Johanson K.O., Kirkpatrick R.B., Ho T.F., Fisher P.W., Mattern M.R. expand/collapse author list , Johnson R.K., Hansbury M.J., Winkler J.D., Ward K.W., Veber D.F., Thompson S.K.
J. Med. Chem. 48:5644-5647(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 110-478 IN COMPLEX WITH 4-ARYL-1,2,3-TRIAZOLE AND COBALT IONS.
[18]"Human methionine aminopeptidase type 2 in complex with L- and D-methionine."
Nonato M.C., Widom J., Clardy J.
Bioorg. Med. Chem. Lett. 16:2580-2583(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH ZINC IONS AND METHIONINE, PARTIAL PROTEIN SEQUENCE.
[19]"Lead optimization of methionine aminopeptidase-2 (MetAP2) inhibitors containing sulfonamides of 5,6-disubstituted anthranilic acids."
Wang G.T., Mantei R.A., Kawai M., Tedrow J.S., Barnes D.M., Wang J., Zhang Q., Lou P., Garcia L.A., Bouska J., Yates M., Park C., Judge R.A., Lesniewski R., Sheppard G.S., Bell R.L.
Bioorg. Med. Chem. Lett. 17:2817-2822(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 110-478 IN COMPLEX WITH MANGANESE AND INHIBITOR.
[20]"Highly potent inhibitors of methionine aminopeptidase-2 based on a 1,2,4-triazole pharmacophore."
Marino J.P. Jr., Fisher P.W., Hofmann G.A., Kirkpatrick R.B., Janson C.A., Johnson R.K., Ma C., Mattern M., Meek T.D., Ryan M.D., Schulz C., Smith W.W., Tew D.G., Tomazek T.A. Jr., Veber D.F., Xiong W.C., Yamamoto Y., Yamashita K., Yang G., Thompson S.K.
J. Med. Chem. 50:3777-3785(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 110-478 IN COMPLEX WITH COBALT IONS AND INHIBITOR, COFACTOR, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U29607 mRNA. Translation: AAA82930.1.
U13261 mRNA. Translation: AAC63402.1.
AK315559 mRNA. Translation: BAG37935.1.
CH471054 Genomic DNA. Translation: EAW97537.1.
BC013782 mRNA. Translation: AAH13782.1.
CCDSCCDS9052.1.
PIRDPHUM2. S52112.
RefSeqNP_006829.1. NM_006838.3.
UniGeneHs.444986.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B59X-ray1.80A109-478[»]
1B6AX-ray1.60A1-478[»]
1BN5X-ray1.80A1-478[»]
1BOAX-ray1.80A1-478[»]
1KQ0X-ray2.00A1-478[»]
1KQ9X-ray1.90A1-478[»]
1QZYX-ray1.60A1-478[»]
1R58X-ray1.90A110-478[»]
1R5GX-ray2.00A110-478[»]
1R5HX-ray2.40A110-478[»]
1YW7X-ray1.85A110-478[»]
1YW8X-ray2.65A110-478[»]
1YW9X-ray1.64A110-478[»]
2ADUX-ray1.90A110-478[»]
2EA2X-ray2.50A110-478[»]
2EA4X-ray2.35A110-478[»]
2GA2X-ray1.95A110-478[»]
2OAZX-ray1.90A110-478[»]
ProteinModelPortalP50579.
SMRP50579. Positions 110-478.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116184. 12 interactions.
IntActP50579. 2 interactions.
MINTMINT-2803706.
STRING9606.ENSP00000325312.

Chemistry

BindingDBP50579.
ChEMBLCHEMBL3922.
DrugBankDB00134. L-Methionine.
GuidetoPHARMACOLOGY1573.

Protein family/group databases

MEROPSM24.002.

PTM databases

PhosphoSiteP50579.

Polymorphism databases

DMDM1703273.

2D gel databases

REPRODUCTION-2DPAGEIPI00033036.

Proteomic databases

MaxQBP50579.
PaxDbP50579.
PeptideAtlasP50579.
PRIDEP50579.

Protocols and materials databases

DNASU10988.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323666; ENSP00000325312; ENSG00000111142.
GeneID10988.
KEGGhsa:10988.
UCSCuc001tec.3. human.

Organism-specific databases

CTD10988.
GeneCardsGC12P095800.
HGNCHGNC:16672. METAP2.
HPACAB013025.
HPA019095.
MIM601870. gene.
neXtProtNX_P50579.
PharmGKBPA30765.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0024.
HOGENOMHOG000226278.
HOVERGENHBG050495.
InParanoidP50579.
KOK01265.
OMAIQICEEL.
PhylomeDBP50579.
TreeFamTF300426.

Enzyme and pathway databases

BRENDA3.4.11.18. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP50579.
BgeeP50579.
CleanExHS_METAP2.
GenevestigatorP50579.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPMF_03175. MetAP_2_euk.
InterProIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSPR00599. MAPEPTIDASE.
SUPFAMSSF55920. SSF55920. 2 hits.
TIGRFAMsTIGR00501. met_pdase_II. 1 hit.
PROSITEPS01202. MAP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMETAP2. human.
EvolutionaryTraceP50579.
GeneWikiMETAP2.
GenomeRNAi10988.
NextBio41747.
PROP50579.
SOURCESearch...

Entry information

Entry nameMAP2_HUMAN
AccessionPrimary (citable) accession number: P50579
Secondary accession number(s): B2RDI8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM