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Protein

Methionine aminopeptidase 2B

Gene

MAP2B

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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

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 sitei192 – 1921SubstrateUniRule annotation
Metal bindingi212 – 2121Divalent metal cation 1UniRule annotation
Metal bindingi223 – 2231Divalent metal cation 1UniRule annotation
Metal bindingi223 – 2231Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi292 – 2921Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei300 – 3001SubstrateUniRule annotation
Metal bindingi325 – 3251Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi420 – 4201Divalent metal cation 1UniRule annotation
Metal bindingi420 – 4201Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. protein initiator methionine removal Source: UniProtKB-HAMAP
  2. protein processing Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciARA:AT3G59990-MONOMER.
ARA:GQT-1753-MONOMER.
ARA:GQT-2672-MONOMER.
ARA:GQT-2673-MONOMER.
ReactomeiREACT_307091. Inactivation, recovery and regulation of the phototransduction cascade.

Protein family/group databases

MEROPSiM24.A02.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2BUniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2BUniRule annotation
Short name:
MetAP 2BUniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
Name:MAP2BUniRule annotation
Ordered Locus Names:At3g59990
ORF Names:F24G16.26
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G59990.

Subcellular locationi

Cytoplasm UniRule annotation1 Publication

GO - Cellular componenti

  1. cytoplasm Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439Methionine aminopeptidase 2BPRO_0000148971Add
BLAST

Proteomic databases

PaxDbiQ56Y85.
PRIDEiQ56Y85.

Expressioni

Tissue specificityi

Ubiquitous. Preferentially expressed in roots.1 Publication

Gene expression databases

GenevestigatoriQ56Y85.

Structurei

3D structure databases

ProteinModelPortaliQ56Y85.
SMRiQ56Y85. Positions 78-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi61 – 7313Lys-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
InParanoidiQ56Y85.
KOiK01265.
OMAiSTRMEED.
PhylomeDBiQ56Y85.

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]
PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
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.

Q56Y85-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASESPDVAV VAPVVENGGA ESSNGKEEQL ESELSKKLEI AEDGQEENDG
60 70 80 90 100
EEGSKAETST KKKKKKNKSK KKKELPQQTD PPSIPVVELF PSGEFPEGEI
110 120 130 140 150
QEYKDDNLWR TTSEEKRELE RFEKPIYNSV RRAAEVHRQV RKYVRSIVKP
160 170 180 190 200
GMLMTDICET LENTVRKLIS ENGLQAGIAF PTGCSLNWVA AHWTPNSGDK
210 220 230 240 250
TVLQYDDVMK LDFGTHIDGH IIDCAFTVAF NPMFDPLLAA SREATYTGIK
260 270 280 290 300
EAGIDVRLCD IGAAIQEVME SYEVEINGKV FQVKSIRNLN GHSIGPYQIH
310 320 330 340 350
AGKSVPIVKG GEQTKMEEGE FYAIETFGST GKGYVREDLE CSHYMKNFDA
360 370 380 390 400
GHVPLRLPRA KQLLATINKN FSTLAFCRRY LDRIGETKYL MALKNLCDSG
410 420 430
IVQPYPPLCD VKGSYVSQFE HTILLRPTCK EVLSKGDDY
Length:439
Mass (Da):49,060
Last modified:January 23, 2006 - v2
Checksum:iEC1C79EA1B49D3BF
GO

Sequence cautioni

The sequence BAD94472.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAB75818.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti270 – 2701E → K in AAL38337 (PubMed:14593172).Curated
Sequence conflicti270 – 2701E → K in AAN15382 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF300880 mRNA. Translation: AAG34551.1.
AL138647 Genomic DNA. Translation: CAB75818.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE79996.1.
CP002686 Genomic DNA. Translation: AEE79997.1.
CP002686 Genomic DNA. Translation: AEE79998.1.
CP002686 Genomic DNA. Translation: AEE79999.1.
AY065161 mRNA. Translation: AAL38337.1.
BT000063 mRNA. Translation: AAN15382.1.
AY084710 mRNA. Translation: AAM61284.1.
AK221438 mRNA. Translation: BAD94472.1. Different initiation.
PIRiT47823.
RefSeqiNP_001030898.1. NM_001035821.1.
NP_001190139.1. NM_001203210.1.
NP_567089.1. NM_115862.3.
NP_850725.1. NM_180394.1.
UniGeneiAt.16912.

Genome annotation databases

EnsemblPlantsiAT3G59990.1; AT3G59990.1; AT3G59990.
AT3G59990.2; AT3G59990.2; AT3G59990.
AT3G59990.3; AT3G59990.3; AT3G59990.
AT3G59990.4; AT3G59990.4; AT3G59990.
GeneIDi825169.
KEGGiath:AT3G59990.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF300880 mRNA. Translation: AAG34551.1.
AL138647 Genomic DNA. Translation: CAB75818.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE79996.1.
CP002686 Genomic DNA. Translation: AEE79997.1.
CP002686 Genomic DNA. Translation: AEE79998.1.
CP002686 Genomic DNA. Translation: AEE79999.1.
AY065161 mRNA. Translation: AAL38337.1.
BT000063 mRNA. Translation: AAN15382.1.
AY084710 mRNA. Translation: AAM61284.1.
AK221438 mRNA. Translation: BAD94472.1. Different initiation.
PIRiT47823.
RefSeqiNP_001030898.1. NM_001035821.1.
NP_001190139.1. NM_001203210.1.
NP_567089.1. NM_115862.3.
NP_850725.1. NM_180394.1.
UniGeneiAt.16912.

3D structure databases

ProteinModelPortaliQ56Y85.
SMRiQ56Y85. Positions 78-439.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM24.A02.

Proteomic databases

PaxDbiQ56Y85.
PRIDEiQ56Y85.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G59990.1; AT3G59990.1; AT3G59990.
AT3G59990.2; AT3G59990.2; AT3G59990.
AT3G59990.3; AT3G59990.3; AT3G59990.
AT3G59990.4; AT3G59990.4; AT3G59990.
GeneIDi825169.
KEGGiath:AT3G59990.

Organism-specific databases

GeneFarmi1944. 191.
TAIRiAT3G59990.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
InParanoidiQ56Y85.
KOiK01265.
OMAiSTRMEED.
PhylomeDBiQ56Y85.

Enzyme and pathway databases

BioCyciARA:AT3G59990-MONOMER.
ARA:GQT-1753-MONOMER.
ARA:GQT-2672-MONOMER.
ARA:GQT-2673-MONOMER.
ReactomeiREACT_307091. Inactivation, recovery and regulation of the phototransduction cascade.

Miscellaneous databases

PROiQ56Y85.

Gene expression databases

GenevestigatoriQ56Y85.

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]
PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
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. "Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms."
    Giglione C., Serero A., Pierre M., Boisson B., Meinnel T.
    EMBO J. 19:5916-5929(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 263-439.
    Strain: cv. Columbia.

Entry informationi

Entry nameiMAP22_ARATH
AccessioniPrimary (citable) accession number: Q56Y85
Secondary accession number(s): Q8VZ89, Q9FPV8, Q9M1X7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2006
Last sequence update: January 23, 2006
Last modified: March 31, 2015
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.