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Q8BP48

- MAP11_MOUSE

UniProt

Q8BP48 - MAP11_MOUSE

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Protein
Methionine aminopeptidase 1
Gene
Metap1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 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) 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 sitei203 – 2031Substrate By similarity
Metal bindingi220 – 2201Divalent metal cation 1 By similarity
Metal bindingi231 – 2311Divalent metal cation 1 By similarity
Metal bindingi231 – 2311Divalent metal cation 2; catalytic By similarity
Metal bindingi294 – 2941Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei301 – 3011Substrate By similarity
Metal bindingi327 – 3271Divalent metal cation 2; catalytic By similarity
Metal bindingi358 – 3581Divalent metal cation 1 By similarity
Metal bindingi358 – 3581Divalent metal cation 2; catalytic By similarity

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
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

ReactomeiREACT_188266. Inactivation, recovery and regulation of the phototransduction cascade.

Protein family/group databases

MEROPSiM24.017.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 1 (EC:3.4.11.18)
Short name:
MAP 1
Short name:
MetAP 1
Alternative name(s):
Peptidase M 1
Gene namesi
Name:Metap1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1922874. Metap1.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytosolic ribosome Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 386385Methionine aminopeptidase 1UniRule annotation
PRO_0000148968Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8BP48.
PaxDbiQ8BP48.
PRIDEiQ8BP48.

PTM databases

PhosphoSiteiQ8BP48.

Expressioni

Gene expression databases

ArrayExpressiQ8BP48.
BgeeiQ8BP48.
CleanExiMM_METAP1.
GenevestigatoriQ8BP48.

Interactioni

Subunit structurei

Associates with the 60S ribosomal subunit of the 80S translational complex By similarity.

Protein-protein interaction databases

IntActiQ8BP48. 4 interactions.
MINTiMINT-1857104.

Structurei

3D structure databases

ProteinModelPortaliQ8BP48.
SMRiQ8BP48. Positions 81-384.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 5244Zinc finger-like; important for proper ribosome association By similarity
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
GeneTreeiENSGT00390000002284.
HOGENOMiHOG000030427.
HOVERGENiHBG067178.
InParanoidiQ8BP48.
KOiK01265.
OMAiVEASYDV.
OrthoDBiEOG786H38.
PhylomeDBiQ8BP48.
TreeFamiTF105753.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BP48-1 [UniParc]FASTAAdd to Basket

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MAAVETRVCE TDGCSSEAKL QCPTCIKLGI QGSYFCSQEC FKGSWATHKL    50
LHKKAKDEKA KREVCSWTVE GDVNTDPWAG YRYTGKLRPH YPLMPTRPVP 100
SYIQRPDYAD HPLGMSESEQ ALKGTSQIKL LSSEDIEGMR LVCRLAREVL 150
DIAAGMIKAG VTTEEIDHAV HLACIARNCY PSPLNYYNFP KSCCTSVNEV 200
ICHGIPDRRP LQEGDIVNVD ITLYRNGYHG DLNETFFVGD VDEGARKLVQ 250
TTYECLMQAI DAVKPGVRYR ELGNIIQKHA QANGFSVVRS YCGHGIHKLF 300
HTAPNVPHYA KNKAVGVMKS GHVFTIEPMI CEGGWQDETW PDGWTAVTRD 350
GKRSAQFEHT LLVTDTGCEI LTRRLDSSRP HFMSQF 386
Length:386
Mass (Da):43,221
Last modified:March 1, 2003 - v1
Checksum:iC768875645674B97
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK077694 mRNA. Translation: BAC36961.1.
CCDSiCCDS17869.1.
RefSeqiNP_780433.1. NM_175224.4.
UniGeneiMm.26833.

Genome annotation databases

EnsembliENSMUST00000029804; ENSMUSP00000029804; ENSMUSG00000005813.
GeneIDi75624.
KEGGimmu:75624.
UCSCiuc008rnl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK077694 mRNA. Translation: BAC36961.1 .
CCDSi CCDS17869.1.
RefSeqi NP_780433.1. NM_175224.4.
UniGenei Mm.26833.

3D structure databases

ProteinModelPortali Q8BP48.
SMRi Q8BP48. Positions 81-384.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8BP48. 4 interactions.
MINTi MINT-1857104.

Protein family/group databases

MEROPSi M24.017.

PTM databases

PhosphoSitei Q8BP48.

Proteomic databases

MaxQBi Q8BP48.
PaxDbi Q8BP48.
PRIDEi Q8BP48.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029804 ; ENSMUSP00000029804 ; ENSMUSG00000005813 .
GeneIDi 75624.
KEGGi mmu:75624.
UCSCi uc008rnl.1. mouse.

Organism-specific databases

CTDi 23173.
MGIi MGI:1922874. Metap1.

Phylogenomic databases

eggNOGi COG0024.
GeneTreei ENSGT00390000002284.
HOGENOMi HOG000030427.
HOVERGENi HBG067178.
InParanoidi Q8BP48.
KOi K01265.
OMAi VEASYDV.
OrthoDBi EOG786H38.
PhylomeDBi Q8BP48.
TreeFami TF105753.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi 343556.
PROi Q8BP48.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8BP48.
Bgeei Q8BP48.
CleanExi MM_METAP1.
Genevestigatori Q8BP48.

Family and domain databases

Gene3Di 3.90.230.10. 1 hit.
HAMAPi MF_01974. MetAP_1.
InterProi IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 1 hit.
TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
PROSITEi PS00680. MAP_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "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.

Entry informationi

Entry nameiMAP11_MOUSE
AccessioniPrimary (citable) accession number: Q8BP48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: March 1, 2003
Last modified: September 3, 2014
This is version 106 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, 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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