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Q6UB28

- MAP12_HUMAN

UniProt

Q6UB28 - MAP12_HUMAN

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Protein

Methionine aminopeptidase 1D, mitochondrial

Gene

METAP1D

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed (By similarity). May play a role in colon tumorigenesis.1 PublicationUniRule 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.UniRule annotation

Kineticsi

  1. KM=573 µM for Met-pro-p-nitroanilide (at pH 8)1 Publication

pH dependencei

Optimum pH is 7.5-8.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei161 – 1611SubstrateUniRule annotation
Metal bindingi178 – 1781Divalent metal cation 1UniRule annotation
Metal bindingi189 – 1891Divalent metal cation 1UniRule annotation
Metal bindingi189 – 1891Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi252 – 2521Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei259 – 2591SubstrateUniRule annotation
Metal bindingi284 – 2841Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi315 – 3151Divalent metal cation 1UniRule annotation
Metal bindingi315 – 3151Divalent metal cation 2; catalyticUniRule annotation

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

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
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BRENDAi3.4.11.18. 2681.
SABIO-RKQ6UB28.

Protein family/group databases

MEROPSiM24.028.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 1D, mitochondrialUniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 1DUniRule annotation
Short name:
MetAP 1DUniRule annotation
Alternative name(s):
Methionyl aminopeptidase type 1D, mitochondrial
Peptidase M 1DUniRule annotation
Gene namesi
Name:METAP1D
Synonyms:MAP1D
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:32583. METAP1D.

Subcellular locationi

Mitochondrion 1 PublicationUniRule annotation

GO - Cellular componenti

  1. mitochondrion Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1919MitochondrionUniRule annotationAdd
BLAST
Chaini20 – 335316Methionine aminopeptidase 1D, mitochondrialPRO_0000314126Add
BLAST

Proteomic databases

MaxQBiQ6UB28.
PaxDbiQ6UB28.
PRIDEiQ6UB28.

PTM databases

PhosphoSiteiQ6UB28.

Expressioni

Tissue specificityi

Overexpressed in colon cancer cell lines and colon tumors as compared to normal tissues (at protein level).1 Publication

Gene expression databases

BgeeiQ6UB28.
GenevestigatoriQ6UB28.

Organism-specific databases

HPAiHPA030299.

Interactioni

Protein-protein interaction databases

BioGridi129008. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ6UB28.
SMRiQ6UB28. Positions 63-330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0024.
GeneTreeiENSGT00390000002284.
HOGENOMiHOG000030427.
HOVERGENiHBG067178.
InParanoidiQ6UB28.
KOiK01265.
OMAiLNHIYLH.
OrthoDBiEOG786H38.
PhylomeDBiQ6UB28.
TreeFamiTF325318.

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.

Q6UB28-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAPSGVHLL VRRGSHRIFS SPLNHIYLHK QSSSQQRRNF FFRRQRDISH
60 70 80 90 100
SIVLPAAVSS AHPVPKHIKK PDYVTTGIVP DWGDSIEVKN EDQIQGLHQA
110 120 130 140 150
CQLARHVLLL AGKSLKVDMT TEEIDALVHR EIISHNAYPS PLGYGGFPKS
160 170 180 190 200
VCTSVNNVLC HGIPDSRPLQ DGDIINIDVT VYYNGYHGDT SETFLVGNVD
210 220 230 240 250
ECGKKLVEVA RRCRDEAIAA CRAGAPFSVI GNTISHITHQ NGFQVCPHFV
260 270 280 290 300
GHGIGSYFHG HPEIWHHAND SDLPMEEGMA FTIEPIITEG SPEFKVLEDA
310 320 330
WTVVSLDNQR SAQFEHTVLI TSRGAQILTK LPHEA
Length:335
Mass (Da):37,088
Last modified:July 5, 2004 - v1
Checksum:i2EB90946DC983D7B
GO

Sequence cautioni

The sequence AAY55948.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141G → V.1 Publication
Corresponds to variant rs10497377 [ dbSNP | Ensembl ].
VAR_050273

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY374142 mRNA. Translation: AAR27795.1.
DQ005576 mRNA. Translation: AAY55948.1. Different initiation.
CH471058 Genomic DNA. Translation: EAX11190.1.
BC113644 mRNA. Translation: AAI13645.1.
CCDSiCCDS2246.1.
RefSeqiNP_954697.1. NM_199227.1.
UniGeneiHs.298250.

Genome annotation databases

EnsembliENST00000315796; ENSP00000315152; ENSG00000172878.
GeneIDi254042.
KEGGihsa:254042.
UCSCiuc002uhk.3. human.

Polymorphism databases

DMDMi74710242.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY374142 mRNA. Translation: AAR27795.1 .
DQ005576 mRNA. Translation: AAY55948.1 . Different initiation.
CH471058 Genomic DNA. Translation: EAX11190.1 .
BC113644 mRNA. Translation: AAI13645.1 .
CCDSi CCDS2246.1.
RefSeqi NP_954697.1. NM_199227.1.
UniGenei Hs.298250.

3D structure databases

ProteinModelPortali Q6UB28.
SMRi Q6UB28. Positions 63-330.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 129008. 2 interactions.

Protein family/group databases

MEROPSi M24.028.

PTM databases

PhosphoSitei Q6UB28.

Polymorphism databases

DMDMi 74710242.

Proteomic databases

MaxQBi Q6UB28.
PaxDbi Q6UB28.
PRIDEi Q6UB28.

Protocols and materials databases

DNASUi 254042.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000315796 ; ENSP00000315152 ; ENSG00000172878 .
GeneIDi 254042.
KEGGi hsa:254042.
UCSCi uc002uhk.3. human.

Organism-specific databases

CTDi 254042.
GeneCardsi GC02P172865.
HGNCi HGNC:32583. METAP1D.
HPAi HPA030299.
MIMi 610267. gene.
neXtProti NX_Q6UB28.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0024.
GeneTreei ENSGT00390000002284.
HOGENOMi HOG000030427.
HOVERGENi HBG067178.
InParanoidi Q6UB28.
KOi K01265.
OMAi LNHIYLH.
OrthoDBi EOG786H38.
PhylomeDBi Q6UB28.
TreeFami TF325318.

Enzyme and pathway databases

BRENDAi 3.4.11.18. 2681.
SABIO-RK Q6UB28.

Miscellaneous databases

ChiTaRSi METAP1D. human.
GenomeRNAii 254042.
NextBioi 92234.
PROi Q6UB28.
SOURCEi Search...

Gene expression databases

Bgeei Q6UB28.
Genevestigatori Q6UB28.

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

« Hide 'large scale' publications
  1. "An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathway."
    Serero A., Giglione C., Sardini A., Martinez-Sanz J., Meinnel T.
    J. Biol. Chem. 278:52953-52963(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
  2. "MAP1D, a novel methionine aminopeptidase family member is overexpressed in colon cancer."
    Leszczyniecka M., Bhatia U., Cueto M., Nirmala N.R., Towbin H., Vattay A., Wang B., Zabludoff S., Phillips P.E.
    Oncogene 25:3471-3478(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT VAL-14.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Brain.
  5. "Kinetic and mutational studies of the number of interacting divalent cations required by bacterial and human methionine aminopeptidases."
    Hu X.V., Chen X., Han K.C., Mildvan A.S., Liu J.O.
    Biochemistry 46:12833-12843(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiMAP12_HUMAN
AccessioniPrimary (citable) accession number: Q6UB28
Secondary accession number(s): Q1WNX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

It is uncertain whether Met-1 or a Met upstream of this sequence is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3