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P28838 (AMPL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytosol aminopeptidase

EC=3.4.11.1
Alternative name(s):
Leucine aminopeptidase 3
Short name=LAP-3
Leucyl aminopeptidase
Peptidase S
Proline aminopeptidase
EC=3.4.11.5
Prolyl aminopeptidase
Gene names
Name:LAP3
Synonyms:LAPEP, PEPS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. HAMAP-Rule MF_00181

Catalytic activity

Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. HAMAP-Rule MF_00181

Release of N-terminal proline from a peptide. HAMAP-Rule MF_00181

Cofactor

Binds 2 zinc ions per subunit. One zinc ion is tightly bound and essential for enzyme activity, while the second metal coordination site can be occupied by zinc, magnesium or manganese to give enzymes of different activities By similarity.

Subunit structure

Homohexamer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00181.

Sequence similarities

Belongs to the peptidase M17 family.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: P28838-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P28838-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.
Note: Initiator Met-1 is removed.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 519519Cytosol aminopeptidase HAMAP-Rule MF_00181
PRO_0000165825

Sites

Active site2941 By similarity
Active site3681 By similarity
Metal binding2821Zinc 2 By similarity
Metal binding2871Zinc 1 By similarity
Metal binding2871Zinc 2 By similarity
Metal binding3051Zinc 2 By similarity
Metal binding3641Zinc 1 By similarity
Metal binding3661Zinc 1 By similarity
Metal binding3661Zinc 2 By similarity

Amino acid modifications

Modified residue451N6-succinyllysine By similarity
Modified residue611N6-succinyllysine By similarity
Modified residue1031N6-succinyllysine By similarity
Modified residue1801Phosphoserine By similarity
Modified residue2211N6-acetyllysine; alternate Ref.6
Modified residue2211N6-succinyllysine; alternate By similarity
Modified residue2381Phosphoserine Ref.7
Modified residue4551N6-acetyllysine; alternate By similarity
Modified residue4551N6-succinyllysine; alternate By similarity
Modified residue4761N6-succinyllysine By similarity
Modified residue4891N6-acetyllysine; alternate By similarity
Modified residue4891N6-succinyllysine; alternate By similarity

Natural variations

Alternative sequence1 – 3131Missing in isoform 2.
VSP_022631

Experimental info

Sequence conflict201R → V in AAD17527. Ref.1
Sequence conflict221F → S in AAD17527. Ref.1
Sequence conflict291T → A in CAG33409. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D960F8F5B9024585

FASTA51956,166
        10         20         30         40         50         60 
MFLLPLPAAG RVVVRRLAVR RFGSRSLSTA DMTKGLVLGI YSKEKEDDVP QFTSAGENFD 

        70         80         90        100        110        120 
KLLAGKLRET LNISGPPLKA GKTRTFYGLH QDFPSVVLVG LGKKAAGIDE QENWHEGKEN 

       130        140        150        160        170        180 
IRAAVAAGCR QIQDLELSSV EVDPCGDAQA AAEGAVLGLY EYDDLKQKKK MAVSAKLYGS 

       190        200        210        220        230        240 
GDQEAWQKGV LFASGQNLAR QLMETPANEM TPTRFAEIIE KNLKSASSKT EVHIRPKSWI 

       250        260        270        280        290        300 
EEQAMGSFLS VAKGSDEPPV FLEIHYKGSP NANEPPLVFV GKGITFDSGG ISIKASANMD 

       310        320        330        340        350        360 
LMRADMGGAA TICSAIVSAA KLNLPINIIG LAPLCENMPS GKANKPGDVV RAKNGKTIQV 

       370        380        390        400        410        420 
DNTDAEGRLI LADALCYAHT FNPKVILNAA TLTGAMDVAL GSGATGVFTN SSWLWNKLFE 

       430        440        450        460        470        480 
ASIETGDRVW RMPLFEHYTR QVVDCQLADV NNIGKYRSAG ACTAAAFLKE FVTHPKWAHL 

       490        500        510 
DIAGVMTNKD EVPYLRKGMT GRPTRTLIEF LLRFSQDNA 

« Hide

Isoform 2 [UniParc].

Checksum: 0CADB3E07FD10B8B
Show »

FASTA48852,771

References

« Hide 'large scale' references
[1]Mao M., Liu T., Zhang J., Wu J., Zhang Q., Fu G., Shen Y., Zhou J., Yu Y., Wang Z., Chen S., Chen Z.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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] (ISOFORM 2).
Tissue: Embryo.
[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] (ISOFORM 1).
Tissue: Eye and Lung.
[5]"Structural and immunological evidence for the identity of prolyl aminopeptidase with leucyl aminopeptidase."
Matsushima M., Takahashi T., Ichinose M., Miki K., Kurokawa K., Takahashi K.
Biochem. Biophys. Res. Commun. 178:1459-1464(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-54.
Tissue: Liver.
[6]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF061738 mRNA. Translation: AAD17527.1.
CR457128 mRNA. Translation: CAG33409.1.
AK022055 mRNA. Translation: BAG51065.1.
AK298613 mRNA. Translation: BAG60795.1.
BC065564 mRNA. Translation: AAH65564.1.
BC006199 mRNA. Translation: AAH06199.3.
CCDSCCDS3422.1. [P28838-1]
PIRPT0431.
RefSeqNP_056991.2. NM_015907.2. [P28838-1]
UniGeneHs.570791.

3D structure databases

ProteinModelPortalP28838.
SMRP28838. Positions 33-516.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119248. 18 interactions.
IntActP28838. 7 interactions.
MINTMINT-2802173.
STRING9606.ENSP00000226299.

Chemistry

BindingDBP28838.
ChEMBLCHEMBL3965.

Protein family/group databases

MEROPSM17.001.

PTM databases

PhosphoSiteP28838.

Polymorphism databases

DMDM124028615.

2D gel databases

REPRODUCTION-2DPAGEIPI00789806.
P28838.
UCD-2DPAGEP28838.

Proteomic databases

MaxQBP28838.
PaxDbP28838.
PRIDEP28838.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000226299; ENSP00000226299; ENSG00000002549. [P28838-1]
ENST00000606142; ENSP00000476028; ENSG00000002549. [P28838-2]
GeneID51056.
KEGGhsa:51056.
UCSCuc003gph.1. human. [P28838-1]

Organism-specific databases

CTD51056.
GeneCardsGC04P017578.
H-InvDBHIX0004121.
HGNCHGNC:18449. LAP3.
HPAHPA029606.
HPA029607.
MIM170250. gene.
neXtProtNX_P28838.
PharmGKBPA38537.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0260.
HOGENOMHOG000243129.
HOVERGENHBG003320.
InParanoidP28838.
KOK11142.
OMAGMDAMRA.
OrthoDBEOG7F24SG.
PhylomeDBP28838.
TreeFamTF314954.

Gene expression databases

ArrayExpressP28838.
BgeeP28838.
CleanExHS_LAP3.
GenevestigatorP28838.

Family and domain databases

HAMAPMF_00181. Cytosol_peptidase_M17.
InterProIPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
IPR008283. Peptidase_M17_N.
[Graphical view]
PfamPF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view]
PRINTSPR00481. LAMNOPPTDASE.
PROSITEPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLAP3. human.
GenomeRNAi51056.
NextBio53624.
PROP28838.
SOURCESearch...

Entry information

Entry nameAMPL_HUMAN
AccessionPrimary (citable) accession number: P28838
Secondary accession number(s): B3KMQ3 expand/collapse secondary AC list , Q6IAM6, Q6P0L6, Q9UQE3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 148 of the entry and version 3 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

MIM cross-references

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

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM