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P28838

- AMPL_HUMAN

UniProt

P28838 - AMPL_HUMAN

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Protein
Cytosol aminopeptidase
Gene
LAP3, LAPEP, PEPS
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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.UniRule annotation
Release of N-terminal proline from a peptide.UniRule annotation

Cofactori

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi282 – 2821Zinc 2 By similarity
Metal bindingi287 – 2871Zinc 1 By similarity
Metal bindingi287 – 2871Zinc 2 By similarity
Active sitei294 – 2941 By similarity
Metal bindingi305 – 3051Zinc 2 By similarity
Metal bindingi364 – 3641Zinc 1 By similarity
Metal bindingi366 – 3661Zinc 1 By similarity
Metal bindingi366 – 3661Zinc 2 By similarity
Active sitei368 – 3681 By similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB
  2. manganese ion binding Source: InterPro
  3. metalloexopeptidase activity Source: UniProtKB

GO - Biological processi

  1. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, Zinc

Protein family/group databases

MEROPSiM17.001.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:LAP3
Synonyms:LAPEP, PEPS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:18449. LAP3.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. extracellular vesicular exosome Source: UniProt
  3. mitochondrion Source: Ensembl
  4. nucleus Source: UniProt
  5. trans-Golgi network Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38537.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 519519Cytosol aminopeptidaseUniRule annotation
PRO_0000165825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei45 – 451N6-succinyllysine By similarity
Modified residuei61 – 611N6-succinyllysine By similarity
Modified residuei103 – 1031N6-succinyllysine By similarity
Modified residuei180 – 1801Phosphoserine By similarity
Modified residuei221 – 2211N6-acetyllysine; alternate1 Publication
Modified residuei221 – 2211N6-succinyllysine; alternate By similarity
Modified residuei238 – 2381Phosphoserine1 Publication
Modified residuei455 – 4551N6-acetyllysine; alternate By similarity
Modified residuei455 – 4551N6-succinyllysine; alternate By similarity
Modified residuei476 – 4761N6-succinyllysine By similarity
Modified residuei489 – 4891N6-acetyllysine; alternate By similarity
Modified residuei489 – 4891N6-succinyllysine; alternate By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP28838.
PaxDbiP28838.
PRIDEiP28838.

2D gel databases

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

PTM databases

PhosphoSiteiP28838.

Expressioni

Gene expression databases

ArrayExpressiP28838.
BgeeiP28838.
CleanExiHS_LAP3.
GenevestigatoriP28838.

Organism-specific databases

HPAiHPA029606.
HPA029607.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

BioGridi119248. 19 interactions.
IntActiP28838. 7 interactions.
MINTiMINT-2802173.
STRINGi9606.ENSP00000226299.

Structurei

3D structure databases

ProteinModelPortaliP28838.
SMRiP28838. Positions 33-516.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M17 family.

Phylogenomic databases

eggNOGiCOG0260.
HOGENOMiHOG000243129.
HOVERGENiHBG003320.
InParanoidiP28838.
KOiK11142.
OMAiGMDAMRA.
OrthoDBiEOG7F24SG.
PhylomeDBiP28838.
TreeFamiTF314954.

Family and domain databases

HAMAPiMF_00181. Cytosol_peptidase_M17.
InterProiIPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
IPR008283. Peptidase_M17_N.
[Graphical view]
PfamiPF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view]
PRINTSiPR00481. LAMNOPPTDASE.
PROSITEiPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform 1 (identifier: P28838-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MFLLPLPAAG RVVVRRLAVR RFGSRSLSTA DMTKGLVLGI YSKEKEDDVP    50
QFTSAGENFD KLLAGKLRET LNISGPPLKA GKTRTFYGLH QDFPSVVLVG 100
LGKKAAGIDE QENWHEGKEN IRAAVAAGCR QIQDLELSSV EVDPCGDAQA 150
AAEGAVLGLY EYDDLKQKKK MAVSAKLYGS GDQEAWQKGV LFASGQNLAR 200
QLMETPANEM TPTRFAEIIE KNLKSASSKT EVHIRPKSWI EEQAMGSFLS 250
VAKGSDEPPV FLEIHYKGSP NANEPPLVFV GKGITFDSGG ISIKASANMD 300
LMRADMGGAA TICSAIVSAA KLNLPINIIG LAPLCENMPS GKANKPGDVV 350
RAKNGKTIQV DNTDAEGRLI LADALCYAHT FNPKVILNAA TLTGAMDVAL 400
GSGATGVFTN SSWLWNKLFE ASIETGDRVW RMPLFEHYTR QVVDCQLADV 450
NNIGKYRSAG ACTAAAFLKE FVTHPKWAHL DIAGVMTNKD EVPYLRKGMT 500
GRPTRTLIEF LLRFSQDNA 519
Length:519
Mass (Da):56,166
Last modified:January 23, 2007 - v3
Checksum:iD960F8F5B9024585
GO
Isoform 2 (identifier: P28838-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.

Note: Initiator Met-1 is removed.

Show »
Length:488
Mass (Da):52,771
Checksum:i0CADB3E07FD10B8B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3131Missing in isoform 2.
VSP_022631Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201R → V in AAD17527. 1 Publication
Sequence conflicti22 – 221F → S in AAD17527. 1 Publication
Sequence conflicti29 – 291T → A in CAG33409. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3422.1. [P28838-1]
PIRiPT0431.
RefSeqiNP_056991.2. NM_015907.2. [P28838-1]
UniGeneiHs.570791.

Genome annotation databases

EnsembliENST00000226299; ENSP00000226299; ENSG00000002549. [P28838-1]
ENST00000606142; ENSP00000476028; ENSG00000002549. [P28838-2]
GeneIDi51056.
KEGGihsa:51056.
UCSCiuc003gph.1. human. [P28838-1]

Polymorphism databases

DMDMi124028615.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3422.1. [P28838-1 ]
PIRi PT0431.
RefSeqi NP_056991.2. NM_015907.2. [P28838-1 ]
UniGenei Hs.570791.

3D structure databases

ProteinModelPortali P28838.
SMRi P28838. Positions 33-516.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119248. 19 interactions.
IntActi P28838. 7 interactions.
MINTi MINT-2802173.
STRINGi 9606.ENSP00000226299.

Chemistry

BindingDBi P28838.
ChEMBLi CHEMBL3965.

Protein family/group databases

MEROPSi M17.001.

PTM databases

PhosphoSitei P28838.

Polymorphism databases

DMDMi 124028615.

2D gel databases

REPRODUCTION-2DPAGE IPI00789806.
P28838.
UCD-2DPAGE P28838.

Proteomic databases

MaxQBi P28838.
PaxDbi P28838.
PRIDEi P28838.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000226299 ; ENSP00000226299 ; ENSG00000002549 . [P28838-1 ]
ENST00000606142 ; ENSP00000476028 ; ENSG00000002549 . [P28838-2 ]
GeneIDi 51056.
KEGGi hsa:51056.
UCSCi uc003gph.1. human. [P28838-1 ]

Organism-specific databases

CTDi 51056.
GeneCardsi GC04P017578.
H-InvDB HIX0004121.
HGNCi HGNC:18449. LAP3.
HPAi HPA029606.
HPA029607.
MIMi 170250. gene.
neXtProti NX_P28838.
PharmGKBi PA38537.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0260.
HOGENOMi HOG000243129.
HOVERGENi HBG003320.
InParanoidi P28838.
KOi K11142.
OMAi GMDAMRA.
OrthoDBi EOG7F24SG.
PhylomeDBi P28838.
TreeFami TF314954.

Miscellaneous databases

ChiTaRSi LAP3. human.
GenomeRNAii 51056.
NextBioi 53624.
PROi P28838.
SOURCEi Search...

Gene expression databases

ArrayExpressi P28838.
Bgeei P28838.
CleanExi HS_LAP3.
Genevestigatori P28838.

Family and domain databases

HAMAPi MF_00181. Cytosol_peptidase_M17.
InterProi IPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
IPR008283. Peptidase_M17_N.
[Graphical view ]
Pfami PF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view ]
PRINTSi PR00481. LAMNOPPTDASE.
PROSITEi PS00631. CYTOSOL_AP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAMPL_HUMAN
AccessioniPrimary (citable) accession number: P28838
Secondary accession number(s): B3KMQ3
, Q6IAM6, Q6P0L6, Q9UQE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 149 of the entry and version 3 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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

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