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Protein

Puromycin-sensitive aminopeptidase

Gene

NPEPPS

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

Functioni

Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. May act as regulator of neuropeptide activity. Plays a role in the antigen-processing pathway for MHC class I molecules. Involved in the N-terminal trimming of cytotoxic T-cell epitope precursors. Digests the poly-Q peptides found in many cellular proteins. Digests tau from normal brain more efficiently than tau from Alzheimer disease brain.5 Publications

Catalytic activityi

Release of an N-terminal amino acid, preferentially alanine, from a wide range of peptides, amides and arylamides.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

Strongly inhibited by bestatin, leuhistin, actinonin, amastatin, 1,10-phenanthroline, DFP, PCMBS, Zn2+, Cd2+, Co2+, Cu2+, Hg2+, EDTA and puromycin. Not inhibited by PMSF, and only slightly inhibited by leupeptin and aprotinin. Activity is increased by Mg2+ and Ca2+.3 Publications

Kineticsi

  1. KM=2.20 mM for Lys-p-NA2 Publications
  2. KM=0.25 mM for Leu-p-NA2 Publications
  3. KM=0.27 mM for Ala-p-NA2 Publications
  4. KM=0.80 mM for Met-p-NA2 Publications
  5. KM=0.47 mM for Pro-p-NA2 Publications
  6. KM=0.21 mM for Val-p-NA2 Publications
  7. KM=182 µM for Ala-MCA2 Publications
  8. KM=189 µM for Met-MCA2 Publications
  9. KM=220 µM for Lys-MCA2 Publications
  10. KM=91 µM for Leu-MCA2 Publications
  11. KM=167 µM for Phe-MCA2 Publications

    pH dependencei

    Optimum pH is 7.5. Stable from pH 5.0 to 8.0.2 Publications

    Temperature dependencei

    Stable up to 40 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei180 – 1801SubstrateBy similarity
    Metal bindingi352 – 3521Zinc; catalyticPROSITE-ProRule annotation
    Active sitei353 – 3531Proton acceptorPROSITE-ProRule annotation
    Metal bindingi356 – 3561Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi375 – 3751Zinc; catalyticPROSITE-ProRule annotation
    Sitei438 – 4381Transition state stabilizerBy similarity

    GO - Molecular functioni

    • aminopeptidase activity Source: ProtInc
    • metallopeptidase activity Source: UniProtKB-KW
    • zinc ion binding Source: InterPro

    GO - Biological processi

    • antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    • cellular response to hypoxia Source: UniProtKB
    • positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
    • protein polyubiquitination Source: Reactome
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Protein family/group databases

    MEROPSiM01.010.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Puromycin-sensitive aminopeptidase (EC:3.4.11.14)
    Short name:
    PSA
    Alternative name(s):
    Cytosol alanyl aminopeptidase
    Short name:
    AAP-S
    Gene namesi
    Name:NPEPPS
    Synonyms:PSA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:7900. NPEPPS.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • nucleus Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi353 – 3531E → A: Reduces catalytic activity by 25,000-fold to 100,000-fold. 1 Publication
    Mutagenesisi353 – 3531E → Q: Reduces catalytic activity by 5,000-fold to 15,000-fold. 1 Publication
    Mutagenesisi353 – 3531E → V: Reduces catalytic activity by 300,000-fold to 500,000-fold. 1 Publication
    Mutagenesisi438 – 4381Y → F: Reduces catalytic activity by 1,000-fold to 2,500-fold. 1 Publication

    Organism-specific databases

    PharmGKBiPA31703.

    Polymorphism and mutation databases

    BioMutaiNPEPPS.
    DMDMi51704228.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 919919Puromycin-sensitive aminopeptidasePRO_0000095116Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei464 – 4641Nitrated tyrosineBy similarity

    Keywords - PTMi

    Nitration

    Proteomic databases

    MaxQBiP55786.
    PaxDbiP55786.
    PeptideAtlasiP55786.
    PRIDEiP55786.

    PTM databases

    PhosphoSiteiP55786.

    Miscellaneous databases

    PMAP-CutDBP55786.

    Expressioni

    Tissue specificityi

    Detected in liver, epithelium of renal tubules, epithelium of small and large intestine, gastric epithelial cells, and alveoli of the lung (at protein level).1 Publication

    Gene expression databases

    BgeeiP55786.
    CleanExiHS_NPEPPS.
    ExpressionAtlasiP55786. baseline and differential.
    GenevisibleiP55786. HS.

    Organism-specific databases

    HPAiHPA021453.
    HPA045649.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi114897. 42 interactions.
    IntActiP55786. 6 interactions.
    MINTiMINT-4999844.
    STRINGi9606.ENSP00000320324.

    Structurei

    3D structure databases

    ProteinModelPortaliP55786.
    SMRiP55786. Positions 42-910.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni316 – 3205Substrate bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi726 – 7305Nuclear localization signalSequence Analysis

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Phylogenomic databases

    eggNOGiCOG0308.
    GeneTreeiENSGT00760000119082.
    HOGENOMiHOG000106482.
    HOVERGENiHBG106325.
    InParanoidiP55786.
    KOiK08776.
    OMAiISICTSE.
    PhylomeDBiP55786.
    TreeFamiTF300395.

    Family and domain databases

    InterProiIPR024571. ERAP1-like_C_dom.
    IPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    [Graphical view]
    PANTHERiPTHR11533. PTHR11533. 1 hit.
    PfamiPF11838. ERAP1_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view]
    PRINTSiPR00756. ALADIPTASE.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P55786-1) [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

            10         20         30         40         50
    MWLAAAAPSL ARRLLFLGPP PPPLLLLVFS RSSRRRLHSL GLAAMPEKRP
    60 70 80 90 100
    FERLPADVSP INYSLCLKPD LLDFTFEGKL EAAAQVRQAT NQIVMNCADI
    110 120 130 140 150
    DIITASYAPE GDEEIHATGF NYQNEDEKVT LSFPSTLQTG TGTLKIDFVG
    160 170 180 190 200
    ELNDKMKGFY RSKYTTPSGE VRYAAVTQFE ATDARRAFPC WDEPAIKATF
    210 220 230 240 250
    DISLVVPKDR VALSNMNVID RKPYPDDENL VEVKFARTPV MSTYLVAFVV
    260 270 280 290 300
    GEYDFVETRS KDGVCVRVYT PVGKAEQGKF ALEVAAKTLP FYKDYFNVPY
    310 320 330 340 350
    PLPKIDLIAI ADFAAGAMEN WGLVTYRETA LLIDPKNSCS SSRQWVALVV
    360 370 380 390 400
    GHELAHQWFG NLVTMEWWTH LWLNEGFASW IEYLCVDHCF PEYDIWTQFV
    410 420 430 440 450
    SADYTRAQEL DALDNSHPIE VSVGHPSEVD EIFDAISYSK GASVIRMLHD
    460 470 480 490 500
    YIGDKDFKKG MNMYLTKFQQ KNAATEDLWE SLENASGKPI AAVMNTWTKQ
    510 520 530 540 550
    MGFPLIYVEA EQVEDDRLLR LSQKKFCAGG SYVGEDCPQW MVPITISTSE
    560 570 580 590 600
    DPNQAKLKIL MDKPEMNVVL KNVKPDQWVK LNLGTVGFYR TQYSSAMLES
    610 620 630 640 650
    LLPGIRDLSL PPVDRLGLQN DLFSLARAGI ISTVEVLKVM EAFVNEPNYT
    660 670 680 690 700
    VWSDLSCNLG ILSTLLSHTD FYEEIQEFVK DVFSPIGERL GWDPKPGEGH
    710 720 730 740 750
    LDALLRGLVL GKLGKAGHKA TLEEARRRFK DHVEGKQILS ADLRSPVYLT
    760 770 780 790 800
    VLKHGDGTTL DIMLKLHKQA DMQEEKNRIE RVLGATLLPD LIQKVLTFAL
    810 820 830 840 850
    SEEVRPQDTV SVIGGVAGGS KHGRKAAWKF IKDNWEELYN RYQGGFLISR
    860 870 880 890 900
    LIKLSVEGFA VDKMAGEVKA FFESHPAPSA ERTIQQCCEN ILLNAAWLKR
    910
    DAESIHQYLL QRKASPPTV
    Length:919
    Mass (Da):103,276
    Last modified:August 31, 2004 - v2
    Checksum:i873C9BF75494A057
    GO
    Isoform 2 (identifier: P55786-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-44: Missing.
         181-216: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:839
    Mass (Da):94,516
    Checksum:iA4D3EBEC951133E7
    GO

    Sequence cautioni

    The sequence AAH65294.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence CAA68964.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti184 – 1841A → P in CAA68964 (PubMed:9048733).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4444Missing in isoform 2. 1 PublicationVSP_056446Add
    BLAST
    Alternative sequencei181 – 21636Missing in isoform 2. 1 PublicationVSP_056447Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y07701 mRNA. Translation: CAA68964.1. Different initiation.
    AK296887 mRNA. Translation: BAH12449.1.
    AC025682 Genomic DNA. No translation available.
    BC065294 mRNA. Translation: AAH65294.2. Different initiation.
    AJ132583 mRNA. Translation: CAA10709.1.
    AF252387 Genomic DNA. Translation: AAF70086.1.
    CCDSiCCDS45721.1. [P55786-1]
    RefSeqiNP_006301.3. NM_006310.3. [P55786-1]
    UniGeneiHs.443837.

    Genome annotation databases

    EnsembliENST00000322157; ENSP00000320324; ENSG00000141279.
    GeneIDi9520.
    KEGGihsa:9520.
    UCSCiuc002ilr.4. human. [P55786-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y07701 mRNA. Translation: CAA68964.1. Different initiation.
    AK296887 mRNA. Translation: BAH12449.1.
    AC025682 Genomic DNA. No translation available.
    BC065294 mRNA. Translation: AAH65294.2. Different initiation.
    AJ132583 mRNA. Translation: CAA10709.1.
    AF252387 Genomic DNA. Translation: AAF70086.1.
    CCDSiCCDS45721.1. [P55786-1]
    RefSeqiNP_006301.3. NM_006310.3. [P55786-1]
    UniGeneiHs.443837.

    3D structure databases

    ProteinModelPortaliP55786.
    SMRiP55786. Positions 42-910.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114897. 42 interactions.
    IntActiP55786. 6 interactions.
    MINTiMINT-4999844.
    STRINGi9606.ENSP00000320324.

    Chemistry

    BindingDBiP55786.
    ChEMBLiCHEMBL2264.

    Protein family/group databases

    MEROPSiM01.010.

    PTM databases

    PhosphoSiteiP55786.

    Polymorphism and mutation databases

    BioMutaiNPEPPS.
    DMDMi51704228.

    Proteomic databases

    MaxQBiP55786.
    PaxDbiP55786.
    PeptideAtlasiP55786.
    PRIDEiP55786.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000322157; ENSP00000320324; ENSG00000141279.
    GeneIDi9520.
    KEGGihsa:9520.
    UCSCiuc002ilr.4. human. [P55786-1]

    Organism-specific databases

    CTDi9520.
    GeneCardsiGC17P045608.
    H-InvDBHIX0013922.
    HGNCiHGNC:7900. NPEPPS.
    HPAiHPA021453.
    HPA045649.
    MIMi606793. gene.
    neXtProtiNX_P55786.
    PharmGKBiPA31703.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0308.
    GeneTreeiENSGT00760000119082.
    HOGENOMiHOG000106482.
    HOVERGENiHBG106325.
    InParanoidiP55786.
    KOiK08776.
    OMAiISICTSE.
    PhylomeDBiP55786.
    TreeFamiTF300395.

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSiNPEPPS. human.
    GeneWikiiNPEPPS.
    GenomeRNAii9520.
    NextBioi35479397.
    PMAP-CutDBP55786.
    PROiP55786.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP55786.
    CleanExiHS_NPEPPS.
    ExpressionAtlasiP55786. baseline and differential.
    GenevisibleiP55786. HS.

    Family and domain databases

    InterProiIPR024571. ERAP1-like_C_dom.
    IPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    [Graphical view]
    PANTHERiPTHR11533. PTHR11533. 1 hit.
    PfamiPF11838. ERAP1_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view]
    PRINTSiPR00756. ALADIPTASE.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning of the human puromycin-sensitive aminopeptidase and evidence for expression in neurons."
      Tobler A.R., Constam D.B., Schmitt-Graeff A., Malipiero U., Schlapbach R., Fontana A.
      J. Neurochem. 68:889-897(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    2. "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: Tongue.
    3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      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] OF 31-919 (ISOFORM 1).
      Tissue: Lung.
    5. "Human puromycin-sensitive aminopeptidase: cloning of 3' UTR, evidence for a polymorphism at a.a. 140 and refined chromosomal localization to 17q21."
      Bauer W.O., Nanda I., Beck G., Schmid M., Jakob F.
      Cytogenet. Cell Genet. 92:221-224(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 45-919 (ISOFORM 1).
      Tissue: Skeletal muscle.
    6. "Cloning and analysis of the gene for the human puromycin-sensitive aminopeptidase."
      Thompson M.W., Tobler A., Fontana A., Hersh L.B.
      Biochem. Biophys. Res. Commun. 258:234-240(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 45-85.
    7. "Puromycin-sensitive alanyl aminopeptidase from human liver cytosol: purification and characterization."
      Yamamoto Y., Li Y.H., Ushiyama I., Nishimura A., Ohkubo I., Nishi K.
      Forensic Sci. Int. 113:143-146(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 46-105, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Liver.
    8. Cited for: FUNCTION.
    9. "Mutation of active site residues of the puromycin-sensitive aminopeptidase: conversion of the enzyme into a catalytically inactive binding protein."
      Thompson M.W., Govindaswami M., Hersh L.B.
      Arch. Biochem. Biophys. 413:236-242(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLU-353 AND TYR-438, ACTIVE SITE.
    10. "Degradation of tau protein by puromycin-sensitive aminopeptidase in vitro."
      Sengupta S., Horowitz P.M., Karsten S.L., Jackson G.R., Geschwind D.H., Fu Y., Berry R.W., Binder L.I.
      Biochemistry 45:15111-15119(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    11. "Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation."
      Bhutani N., Venkatraman P., Goldberg A.L.
      EMBO J. 26:1385-1396(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    12. "Cytosolic aminopeptidases influence MHC class I-mediated antigen presentation in an allele-dependent manner."
      Kim E., Kwak H., Ahn K.
      J. Immunol. 183:7379-7387(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiPSA_HUMAN
    AccessioniPrimary (citable) accession number: P55786
    Secondary accession number(s): B7Z463
    , Q6P145, Q9NP16, Q9UEM2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: August 31, 2004
    Last modified: July 22, 2015
    This is version 146 of the entry and version 2 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 Met-45 is the initiator. N-terminal sequencing in PubMed:10978616 suggests that Met-45 is used, followed by methionine initiator removal.Curated

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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

    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.