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P55786

- PSA_HUMAN

UniProt

P55786 - PSA_HUMAN

Protein

Puromycin-sensitive aminopeptidase

Gene

NPEPPS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (31 Aug 2004)
      Previous versions | rss
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    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

    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

    1. aminopeptidase activity Source: ProtInc
    2. metallopeptidase activity Source: UniProtKB-KW
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    2. cellular response to hypoxia Source: UniProtKB
    3. protein polyubiquitination Source: Reactome

    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: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:7900. NPEPPS.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Nucleus Curated

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: UniProtKB-SubCell

    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.

    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

    ArrayExpressiP55786.
    BgeeiP55786.
    CleanExiHS_NPEPPS.
    GenevestigatoriP55786.

    Organism-specific databases

    HPAiHPA021453.
    HPA045649.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi114897. 40 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.
    HOGENOMiHOG000106482.
    HOVERGENiHBG106325.
    InParanoidiP55786.
    KOiK08776.
    OMAiRTVQQCC.
    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. Align

    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

    MWLAAAAPSL ARRLLFLGPP PPPLLLLVFS RSSRRRLHSL GLAAMPEKRP    50
    FERLPADVSP INYSLCLKPD LLDFTFEGKL EAAAQVRQAT NQIVMNCADI 100
    DIITASYAPE GDEEIHATGF NYQNEDEKVT LSFPSTLQTG TGTLKIDFVG 150
    ELNDKMKGFY RSKYTTPSGE VRYAAVTQFE ATDARRAFPC WDEPAIKATF 200
    DISLVVPKDR VALSNMNVID RKPYPDDENL VEVKFARTPV MSTYLVAFVV 250
    GEYDFVETRS KDGVCVRVYT PVGKAEQGKF ALEVAAKTLP FYKDYFNVPY 300
    PLPKIDLIAI ADFAAGAMEN WGLVTYRETA LLIDPKNSCS SSRQWVALVV 350
    GHELAHQWFG NLVTMEWWTH LWLNEGFASW IEYLCVDHCF PEYDIWTQFV 400
    SADYTRAQEL DALDNSHPIE VSVGHPSEVD EIFDAISYSK GASVIRMLHD 450
    YIGDKDFKKG MNMYLTKFQQ KNAATEDLWE SLENASGKPI AAVMNTWTKQ 500
    MGFPLIYVEA EQVEDDRLLR LSQKKFCAGG SYVGEDCPQW MVPITISTSE 550
    DPNQAKLKIL MDKPEMNVVL KNVKPDQWVK LNLGTVGFYR TQYSSAMLES 600
    LLPGIRDLSL PPVDRLGLQN DLFSLARAGI ISTVEVLKVM EAFVNEPNYT 650
    VWSDLSCNLG ILSTLLSHTD FYEEIQEFVK DVFSPIGERL GWDPKPGEGH 700
    LDALLRGLVL GKLGKAGHKA TLEEARRRFK DHVEGKQILS ADLRSPVYLT 750
    VLKHGDGTTL DIMLKLHKQA DMQEEKNRIE RVLGATLLPD LIQKVLTFAL 800
    SEEVRPQDTV SVIGGVAGGS KHGRKAAWKF IKDNWEELYN RYQGGFLISR 850
    LIKLSVEGFA VDKMAGEVKA FFESHPAPSA ERTIQQCCEN ILLNAAWLKR 900
    DAESIHQYLL QRKASPPTV 919
    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.
    The sequence CAA68964.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    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:
    EMBL
    GenBank
    DDBJ
    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.
    RefSeqiNP_006301.3. NM_006310.3.
    UniGeneiHs.443837.

    Genome annotation databases

    EnsembliENST00000322157; ENSP00000320324; ENSG00000141279.
    ENST00000544660; ENSP00000442461; ENSG00000141279.
    GeneIDi9520.
    KEGGihsa:9520.
    UCSCiuc002ilr.4. human.

    Polymorphism databases

    DMDMi51704228.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS45721.1.
    RefSeqi NP_006301.3. NM_006310.3.
    UniGenei Hs.443837.

    3D structure databases

    ProteinModelPortali P55786.
    SMRi P55786. Positions 42-910.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114897. 40 interactions.
    IntActi P55786. 6 interactions.
    MINTi MINT-4999844.
    STRINGi 9606.ENSP00000320324.

    Chemistry

    BindingDBi P55786.
    ChEMBLi CHEMBL2264.

    Protein family/group databases

    MEROPSi M01.010.

    PTM databases

    PhosphoSitei P55786.

    Polymorphism databases

    DMDMi 51704228.

    Proteomic databases

    MaxQBi P55786.
    PaxDbi P55786.
    PeptideAtlasi P55786.
    PRIDEi P55786.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322157 ; ENSP00000320324 ; ENSG00000141279 .
    ENST00000544660 ; ENSP00000442461 ; ENSG00000141279 .
    GeneIDi 9520.
    KEGGi hsa:9520.
    UCSCi uc002ilr.4. human.

    Organism-specific databases

    CTDi 9520.
    GeneCardsi GC17P045608.
    H-InvDB HIX0013922.
    HGNCi HGNC:7900. NPEPPS.
    HPAi HPA021453.
    HPA045649.
    MIMi 606793. gene.
    neXtProti NX_P55786.
    PharmGKBi PA31703.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0308.
    HOGENOMi HOG000106482.
    HOVERGENi HBG106325.
    InParanoidi P55786.
    KOi K08776.
    OMAi RTVQQCC.
    PhylomeDBi P55786.
    TreeFami TF300395.

    Enzyme and pathway databases

    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi NPEPPS. human.
    GeneWikii NPEPPS.
    GenomeRNAii 9520.
    NextBioi 35678.
    PMAP-CutDB P55786.
    PROi P55786.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55786.
    Bgeei P55786.
    CleanExi HS_NPEPPS.
    Genevestigatori P55786.

    Family and domain databases

    InterProi IPR024571. ERAP1-like_C_dom.
    IPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    [Graphical view ]
    PANTHERi PTHR11533. PTHR11533. 1 hit.
    Pfami PF11838. ERAP1_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view ]
    PRINTSi PR00756. ALADIPTASE.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].

    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: October 1, 2014
    This is version 138 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

    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