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P12955

- PEPD_HUMAN

UniProt

P12955 - PEPD_HUMAN

Protein

Xaa-Pro dipeptidase

Gene

PEPD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.

    Catalytic activityi

    Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.

    Cofactori

    Binds 2 manganese ions per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi276 – 2761Manganese 1
    Metal bindingi287 – 2871Manganese 1
    Metal bindingi287 – 2871Manganese 2
    Metal bindingi370 – 3701Manganese 2
    Metal bindingi412 – 4121Manganese 2
    Metal bindingi452 – 4521Manganese 1
    Metal bindingi452 – 4521Manganese 2

    GO - Molecular functioni

    1. aminopeptidase activity Source: InterPro
    2. dipeptidase activity Source: UniProtKB-KW
    3. manganese ion binding Source: InterPro
    4. metallocarboxypeptidase activity Source: ProtInc

    GO - Biological processi

    1. cellular amino acid metabolic process Source: ProtInc
    2. collagen catabolic process Source: UniProtKB-KW
    3. proteolysis Source: ProtInc

    Keywords - Molecular functioni

    Dipeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Collagen degradation

    Keywords - Ligandi

    Manganese, Metal-binding

    Protein family/group databases

    MEROPSiM24.007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Xaa-Pro dipeptidase (EC:3.4.13.9)
    Short name:
    X-Pro dipeptidase
    Alternative name(s):
    Imidodipeptidase
    Peptidase D
    Proline dipeptidase
    Short name:
    Prolidase
    Gene namesi
    Name:PEPD
    Synonyms:PRD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:8840. PEPD.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Involvement in diseasei

    Prolidase deficiency (PD) [MIM:170100]: A multisystem disorder associated with massive iminodipeptiduria and lack of or reduced prolidase activity in erythrocytes, leukocytes, or cultured fibroblasts. Clinical features include skin ulcers, developmental delay, recurrent infections, and a characteristic facies.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti184 – 1841R → Q in PD. 1 Publication
    VAR_011614
    Natural varianti276 – 2761D → N in PD. 1 Publication
    VAR_004404
    Natural varianti278 – 2781G → D in PD. 1 Publication
    VAR_011615
    Natural varianti448 – 4481G → R in PD. 3 Publications
    VAR_004405
    Natural varianti452 – 4521Missing in PD. 2 Publications
    VAR_004406

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi170100. phenotype.
    Orphaneti742. Prolidase deficiency.
    PharmGKBiPA33181.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 493492Xaa-Pro dipeptidasePRO_0000185087Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP12955.
    PaxDbiP12955.
    PeptideAtlasiP12955.
    PRIDEiP12955.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00257882.

    PTM databases

    PhosphoSiteiP12955.

    Expressioni

    Gene expression databases

    ArrayExpressiP12955.
    BgeeiP12955.
    CleanExiHS_PEPD.
    GenevestigatoriP12955.

    Organism-specific databases

    HPAiHPA015599.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi111208. 31 interactions.
    IntActiP12955. 9 interactions.
    MINTiMINT-5000488.
    STRINGi9606.ENSP00000244137.

    Structurei

    Secondary structure

    1
    493
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 3616
    Beta strandi45 – 495
    Beta strandi54 – 563
    Helixi69 – 757
    Beta strandi79 – 813
    Beta strandi83 – 875
    Turni88 – 903
    Beta strandi93 – 975
    Helixi102 – 1043
    Turni105 – 1073
    Helixi114 – 1218
    Beta strandi124 – 1285
    Helixi129 – 1313
    Helixi132 – 1387
    Turni152 – 1543
    Helixi166 – 1683
    Helixi176 – 18510
    Helixi189 – 21224
    Helixi219 – 23416
    Beta strandi238 – 2414
    Beta strandi244 – 2474
    Helixi248 – 2525
    Beta strandi272 – 2776
    Beta strandi279 – 2813
    Beta strandi288 – 2936
    Helixi300 – 31920
    Helixi326 – 34318
    Helixi351 – 3566
    Turni357 – 3593
    Helixi360 – 3634
    Beta strandi373 – 3775
    Helixi394 – 3963
    Beta strandi408 – 4114
    Beta strandi414 – 4163
    Helixi419 – 4279
    Helixi429 – 4324
    Helixi437 – 4437
    Beta strandi448 – 4503
    Beta strandi452 – 4576
    Beta strandi459 – 4646
    Helixi472 – 4798

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IW2X-ray1.82A/B2-493[»]
    2OKNX-ray2.45A/B2-493[»]
    ProteinModelPortaliP12955.
    SMRiP12955. Positions 6-482.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12955.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0006.
    HOGENOMiHOG000008763.
    HOVERGENiHBG053562.
    InParanoidiP12955.
    KOiK14213.
    OMAiPIVACGE.
    OrthoDBiEOG7FNC76.
    PhylomeDBiP12955.
    TreeFamiTF313396.

    Family and domain databases

    Gene3Di3.40.350.10. 1 hit.
    3.90.230.10. 1 hit.
    InterProiIPR007865. Aminopep_P_N.
    IPR029149. Creatin/AminoP/Spt16_NTD.
    IPR028980. Creatinase/Aminopeptidase_P_N.
    IPR000994. Pept_M24_structural-domain.
    IPR001131. Peptidase_M24B_aminopep-P_CS.
    [Graphical view]
    PfamiPF05195. AMP_N. 1 hit.
    PF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    SMARTiSM01011. AMP_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF53092. SSF53092. 1 hit.
    SSF55920. SSF55920. 1 hit.
    PROSITEiPS00491. PROLINE_PEPTIDASE. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P12955-1) [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

    MAAATGPSFW LGNETLKVPL ALFALNRQRL CERLRKNPAV QAGSIVVLQG    50
    GEETQRYCTD TGVLFRQESF FHWAFGVTEP GCYGVIDVDT GKSTLFVPRL 100
    PASHATWMGK IHSKEHFKEK YAVDDVQYVD EIASVLTSQK PSVLLTLRGV 150
    NTDSGSVCRE ASFDGISKFE VNNTILHPEI VECRVFKTDM ELEVLRYTNK 200
    ISSEAHREVM KAVKVGMKEY ELESLFEHYC YSRGGMRHSS YTCICGSGEN 250
    SAVLHYGHAG APNDRTIQNG DMCLFDMGGE YYCFASDITC SFPANGKFTA 300
    DQKAVYEAVL RSSRAVMGAM KPGVWWPDMH RLADRIHLEE LAHMGILSGS 350
    VDAMVQAHLG AVFMPHGLGH FLGIDVHDVG GYPEGVERID EPGLRSLRTA 400
    RHLQPGMVLT VEPGIYFIDH LLDEALADPA RASFLNREVL QRFRGFGGVR 450
    IEEDVVVTDS GIELLTCVPR TVEEIEACMA GCDKAFTPFS GPK 493
    Length:493
    Mass (Da):54,548
    Last modified:January 23, 2007 - v3
    Checksum:iE8C4A2497E44BA22
    GO
    Isoform 2 (identifier: P12955-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         184-224: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:452
    Mass (Da):49,691
    Checksum:iEA1B0DFBE694A180
    GO
    Isoform 3 (identifier: P12955-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         68-131: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:429
    Mass (Da):47,261
    Checksum:i2D094B4069E39CF5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 481L → R in BAF84250. (PubMed:14702039)Curated
    Sequence conflicti66 – 661R → L in AAA60064. (PubMed:2925654)Curated
    Sequence conflicti107 – 1071W → R in BAF83470. (PubMed:14702039)Curated
    Sequence conflicti108 – 1081M → I in BAF83445. (PubMed:14702039)Curated
    Sequence conflicti183 – 1831C → S in AAA60064. (PubMed:2925654)Curated
    Sequence conflicti221 – 2211E → G in AAA60064. (PubMed:2925654)Curated
    Sequence conflicti283 – 2842CF → SV in AAA60064. (PubMed:2925654)Curated
    Sequence conflicti294 – 2941A → R in AAA60064. (PubMed:2925654)Curated
    Sequence conflicti311 – 3111R → L in AAA60064. (PubMed:2925654)Curated
    Sequence conflicti324 – 3241V → D in AAA60064. (PubMed:2925654)Curated
    Sequence conflicti329 – 3302MH → ID in AAA60064. (PubMed:2925654)Curated
    Sequence conflicti408 – 4081V → A in BAG56678. (PubMed:14702039)Curated
    Sequence conflicti458 – 4581T → I in AAA60064. (PubMed:2925654)Curated
    Sequence conflicti478 – 4781C → R in BAF83470. (PubMed:14702039)Curated

    Mass spectrometryi

    Molecular mass is 54251.73 Da from positions 2 - 493. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti184 – 1841R → Q in PD. 1 Publication
    VAR_011614
    Natural varianti276 – 2761D → N in PD. 1 Publication
    VAR_004404
    Natural varianti278 – 2781G → D in PD. 1 Publication
    VAR_011615
    Natural varianti388 – 3881R → H.
    Corresponds to variant rs2230062 [ dbSNP | Ensembl ].
    VAR_051574
    Natural varianti435 – 4351L → F.2 Publications
    Corresponds to variant rs17570 [ dbSNP | Ensembl ].
    VAR_014723
    Natural varianti448 – 4481G → R in PD. 3 Publications
    VAR_004405
    Natural varianti452 – 4521Missing in PD. 2 Publications
    VAR_004406

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei68 – 13164Missing in isoform 3. 1 PublicationVSP_045370Add
    BLAST
    Alternative sequencei184 – 22441Missing in isoform 2. 1 PublicationVSP_042629Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04605 mRNA. Translation: AAA60064.1.
    BT006692 mRNA. Translation: AAP35338.1.
    AK290756 mRNA. Translation: BAF83445.1.
    AK290781 mRNA. Translation: BAF83470.1.
    AK291561 mRNA. Translation: BAF84250.1.
    AK293126 mRNA. Translation: BAG56678.1.
    AK294619 mRNA. Translation: BAG57802.1.
    AC008744 Genomic DNA. No translation available.
    AC010485 Genomic DNA. No translation available.
    BC004305 mRNA. Translation: AAH04305.1.
    BC015027 mRNA. Translation: AAH15027.1.
    BC028295 mRNA. Translation: AAH28295.1.
    CCDSiCCDS42544.1. [P12955-1]
    CCDS54244.1. [P12955-3]
    CCDS54245.1. [P12955-2]
    PIRiA32454.
    RefSeqiNP_000276.2. NM_000285.3. [P12955-1]
    NP_001159528.1. NM_001166056.1. [P12955-2]
    NP_001159529.1. NM_001166057.1. [P12955-3]
    UniGeneiHs.36473.

    Genome annotation databases

    EnsembliENST00000244137; ENSP00000244137; ENSG00000124299. [P12955-1]
    ENST00000397032; ENSP00000380226; ENSG00000124299. [P12955-2]
    ENST00000436370; ENSP00000391890; ENSG00000124299. [P12955-3]
    GeneIDi5184.
    KEGGihsa:5184.
    UCSCiuc002nur.4. human. [P12955-1]
    uc010xrr.2. human. [P12955-2]

    Polymorphism databases

    DMDMi50403718.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04605 mRNA. Translation: AAA60064.1 .
    BT006692 mRNA. Translation: AAP35338.1 .
    AK290756 mRNA. Translation: BAF83445.1 .
    AK290781 mRNA. Translation: BAF83470.1 .
    AK291561 mRNA. Translation: BAF84250.1 .
    AK293126 mRNA. Translation: BAG56678.1 .
    AK294619 mRNA. Translation: BAG57802.1 .
    AC008744 Genomic DNA. No translation available.
    AC010485 Genomic DNA. No translation available.
    BC004305 mRNA. Translation: AAH04305.1 .
    BC015027 mRNA. Translation: AAH15027.1 .
    BC028295 mRNA. Translation: AAH28295.1 .
    CCDSi CCDS42544.1. [P12955-1 ]
    CCDS54244.1. [P12955-3 ]
    CCDS54245.1. [P12955-2 ]
    PIRi A32454.
    RefSeqi NP_000276.2. NM_000285.3. [P12955-1 ]
    NP_001159528.1. NM_001166056.1. [P12955-2 ]
    NP_001159529.1. NM_001166057.1. [P12955-3 ]
    UniGenei Hs.36473.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IW2 X-ray 1.82 A/B 2-493 [» ]
    2OKN X-ray 2.45 A/B 2-493 [» ]
    ProteinModelPortali P12955.
    SMRi P12955. Positions 6-482.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111208. 31 interactions.
    IntActi P12955. 9 interactions.
    MINTi MINT-5000488.
    STRINGi 9606.ENSP00000244137.

    Chemistry

    BindingDBi P12955.
    ChEMBLi CHEMBL4185.

    Protein family/group databases

    MEROPSi M24.007.

    PTM databases

    PhosphoSitei P12955.

    Polymorphism databases

    DMDMi 50403718.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00257882.

    Proteomic databases

    MaxQBi P12955.
    PaxDbi P12955.
    PeptideAtlasi P12955.
    PRIDEi P12955.

    Protocols and materials databases

    DNASUi 5184.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000244137 ; ENSP00000244137 ; ENSG00000124299 . [P12955-1 ]
    ENST00000397032 ; ENSP00000380226 ; ENSG00000124299 . [P12955-2 ]
    ENST00000436370 ; ENSP00000391890 ; ENSG00000124299 . [P12955-3 ]
    GeneIDi 5184.
    KEGGi hsa:5184.
    UCSCi uc002nur.4. human. [P12955-1 ]
    uc010xrr.2. human. [P12955-2 ]

    Organism-specific databases

    CTDi 5184.
    GeneCardsi GC19M033877.
    HGNCi HGNC:8840. PEPD.
    HPAi HPA015599.
    MIMi 170100. phenotype.
    613230. gene.
    neXtProti NX_P12955.
    Orphaneti 742. Prolidase deficiency.
    PharmGKBi PA33181.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0006.
    HOGENOMi HOG000008763.
    HOVERGENi HBG053562.
    InParanoidi P12955.
    KOi K14213.
    OMAi PIVACGE.
    OrthoDBi EOG7FNC76.
    PhylomeDBi P12955.
    TreeFami TF313396.

    Miscellaneous databases

    ChiTaRSi PEPD. human.
    EvolutionaryTracei P12955.
    GeneWikii PEPD.
    GenomeRNAii 5184.
    NextBioi 20054.
    PROi P12955.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P12955.
    Bgeei P12955.
    CleanExi HS_PEPD.
    Genevestigatori P12955.

    Family and domain databases

    Gene3Di 3.40.350.10. 1 hit.
    3.90.230.10. 1 hit.
    InterProi IPR007865. Aminopep_P_N.
    IPR029149. Creatin/AminoP/Spt16_NTD.
    IPR028980. Creatinase/Aminopeptidase_P_N.
    IPR000994. Pept_M24_structural-domain.
    IPR001131. Peptidase_M24B_aminopep-P_CS.
    [Graphical view ]
    Pfami PF05195. AMP_N. 1 hit.
    PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    SMARTi SM01011. AMP_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53092. SSF53092. 1 hit.
    SSF55920. SSF55920. 1 hit.
    PROSITEi PS00491. PROLINE_PEPTIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure and gene localization of human prolidase."
      Endo F., Tanoue A., Nakai H., Hata A., Indo Y., Titani K., Matsuda I.
      J. Biol. Chem. 264:4476-4481(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver and Placenta.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) 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] (ISOFORMS 1; 2 AND 3), VARIANT PHE-435.
      Tissue: Brain and Kidney.
    4. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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), VARIANT PHE-435.
      Tissue: Kidney, Skin and Uterus.
    6. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
      Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
      Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
      Tissue: Mammary cancer.
    7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Crystal structure of human prolidase: the molecular basis of PD disease."
      Protein structure factory (PSF)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS, COFACTOR.
    11. "A single nucleotide change in the prolidase gene in fibroblasts from two patients with polypeptide positive prolidase deficiency. Expression of the mutant enzyme in NIH 3T3 cells."
      Tanoue A., Endo F., Kitano A., Matsuda I.
      J. Clin. Invest. 86:351-355(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PD ASN-276.
    12. "Four novel PEPD alleles causing prolidase deficiency."
      Ledoux P., Scriver C.R., Hechtman P.
      Am. J. Hum. Genet. 54:1014-1021(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PD ARG-448 AND GLU-452 DEL.
    13. "Expression and molecular analysis of mutations in prolidase deficiency."
      Ledoux P., Scriver C.R., Hechtman P.
      Am. J. Hum. Genet. 59:1035-1039(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PD GLN-184; ASP-278; ARG-448 AND GLU-452 DEL.
    14. "Mutation analysis of five new patients affected by prolidase deficiency: the lack of enzyme activity causes necrosis-like cell death in cultured fibroblasts."
      Forlino A., Lupi A., Vaghi P., Icaro Cornaglia A., Calligaro A., Campari E., Cetta G.
      Hum. Genet. 111:314-322(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PD ARG-448.

    Entry informationi

    Entry nameiPEPD_HUMAN
    AccessioniPrimary (citable) accession number: P12955
    Secondary accession number(s): A8K3Z1
    , A8K416, A8K696, A8MX47, B4DDB7, B4DGJ1, E9PCE8, Q8TBN9, Q9BT75
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 172 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3