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Q96KP4

- CNDP2_HUMAN

UniProt

Q96KP4 - CNDP2_HUMAN

Protein

Cytosolic non-specific dipeptidase

Gene

CNDP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (19 Sep 2002)
      Previous versions | rss
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    Functioni

    Hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. Isoform 2 may be play a role as tumor suppressor in hepatocellular carcinoma (HCC) cells.2 Publications

    Catalytic activityi

    Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids.1 Publication

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Enzyme regulationi

    Inhibited by p-hydroxymercurybenzoate. The inhibitory concentration 50% (IC50) is 13 µM. Inhibited by bestatin. The inhibitory concentration 50% (IC50) is 7 nM at pH 9.5.1 Publication

    Kineticsi

    1. KM=1.04 mM for Ser-Gln (at pH 7.5 and in the presence of 0.1 mM manganese ions)2 Publications
    2. KM=0.6 mM for Cys-Gly (at pH 8.0 and in the presence of 50 µM manganese ions)2 Publications
    3. KM=15 mM for carnosine (at pH 9.5 and in the presence of 0.1 mM manganese ions)2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi99 – 991Manganese 2By similarity
    Active sitei101 – 1011By similarity
    Metal bindingi132 – 1321Manganese 1By similarity
    Metal bindingi132 – 1321Manganese 2By similarity
    Active sitei166 – 1661Proton acceptorBy similarity
    Metal bindingi167 – 1671Manganese 1By similarity
    Metal bindingi195 – 1951Manganese 2By similarity
    Binding sitei195 – 1951Substrate; via carbonyl oxygenBy similarity
    Binding sitei228 – 2281Substrate; shared with homodimeric partnerBy similarity
    Sitei228 – 2281Important for catalytic activityBy similarity
    Binding sitei330 – 3301Substrate; shared with homodimeric partnerBy similarity
    Binding sitei343 – 3431SubstrateBy similarity
    Binding sitei417 – 4171Substrate; via amide nitrogen and carbonyl oxygenBy similarity
    Metal bindingi445 – 4451Manganese 1By similarity
    Binding sitei445 – 4451SubstrateBy similarity

    GO - Molecular functioni

    1. carboxypeptidase activity Source: Reactome
    2. dipeptidase activity Source: InterPro
    3. metal ion binding Source: UniProtKB-KW
    4. metallopeptidase activity Source: UniProtKB-KW
    5. tripeptidase activity Source: InterPro

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. glutathione biosynthetic process Source: Reactome
    3. glutathione derivative biosynthetic process Source: Reactome
    4. small molecule metabolic process Source: Reactome
    5. sulfur amino acid metabolic process Source: Reactome
    6. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.4.13.18. 2681.
    ReactomeiREACT_115639. Sulfur amino acid metabolism.
    REACT_6960. Glutathione synthesis and recycling.
    SABIO-RKQ96KP4.

    Protein family/group databases

    MEROPSiM20.005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytosolic non-specific dipeptidase (EC:3.4.13.18)
    Alternative name(s):
    CNDP dipeptidase 2
    Glutamate carboxypeptidase-like protein 1
    Peptidase A
    Gene namesi
    Name:CNDP2
    Synonyms:CN2, CPGL, PEPA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:24437. CNDP2.

    Subcellular locationi

    Cytoplasm 2 Publications

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134975242.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 475474Cytosolic non-specific dipeptidasePRO_0000185272Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei9 – 91N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ96KP4.
    PaxDbiQ96KP4.
    PRIDEiQ96KP4.

    2D gel databases

    OGPiQ96KP4.

    PTM databases

    PhosphoSiteiQ96KP4.

    Expressioni

    Tissue specificityi

    Isoform 1 is ubiquitously expressed with higher levels in kidney and liver (at protein level). Isoform 2 is expressed in fetal tissues, it is only expressed in adult liver and placental tissues.2 Publications

    Gene expression databases

    ArrayExpressiQ96KP4.
    BgeeiQ96KP4.
    CleanExiHS_CNDP2.
    GenevestigatoriQ96KP4.

    Organism-specific databases

    HPAiCAB026196.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NDRG1Q925971EBI-1190734,EBI-716486

    Protein-protein interaction databases

    BioGridi120866. 36 interactions.
    IntActiQ96KP4. 2 interactions.
    STRINGi9606.ENSP00000325548.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96KP4.
    SMRiQ96KP4. Positions 1-474.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni166 – 1672Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the peptidase M20A family.Curated

    Phylogenomic databases

    eggNOGiCOG0624.
    HOGENOMiHOG000216709.
    HOVERGENiHBG051103.
    InParanoidiQ96KP4.
    KOiK08660.
    OMAiTDGAHSI.
    PhylomeDBiQ96KP4.
    TreeFamiTF300633.

    Family and domain databases

    Gene3Di3.30.70.360. 1 hit.
    InterProiIPR001261. ArgE/DapE_CS.
    IPR017153. GSH_degradosome_DUG1.
    IPR002933. Peptidase_M20.
    IPR011650. Peptidase_M20_dimer.
    [Graphical view]
    PfamiPF07687. M20_dimer. 1 hit.
    PF01546. Peptidase_M20. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037242. CNDP_dipeptidase. 1 hit.
    PROSITEiPS00759. ARGE_DAPE_CPG2_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96KP4-1) [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

    MAALTTLFKY IDENQDRYIK KLAKWVAIQS VSAWPEKRGE IRRMMEVAAA    50
    DVKQLGGSVE LVDIGKQKLP DGSEIPLPPI LLGRLGSDPQ KKTVCIYGHL 100
    DVQPAALEDG WDSEPFTLVE RDGKLYGRGS TDDKGPVAGW INALEAYQKT 150
    GQEIPVNVRF CLEGMEESGS EGLDELIFAR KDTFFKDVDY VCISDNYWLG 200
    KKKPCITYGL RGICYFFIEV ECSNKDLHSG VYGGSVHEAM TDLILLMGSL 250
    VDKRGNILIP GINEAVAAVT EEEHKLYDDI DFDIEEFAKD VGAQILLHSH 300
    KKDILMHRWR YPSLSLHGIE GAFSGSGAKT VIPRKVVGKF SIRLVPNMTP 350
    EVVGEQVTSY LTKKFAELRS PNEFKVYMGH GGKPWVSDFS HPHYLAGRRA 400
    MKTVFGVEPD LTREGGSIPV TLTFQEATGK NVMLLPVGSA DDGAHSQNEK 450
    LNRYNYIEGT KMLAAYLYEV SQLKD 475
    Length:475
    Mass (Da):52,878
    Last modified:September 19, 2002 - v2
    Checksum:i43FA0668B0587A39
    GO
    Isoform 2 (identifier: Q96KP4-2) [UniParc]FASTAAdd to Basket

    Also known as: CPGL-B

    The sequence of this isoform differs from the canonical sequence as follows:
         69-152: Missing.

    Show »
    Length:391
    Mass (Da):43,833
    Checksum:i07E5F4464C8FC179
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti128 – 1281R → G in BAA91840. (PubMed:14702039)Curated
    Sequence conflicti348 – 3481M → T in BAG53426. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti126 – 1261Y → H.1 Publication
    Corresponds to variant rs2278161 [ dbSNP | Ensembl ].
    VAR_057154

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei69 – 15284Missing in isoform 2. 1 PublicationVSP_038203Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AX523938 Unassigned DNA. Translation: CAD56843.1.
    AJ347717 mRNA. Translation: CAC69883.1.
    AK001692 mRNA. Translation: BAA91840.1.
    AK097155 mRNA. Translation: BAG53426.1.
    AF258592 mRNA. Translation: AAG23795.1.
    AC009704 Genomic DNA. No translation available.
    CH471117 Genomic DNA. Translation: EAW66551.1.
    BC001375 mRNA. Translation: AAH01375.1.
    BC003176 mRNA. Translation: AAH03176.1.
    CCDSiCCDS12006.1. [Q96KP4-1]
    CCDS54190.1. [Q96KP4-2]
    RefSeqiNP_001161971.1. NM_001168499.1. [Q96KP4-2]
    NP_060705.2. NM_018235.2. [Q96KP4-1]
    XP_005266785.1. XM_005266728.1. [Q96KP4-1]
    XP_006722565.1. XM_006722502.1. [Q96KP4-1]
    XP_006722566.1. XM_006722503.1. [Q96KP4-1]
    UniGeneiHs.149185.

    Genome annotation databases

    EnsembliENST00000324262; ENSP00000325548; ENSG00000133313. [Q96KP4-1]
    ENST00000324301; ENSP00000325756; ENSG00000133313. [Q96KP4-2]
    ENST00000579847; ENSP00000462311; ENSG00000133313. [Q96KP4-1]
    GeneIDi55748.
    KEGGihsa:55748.
    UCSCiuc002llm.2. human. [Q96KP4-1]
    uc002lln.2. human. [Q96KP4-2]

    Polymorphism databases

    DMDMi23396498.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AX523938 Unassigned DNA. Translation: CAD56843.1 .
    AJ347717 mRNA. Translation: CAC69883.1 .
    AK001692 mRNA. Translation: BAA91840.1 .
    AK097155 mRNA. Translation: BAG53426.1 .
    AF258592 mRNA. Translation: AAG23795.1 .
    AC009704 Genomic DNA. No translation available.
    CH471117 Genomic DNA. Translation: EAW66551.1 .
    BC001375 mRNA. Translation: AAH01375.1 .
    BC003176 mRNA. Translation: AAH03176.1 .
    CCDSi CCDS12006.1. [Q96KP4-1 ]
    CCDS54190.1. [Q96KP4-2 ]
    RefSeqi NP_001161971.1. NM_001168499.1. [Q96KP4-2 ]
    NP_060705.2. NM_018235.2. [Q96KP4-1 ]
    XP_005266785.1. XM_005266728.1. [Q96KP4-1 ]
    XP_006722565.1. XM_006722502.1. [Q96KP4-1 ]
    XP_006722566.1. XM_006722503.1. [Q96KP4-1 ]
    UniGenei Hs.149185.

    3D structure databases

    ProteinModelPortali Q96KP4.
    SMRi Q96KP4. Positions 1-474.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120866. 36 interactions.
    IntActi Q96KP4. 2 interactions.
    STRINGi 9606.ENSP00000325548.

    Protein family/group databases

    MEROPSi M20.005.

    PTM databases

    PhosphoSitei Q96KP4.

    Polymorphism databases

    DMDMi 23396498.

    2D gel databases

    OGPi Q96KP4.

    Proteomic databases

    MaxQBi Q96KP4.
    PaxDbi Q96KP4.
    PRIDEi Q96KP4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324262 ; ENSP00000325548 ; ENSG00000133313 . [Q96KP4-1 ]
    ENST00000324301 ; ENSP00000325756 ; ENSG00000133313 . [Q96KP4-2 ]
    ENST00000579847 ; ENSP00000462311 ; ENSG00000133313 . [Q96KP4-1 ]
    GeneIDi 55748.
    KEGGi hsa:55748.
    UCSCi uc002llm.2. human. [Q96KP4-1 ]
    uc002lln.2. human. [Q96KP4-2 ]

    Organism-specific databases

    CTDi 55748.
    GeneCardsi GC18P072163.
    H-InvDB HIX0136845.
    HGNCi HGNC:24437. CNDP2.
    HPAi CAB026196.
    MIMi 169800. gene.
    neXtProti NX_Q96KP4.
    PharmGKBi PA134975242.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0624.
    HOGENOMi HOG000216709.
    HOVERGENi HBG051103.
    InParanoidi Q96KP4.
    KOi K08660.
    OMAi TDGAHSI.
    PhylomeDBi Q96KP4.
    TreeFami TF300633.

    Enzyme and pathway databases

    BRENDAi 3.4.13.18. 2681.
    Reactomei REACT_115639. Sulfur amino acid metabolism.
    REACT_6960. Glutathione synthesis and recycling.
    SABIO-RK Q96KP4.

    Miscellaneous databases

    ChiTaRSi CNDP2. human.
    GenomeRNAii 55748.
    NextBioi 60729.
    PROi Q96KP4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96KP4.
    Bgeei Q96KP4.
    CleanExi HS_CNDP2.
    Genevestigatori Q96KP4.

    Family and domain databases

    Gene3Di 3.30.70.360. 1 hit.
    InterProi IPR001261. ArgE/DapE_CS.
    IPR017153. GSH_degradosome_DUG1.
    IPR002933. Peptidase_M20.
    IPR011650. Peptidase_M20_dimer.
    [Graphical view ]
    Pfami PF07687. M20_dimer. 1 hit.
    PF01546. Peptidase_M20. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037242. CNDP_dipeptidase. 1 hit.
    PROSITEi PS00759. ARGE_DAPE_CPG2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase."
      Teufel M., Saudek V., Ledig J.P., Bernhardt A., Boularand S., Carreau A., Cairns N.J., Carter C., Cowley D.J., Duverger D., Ganzhorn A.J., Guenet C., Heintzelmann B., Laucher V., Sauvage C., Smirnova T.
      J. Biol. Chem. 278:6521-6531(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 129-137; 276-289; 311-329; 370-375 AND 462-474, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Brain.
    2. "Cloning and sequencing of human glutamate carboxypeptidase homologue in peptidase family M20."
      Chen J.M., Barrett A.J.
      Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT HIS-126.
      Tissue: Uterus.
    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 1).
      Tissue: Spleen and Teratocarcinoma.
    4. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Colon and Kidney.
    8. Bienvenut W.V., Heiserich L., Gottlieb E.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-9; 54-66; 255-275 AND 403-430, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    9. "Identification of carboxypeptidase of glutamate like-B as a candidate suppressor in cell growth and metastasis in human hepatocellular carcinoma."
      Zhang P., Chan D.W., Zhu Y., Li J.J., Ng I.-O., Wan D., Gu J.
      Clin. Cancer Res. 12:6617-6625(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION.
    10. "Dug1p Is a Cys-Gly peptidase of the gamma-glutamyl cycle of Saccharomyces cerevisiae and represents a novel family of Cys-Gly peptidases."
      Kaur H., Kumar C., Junot C., Toledano M.B., Bachhawat A.K.
      J. Biol. Chem. 284:14493-14502(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    11. "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 ALA-2 AND LYS-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCNDP2_HUMAN
    AccessioniPrimary (citable) accession number: Q96KP4
    Secondary accession number(s): B3KUG4
    , Q8WY59, Q9BQ94, Q9NVB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: September 19, 2002
    Last modified: October 1, 2014
    This is version 119 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 18
      Human chromosome 18: 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. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3