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P80188

- NGAL_HUMAN

UniProt

P80188 - NGAL_HUMAN

Protein

Neutrophil gelatinase-associated lipocalin

Gene

LCN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development. Binds iron through association with 2,5-dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares structural similarities with bacterial enterobactin, and delivers or removes iron from the cell, depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor, leading to release of iron and subsequent increase of intracellular iron concentration. In contrast, association of the iron-free form (apo-24p3) with the SLC22A17 (24p3R) receptor is followed by association with an intracellular siderophore, iron chelation and iron transfer to the extracellular medium, thereby reducing intracellular iron concentration. Involved in apoptosis due to interleukin-3 (IL3) deprivation: iron-loaded form increases intracellular iron concentration without promoting apoptosis, while iron-free form decreases intracellular iron levels, inducing expression of the proapoptotic protein BCL2L11/BIM, resulting in apoptosis. Involved in innate immunity, possibly by sequestrating iron, leading to limit bacterial growth.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei126 – 1261Catecholate-type ferric siderophore
    Binding sitei145 – 1451Catecholate-type ferric siderophore
    Binding sitei154 – 1541Catecholate-type ferric siderophore

    GO - Molecular functioni

    1. iron ion binding Source: UniProtKB
    2. small molecule binding Source: InterPro
    3. transporter activity Source: InterPro

    GO - Biological processi

    1. cellular response to hydrogen peroxide Source: Ensembl
    2. cellular response to interleukin-1 Source: Ensembl
    3. cellular response to lipopolysaccharide Source: Ensembl
    4. cellular response to nutrient levels Source: Ensembl
    5. cellular response to tumor necrosis factor Source: Ensembl
    6. extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    7. innate immune response Source: UniProtKB
    8. ion transport Source: UniProtKB-KW
    9. positive regulation of cell projection organization Source: Ensembl
    10. positive regulation of gene expression Source: Ensembl
    11. protein homotrimerization Source: Ensembl
    12. response to drug Source: Ensembl
    13. response to herbicide Source: Ensembl
    14. response to virus Source: Ensembl
    15. siderophore transport Source: UniProtKB

    Keywords - Biological processi

    Apoptosis, Immunity, Innate immunity, Ion transport, Iron transport, Transport

    Keywords - Ligandi

    Iron

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neutrophil gelatinase-associated lipocalin
    Short name:
    NGAL
    Alternative name(s):
    25 kDa alpha-2-microglobulin-related subunit of MMP-9
    Lipocalin-2
    Oncogene 24p3
    Siderocalin LCN2
    p25
    Gene namesi
    Name:LCN2
    Synonyms:HNL, NGAL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:6526. LCN2.

    Subcellular locationi

    Secreted 1 Publication
    Note: Upon binding to the SLC22A17 (24p3R) receptor, it is internalized.

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. extracellular region Source: UniProtKB
    3. extracellular space Source: UniProt
    4. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30309.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20201 PublicationAdd
    BLAST
    Chaini21 – 198178Neutrophil gelatinase-associated lipocalinPRO_0000017933Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211Pyrrolidone carboxylic acid1 Publication
    Glycosylationi85 – 851N-linked (GlcNAc...)5 Publications
    Disulfide bondi96 ↔ 195

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    MaxQBiP80188.
    PaxDbiP80188.
    PRIDEiP80188.

    PTM databases

    PhosphoSiteiP80188.

    Expressioni

    Tissue specificityi

    Expressed in bone marrow and in tissues that are prone to exposure to microorganism. High expression is found in bone marrow as well as in uterus, prostate, salivary gland, stomach, appendix, colon, trachea and lung. Not found in the small intestine or peripheral blood leukocytes.1 Publication

    Inductioni

    Expression is activated by the oncoprotein BCR-ABL; BCR-ABL misregulates expression via the JAK/STAT pathway and binding of STAT5A to the promoter.1 Publication

    Gene expression databases

    BgeeiP80188.
    CleanExiHS_LCN2.
    GenevestigatoriP80188.

    Organism-specific databases

    HPAiCAB016549.
    CAB016550.
    HPA002695.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Heterodimer; disulfide-linked with MMP9.1 Publication

    Protein-protein interaction databases

    BioGridi110126. 2 interactions.
    DIPiDIP-29952N.
    STRINGi9606.ENSP00000277480.

    Structurei

    Secondary structure

    1
    198
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi33 – 353
    Helixi44 – 474
    Beta strandi49 – 6012
    Helixi66 – 694
    Beta strandi73 – 786
    Turni80 – 823
    Beta strandi84 – 929
    Beta strandi95 – 10511
    Beta strandi111 – 1144
    Helixi117 – 1193
    Beta strandi123 – 13311
    Beta strandi135 – 14713
    Beta strandi150 – 16213
    Helixi166 – 17813
    Helixi183 – 1853
    Turni194 – 1963

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DFVX-ray2.60A/B21-197[»]
    1L6MX-ray2.40A/B/C21-198[»]
    1NGLNMR-A21-198[»]
    1QQSX-ray2.40A24-197[»]
    1X71X-ray2.10A/B/C21-198[»]
    1X89X-ray2.10A/B/C21-198[»]
    1X8UX-ray2.20A/B/C21-198[»]
    3BY0X-ray2.57A/B/C1-198[»]
    3CBCX-ray2.17A/B/C1-198[»]
    3CMPX-ray2.80A/B/C1-198[»]
    3DSZX-ray2.00A/B21-198[»]
    3DTQX-ray2.50A/B/C21-198[»]
    3FW4X-ray2.30A/B/C21-198[»]
    3FW5X-ray2.30A/B/C21-198[»]
    3HWDX-ray2.95A/B/C1-198[»]
    3HWEX-ray2.80A/B/C1-198[»]
    3HWFX-ray3.20A/B/C1-198[»]
    3HWGX-ray2.19A/B/C1-198[»]
    3I0AX-ray2.60A/B/C1-198[»]
    3K3LX-ray2.62A/B/C21-198[»]
    3PECX-ray2.19A/B/C21-198[»]
    3PEDX-ray2.30A/B/C21-198[»]
    3T1DX-ray2.30A/B/C1-198[»]
    3TF6X-ray2.35A/B/C21-198[»]
    3TZSX-ray2.45A/B/C21-198[»]
    3U03X-ray2.40A/C1-198[»]
    3U0DX-ray2.51A/B/C/D1-198[»]
    4GH7X-ray2.60A/C21-198[»]
    4IAWX-ray2.40A/B/C21-198[»]
    4IAXX-ray1.90A21-198[»]
    4K19X-ray2.74A/B/C21-198[»]
    ProteinModelPortaliP80188.
    SMRiP80188. Positions 24-197.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP80188.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the calycin superfamily. Lipocalin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG40148.
    HOVERGENiHBG106490.
    OrthoDBiEOG78M03G.
    PhylomeDBiP80188.
    TreeFamiTF336103.

    Family and domain databases

    Gene3Di2.40.128.20. 1 hit.
    InterProiIPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR002345. Lipocalin.
    IPR022272. Lipocalin_CS.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    IPR003087. N_gelatinase.
    [Graphical view]
    PfamiPF00061. Lipocalin. 1 hit.
    [Graphical view]
    PRINTSiPR00179. LIPOCALIN.
    PR01275. NGELATINASE.
    SUPFAMiSSF50814. SSF50814. 1 hit.
    PROSITEiPS00213. LIPOCALIN. 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: P80188-1) [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

    MPLGLLWLGL ALLGALHAQA QDSTSDLIPA PPLSKVPLQQ NFQDNQFQGK    50
    WYVVGLAGNA ILREDKDPQK MYATIYELKE DKSYNVTSVL FRKKKCDYWI 100
    RTFVPGCQPG EFTLGNIKSY PGLTSYLVRV VSTNYNQHAM VFFKKVSQNR 150
    EYFKITLYGR TKELTSELKE NFIRFSKSLG LPENHIVFPV PIDQCIDG 198
    Length:198
    Mass (Da):22,588
    Last modified:November 1, 1995 - v2
    Checksum:iCD761805723FEF1E
    GO
    Isoform 2 (identifier: P80188-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         193-198: DQCIDG → GNGQSG

    Show »
    Length:198
    Mass (Da):22,457
    Checksum:iCD691E83A0AD3F1E
    GO

    Sequence cautioni

    The sequence CAI13824.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91G → R in BAG63166. (PubMed:14702039)Curated
    Sequence conflicti13 – 131L → S in CAG46889. 1 PublicationCurated
    Sequence conflicti82 – 821K → N AA sequence (PubMed:1281792)Curated
    Sequence conflicti155 – 1551I → V AA sequence (PubMed:1281792)Curated
    Sequence conflicti178 – 1781S → Y in CAA67574. (PubMed:9339356)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei193 – 1986DQCIDG → GNGQSG in isoform 2. 1 PublicationVSP_039780

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83006 mRNA. Translation: CAA58127.1.
    X99133 Genomic DNA. Translation: CAA67574.1.
    AK301694 mRNA. Translation: BAG63166.1.
    AK316217 mRNA. Translation: BAH14588.1.
    CR542092 mRNA. Translation: CAG46889.1.
    AL590708 Genomic DNA. Translation: CAI13823.1.
    AL590708 Genomic DNA. Translation: CAI13824.1. Sequence problems.
    CH471090 Genomic DNA. Translation: EAW87750.1.
    BC033089 mRNA. Translation: AAH33089.1.
    S75256 mRNA. Translation: AAD14168.1.
    CCDSiCCDS6892.1. [P80188-1]
    PIRiJC2339.
    RefSeqiNP_005555.2. NM_005564.3. [P80188-1]
    UniGeneiHs.204238.

    Genome annotation databases

    EnsembliENST00000277480; ENSP00000277480; ENSG00000148346. [P80188-1]
    ENST00000373017; ENSP00000362108; ENSG00000148346. [P80188-1]
    GeneIDi3934.
    KEGGihsa:3934.
    UCSCiuc004bto.1. human. [P80188-1]
    uc011map.1. human. [P80188-2]

    Polymorphism databases

    DMDMi1171700.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83006 mRNA. Translation: CAA58127.1 .
    X99133 Genomic DNA. Translation: CAA67574.1 .
    AK301694 mRNA. Translation: BAG63166.1 .
    AK316217 mRNA. Translation: BAH14588.1 .
    CR542092 mRNA. Translation: CAG46889.1 .
    AL590708 Genomic DNA. Translation: CAI13823.1 .
    AL590708 Genomic DNA. Translation: CAI13824.1 . Sequence problems.
    CH471090 Genomic DNA. Translation: EAW87750.1 .
    BC033089 mRNA. Translation: AAH33089.1 .
    S75256 mRNA. Translation: AAD14168.1 .
    CCDSi CCDS6892.1. [P80188-1 ]
    PIRi JC2339.
    RefSeqi NP_005555.2. NM_005564.3. [P80188-1 ]
    UniGenei Hs.204238.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DFV X-ray 2.60 A/B 21-197 [» ]
    1L6M X-ray 2.40 A/B/C 21-198 [» ]
    1NGL NMR - A 21-198 [» ]
    1QQS X-ray 2.40 A 24-197 [» ]
    1X71 X-ray 2.10 A/B/C 21-198 [» ]
    1X89 X-ray 2.10 A/B/C 21-198 [» ]
    1X8U X-ray 2.20 A/B/C 21-198 [» ]
    3BY0 X-ray 2.57 A/B/C 1-198 [» ]
    3CBC X-ray 2.17 A/B/C 1-198 [» ]
    3CMP X-ray 2.80 A/B/C 1-198 [» ]
    3DSZ X-ray 2.00 A/B 21-198 [» ]
    3DTQ X-ray 2.50 A/B/C 21-198 [» ]
    3FW4 X-ray 2.30 A/B/C 21-198 [» ]
    3FW5 X-ray 2.30 A/B/C 21-198 [» ]
    3HWD X-ray 2.95 A/B/C 1-198 [» ]
    3HWE X-ray 2.80 A/B/C 1-198 [» ]
    3HWF X-ray 3.20 A/B/C 1-198 [» ]
    3HWG X-ray 2.19 A/B/C 1-198 [» ]
    3I0A X-ray 2.60 A/B/C 1-198 [» ]
    3K3L X-ray 2.62 A/B/C 21-198 [» ]
    3PEC X-ray 2.19 A/B/C 21-198 [» ]
    3PED X-ray 2.30 A/B/C 21-198 [» ]
    3T1D X-ray 2.30 A/B/C 1-198 [» ]
    3TF6 X-ray 2.35 A/B/C 21-198 [» ]
    3TZS X-ray 2.45 A/B/C 21-198 [» ]
    3U03 X-ray 2.40 A/C 1-198 [» ]
    3U0D X-ray 2.51 A/B/C/D 1-198 [» ]
    4GH7 X-ray 2.60 A/C 21-198 [» ]
    4IAW X-ray 2.40 A/B/C 21-198 [» ]
    4IAX X-ray 1.90 A 21-198 [» ]
    4K19 X-ray 2.74 A/B/C 21-198 [» ]
    ProteinModelPortali P80188.
    SMRi P80188. Positions 24-197.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110126. 2 interactions.
    DIPi DIP-29952N.
    STRINGi 9606.ENSP00000277480.

    PTM databases

    PhosphoSitei P80188.

    Polymorphism databases

    DMDMi 1171700.

    Proteomic databases

    MaxQBi P80188.
    PaxDbi P80188.
    PRIDEi P80188.

    Protocols and materials databases

    DNASUi 3934.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000277480 ; ENSP00000277480 ; ENSG00000148346 . [P80188-1 ]
    ENST00000373017 ; ENSP00000362108 ; ENSG00000148346 . [P80188-1 ]
    GeneIDi 3934.
    KEGGi hsa:3934.
    UCSCi uc004bto.1. human. [P80188-1 ]
    uc011map.1. human. [P80188-2 ]

    Organism-specific databases

    CTDi 3934.
    GeneCardsi GC09P130911.
    HGNCi HGNC:6526. LCN2.
    HPAi CAB016549.
    CAB016550.
    HPA002695.
    MIMi 600181. gene.
    neXtProti NX_P80188.
    PharmGKBi PA30309.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40148.
    HOVERGENi HBG106490.
    OrthoDBi EOG78M03G.
    PhylomeDBi P80188.
    TreeFami TF336103.

    Miscellaneous databases

    ChiTaRSi LCN2. human.
    EvolutionaryTracei P80188.
    GeneWikii LCN2.
    GenomeRNAii 3934.
    NextBioi 15451.
    PROi P80188.
    SOURCEi Search...

    Gene expression databases

    Bgeei P80188.
    CleanExi HS_LCN2.
    Genevestigatori P80188.

    Family and domain databases

    Gene3Di 2.40.128.20. 1 hit.
    InterProi IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR002345. Lipocalin.
    IPR022272. Lipocalin_CS.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    IPR003087. N_gelatinase.
    [Graphical view ]
    Pfami PF00061. Lipocalin. 1 hit.
    [Graphical view ]
    PRINTSi PR00179. LIPOCALIN.
    PR01275. NGELATINASE.
    SUPFAMi SSF50814. SSF50814. 1 hit.
    PROSITEi PS00213. LIPOCALIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of a cDNA encoding NGAL: a lipocalin expressed in human neutrophils."
      Bundgaard J.R., Sengelov H., Borregaard N., Kjeldsen L.
      Biochem. Biophys. Res. Commun. 202:1468-1475(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Molecular characterization and pattern of tissue expression of the gene for neutrophil gelatinase-associated lipocalin from humans."
      Cowland J.B., Borregaard N.
      Genomics 45:17-23(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
      Tissue: Bone marrow.
    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: Esophagus.
    4. "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).
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      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: Pancreas.
    8. "Cloning and expression of human neutrophil lipocalin cDNA derived from bone marrow and ovarian cancer cells."
      Bartsch S., Tschesche H.
      FEBS Lett. 357:255-259(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-198, PARTIAL PROTEIN SEQUENCE.
    9. "Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase."
      Kjeldsen L., Johnsen A.H., Sengelov H., Borregaard N.
      J. Biol. Chem. 268:10425-10432(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-198, PYROGLUTAMATE FORMATION AT GLN-21.
      Tissue: Neutrophil.
    10. "A 25 kDa alpha 2-microglobulin-related protein is a component of the 125 kDa form of human gelatinase."
      Triebel S., Blaeser J., Reinke H., Tschesche H.
      FEBS Lett. 314:386-388(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 51-61; 71-90; 132-136; 152-160 AND 178-192.
      Tissue: Neutrophil.
    11. Cited for: FUNCTION, IRON-BINDING, SIDEROPHORE-BINDING, SUBCELLULAR LOCATION.
    12. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
      Tissue: Bile.
    13. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
      Tissue: Plasma.
    14. "Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
      Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
      J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
      Tissue: Saliva.
    15. "Transcription and signalling pathways involved in BCR-ABL-mediated misregulation of 24p3 and 24p3R."
      Sheng Z., Wang S.Z., Green M.R.
      EMBO J. 28:866-876(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    16. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
      Tissue: Liver.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Ligand preference inferred from the structure of neutrophil gelatinase associated lipocalin."
      Goetz D.H., Willie S.T., Armen R.S., Bratt T., Borregaard N., Strong R.K.
      Biochemistry 39:1935-1941(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-298.
    19. "The solution structure and dynamics of human neutrophil gelatinase-associated lipocalin."
      Coles M., Diercks T., Muehlenweg B., Bartsch S., Zolzer V., Tschesche H., Kessler H.
      J. Mol. Biol. 289:139-157(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 21-198.
    20. "The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition."
      Goetz D.H., Holmes M.A., Borregaard N., Bluhm M.E., Raymond K.N., Strong R.K.
      Mol. Cell 10:1033-1043(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-198 IN COMPLEX WITH SIDEROPHORE AND IRON, SUBUNIT.

    Entry informationi

    Entry nameiNGAL_HUMAN
    AccessioniPrimary (citable) accession number: P80188
    Secondary accession number(s): A6NII8
    , B4DWV4, B7ZAA2, P30150, Q5SYV9, Q5SYW0, Q6FGL5, Q92683
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 153 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

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

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3