Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P80188 (NGAL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:LCN2
Synonyms:HNL, NGAL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11

Subunit structure

Homodimer; disulfide-linked. Heterodimer; disulfide-linked with MMP9. Ref.20

Subcellular location

Secreted. Note: Upon binding to the SLC22A17 (24p3R) receptor, it is internalized. Ref.11

Tissue specificity

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. Ref.2

Induction

Expression is activated by the oncoprotein BCR-ABL; BCR-ABL misregulates expression via the JAK/STAT pathway and binding of STAT5A to the promoter. Ref.15

Sequence similarities

Belongs to the calycin superfamily. Lipocalin family.

Sequence caution

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

Ontologies

Keywords
   Biological processApoptosis
Immunity
Innate immunity
Ion transport
Iron transport
Transport
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   LigandIron
   PTMDisulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

cellular response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

cellular response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

cellular response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

cellular response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

innate immune response

Inferred from sequence or structural similarity. Source: UniProtKB

ion transport

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell projection organization

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

protein homotrimerization

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to herbicide

Inferred from electronic annotation. Source: Ensembl

response to virus

Inferred from electronic annotation. Source: Ensembl

siderophore transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

extracellular region

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

   Molecular_functioniron ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

small molecule binding

Inferred from electronic annotation. Source: InterPro

transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P80188-1)

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.
Isoform 2 (identifier: P80188-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.9
Chain21 – 198178Neutrophil gelatinase-associated lipocalin
PRO_0000017933

Sites

Binding site1261Catecholate-type ferric siderophore
Binding site1451Catecholate-type ferric siderophore
Binding site1541Catecholate-type ferric siderophore

Amino acid modifications

Modified residue211Pyrrolidone carboxylic acid Ref.9
Glycosylation851N-linked (GlcNAc...) Ref.9 Ref.12 Ref.13 Ref.14 Ref.16
Disulfide bond96 ↔ 195

Natural variations

Alternative sequence193 – 1986DQCIDG → GNGQSG in isoform 2.
VSP_039780

Experimental info

Sequence conflict91G → R in BAG63166. Ref.3
Sequence conflict131L → S in CAG46889. Ref.4
Sequence conflict821K → N AA sequence Ref.10
Sequence conflict1551I → V AA sequence Ref.10
Sequence conflict1781S → Y in CAA67574. Ref.2

Secondary structure

................................. 198
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: CD761805723FEF1E

FASTA19822,588
        10         20         30         40         50         60 
MPLGLLWLGL ALLGALHAQA QDSTSDLIPA PPLSKVPLQQ NFQDNQFQGK WYVVGLAGNA 

        70         80         90        100        110        120 
ILREDKDPQK MYATIYELKE DKSYNVTSVL FRKKKCDYWI RTFVPGCQPG EFTLGNIKSY 

       130        140        150        160        170        180 
PGLTSYLVRV VSTNYNQHAM VFFKKVSQNR EYFKITLYGR TKELTSELKE NFIRFSKSLG 

       190 
LPENHIVFPV PIDQCIDG 

« Hide

Isoform 2 [UniParc].

Checksum: CD691E83A0AD3F1E
Show »

FASTA19822,457

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"An iron delivery pathway mediated by a lipocalin."
Yang J., Goetz D., Li J.Y., Wang W., Mori K., Setlik D., Du T., Erdjument-Bromage H., Tempst P., Strong R., Barasch J.
Mol. Cell 10:1045-1056(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IRON-BINDING, SIDEROPHORE-BINDING, SUBCELLULAR LOCATION.
[12]"A proteomic analysis of human bile."
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.
Mol. Cell. Proteomics 3:715-728(2004) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC2339.
RefSeqNP_005555.2. NM_005564.3.
UniGeneHs.204238.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP80188.
SMRP80188. Positions 24-197.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110126. 2 interactions.
DIPDIP-29952N.
STRING9606.ENSP00000277480.

PTM databases

PhosphoSiteP80188.

Polymorphism databases

DMDM1171700.

Proteomic databases

PaxDbP80188.
PRIDEP80188.

Protocols and materials databases

DNASU3934.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000277480; ENSP00000277480; ENSG00000148346. [P80188-1]
ENST00000373017; ENSP00000362108; ENSG00000148346. [P80188-1]
ENST00000540948; ENSP00000441666; ENSG00000148346. [P80188-2]
GeneID3934.
KEGGhsa:3934.
UCSCuc004bto.1. human. [P80188-1]
uc011map.1. human. [P80188-2]

Organism-specific databases

CTD3934.
GeneCardsGC09P130911.
HGNCHGNC:6526. LCN2.
HPACAB016549.
CAB016550.
HPA002695.
MIM600181. gene.
neXtProtNX_P80188.
PharmGKBPA30309.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40148.
HOVERGENHBG106490.
OrthoDBEOG78M03G.
PhylomeDBP80188.
TreeFamTF336103.

Gene expression databases

BgeeP80188.
CleanExHS_LCN2.
GenevestigatorP80188.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR003087. N_gelatinase.
[Graphical view]
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR00179. LIPOCALIN.
PR01275. NGELATINASE.
SUPFAMSSF50814. SSF50814. 1 hit.
PROSITEPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLCN2. human.
EvolutionaryTraceP80188.
GeneWikiLCN2.
GenomeRNAi3934.
NextBio15451.
PROP80188.
SOURCESearch...

Entry information

Entry nameNGAL_HUMAN
AccessionPrimary (citable) accession number: P80188
Secondary accession number(s): A6NII8 expand/collapse secondary AC list , B4DWV4, B7ZAA2, P30150, Q5SYV9, Q5SYW0, Q6FGL5, Q92683
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM