P80188 (NGAL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	LCN2
Synonyms:	HNL, NGAL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	198 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Apoptosis Immunity Innate immunity Ion transport Iron transport Transport
Cellular component	Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal
Ligand	Iron
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cellular response to hydrogen peroxide Inferred from electronic annotation. Source: Compara cellular response to interleukin-1 Inferred from electronic annotation. Source: Compara cellular response to lipopolysaccharide Inferred from electronic annotation. Source: Compara cellular response to nutrient levels Inferred from electronic annotation. Source: Compara cellular response to tumor necrosis factor Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of gene expression Inferred from electronic annotation. Source: Compara protein homotrimerization Inferred from electronic annotation. Source: Compara regulation of apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB response to drug Inferred from electronic annotation. Source: Compara response to herbicide Inferred from electronic annotation. Source: Compara response to virus Inferred from electronic annotation. Source: Compara siderophore transport Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA cytosol Inferred from electronic annotation. Source: Compara extracellular region Inferred from sequence or structural similarity. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: Compara
Molecular_function	iron 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Ref.9

Chain

21 – 198

178

Neutrophil gelatinase-associated lipocalin

PRO_0000017933

Sites

Binding site

126

1

Catecholate-type ferric siderophore

Binding site

145

1

Catecholate-type ferric siderophore

Binding site

154

1

Catecholate-type ferric siderophore

Amino acid modifications

Modified residue

21

1

Pyrrolidone carboxylic acid Ref.9

Glycosylation

85

1

N-linked (GlcNAc...) Ref.9 Ref.12 Ref.13 Ref.14 Ref.16

Disulfide bond

96 ↔ 195

Natural variations

Alternative sequence

193 – 198

6

DQCIDG → GNGQSG in isoform 2.

VSP_039780

Experimental info

Sequence conflict

9

1

G → R in BAG63166. Ref.3

Sequence conflict

13

1

L → S in CAG46889. Ref.4

Sequence conflict

82

1

K → N AA sequence Ref.10

Sequence conflict

155

1

I → V AA sequence Ref.10

Sequence conflict

178

1

S → Y in CAA67574. Ref.2

Secondary structure

1

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198

Helix Strand Turn

Details...

Helix

33 – 35

3

Helix

44 – 47

4

Beta strand

49 – 60

12

Beta strand

65 – 67

3

Beta strand

73 – 78

6

Turn

80 – 82

3

Beta strand

84 – 92

9

Beta strand

95 – 105

11

Beta strand

111 – 114

4

Helix

117 – 119

3

Beta strand

123 – 133

11

Beta strand

135 – 147

13

Beta strand

150 – 162

13

Helix

166 – 178

13

Helix

183 – 185

3

Turn

194 – 197

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: CD761805723FEF1E	FASTA	198	22,588
	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
	Isoform 2 [UniParc]. Checksum: CD691E83A0AD3F1E	FASTA	198	22,457
	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 PIGNGQSG

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.

IPI

IPI00299547.
IPI01013763.

PIR

JC2339.

RefSeq

NP_005555.2. NM_005564.3.

UniGene

Hs.204238.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P80188.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29952N.

STRING

9606.ENSP00000277480.

PTM databases

PhosphoSite

P80188.

Polymorphism databases

DMDM

1171700.

Proteomic databases

PaxDb

P80188.

PRIDE

P80188.

Protocols and materials databases

DNASU

3934.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000277480; ENSP00000277480; ENSG00000148346.
ENST00000372998; ENSP00000362089; ENSG00000148346.
ENST00000373017; ENSP00000362108; ENSG00000148346.
ENST00000540948; ENSP00000441666; ENSG00000148346.

GeneID

3934.

KEGG

hsa:3934.

UCSC

uc004bto.1. human.
uc011map.1. human.

Organism-specific databases

CTD

3934.

GeneCards

GC09P130911.

HGNC

HGNC:6526. LCN2.

HPA

CAB016549.
CAB016550.
HPA002695.

MIM

600181. gene.

neXtProt

NX_P80188.

PharmGKB

PA30309.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG40148.

HOVERGEN

HBG106490.

OrthoDB

EOG447FVG.

Gene expression databases

ArrayExpress

P80188.

Bgee

P80188.

CleanEx

HS_LCN2.

Genevestigator

P80188.

GermOnline

ENSG00000148346. Homo sapiens.

Family and domain databases

Gene3D

2.40.128.20. 1 hit.

InterPro

IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR003087. N_gelatinase.
[Graphical view]

Pfam

PF00061. Lipocalin. 1 hit.
[Graphical view]

PRINTS

PR00179. LIPOCALIN.
PR01275. NGELATINASE.

SUPFAM

SSF50814. Calycin. 1 hit.

PROSITE

PS00213. LIPOCALIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1741308.

ChiTaRS

LCN2. human.

EvolutionaryTrace

P80188.

GenomeRNAi

3934.

NextBio

15451.

SOURCE

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Entry information

Entry name

NGAL_HUMAN

Accession

Primary (citable) accession number: P80188
Secondary accession number(s): A6NII8 , 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:	May 1, 2013
This is version 142 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.