P61626 (LYSC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lysozyme C
EC=3.2.1.17

Alternative name(s):
1,4-beta-N-acetylmuramidase C

Gene names

Name:	LYZ
Synonyms:	LZM

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	148 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	Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
Catalytic activity	Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Subunit structure	Monomer.
Subcellular location	Secreted.
Involvement in disease	Amyloidosis 8 (AMYL8) [MIM:105200]: A hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20
Miscellaneous	Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides.
Sequence similarities	Belongs to the glycosyl hydrolase 22 family.
Sequence caution	The sequence CAA32175.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Amyloid Secreted
Coding sequence diversity	Polymorphism
Disease	Amyloidosis Disease mutation
Domain	Signal
Molecular function	Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW inflammatory response Traceable author statement PubMed 366724. Source: UniProtKB
Cellular_component	extracellular space Traceable author statement Ref.3. Source: UniProtKB
Molecular_function	lysozyme activity Traceable author statement Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Ref.7 Ref.8 Ref.9 Ref.10

Chain

19 – 148

130

Lysozyme C

PRO_0000018467

Sites

Active site

53

1

Active site

71

1

Amino acid modifications

Disulfide bond

24 ↔ 146

Disulfide bond

48 ↔ 134

Disulfide bond

83 ↔ 99

Disulfide bond

95 ↔ 113

Natural variations

Natural variant

74

1

I → T in AMYL8. Ref.20

VAR_004280

Natural variant

85

1

D → H in AMYL8. Ref.20

VAR_004281

Natural variant

88

1

T → N.
Corresponds to variant rs1800973 [ dbSNP | Ensembl ].

VAR_012050

Experimental info

Sequence conflict

10

1

V → A in AAC63078. Ref.5

Sequence conflict

41

1

I → M in AAA36188. Ref.1

Sequence conflict

111

1

V → A in AAC63078. Ref.5

Sequence conflict

124

1

I → V in AAC63078. Ref.5

Sequence conflict

128

1

V → A in AAC63078. Ref.5

Sequence conflict

136

1

N → D in AAC63078. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

148

Helix Strand Turn

Details...

Helix

23 – 32

10

Helix

38 – 40

3

Helix

43 – 54

12

Beta strand

55 – 57

3

Beta strand

61 – 63

3

Turn

65 – 67

3

Beta strand

70 – 72

3

Turn

73 – 76

4

Turn

79 – 81

3

Beta strand

82 – 84

3

Beta strand

88 – 90

3

Helix

99 – 103

5

Beta strand

104 – 106

3

Helix

108 – 119

12

Beta strand

120 – 122

3

Helix

123 – 126

4

Helix

128 – 133

6

Turn

134 – 136

3

Helix

140 – 142

3

Turn

143 – 145

3

Sequences

	Sequence		Length	Mass (Da)
	P61626 [UniParc]. Last modified June 7, 2004. Version 1. Checksum: 8ECFD276BEB2678A	FASTA	148	16,537
	10 20 30 40 50 60 MKALIVLGLV LLSVTVQGKV FERCELARTL KRLGMDGYRG ISLANWMCLA KWESGYNTRA 70 80 90 100 110 120 TNYNAGDRST DYGIFQINSR YWCNDGKTPG AVNACHLSCS ALLQDNIADA VACAKRVVRD 130 140 PQGIRAWVAW RNRCQNRDVR QYVQGCGV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of human lysozyme gene and expression in the yeast Saccharomyces cerevisiae." Castanon M.J., Spevak W., Adolf G.R., Chlebowicz-Sledziewska E., Sledziewski A. Gene 66:223-234(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning the human lysozyme cDNA: inverted Alu repeat in the mRNA and in situ hybridization for macrophages and Paneth cells." Chung L.P., Keshav S., Gordon S. Proc. Natl. Acad. Sci. U.S.A. 85:6227-6231(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Human lysozyme: sequencing of a cDNA, and expression and secretion by Saccharomyces cerevisiae." Yoshimura K., Toibana A., Nakahama K. Biochem. Biophys. Res. Commun. 150:794-801(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"The human lysozyme gene. Sequence organization and chromosomal localization." Peters C.W.B., Kruse U., Pollwein R., Grzeschik K.H., Sippel A.E. Eur. J. Biochem. 182:507-516(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The cloning, sequencing and analysis of Chinese human lysozyme gene cDNA amplified with RT-PCR from human placental total RNA." Huang B., Zhao C., Lei X., Cai L. Sheng Wu Hua Hsueh Tsa Chih 9:269-273(1993) Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"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]. Tissue: Colon.
[7]	"Primary structure of lysozymes from man and goose." Canfield R.E., Kammerman S., Sobel H.H., Morgan F.J. Nature New Biol. 232:16-17(1971) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-148. Tissue: Urine.
[8]	"A Val-Val sequence found in a human monocytic leukemia lysozyme." Thomsen J., Lund E.H., Kristiansen K., Brunfeldt K., Malmquist J. FEBS Lett. 22:34-36(1972) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-148, SEQUENCE REVISION TO 118. Tissue: Urine.
[9]	"Human milk lysozyme: unpublished data concerning the establishment of the complete primary structure; comparison with lysozymes of various origins." Jolles J., Jolles P. Helv. Chim. Acta 54:2668-2675(1971) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-148. Tissue: Milk.
[10]	"Comparison between human and bird lysozymes: note concerning the previously observed deletion." Jolles J., Jolles P. FEBS Lett. 22:31-33(1972) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-148, SEQUENCE REVISION TO 118. Tissue: Milk.
[11]	"Indication of possible post-translational formation of disulphide bonds in the beta-sheet domain of human lysozyme." Kanaya E., Ishihara K., Tsunasawa S., Nokihara K., Kikuchi M. Biochem. J. 292:469-476(1993) [PubMed] [Europe PMC] [Abstract] Cited for: FOLDING, MUTAGENESIS.
[12]	"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].
[13]	"The high resolution X-ray study of human. lysozyme: a preliminary analysis." Banyard S.H., Blake C.C.F., Swan I.D.A. (In) Osserman E.F., Canfield R.E., Beychok S. (eds.); Lysozyme, pp.71-79, Academic Press, New York (1974) Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[14]	"Refinement of human lysozyme at 1.5-A resolution analysis of non-bonded and hydrogen-bond interactions." Artymiuk P.J., Blake C.C.F. J. Mol. Biol. 152:737-762(1981) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[15]	"X-ray studies of water in crystals of lysozyme." Blake C.C.F., Pulford W.C.A., Artymiuk P.J. J. Mol. Biol. 167:693-723(1983) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[16]	"The crystal structure of a mutant human lysozyme C77/95A with increased secretion efficiency in yeast." Inaka K., Taniyama Y., Kikuchi M., Morikawa K., Matsushima M. J. Biol. Chem. 266:12599-12603(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ALA-99 AND ALA-113.
[17]	"Structures of monoclinic lysozyme iodide at 1.6 A and of triclinic lysozyme nitrate at 1.1 A." Steinrauf L.K. Acta Crystallogr. D 54:767-780(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 AND 1.1 ANGSTROMS).
[18]	"1H NMR studies of human lysozyme: spectral assignment and comparison with hen lysozyme." Redfield C., Dobson C.M. Biochemistry 29:7201-7214(1990) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[19]	"1H and 15N NMR study of human lysozyme." Ohkubo T., Taniyama Y., Kikuchi M. J. Biochem. 110:1022-1029(1991) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[20]	"Human lysozyme gene mutations cause hereditary systemic amyloidosis." Pepy M.B., Hawkins P.N., Booth D.R., Vigushin D.M., Tennent G.A., Soutar A.K., Totty N., Nguyen O., Blake C.C.F., Terry C.J., Feest T.G., Zalin A.M., Hsuan J.J. Nature 362:553-557(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AMYL8 THR-74 AND HIS-85.
+	Additional computationally mapped references.

Web resources

GeneReviews

Wikipedia

Lysozyme entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M21119 mRNA. Translation: AAA36188.1.
J03801 mRNA. Translation: AAA59535.1.
M19045 mRNA. Translation: AAA59536.1.
X14008 Genomic DNA. Translation: CAA32175.1. Different initiation.
U25677 mRNA. Translation: AAC63078.1.
BC004147 mRNA. Translation: AAH04147.1.

IPI

IPI00019038.

PIR

LZHU. S04938.

RefSeq

NP_000230.1. NM_000239.2.

UniGene

Hs.524579.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
133L	X-ray	1.77	A	19-148	[»]
134L	X-ray	1.77	A	19-148	[»]
1B5U	X-ray	1.80	A	19-148	[»]
1B5V	X-ray	2.17	A	19-148	[»]
1B5W	X-ray	2.17	A	19-148	[»]
1B5X	X-ray	2.00	A	19-148	[»]
1B5Y	X-ray	2.20	A	19-148	[»]
1B5Z	X-ray	2.20	A/B	19-148	[»]
1B7L	X-ray	1.80	A	19-148	[»]
1B7M	X-ray	2.20	A	19-148	[»]
1B7N	X-ray	1.80	A	19-148	[»]
1B7O	X-ray	1.80	A	19-148	[»]
1B7P	X-ray	2.00	A	19-148	[»]
1B7Q	X-ray	2.00	A	19-148	[»]
1B7R	X-ray	1.80	A	19-148	[»]
1B7S	X-ray	2.00	A	19-148	[»]
1BB3	X-ray	1.80	A/B	19-148	[»]
1BB4	X-ray	2.23	A/B	19-148	[»]
1BB5	X-ray	1.80	A/B	19-148	[»]
1C43	X-ray	1.80	A	20-148	[»]
1C45	X-ray	1.80	A	20-148	[»]
1C46	X-ray	2.20	A	18-148	[»]
1C7P	X-ray	2.40	A	19-148	[»]
1CJ6	X-ray	1.80	A	19-148	[»]
1CJ7	X-ray	1.80	A	19-148	[»]
1CJ8	X-ray	1.80	A	19-148	[»]
1CJ9	X-ray	1.80	A	19-148	[»]
1CKC	X-ray	1.80	A	19-148	[»]
1CKD	X-ray	1.80	A	19-148	[»]
1CKF	X-ray	1.80	A	19-148	[»]
1CKG	X-ray	2.20	A/B	19-148	[»]
1CKH	X-ray	2.00	A	19-148	[»]
1D6P	X-ray	2.23	A	19-148	[»]
1D6Q	X-ray	1.96	A	19-148	[»]
1DI3	X-ray	1.80	A	19-148	[»]
1DI4	X-ray	2.00	A	19-148	[»]
1DI5	X-ray	2.20	A	19-148	[»]
1EQ4	X-ray	1.80	A	19-148	[»]
1EQ5	X-ray	1.80	A	19-148	[»]
1EQE	X-ray	1.80	A	19-148	[»]
1GAY	X-ray	1.80	A	21-148	[»]
1GAZ	X-ray	1.80	A	21-148	[»]
1GB0	X-ray	1.80	A	21-148	[»]
1GB2	X-ray	1.80	A	21-148	[»]
1GB3	X-ray	1.80	A	21-148	[»]
1GB5	X-ray	1.80	A	19-148	[»]
1GB6	X-ray	1.80	A	19-148	[»]
1GB7	X-ray	1.80	A	19-148	[»]
1GB8	X-ray	1.80	A	19-148	[»]
1GB9	X-ray	1.80	A	19-148	[»]
1GBO	X-ray	1.80	A	19-148	[»]
1GBW	X-ray	1.80	A	19-148	[»]
1GBX	X-ray	1.80	A	19-148	[»]
1GBY	X-ray	1.80	A	19-148	[»]
1GBZ	X-ray	1.80	A	19-148	[»]
1GDW	X-ray	1.80	A	19-148	[»]
1GDX	X-ray	1.80	A	19-148	[»]
1GE0	X-ray	1.80	A	19-148	[»]
1GE1	X-ray	1.70	A	19-148	[»]
1GE2	X-ray	2.00	A	19-148	[»]
1GE3	X-ray	1.80	A	19-148	[»]
1GE4	X-ray	1.80	A	19-148	[»]
1GEV	X-ray	2.10	A	19-148	[»]
1GEZ	X-ray	1.80	A	19-148	[»]
1GF0	X-ray	1.80	A	19-148	[»]
1GF3	X-ray	1.80	A	19-148	[»]
1GF4	X-ray	1.80	A	19-148	[»]
1GF5	X-ray	1.80	A	19-148	[»]
1GF6	X-ray	1.80	A	19-148	[»]
1GF7	X-ray	1.80	A	19-148	[»]
1GF8	X-ray	1.80	A	21-148	[»]
1GF9	X-ray	1.80	A	21-148	[»]
1GFA	X-ray	1.80	A	21-148	[»]
1GFE	X-ray	1.80	A	21-148	[»]
1GFG	X-ray	1.80	A	21-148	[»]
1GFH	X-ray	1.80	A	19-148	[»]
1GFJ	X-ray	1.80	A	19-148	[»]
1GFK	X-ray	1.80	A	19-148	[»]
1GFR	X-ray	1.80	A	19-148	[»]
1GFT	X-ray	1.80	A	19-148	[»]
1GFU	X-ray	1.80	A	19-148	[»]
1GFV	X-ray	1.80	A	19-148	[»]
1HNL	X-ray	1.80	A	19-148	[»]
1I1Z	X-ray	1.80	A	19-148	[»]
1I20	X-ray	1.90	A	19-148	[»]
1I22	X-ray	1.80	A/B/C/D	19-148	[»]
1INU	X-ray	1.80	A	19-148	[»]
1IOC	X-ray	2.40	A	19-148	[»]
1IP1	X-ray	1.80	A	19-148	[»]
1IP2	X-ray	1.80	A	19-148	[»]
1IP3	X-ray	1.80	A/B	19-148	[»]
1IP4	X-ray	1.80	A	19-148	[»]
1IP5	X-ray	1.80	A	19-148	[»]
1IP6	X-ray	1.80	A	19-148	[»]
1IP7	X-ray	1.90	A/B	19-146	[»]
1IWT	X-ray	1.40	A	19-148	[»]
1IWU	X-ray	1.40	A	19-148	[»]
1IWV	X-ray	1.40	A	19-148	[»]
1IWW	X-ray	1.40	A	19-148	[»]
1IWX	X-ray	1.40	A	19-148	[»]
1IWY	X-ray	1.40	A	19-148	[»]
1IWZ	X-ray	1.48	A	19-148	[»]
1IX0	X-ray	1.80	A	19-148	[»]
1IY3	NMR	-	A	19-148	[»]
1IY4	NMR	-	A	19-148	[»]
1JKA	X-ray	1.66	A	19-148	[»]
1JKB	X-ray	1.66	A	19-148	[»]
1JKC	X-ray	1.60	A	19-148	[»]
1JKD	X-ray	1.80	A	19-148	[»]
1JSF	X-ray	1.15	A	19-148	[»]
1JWR	X-ray	1.40	A	19-148	[»]
1LAA	X-ray	1.77	A	19-148	[»]
1LHH	X-ray	1.80	A	19-148	[»]
1LHI	X-ray	1.80	A	19-148	[»]
1LHJ	X-ray	1.80	A	19-148	[»]
1LHK	X-ray	1.80	A	19-148	[»]
1LHL	X-ray	1.80	A	19-148	[»]
1LHM	X-ray	1.80	A	19-148	[»]
1LMT	X-ray	1.60	A	19-148	[»]
1LOZ	X-ray	1.80	A	19-148	[»]
1LYY	X-ray	1.80	A	19-148	[»]
1LZ1	X-ray	1.50	A	19-148	[»]
1LZ4	X-ray	1.80	A	19-148	[»]
1LZ5	X-ray	1.80	A	19-144	[»]
1LZ6	X-ray	1.80	A	19-148	[»]
1LZR	X-ray	1.50	A	19-148	[»]
1LZS	X-ray	1.60	A/B	19-148	[»]
1OP9	X-ray	1.86	B	19-148	[»]
1OUA	X-ray	1.80	A	19-148	[»]
1OUB	X-ray	1.80	A	19-148	[»]
1OUC	X-ray	1.80	A	19-148	[»]
1OUD	X-ray	1.80	A	19-148	[»]
1OUE	X-ray	1.80	A	19-148	[»]
1OUF	X-ray	1.80	A	19-147	[»]
1OUG	X-ray	1.80	A	21-148	[»]
1OUH	X-ray	1.80	A	19-148	[»]
1OUI	X-ray	1.80	A	19-148	[»]
1OUJ	X-ray	1.80	A	19-148	[»]
1QSW	X-ray	1.85	A/B/C/D	19-148	[»]
1RE2	X-ray	2.30	A	19-148	[»]
1REM	X-ray	2.10	A	19-148	[»]
1REX	X-ray	1.50	A	19-148	[»]
1REY	X-ray	1.70	A	19-148	[»]
1REZ	X-ray	1.70	A	19-148	[»]
1TAY	X-ray	1.70	A	19-148	[»]
1TBY	X-ray	1.77	A	19-148	[»]
1TCY	X-ray	1.70	A	19-148	[»]
1TDY	X-ray	1.70	A	19-148	[»]
1UBZ	X-ray	2.00	A	19-148	[»]
1W08	X-ray	2.50	A	19-148	[»]
1WQM	X-ray	1.80	A	19-148	[»]
1WQN	X-ray	1.80	A	19-148	[»]
1WQO	X-ray	1.80	A	19-148	[»]
1WQP	X-ray	1.80	A	19-148	[»]
1WQQ	X-ray	1.80	A	19-148	[»]
1WQR	X-ray	1.80	A	19-148	[»]
1YAM	X-ray	1.80	A	19-148	[»]
1YAN	X-ray	1.80	A	19-148	[»]
1YAO	X-ray	1.80	A	19-148	[»]
1YAP	X-ray	1.80	A	19-148	[»]
1YAQ	X-ray	1.80	A	19-148	[»]
207L	X-ray	1.80	A	19-148	[»]
208L	X-ray	2.20	A	19-148	[»]
2BQA	X-ray	1.80	A	19-148	[»]
2BQB	X-ray	1.80	A	19-148	[»]
2BQC	X-ray	1.80	A	19-148	[»]
2BQD	X-ray	1.80	A	19-148	[»]
2BQE	X-ray	1.80	A	19-148	[»]
2BQF	X-ray	1.80	A	19-148	[»]
2BQG	X-ray	1.80	A	19-148	[»]
2BQH	X-ray	1.80	A	19-148	[»]
2BQI	X-ray	1.80	A	19-148	[»]
2BQJ	X-ray	1.80	A	19-148	[»]
2BQK	X-ray	1.80	A	19-147	[»]
2BQL	X-ray	1.80	A	21-148	[»]
2BQM	X-ray	1.80	A	19-148	[»]
2BQN	X-ray	1.80	A	19-148	[»]
2BQO	X-ray	1.80	A	19-148	[»]
2HEA	X-ray	1.80	A	19-148	[»]
2HEB	X-ray	2.20	A	19-148	[»]
2HEC	X-ray	1.80	A	19-148	[»]
2HED	X-ray	1.80	A	19-148	[»]
2HEE	X-ray	1.80	A	19-148	[»]
2HEF	X-ray	1.80	A	19-148	[»]
2LHM	X-ray	1.80	A	19-148	[»]
2MEA	X-ray	2.20	A/B	19-148	[»]
2MEB	X-ray	1.80	A	19-148	[»]
2MEC	X-ray	2.20	A/B	19-148	[»]
2MED	X-ray	1.80	A	19-148	[»]
2MEE	X-ray	1.80	A	19-148	[»]
2MEF	X-ray	1.80	A	19-148	[»]
2MEG	X-ray	1.80	A	19-148	[»]
2MEH	X-ray	1.80	A	19-148	[»]
2MEI	X-ray	1.80	A	19-148	[»]
2NWD	X-ray	1.04	X	19-148	[»]
2ZIJ	X-ray	1.90	A	19-148	[»]
2ZIK	X-ray	1.81	A	19-148	[»]
2ZIL	X-ray	1.80	A	19-148	[»]
2ZWB	neutron diffraction	1.80	A	19-148	[»]
3EBA	X-ray	1.85	B	19-148	[»]
3FE0	X-ray	1.50	A	19-148	[»]
3LHM	X-ray	1.80	A	19-148	[»]
3LN2	X-ray	2.04	A/B	19-148	[»]

ProteinModelPortal

P61626.

ModBase

Search...

Protein-protein interaction databases

IntAct

P61626. 6 interactions.

MINT

MINT-5002660.

STRING

9606.ENSP00000261267.

Protein family/group databases

CAZy

GH22. Glycoside Hydrolase Family 22.

PTM databases

PhosphoSite

P61626.

Polymorphism databases

DMDM

48428995.

2D gel databases

UCD-2DPAGE

P61626.

Proteomic databases

PaxDb

P61626.

PeptideAtlas

P61626.

PRIDE

P61626.

Protocols and materials databases

DNASU

4069.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261267; ENSP00000261267; ENSG00000090382.

GeneID

4069.

KEGG

hsa:4069.

UCSC

uc001suw.2. human.

Organism-specific databases

CTD

4069.

GeneCards

GC12P069681.

HGNC

HGNC:6740. LYZ.

HPA

CAB000055.

MIM

105200. phenotype.
153450. gene.

neXtProt

NX_P61626.

Orphanet

93561. Familial renal amyloidosis due to lysozyme variant.

PharmGKB

PA30503.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG85133.

HOGENOM

HOG000037357.

HOVERGEN

HBG052297.

InParanoid

P61626.

KO

K13915.

OMA

CNALLQD.

OrthoDB

EOG48KRCP.

PhylomeDB

P61626.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.

Gene expression databases

ArrayExpress

P61626.

Bgee

P61626.

CleanEx

HS_LYZ.

Genevestigator

P61626.

GermOnline

ENSG00000090382. Homo sapiens.

Family and domain databases

InterPro

IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]

Pfam

PF00062. Lys. 1 hit.
[Graphical view]

PRINTS

PR00137. LYSOZYME.
PR00135. LYZLACT.

SMART

SM00263. LYZ1. 1 hit.
[Graphical view]

SUPFAM

SSF53955. SSF53955. 1 hit.

PROSITE

PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

LYZ. human.

EvolutionaryTrace

P61626.

GenomeRNAi

4069.

NextBio

15952.

SOURCE

Search...

Entry information

Entry name

LYSC_HUMAN

Accession

Primary (citable) accession number: P61626
Secondary accession number(s): P00695, Q13170, Q9UCF8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	June 7, 2004
Last modified:	May 1, 2013
This is version 113 of the entry and version 1 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.