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P61626

- LYSC_HUMAN

UniProt

P61626 - LYSC_HUMAN

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Protein

Lysozyme C

Gene

LYZ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei53 – 531
Active sitei71 – 711

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. lysozyme activity Source: UniProtKB

GO - Biological processi

  1. cell wall macromolecule catabolic process Source: InterPro
  2. cytolysis Source: UniProtKB-KW
  3. defense response to bacterium Source: UniProtKB-KW
  4. inflammatory response Source: UniProtKB
  5. retina homeostasis Source: UniProt
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Enzyme and pathway databases

ReactomeiREACT_75925. Amyloids.

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Gene namesi
Name:LYZ
Synonyms:LZM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:6740. LYZ.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Amyloid, Secreted

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti74 – 741I → T in AMYL8. 1 Publication
VAR_004280
Natural varianti85 – 851D → H in AMYL8. 1 Publication
VAR_004281

Keywords - Diseasei

Amyloidosis, Disease mutation

Organism-specific databases

MIMi105200. phenotype.
Orphaneti93561. Familial renal amyloidosis due to lysozyme variant.
PharmGKBiPA30503.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18184 PublicationsAdd
BLAST
Chaini19 – 148130Lysozyme CPRO_0000018467Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 146
Disulfide bondi48 ↔ 134
Disulfide bondi83 ↔ 99
Disulfide bondi95 ↔ 113

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP61626.
PaxDbiP61626.
PeptideAtlasiP61626.
PRIDEiP61626.

2D gel databases

UCD-2DPAGEP61626.

PTM databases

PhosphoSiteiP61626.

Expressioni

Gene expression databases

BgeeiP61626.
CleanExiHS_LYZ.
ExpressionAtlasiP61626. baseline and differential.
GenevestigatoriP61626.

Organism-specific databases

HPAiCAB000055.
HPA048284.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-355360,EBI-355360

Protein-protein interaction databases

BioGridi110247. 19 interactions.
IntActiP61626. 7 interactions.
MINTiMINT-5002660.
STRINGi9606.ENSP00000261267.

Structurei

Secondary structure

1
148
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 3210Combined sources
Helixi38 – 403Combined sources
Helixi43 – 5412Combined sources
Beta strandi55 – 573Combined sources
Beta strandi61 – 633Combined sources
Turni65 – 673Combined sources
Beta strandi70 – 723Combined sources
Turni73 – 764Combined sources
Turni79 – 813Combined sources
Beta strandi82 – 843Combined sources
Beta strandi88 – 903Combined sources
Helixi99 – 1035Combined sources
Beta strandi104 – 1063Combined sources
Helixi108 – 11912Combined sources
Beta strandi120 – 1223Combined sources
Helixi123 – 1264Combined sources
Helixi128 – 1336Combined sources
Turni134 – 1363Combined sources
Helixi140 – 1423Combined sources
Turni143 – 1453Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
133LX-ray1.77A19-148[»]
134LX-ray1.77A19-148[»]
1B5UX-ray1.80A19-148[»]
1B5VX-ray2.17A19-148[»]
1B5WX-ray2.17A19-148[»]
1B5XX-ray2.00A19-148[»]
1B5YX-ray2.20A19-148[»]
1B5ZX-ray2.20A/B19-148[»]
1B7LX-ray1.80A19-148[»]
1B7MX-ray2.20A19-148[»]
1B7NX-ray1.80A19-148[»]
1B7OX-ray1.80A19-148[»]
1B7PX-ray2.00A19-148[»]
1B7QX-ray2.00A19-148[»]
1B7RX-ray1.80A19-148[»]
1B7SX-ray2.00A19-148[»]
1BB3X-ray1.80A/B19-148[»]
1BB4X-ray2.23A/B19-148[»]
1BB5X-ray1.80A/B19-148[»]
1C43X-ray1.80A19-148[»]
1C45X-ray1.80A19-148[»]
1C46X-ray2.20A19-148[»]
1C7PX-ray2.40A16-148[»]
1CJ6X-ray1.80A19-148[»]
1CJ7X-ray1.80A19-148[»]
1CJ8X-ray1.80A19-148[»]
1CJ9X-ray1.80A19-148[»]
1CKCX-ray1.80A19-148[»]
1CKDX-ray1.80A19-148[»]
1CKFX-ray1.80A19-148[»]
1CKGX-ray2.20A/B19-148[»]
1CKHX-ray2.00A19-148[»]
1D6PX-ray2.23A19-148[»]
1D6QX-ray1.96A19-148[»]
1DI3X-ray1.80A19-148[»]
1DI4X-ray2.00A19-148[»]
1DI5X-ray2.20A19-148[»]
1EQ4X-ray1.80A19-148[»]
1EQ5X-ray1.80A19-148[»]
1EQEX-ray1.80A19-148[»]
1GAYX-ray1.80A19-148[»]
1GAZX-ray1.80A19-148[»]
1GB0X-ray1.80A19-148[»]
1GB2X-ray1.80A19-148[»]
1GB3X-ray1.80A19-148[»]
1GB5X-ray1.80A19-148[»]
1GB6X-ray1.80A19-148[»]
1GB7X-ray1.80A19-148[»]
1GB8X-ray1.80A19-148[»]
1GB9X-ray1.80A19-148[»]
1GBOX-ray1.80A19-148[»]
1GBWX-ray1.80A19-148[»]
1GBXX-ray1.80A19-148[»]
1GBYX-ray1.80A19-148[»]
1GBZX-ray1.80A19-148[»]
1GDWX-ray1.80A19-148[»]
1GDXX-ray1.80A19-148[»]
1GE0X-ray1.80A19-148[»]
1GE1X-ray1.70A19-148[»]
1GE2X-ray2.00A19-148[»]
1GE3X-ray1.80A19-148[»]
1GE4X-ray1.80A19-148[»]
1GEVX-ray2.10A19-148[»]
1GEZX-ray1.80A19-148[»]
1GF0X-ray1.80A19-148[»]
1GF3X-ray1.80A19-148[»]
1GF4X-ray1.80A19-148[»]
1GF5X-ray1.80A19-148[»]
1GF6X-ray1.80A19-148[»]
1GF7X-ray1.80A19-148[»]
1GF8X-ray1.80A19-148[»]
1GF9X-ray1.80A19-148[»]
1GFAX-ray1.80A19-148[»]
1GFEX-ray1.80A19-148[»]
1GFGX-ray1.80A19-148[»]
1GFHX-ray1.80A19-148[»]
1GFJX-ray1.80A19-148[»]
1GFKX-ray1.80A19-148[»]
1GFRX-ray1.80A19-148[»]
1GFTX-ray1.80A19-148[»]
1GFUX-ray1.80A19-148[»]
1GFVX-ray1.80A19-148[»]
1HNLX-ray1.80A19-148[»]
1I1ZX-ray1.80A19-148[»]
1I20X-ray1.90A19-148[»]
1I22X-ray1.80A/B/C/D19-148[»]
1INUX-ray1.80A19-148[»]
1IOCX-ray2.40A19-148[»]
1IP1X-ray1.80A19-148[»]
1IP2X-ray1.80A19-148[»]
1IP3X-ray1.80A/B19-148[»]
1IP4X-ray1.80A19-148[»]
1IP5X-ray1.80A19-148[»]
1IP6X-ray1.80A19-148[»]
1IP7X-ray1.90A/B19-146[»]
1IWTX-ray1.40A19-148[»]
1IWUX-ray1.40A19-148[»]
1IWVX-ray1.40A19-148[»]
1IWWX-ray1.40A19-148[»]
1IWXX-ray1.40A19-148[»]
1IWYX-ray1.40A19-148[»]
1IWZX-ray1.48A19-148[»]
1IX0X-ray1.80A19-148[»]
1IY3NMR-A19-148[»]
1IY4NMR-A19-148[»]
1JKAX-ray1.66A19-148[»]
1JKBX-ray1.66A19-148[»]
1JKCX-ray1.60A19-148[»]
1JKDX-ray1.80A19-148[»]
1JSFX-ray1.15A19-148[»]
1JWRX-ray1.40A19-148[»]
1LAAX-ray1.77A19-148[»]
1LHHX-ray1.80A19-148[»]
1LHIX-ray1.80A19-148[»]
1LHJX-ray1.80A19-148[»]
1LHKX-ray1.80A19-148[»]
1LHLX-ray1.80A19-148[»]
1LHMX-ray1.80A19-148[»]
1LMTX-ray1.60A19-148[»]
1LOZX-ray1.80A19-148[»]
1LYYX-ray1.80A19-148[»]
1LZ1X-ray1.50A19-148[»]
1LZ4X-ray1.80A19-148[»]
1LZ5X-ray1.80A19-144[»]
1LZ6X-ray1.80A19-140[»]
1LZRX-ray1.50A19-148[»]
1LZSX-ray1.60A/B19-148[»]
1OP9X-ray1.86B19-148[»]
1OUAX-ray1.80A19-148[»]
1OUBX-ray1.80A19-148[»]
1OUCX-ray1.80A19-148[»]
1OUDX-ray1.80A19-148[»]
1OUEX-ray1.80A19-148[»]
1OUFX-ray1.80A19-147[»]
1OUGX-ray1.80A19-148[»]
1OUHX-ray1.80A19-148[»]
1OUIX-ray1.80A19-148[»]
1OUJX-ray1.80A19-148[»]
1QSWX-ray1.85A/B/C/D19-148[»]
1RE2X-ray2.30A19-148[»]
1REMX-ray2.10A19-148[»]
1REXX-ray1.50A19-148[»]
1REYX-ray1.70A19-148[»]
1REZX-ray1.70A19-148[»]
1TAYX-ray1.70A19-148[»]
1TBYX-ray1.77A19-148[»]
1TCYX-ray1.70A19-148[»]
1TDYX-ray1.70A19-148[»]
1UBZX-ray2.00A19-148[»]
1W08X-ray2.50A19-148[»]
1WQMX-ray1.80A19-148[»]
1WQNX-ray1.80A19-148[»]
1WQOX-ray1.80A19-148[»]
1WQPX-ray1.80A19-148[»]
1WQQX-ray1.80A19-148[»]
1WQRX-ray1.80A19-148[»]
1YAMX-ray1.80A19-148[»]
1YANX-ray1.80A19-148[»]
1YAOX-ray1.80A19-148[»]
1YAPX-ray1.80A19-148[»]
1YAQX-ray1.80A19-148[»]
207LX-ray1.80A19-148[»]
208LX-ray2.20A19-148[»]
2BQAX-ray1.80A19-148[»]
2BQBX-ray1.80A19-148[»]
2BQCX-ray1.80A19-148[»]
2BQDX-ray1.80A19-148[»]
2BQEX-ray1.80A19-148[»]
2BQFX-ray1.80A19-148[»]
2BQGX-ray1.80A19-148[»]
2BQHX-ray1.80A19-148[»]
2BQIX-ray1.80A19-148[»]
2BQJX-ray1.80A19-148[»]
2BQKX-ray1.80A19-147[»]
2BQLX-ray1.80A19-148[»]
2BQMX-ray1.80A19-148[»]
2BQNX-ray1.80A19-148[»]
2BQOX-ray1.80A19-148[»]
2HEAX-ray1.80A19-148[»]
2HEBX-ray2.20A19-148[»]
2HECX-ray1.80A19-148[»]
2HEDX-ray1.80A19-148[»]
2HEEX-ray1.80A19-148[»]
2HEFX-ray1.80A19-148[»]
2LHMX-ray1.80A19-148[»]
2MEAX-ray2.20A/B19-148[»]
2MEBX-ray1.80A19-148[»]
2MECX-ray2.20A/B19-148[»]
2MEDX-ray1.80A19-148[»]
2MEEX-ray1.80A19-148[»]
2MEFX-ray1.80A19-148[»]
2MEGX-ray1.80A19-148[»]
2MEHX-ray1.80A19-148[»]
2MEIX-ray1.80A19-148[»]
2NWDX-ray1.04X19-148[»]
2ZIJX-ray1.90A19-148[»]
2ZIKX-ray1.81A19-148[»]
2ZILX-ray1.80A19-148[»]
2ZWBneutron diffraction1.80A19-148[»]
3EBAX-ray1.85B19-148[»]
3FE0X-ray1.50A19-148[»]
3LHMX-ray1.80A19-148[»]
3LN2X-ray2.04A/B19-148[»]
4I0CX-ray1.95A/B19-148[»]
4ML7X-ray1.80A/C19-148[»]
ProteinModelPortaliP61626.
SMRiP61626. Positions 19-148.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61626.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 22 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG85133.
GeneTreeiENSGT00550000074398.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiP61626.
KOiK13915.
OMAiLQDNIAD.
OrthoDBiEOG7BW0M5.
PhylomeDBiP61626.
TreeFamiTF324882.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00062. Lys. 1 hit.
[Graphical view]
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P61626-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKALIVLGLV LLSVTVQGKV FERCELARTL KRLGMDGYRG ISLANWMCLA
60 70 80 90 100
KWESGYNTRA TNYNAGDRST DYGIFQINSR YWCNDGKTPG AVNACHLSCS
110 120 130 140
ALLQDNIADA VACAKRVVRD PQGIRAWVAW RNRCQNRDVR QYVQGCGV
Length:148
Mass (Da):16,537
Last modified:June 7, 2004 - v1
Checksum:i8ECFD276BEB2678A
GO

Sequence cautioni

The sequence CAA32175.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101V → A in AAC63078. 1 PublicationCurated
Sequence conflicti41 – 411I → M in AAA36188. (PubMed:2971592)Curated
Sequence conflicti111 – 1111V → A in AAC63078. 1 PublicationCurated
Sequence conflicti124 – 1241I → V in AAC63078. 1 PublicationCurated
Sequence conflicti128 – 1281V → A in AAC63078. 1 PublicationCurated
Sequence conflicti136 – 1361N → D in AAC63078. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti74 – 741I → T in AMYL8. 1 Publication
VAR_004280
Natural varianti85 – 851D → H in AMYL8. 1 Publication
VAR_004281
Natural varianti88 – 881T → N.
Corresponds to variant rs1800973 [ dbSNP | Ensembl ].
VAR_012050

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8989.1.
PIRiS04938. LZHU.
RefSeqiNP_000230.1. NM_000239.2.
UniGeneiHs.524579.

Genome annotation databases

EnsembliENST00000261267; ENSP00000261267; ENSG00000090382.
GeneIDi4069.
KEGGihsa:4069.
UCSCiuc001suw.2. human.

Polymorphism databases

DMDMi48428995.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Lysozyme entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS8989.1.
PIRi S04938. LZHU.
RefSeqi NP_000230.1. NM_000239.2.
UniGenei Hs.524579.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 19-148 [» ]
1C45 X-ray 1.80 A 19-148 [» ]
1C46 X-ray 2.20 A 19-148 [» ]
1C7P X-ray 2.40 A 16-148 [» ]
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 19-148 [» ]
1GAZ X-ray 1.80 A 19-148 [» ]
1GB0 X-ray 1.80 A 19-148 [» ]
1GB2 X-ray 1.80 A 19-148 [» ]
1GB3 X-ray 1.80 A 19-148 [» ]
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 19-148 [» ]
1GF9 X-ray 1.80 A 19-148 [» ]
1GFA X-ray 1.80 A 19-148 [» ]
1GFE X-ray 1.80 A 19-148 [» ]
1GFG X-ray 1.80 A 19-148 [» ]
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 19-140 [» ]
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 19-148 [» ]
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 19-148 [» ]
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 [» ]
4I0C X-ray 1.95 A/B 19-148 [» ]
4ML7 X-ray 1.80 A/C 19-148 [» ]
ProteinModelPortali P61626.
SMRi P61626. Positions 19-148.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110247. 19 interactions.
IntActi P61626. 7 interactions.
MINTi MINT-5002660.
STRINGi 9606.ENSP00000261267.

Chemistry

DrugBanki DB00128. L-Aspartic Acid.

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

PTM databases

PhosphoSitei P61626.

Polymorphism databases

DMDMi 48428995.

2D gel databases

UCD-2DPAGE P61626.

Proteomic databases

MaxQBi P61626.
PaxDbi P61626.
PeptideAtlasi P61626.
PRIDEi P61626.

Protocols and materials databases

DNASUi 4069.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261267 ; ENSP00000261267 ; ENSG00000090382 .
GeneIDi 4069.
KEGGi hsa:4069.
UCSCi uc001suw.2. human.

Organism-specific databases

CTDi 4069.
GeneCardsi GC12P069681.
HGNCi HGNC:6740. LYZ.
HPAi CAB000055.
HPA048284.
MIMi 105200. phenotype.
153450. gene.
neXtProti NX_P61626.
Orphaneti 93561. Familial renal amyloidosis due to lysozyme variant.
PharmGKBi PA30503.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG85133.
GeneTreei ENSGT00550000074398.
HOGENOMi HOG000037357.
HOVERGENi HBG052297.
InParanoidi P61626.
KOi K13915.
OMAi LQDNIAD.
OrthoDBi EOG7BW0M5.
PhylomeDBi P61626.
TreeFami TF324882.

Enzyme and pathway databases

Reactomei REACT_75925. Amyloids.

Miscellaneous databases

ChiTaRSi LYZ. human.
EvolutionaryTracei P61626.
GeneWikii Lysozyme.
GenomeRNAii 4069.
NextBioi 15952.
PROi P61626.
SOURCEi Search...

Gene expression databases

Bgeei P61626.
CleanExi HS_LYZ.
ExpressionAtlasi P61626. baseline and differential.
Genevestigatori P61626.

Family and domain databases

InterProi IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view ]
Pfami PF00062. Lys. 1 hit.
[Graphical view ]
PRINTSi PR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTi SM00263. LYZ1. 1 hit.
[Graphical view ]
SUPFAMi SSF53955. SSF53955. 1 hit.
PROSITEi PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: VARIANTS AMYL8 THR-74 AND HIS-85.

Entry informationi

Entry nameiLYSC_HUMAN
AccessioniPrimary (citable) accession number: P61626
Secondary accession number(s): P00695, Q13170, Q9UCF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2004
Last modified: October 29, 2014
This is version 125 of the entry and version 1 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

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.

Keywords - Technical termi

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

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3