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P61626 (LYSC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysozyme C

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Gene names
Name:LYZ
Synonyms:LZM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length148 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-355360,EBI-355360

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.7 Ref.8 Ref.9 Ref.10
Chain19 – 148130Lysozyme C
PRO_0000018467

Sites

Active site531
Active site711

Amino acid modifications

Disulfide bond24 ↔ 146
Disulfide bond48 ↔ 134
Disulfide bond83 ↔ 99
Disulfide bond95 ↔ 113

Natural variations

Natural variant741I → T in AMYL8. Ref.20
VAR_004280
Natural variant851D → H in AMYL8. Ref.20
VAR_004281
Natural variant881T → N.
Corresponds to variant rs1800973 [ dbSNP | Ensembl ].
VAR_012050

Experimental info

Sequence conflict101V → A in AAC63078. Ref.5
Sequence conflict411I → M in AAA36188. Ref.1
Sequence conflict1111V → A in AAC63078. Ref.5
Sequence conflict1241I → V in AAC63078. Ref.5
Sequence conflict1281V → A in AAC63078. Ref.5
Sequence conflict1361N → D in AAC63078. Ref.5

Secondary structure

............................... 148
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61626 [UniParc].

Last modified June 7, 2004. Version 1.
Checksum: 8ECFD276BEB2678A

FASTA14816,537
        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 

« Hide

References

« Hide '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

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.
CCDSCCDS8989.1.
PIRLZHU. S04938.
RefSeqNP_000230.1. NM_000239.2.
UniGeneHs.524579.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP61626.
SMRP61626. Positions 19-148.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110247. 16 interactions.
IntActP61626. 7 interactions.
MINTMINT-5002660.
STRING9606.ENSP00000261267.

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

PTM databases

PhosphoSiteP61626.

Polymorphism databases

DMDM48428995.

2D gel databases

UCD-2DPAGEP61626.

Proteomic databases

MaxQBP61626.
PaxDbP61626.
PeptideAtlasP61626.
PRIDEP61626.

Protocols and materials databases

DNASU4069.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261267; ENSP00000261267; ENSG00000090382.
GeneID4069.
KEGGhsa:4069.
UCSCuc001suw.2. human.

Organism-specific databases

CTD4069.
GeneCardsGC12P069681.
HGNCHGNC:6740. LYZ.
HPACAB000055.
HPA048284.
MIM105200. phenotype.
153450. gene.
neXtProtNX_P61626.
Orphanet93561. Familial renal amyloidosis due to lysozyme variant.
PharmGKBPA30503.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG85133.
HOGENOMHOG000037357.
HOVERGENHBG052297.
InParanoidP61626.
KOK13915.
OMALQDNIAD.
OrthoDBEOG7BW0M5.
PhylomeDBP61626.
TreeFamTF324882.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Gene expression databases

ArrayExpressP61626.
BgeeP61626.
CleanExHS_LYZ.
GenevestigatorP61626.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLYZ. human.
EvolutionaryTraceP61626.
GeneWikiLysozyme.
GenomeRNAi4069.
NextBio15952.
PROP61626.
SOURCESearch...

Entry information

Entry nameLYSC_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 122 of the entry and version 1 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.

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