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Q16719 (KYNU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kynureninase

EC=3.7.1.3
Alternative name(s):
L-kynurenine hydrolase
Gene names
Name:KYNU
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity. HAMAP-Rule MF_03017

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine. Ref.1 Ref.2 Ref.8 Ref.11

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. Ref.1 Ref.2 Ref.8 Ref.11

Cofactor

Pyridoxal phosphate.

Enzyme regulation

Inhibited by o-methoxybenzoylalanine (OMBA). Ref.1 Ref.2

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. HAMAP-Rule MF_03017

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. HAMAP-Rule MF_03017

Subunit structure

Homodimer. Ref.11

Subcellular location

Cytoplasm Ref.1.

Tissue specificity

Expressed in all tissues tested (heart, brain placenta, lung, liver, skeletal muscle, kidney and pancreas). Highest levels found in placenta, liver and lung. Expressed in all brain regions. Ref.1 Ref.2

Induction

Increased levels in several cerebral and systemic inflammatory conditions. Ref.1 Ref.2

Involvement in disease

Xanthurenic aciduria manifesting as massive urinary excretion of large amounts of kynurenine, 3-hydroxykynurenine and xanthurenic acid has been observed in an individual carrying a homozygous missense change in KYNU (Ref.12). The urinary pattern in the patient suggests kynureninase deficiency and a block in the conversion of kynurenine and 3-hydroxykynurenine to anthranilate and 3-hydroxyanthranilate, respectively.

Sequence similarities

Belongs to the kynureninase family.

Caution

It has been reported that this enzyme possesses no measurable activity against L-kynurenine and is subject to inhibition by both L-kynurenine and D-kynurenine at pH 7.9 (Ref.8).

Biophysicochemical properties

Kinetic parameters:

KM=493 µM for L-kynurenine (at pH 7.0) Ref.1 Ref.2 Ref.8 Ref.11

KM=28.3 µM for DL-3-hydroxykynurenine (at pH 7.0)

KM=3.0 µM for DL-3-hydroxykynurenine (at pH 7.9)

pH dependence:

Optimum pH is 8.25 with DL-3-hydroxykynurenine as substrate.

Mass spectrometry

Molecular mass is 52400 Da from positions 1 - 465. Determined by MALDI. The reported mass is given to only three significant figures. Ref.8

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   LigandPyridoxal phosphate
   Molecular functionHydrolase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-kynurenine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

NAD biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

anthranilate metabolic process

Inferred from direct assay Ref.8. Source: UniProtKB

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

quinolinate biosynthetic process

Inferred from direct assay PubMed 9291104. Source: UniProtKB

response to interferon-gamma

Inferred from direct assay PubMed 9291104. Source: UniProtKB

response to vitamin B6

Inferred from mutant phenotype PubMed 1939450. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

tryptophan catabolic process

Inferred from mutant phenotype Ref.12. Source: UniProtKB

tryptophan catabolic process to acetyl-CoA

Inferred from electronic annotation. Source: Ensembl

tryptophan catabolic process to kynurenine

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Inferred from direct assay PubMed 6468727. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 6468727. Source: UniProtKB

   Molecular_functionkynureninase activity

Inferred from direct assay Ref.8Ref.2. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.8. Source: UniProtKB

pyridoxal phosphate binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16719-1)

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: Q16719-2)

The sequence of this isoform differs from the canonical sequence as follows:
     302-307: LVGWFG → RSEFFN
     308-465: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 465465Kynureninase HAMAP-Rule MF_03017
PRO_0000218657

Regions

Region165 – 1684Pyridoxal phosphate binding HAMAP-Rule MF_03017

Sites

Binding site1371Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1381Pyridoxal phosphate
Binding site2211Pyridoxal phosphate By similarity
Binding site2501Pyridoxal phosphate
Binding site2531Pyridoxal phosphate
Binding site2751Pyridoxal phosphate
Binding site3051Pyridoxal phosphate
Binding site3331Pyridoxal phosphate

Amino acid modifications

Modified residue11N-acetylmethionine Ref.10
Modified residue2761N6-(pyridoxal phosphate)lysine HAMAP-Rule MF_03017

Natural variations

Alternative sequence302 – 3076LVGWFG → RSEFFN in isoform 2.
VSP_042739
Alternative sequence308 – 465158Missing in isoform 2.
VSP_042740
Natural variant1881R → Q.
Corresponds to variant rs2304705 [ dbSNP | Ensembl ].
VAR_049724
Natural variant1981T → A Detected in a boy with xanthurenic aciduria. Ref.12
VAR_054401
Natural variant4121K → E. Ref.3
Corresponds to variant rs9013 [ dbSNP | Ensembl ].
VAR_022092

Secondary structure

........................................................................................ 465
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: BDD136BE18C79EBB

FASTA46552,352
        10         20         30         40         50         60 
MEPSSLELPA DTVQRIAAEL KCHPTDERVA LHLDEEDKLR HFRECFYIPK IQDLPPVDLS 

        70         80         90        100        110        120 
LVNKDENAIY FLGNSLGLQP KMVKTYLEEE LDKWAKIAAY GHEVGKRPWI TGDESIVGLM 

       130        140        150        160        170        180 
KDIVGANEKE IALMNALTVN LHLLMLSFFK PTPKRYKILL EAKAFPSDHY AIESQLQLHG 

       190        200        210        220        230        240 
LNIEESMRMI KPREGEETLR IEDILEVIEK EGDSIAVILF SGVHFYTGQH FNIPAITKAG 

       250        260        270        280        290        300 
QAKGCYVGFD LAHAVGNVEL YLHDWGVDFA CWCSYKYLNA GAGGIAGAFI HEKHAHTIKP 

       310        320        330        340        350        360 
ALVGWFGHEL STRFKMDNKL QLIPGVCGFR ISNPPILLVC SLHASLEIFK QATMKALRKK 

       370        380        390        400        410        420 
SVLLTGYLEY LIKHNYGKDK AATKKPVVNI ITPSHVEERG CQLTITFSVP NKDVFQELEK 

       430        440        450        460 
RGVVCDKRNP NGIRVAPVPL YNSFHDVYKF TNLLTSILDS AETKN 

« Hide

Isoform 2 [UniParc].

Checksum: 9219F37B19D2163E
Show »

FASTA30734,635

References

« Hide 'large scale' references
[1]"Isolation and expression of a cDNA clone encoding human kynureninase."
Alberati-Giani D., Buchli R., Malherbe P., Broger C., Lang G., Koehler C., Lahm H.-W., Cesura A.M.
Eur. J. Biochem. 239:460-468(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Tissue: Hepatoma.
[2]"Cloning and recombinant expression of rat and human kynureninase."
Toma S., Nakamura M., Tone S., Okuno E., Kido R., Breton J., Avanzi N., Cozzi L., Speciale C., Mostardini M., Gatti S., Benatti L.
FEBS Lett. 408:5-10(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Tissue: Liver.
[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 1), VARIANT GLU-412.
Tissue: Synovium.
[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]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [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 (SEP-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: Cervix.
[8]"Purification and biochemical characterization of some of the properties of recombinant human kynureninase."
Walsh H.A., Botting N.P.
Eur. J. Biochem. 269:2069-2074(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[9]"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].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Crystal structure of Homo sapiens kynureninase."
Lima S., Khristoforov R., Momany C., Phillips R.S.
Biochemistry 46:2735-2744(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, HOMODIMERIZATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[12]"Xanthurenic aciduria due to a mutation in KYNU encoding kynureninase."
Christensen M., Duno M., Lund A.M., Skovby F., Christensen E.
J. Inherit. Metab. Dis. 30:248-255(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALA-198, POSSIBLE INVOLVEMENT IN XANTHURENIC ACIDURIA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U57721 mRNA. Translation: AAC50650.1.
AK315343 mRNA. Translation: BAG37742.1.
CR457423 mRNA. Translation: CAG33704.1.
AC013437 Genomic DNA. No translation available.
AC013444 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX11599.1.
CH471058 Genomic DNA. Translation: EAX11600.1.
CH471058 Genomic DNA. Translation: EAX11601.1.
BC000879 mRNA. Translation: AAH00879.1.
PIRG02652.
RefSeqNP_001028170.1. NM_001032998.1.
NP_001186170.1. NM_001199241.1.
NP_003928.1. NM_003937.2.
UniGeneHs.470126.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HZPX-ray2.00A1-465[»]
3E9KX-ray1.70A1-465[»]
ProteinModelPortalQ16719.
SMRQ16719. Positions 6-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114454. 31 interactions.
IntActQ16719. 1 interaction.
STRING9606.ENSP00000264170.

Chemistry

BindingDBQ16719.
ChEMBLCHEMBL5100.
DrugBankDB00160. L-Alanine.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSiteQ16719.

Polymorphism databases

DMDM3913982.

Proteomic databases

PaxDbQ16719.
PeptideAtlasQ16719.
PRIDEQ16719.

Protocols and materials databases

DNASU8942.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264170; ENSP00000264170; ENSG00000115919. [Q16719-1]
ENST00000375773; ENSP00000364928; ENSG00000115919. [Q16719-2]
ENST00000409512; ENSP00000386731; ENSG00000115919. [Q16719-1]
GeneID8942.
KEGGhsa:8942.
UCSCuc002tvk.3. human. [Q16719-2]
uc002tvl.3. human. [Q16719-1]

Organism-specific databases

CTD8942.
GeneCardsGC02P143657.
HGNCHGNC:6469. KYNU.
HPAHPA031686.
MIM605197. gene.
neXtProtNX_Q16719.
Orphanet79155. Encephalopathy due to hydroxykynureninuria.
PharmGKBPA30258.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
HOVERGENHBG001170.
InParanoidQ16719.
KOK01556.
OMAGWYGGDK.
OrthoDBEOG7D2FDV.
PhylomeDBQ16719.
TreeFamTF300707.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00253; UER00329.
UPA00334; UER00455.

Gene expression databases

ArrayExpressQ16719.
BgeeQ16719.
CleanExHS_KYNU.
GenevestigatorQ16719.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_01970. Kynureninase.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR14084. PTHR14084. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF038800. KYNU. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Other

ChiTaRSKYNU. human.
EvolutionaryTraceQ16719.
GeneWikiKynureninase.
GenomeRNAi8942.
NextBio33630.
PROQ16719.
SOURCESearch...

Entry information

Entry nameKYNU_HUMAN
AccessionPrimary (citable) accession number: Q16719
Secondary accession number(s): B2RCZ5 expand/collapse secondary AC list , D3DP79, Q6I9T2, Q9BVW3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 130 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM