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P20711 (DDC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aromatic-L-amino-acid decarboxylase

Short name=AADC
EC=4.1.1.28
Alternative name(s):
DOPA decarboxylase
Short name=DDC
Gene names
Name:DDC
Synonyms:AADC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine.

Catalytic activity

L-dopa = dopamine + CO2.

5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO2.

Cofactor

Pyridoxal phosphate. Ref.10

Pathway

Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 2/2.

Subunit structure

Homodimer. Ref.10

Involvement in disease

Aromatic L-amino-acid decarboxylase deficiency (AADCD) [MIM:608643]: An inborn error in neurotransmitter metabolism that leads to combined serotonin and catecholamine deficiency. It causes developmental and psychomotor delay, poor feeding, lethargy, ptosis, intermittent hypothermia, gastrointestinal disturbances. The onset is early in infancy and inheritance is autosomal recessive.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.11 Ref.14 Ref.15

Sequence similarities

Belongs to the group II decarboxylase family.

Ontologies

Keywords
   Biological processCatecholamine biosynthesis
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
   LigandPyridoxal phosphate
   Molecular functionDecarboxylase
Lyase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcatecholamine biosynthetic process

Traceable author statement. Source: Reactome

cellular amino acid metabolic process

Inferred from electronic annotation. Source: InterPro

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

cellular response to alkaloid

Inferred from electronic annotation. Source: Ensembl

cellular response to drug

Inferred from electronic annotation. Source: Ensembl

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

circadian rhythm

Inferred from electronic annotation. Source: Ensembl

dopamine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

indolalkylamine biosynthetic process

Traceable author statement. Source: Reactome

isoquinoline alkaloid metabolic process

Inferred from electronic annotation. Source: Ensembl

multicellular organismal aging

Inferred from electronic annotation. Source: Ensembl

phytoalexin metabolic process

Inferred from electronic annotation. Source: Ensembl

response to pyrethroid

Inferred from electronic annotation. Source: Ensembl

serotonin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

synaptic vesicle amine transport

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionamino acid binding

Inferred from electronic annotation. Source: Ensembl

aromatic-L-amino-acid decarboxylase activity

Inferred from direct assay PubMed 16338639. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12864730. Source: IntAct

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARP102752EBI-1632155,EBI-608057

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P20711-1)

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: P20711-2)

Also known as: alt-DDC;

The sequence of this isoform differs from the canonical sequence as follows:
     316-338: VKKRTDLTGAFRLDPTYLKHSHQ → SRQPVRMLRLKKTCLVSAVVRRS
     339-480: Missing.
Note: High expression in kidney.
Isoform 3 (identifier: P20711-3)

The sequence of this isoform differs from the canonical sequence as follows:
     68-145: Missing.
Note: No experimental confirmation available. Gene prediction based on EST data.
Isoform 4 (identifier: P20711-4)

The sequence of this isoform differs from the canonical sequence as follows:
     146-238: Missing.
Note: No experimental confirmation available. Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 480480Aromatic-L-amino-acid decarboxylase
PRO_0000146939

Regions

Repeat58 – 115581
Repeat118 – 178612
Region58 – 1781212 X approximate tandem repeats

Sites

Binding site821Substrate By similarity
Binding site1481PLP; via amide nitrogen
Binding site1491PLP
Binding site1921Substrate By similarity
Binding site2461PLP; via carbonyl oxygen
Binding site3001PLP

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue3031N6-(pyridoxal phosphate)lysine

Natural variations

Alternative sequence68 – 14578Missing in isoform 3.
VSP_047175
Alternative sequence146 – 23893Missing in isoform 4.
VSP_047176
Alternative sequence316 – 33823VKKRT…KHSHQ → SRQPVRMLRLKKTCLVSAVV RRS in isoform 2.
VSP_046569
Alternative sequence339 – 480142Missing in isoform 2.
VSP_046570
Natural variant171M → V. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8 Ref.12
Corresponds to variant rs6264 [ dbSNP | Ensembl ].
VAR_014788
Natural variant471P → H in AADCD. Ref.15
VAR_046137
Natural variant611E → D. Ref.5
Corresponds to variant rs11575292 [ dbSNP | Ensembl ].
VAR_019214
Natural variant911A → V in AADCD. Ref.11
VAR_046138
Natural variant1021G → S in AADCD. Ref.11 Ref.14
VAR_019309
Natural variant1471S → R in AADCD. Ref.11
VAR_046139
Natural variant2101P → L. Ref.5 Ref.12
Corresponds to variant rs6262 [ dbSNP | Ensembl ].
VAR_014789
Natural variant2171M → V. Ref.5 Ref.12
Corresponds to variant rs6263 [ dbSNP | Ensembl ].
VAR_014790
Natural variant2391M → I. Ref.5
Corresponds to variant rs11575377 [ dbSNP | Ensembl ].
VAR_019215
Natural variant2391M → L. Ref.5
Corresponds to variant rs11575376 [ dbSNP | Ensembl ].
VAR_019216
Natural variant2501S → F in AADCD. Ref.11 Ref.15
VAR_046140
Natural variant2751A → T in AADCD. Ref.11
VAR_046141
Natural variant3091F → L in AADCD. Ref.11
VAR_046142
Natural variant3471R → Q in AADCD. Ref.15
VAR_046143
Natural variant4081L → I in AADCD. Ref.15
VAR_046144
Natural variant4621R → Q. Ref.5
Corresponds to variant rs11575542 [ dbSNP | Ensembl ].
VAR_019217

Experimental info

Sequence conflict491E → G in AAB59432. Ref.8
Sequence conflict1551A → P in AAD40482. Ref.3

Secondary structure

.......................................................................... 480
Helix Strand Turn

Details...

Sequences

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

Last modified November 2, 2010. Version 2.
Checksum: 0A2CFF9A39BDE298

FASTA48053,926
        10         20         30         40         50         60 
MNASEFRRRG KEMVDYMANY MEGIEGRQVY PDVEPGYLRP LIPAAAPQEP DTFEDIINDV 

        70         80         90        100        110        120 
EKIIMPGVTH WHSPYFFAYF PTASSYPAML ADMLCGAIGC IGFSWAASPA CTELETVMMD 

       130        140        150        160        170        180 
WLGKMLELPK AFLNEKAGEG GGVIQGSASE ATLVALLAAR TKVIHRLQAA SPELTQAAIM 

       190        200        210        220        230        240 
EKLVAYSSDQ AHSSVERAGL IGGVKLKAIP SDGNFAMRAS ALQEALERDK AAGLIPFFMV 

       250        260        270        280        290        300 
ATLGTTTCCS FDNLLEVGPI CNKEDIWLHV DAAYAGSAFI CPEFRHLLNG VEFADSFNFN 

       310        320        330        340        350        360 
PHKWLLVNFD CSAMWVKKRT DLTGAFRLDP TYLKHSHQDS GLITDYRHWQ IPLGRRFRSL 

       370        380        390        400        410        420 
KMWFVFRMYG VKGLQAYIRK HVQLSHEFES LVRQDPRFEI CVEVILGLVC FRLKGSNKVN 

       430        440        450        460        470        480 
EALLQRINSA KKIHLVPCHL RDKFVLRFAI CSRTVESAHV QRAWEHIKEL AADVLRAERE 

« Hide

Isoform 2 (alt-DDC) [UniParc].

Checksum: 4197295F0675291A
Show »

FASTA33837,118
Isoform 3 [UniParc].

Checksum: 04119E5E691B06A2
Show »

FASTA40245,479
Isoform 4 [UniParc].

Checksum: C9D8C9459140ADD4
Show »

FASTA38744,239

References

« Hide 'large scale' references
[1]"Isolation and characterization of a cDNA clone encoding human aromatic L-amino acid decarboxylase."
Ichinose H., Kurosawa Y., Titani K., Fujita K., Nagatsu T.
Biochem. Biophys. Res. Commun. 164:1024-1030(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-17.
Tissue: Pheochromocytoma.
[2]"Human dopa decarboxylase: localization to human chromosome 7p11 and characterization of hepatic cDNAs."
Scherer L.J., McPherson J.D., Wasmuth J.J., Marsh L.J.
Genomics 13:469-471(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-17.
[3]"Molecular cloning of genomic DNA and chromosomal assignment of the gene for human aromatic L-amino acid decarboxylase, the enzyme for catecholamine and serotonin biosynthesis."
Sumi-Ichinose C., Ichinose H., Takahashi E., Hori T., Nagatsu T.
Biochemistry 31:2229-2238(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISEASE, VARIANT VAL-17.
[4]"Identification and characterization of a novel form of the human L-dopa decarboxylase mRNA."
Vassilacopoulou D.S., Sideris D.C., Vassiliou A.G., Fragoulis E.G.
Neurochem. Res. 29:1817-1823(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, VARIANT VAL-17.
Tissue: Placenta.
[5]NIEHS SNPs program
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-17; ASP-61; LEU-210; VAL-217; LEU-239; ILE-239 AND GLN-462.
[6]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
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), VARIANT VAL-17.
Tissue: Lung.
[8]"Identification of a neuron-specific promoter of human aromatic L-amino acid decarboxylase gene."
Van Thai A., Coste E., Allen J.M., Palmiter R.D., Weber M.J.
Brain Res. Mol. Brain Res. 17:227-238(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67, VARIANT VAL-17.
[9]"Localisation of the gene for human aromatic L-amino acid decarboxylase (DDC) to chromosome 7p13-->p11 by in situ hybridisation."
Craig S.P., Thai A.L., Weber M., Craig I.W.
Cytogenet. Cell Genet. 61:114-116(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-105.
[10]"Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases."
Giardina G., Montioli R., Gianni S., Cellini B., Paiardini A., Voltattorni C.B., Cutruzzola F.
Proc. Natl. Acad. Sci. U.S.A. 108:20514-20519(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), COFACTOR-BINDING SITES, SUBUNIT.
[11]"Mutations in the human aromatic L-amino acid decarboxylase gene."
Chang Y.T., Mues G., McPherson J.D., Bedell J., Marsh J.L., Hyland K., Courtwright K.H., Summers J.W.
J. Inherit. Metab. Dis. 21:4-4(1998)
Cited for: VARIANTS AADCD VAL-91; SER-102; ARG-147; PHE-250; THR-275 AND LEU-309.
[12]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-17; LEU-210 AND VAL-217.
[13]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
[14]"Levodopa-responsive aromatic L-amino acid decarboxylase deficiency."
Chang Y.T., Sharma R., Marsh J.L., McPherson J.D., Bedell J.A., Knust A., Braeutigam C., Hoffmann G.F., Hyland K.
Ann. Neurol. 55:435-438(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AADCD SER-102.
[15]"Aromatic L-amino acid decarboxylase deficiency: clinical features, treatment, and prognosis."
Pons R., Ford B., Chiriboga C.A., Clayton P.T., Hinton V., Hyland K., Sharma R., De Vivo D.C.
Neurology 62:1058-1065(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AADCD HIS-47; PHE-250; GLN-347 AND ILE-408.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M76180 mRNA. Translation: AAA58437.1.
M88700 mRNA. Translation: AAA20894.1.
M84592 expand/collapse EMBL AC list , M84600, M84593, M84594, M84596, M84597, M84595, M84598, M84599, M84588, M84589, M84590, M84591 Genomic DNA. Translation: AAD40482.1.
AJ310724 mRNA. Translation: CAC84071.1.
AY526322 Genomic DNA. Translation: AAS00092.1.
AC018705 Genomic DNA. Translation: AAS01995.1.
BC000485 mRNA. Translation: AAH00485.1.
BC008366 mRNA. Translation: AAH08366.1.
AH005280 Genomic DNA. Translation: AAB59432.1.
S46516 Genomic DNA. Translation: AAB23675.1.
CCDSCCDS5511.1. [P20711-1]
CCDS56485.1. [P20711-3]
CCDS56486.1. [P20711-4]
CCDS56487.1. [P20711-2]
PIRDCHUA. A33663.
RefSeqNP_000781.1. NM_000790.3.
NP_001076440.1. NM_001082971.1.
NP_001229815.1. NM_001242886.1.
NP_001229816.1. NM_001242887.1.
NP_001229817.1. NM_001242888.1.
NP_001229818.1. NM_001242889.1.
NP_001229819.1. NM_001242890.1.
UniGeneHs.359698.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RBFX-ray2.90A/B1-480[»]
3RBLX-ray3.24A/B1-480[»]
3RCHX-ray2.80A/B1-480[»]
ProteinModelPortalP20711.
SMRP20711. Positions 1-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108011. 2 interactions.
DIPDIP-40563N.
IntActP20711. 4 interactions.
STRING9606.ENSP00000350616.

Chemistry

ChEMBLCHEMBL1843.
DrugBankDB00915. Amantadine.
DB00190. Carbidopa.
DB00875. Flupenthixol.
DB00150. L-Tryptophan.
DB01235. Levodopa.
DB01100. Pimozide.
DB00114. Pyridoxal Phosphate.
DB00409. Remoxipride.

PTM databases

PhosphoSiteP20711.

Polymorphism databases

DMDM311033369.

Proteomic databases

MaxQBP20711.
PaxDbP20711.
PRIDEP20711.

Protocols and materials databases

DNASU1644.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357936; ENSP00000350616; ENSG00000132437. [P20711-1]
ENST00000380984; ENSP00000370371; ENSG00000132437. [P20711-2]
ENST00000426377; ENSP00000395069; ENSG00000132437. [P20711-3]
ENST00000431062; ENSP00000399184; ENSG00000132437. [P20711-4]
ENST00000444124; ENSP00000403644; ENSG00000132437. [P20711-1]
GeneID1644.
KEGGhsa:1644.

Organism-specific databases

CTD1644.
GeneCardsGC07M050526.
H-InvDBHIX0006684.
HGNCHGNC:2719. DDC.
HPAHPA017742.
MIM107930. gene.
608643. phenotype.
neXtProtNX_P20711.
Orphanet35708. Aromatic L-amino acid decarboxylase deficiency.
PharmGKBPA140.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0076.
HOGENOMHOG000121941.
HOVERGENHBG000944.
KOK01593.
OMAPICNKED.
OrthoDBEOG75B851.
PhylomeDBP20711.
TreeFamTF313863.

Enzyme and pathway databases

BioCycMetaCyc:HS05635-MONOMER.
BRENDA4.1.1.28. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00747; UER00734.

Gene expression databases

ArrayExpressP20711.
BgeeP20711.
CleanExHS_DDC.
GenevestigatorP20711.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR010977. Aromatic_deC.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
PRINTSPR00800. YHDCRBOXLASE.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi1644.
NextBio35484171.
PROP20711.
SOURCESearch...

Entry information

Entry nameDDC_HUMAN
AccessionPrimary (citable) accession number: P20711
Secondary accession number(s): C9IYA0 expand/collapse secondary AC list , E7ER62, E7EU95, Q16723, Q5W5T9, Q75MJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 2, 2010
Last modified: July 9, 2014
This is version 152 of the entry and version 2 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 7

Human chromosome 7: entries, gene names and cross-references to MIM