Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

D-dopachrome decarboxylase

Gene

DDT

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

Functioni

Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI).

Catalytic activityi

D-dopachrome = 5,6-dihydroxyindole + CO2.

GO - Molecular functioni

  1. D-dopachrome decarboxylase activity Source: UniProtKB-EC
  2. dopachrome isomerase activity Source: ProtInc

GO - Biological processi

  1. melanin biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Melanin biosynthesis

Enzyme and pathway databases

BRENDAi4.1.1.84. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
D-dopachrome decarboxylase (EC:4.1.1.84)
Alternative name(s):
D-dopachrome tautomerase
Phenylpyruvate tautomerase II
Gene namesi
Name:DDT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componentsi: Chromosome 22, Unplaced

Organism-specific databases

HGNCiHGNC:2732. DDT.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27197.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity2 Publications
Chaini2 – 118117D-dopachrome decarboxylasePRO_0000158070Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylprolineBy similarity
Modified residuei33 – 331N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP30046.
PeptideAtlasiP30046.
PRIDEiP30046.

2D gel databases

SWISS-2DPAGEP30046.
UCD-2DPAGEP30046.

PTM databases

PhosphoSiteiP30046.

Expressioni

Gene expression databases

BgeeiP30046.
CleanExiHS_DDT.
ExpressionAtlasiP30046. baseline and differential.
GenevestigatoriP30046.

Organism-specific databases

HPAiHPA049871.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi108018. 3 interactions.
IntActiP30046. 1 interaction.
MINTiMINT-5000166.
STRINGi9606.ENSP00000215773.

Structurei

Secondary structure

1
118
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Helixi12 – 143Combined sources
Helixi19 – 3113Combined sources
Helixi35 – 373Combined sources
Beta strandi39 – 435Combined sources
Beta strandi58 – 7013Combined sources
Helixi71 – 8919Combined sources
Helixi93 – 953Combined sources
Beta strandi96 – 1038Combined sources
Helixi105 – 1073Combined sources
Helixi115 – 1173Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DPTX-ray1.54A/B/C2-118[»]
3KANX-ray1.13A/B/C2-118[»]
4Q3FX-ray1.80A/B/C2-118[»]
ProteinModelPortaliP30046.
SMRiP30046. Positions 2-118.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30046.

Family & Domainsi

Sequence similaritiesi

Belongs to the MIF family.Curated

Phylogenomic databases

eggNOGiNOG284179.
GeneTreeiENSGT00730000111233.
HOGENOMiHOG000112325.
HOVERGENiHBG003240.
InParanoidiP30046.
KOiK10028.
OrthoDBiEOG7GXPDN.
PhylomeDBiP30046.
TreeFamiTF313853.

Family and domain databases

InterProiIPR001398. Macrophage_inhib_fac.
IPR019829. Macrophage_inhib_fac_CS.
IPR014347. Tautomerase/MIF_sf.
[Graphical view]
PANTHERiPTHR11954. PTHR11954. 1 hit.
PfamiPF01187. MIF. 1 hit.
[Graphical view]
ProDomiPD004816. Macrophage_inhib_fac. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF55331. SSF55331. 1 hit.
PROSITEiPS01158. MIF. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P30046-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MPFLELDTNL PANRVPAGLE KRLCAAAASI LGKPADRVNV TVRPGLAMAL
60 70 80 90 100
SGSTEPCAQL SISSIGVVGT AEDNRSHSAH FFEFLTKELA LGQDRILIRF
110
FPLESWQIGK IGTVMTFL
Length:118
Mass (Da):12,712
Last modified:January 22, 2007 - v3
Checksum:i12FEF51908F342B7
GO
Isoform 2 (identifier: P30046-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     96-118: ILIRFFPLESWQIGKIGTVMTFL → QVPGEVHGRLTE

Note: No experimental confirmation available.

Show »
Length:107
Mass (Da):11,323
Checksum:i74E98DFC0FA5395A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31F → G AA sequence (PubMed:12665801).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei96 – 11823ILIRF…VMTFL → QVPGEVHGRLTE in isoform 2. 1 PublicationVSP_056953Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49785 mRNA. Translation: AAB48546.1.
U84143 mRNA. Translation: AAB41503.1.
Y11151 Genomic DNA. Translation: CAA72037.1.
AF012434, AF012432, AF012433 Genomic DNA. Translation: AAC77468.1.
AF058293 Genomic DNA. Translation: AAC13717.1.
CR456431 mRNA. Translation: CAG30317.1.
AK298326 mRNA. Translation: BAH12758.1.
AP000351 Genomic DNA. No translation available.
Z84718 Genomic DNA. No translation available.
CH471095 Genomic DNA. Translation: EAW59622.1.
BC005971 mRNA. Translation: AAH05971.1.
BC015508 mRNA. Translation: AAH15508.1.
CCDSiCCDS13820.1. [P30046-1]
PIRiG02438.
JE0162.
RefSeqiNP_001077861.1. NM_001084392.1. [P30046-1]
NP_001346.1. NM_001355.3. [P30046-1]
XP_005261356.1. XM_005261299.2. [P30046-2]
UniGeneiHs.656723.
Hs.744172.

Genome annotation databases

EnsembliENST00000350608; ENSP00000215773; ENSG00000099977. [P30046-1]
ENST00000398344; ENSP00000381386; ENSG00000099977. [P30046-1]
ENST00000430101; ENSP00000399768; ENSG00000099977. [P30046-2]
ENST00000615721; ENSP00000481175; ENSG00000275003. [P30046-1]
GeneIDi100037417.
1652.
KEGGihsa:100037417.
hsa:1652.
UCSCiuc002zyz.4. human. [P30046-1]

Polymorphism databases

DMDMi2828192.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49785 mRNA. Translation: AAB48546.1.
U84143 mRNA. Translation: AAB41503.1.
Y11151 Genomic DNA. Translation: CAA72037.1.
AF012434, AF012432, AF012433 Genomic DNA. Translation: AAC77468.1.
AF058293 Genomic DNA. Translation: AAC13717.1.
CR456431 mRNA. Translation: CAG30317.1.
AK298326 mRNA. Translation: BAH12758.1.
AP000351 Genomic DNA. No translation available.
Z84718 Genomic DNA. No translation available.
CH471095 Genomic DNA. Translation: EAW59622.1.
BC005971 mRNA. Translation: AAH05971.1.
BC015508 mRNA. Translation: AAH15508.1.
CCDSiCCDS13820.1. [P30046-1]
PIRiG02438.
JE0162.
RefSeqiNP_001077861.1. NM_001084392.1. [P30046-1]
NP_001346.1. NM_001355.3. [P30046-1]
XP_005261356.1. XM_005261299.2. [P30046-2]
UniGeneiHs.656723.
Hs.744172.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DPTX-ray1.54A/B/C2-118[»]
3KANX-ray1.13A/B/C2-118[»]
4Q3FX-ray1.80A/B/C2-118[»]
ProteinModelPortaliP30046.
SMRiP30046. Positions 2-118.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108018. 3 interactions.
IntActiP30046. 1 interaction.
MINTiMINT-5000166.
STRINGi9606.ENSP00000215773.

PTM databases

PhosphoSiteiP30046.

Polymorphism databases

DMDMi2828192.

2D gel databases

SWISS-2DPAGEP30046.
UCD-2DPAGEP30046.

Proteomic databases

PaxDbiP30046.
PeptideAtlasiP30046.
PRIDEiP30046.

Protocols and materials databases

DNASUi1652.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000350608; ENSP00000215773; ENSG00000099977. [P30046-1]
ENST00000398344; ENSP00000381386; ENSG00000099977. [P30046-1]
ENST00000430101; ENSP00000399768; ENSG00000099977. [P30046-2]
ENST00000615721; ENSP00000481175; ENSG00000275003. [P30046-1]
GeneIDi100037417.
1652.
KEGGihsa:100037417.
hsa:1652.
UCSCiuc002zyz.4. human. [P30046-1]

Organism-specific databases

CTDi100037417.
1652.
GeneCardsiGC22M024313.
HGNCiHGNC:2732. DDT.
HPAiHPA049871.
MIMi602750. gene.
neXtProtiNX_P30046.
PharmGKBiPA27197.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG284179.
GeneTreeiENSGT00730000111233.
HOGENOMiHOG000112325.
HOVERGENiHBG003240.
InParanoidiP30046.
KOiK10028.
OrthoDBiEOG7GXPDN.
PhylomeDBiP30046.
TreeFamiTF313853.

Enzyme and pathway databases

BRENDAi4.1.1.84. 2681.

Miscellaneous databases

ChiTaRSiDDT. human.
EvolutionaryTraceiP30046.
GeneWikiiDDT_(gene).
GenomeRNAii1652.
NextBioi35479618.
PROiP30046.
SOURCEiSearch...

Gene expression databases

BgeeiP30046.
CleanExiHS_DDT.
ExpressionAtlasiP30046. baseline and differential.
GenevestigatoriP30046.

Family and domain databases

InterProiIPR001398. Macrophage_inhib_fac.
IPR019829. Macrophage_inhib_fac_CS.
IPR014347. Tautomerase/MIF_sf.
[Graphical view]
PANTHERiPTHR11954. PTHR11954. 1 hit.
PfamiPF01187. MIF. 1 hit.
[Graphical view]
ProDomiPD004816. Macrophage_inhib_fac. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF55331. SSF55331. 1 hit.
PROSITEiPS01158. MIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Thelin S., Panagopoulos I., Lassen C., Rosengren E., Aman P., Rorsman H.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "Molecular cloning of human D-dopachrome tautomerase cDNA: N-terminal proline is essential for enzyme activation."
    Nishihira J., Fujinaga M., Kuriyama T., Suzuki M., Sugimoto H., Nakagawa A., Tanaka I., Sakai M.
    Biochem. Biophys. Res. Commun. 243:538-544(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Rorsman H.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Conserved gene structure and genomic linkage for D-dopachrome tautomerase (DDT) and MIF."
    Esumi N., Budarf M., Ciccarelli L., Sellinger B., Kozak C.A., Wistow G.
    Mamm. Genome 9:753-757(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. Board P.G., Coggan M.A.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Kidney.
  8. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain and Pancreas.
  11. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-22.
    Tissue: Platelet.
  12. "Human liver protein map: a reference database established by microsequencing and gel comparison."
    Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
    Electrophoresis 13:992-1001(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12.
    Tissue: Liver.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Crystal structure of human D-dopachrome tautomerase, a homologue of macrophage migration inhibitory factor, at 1.54-A resolution."
    Sugimoto H., Taniguchi M., Nakagawa A., Tanaka I., Suzuki M., Nishihira J.
    Biochemistry 38:3268-3279(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiDOPD_HUMAN
AccessioniPrimary (citable) accession number: P30046
Secondary accession number(s): B7Z522
, O00774, O60787, Q13534
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 31, 1993
Last sequence update: January 22, 2007
Last modified: March 3, 2015
This is version 149 of the entry and version 3 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

Keywords - Technical termi

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

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.