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Protein

Dihydropyrimidine dehydrogenase [NADP(+)]

Gene

DPYD

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

Functioni

Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil.

Catalytic activityi

5,6-dihydrouracil + NADP+ = uracil + NADPH.

Cofactori

Protein has several cofactor binding sites:
  • FADNote: Binds 2 FAD.
  • FMNNote: Binds 2 FMN.
  • [4Fe-4S] clusterBy similarityNote: Binds 4 [4Fe-4S] clusters. Contains approximately 16 iron atoms per subunit.By similarity

Pathwayi: beta-alanine biosynthesis

This protein is involved in the pathway beta-alanine biosynthesis, which is part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the pathway beta-alanine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi79Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi82Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi87Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi91Iron-sulfur 2 (4Fe-4S)By similarity1
Binding sitei129FAD; via carbonyl oxygenBy similarity1
Metal bindingi130Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi136Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi140Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi156Iron-sulfur 2 (4Fe-4S)By similarity1
Binding sitei235FADBy similarity1
Binding sitei261FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei371NADPBy similarity1
Binding sitei550FMNBy similarity1
Binding sitei609SubstrateBy similarity1
Active sitei671Proton acceptorBy similarity1
Binding sitei709FMNBy similarity1
Binding sitei767FMN; via amide nitrogenBy similarity1
Metal bindingi953Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi956Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi959Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi963Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi986Iron-sulfur 4 (4Fe-4S)By similarity1
Metal bindingi989Iron-sulfur 4 (4Fe-4S)By similarity1
Metal bindingi992Iron-sulfur 4 (4Fe-4S)By similarity1
Metal bindingi996Iron-sulfur 4 (4Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi194 – 198FADBy similarity5
Nucleotide bindingi218 – 226FADBy similarity9
Nucleotide bindingi340 – 343NADPBy similarity4
Nucleotide bindingi364 – 365NADPBy similarity2
Nucleotide bindingi437 – 439NADPBy similarity3
Nucleotide bindingi480 – 489FADBy similarity10
Nucleotide bindingi481 – 487NADPBy similarity7
Nucleotide bindingi574 – 575FMNBy similarity2
Nucleotide bindingi793 – 795FMNBy similarity3
Nucleotide bindingi816 – 817FMNBy similarity2

GO - Molecular functioni

GO - Biological processi

  • beta-alanine biosynthetic process Source: UniProtKB-UniPathway
  • purine nucleobase catabolic process Source: UniProtKB
  • pyrimidine nucleobase catabolic process Source: UniProtKB
  • pyrimidine nucleoside catabolic process Source: Reactome
  • thymidine catabolic process Source: UniProtKB
  • thymine catabolic process Source: UniProtKB
  • uracil catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

4Fe-4S, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS06975-MONOMER.
ZFISH:HS06975-MONOMER.
BRENDAi1.3.1.2. 2681.
ReactomeiR-HSA-73621. Pyrimidine catabolism.
UniPathwayiUPA00131.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydropyrimidine dehydrogenase [NADP(+)] (EC:1.3.1.2)
Short name:
DHPDHase
Short name:
DPD
Alternative name(s):
Dihydrothymine dehydrogenase
Dihydrouracil dehydrogenase
Gene namesi
Name:DPYD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3012. DPYD.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Dihydropyrimidine dehydrogenase deficiency (DPYDD)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA metabolic disorder with large phenotypic variability, ranging from no symptoms to a convulsive disorder with motor and mental retardation. It is characterized by persistent urinary excretion of excessive amounts of uracil, thymine and 5-hydroxymethyluracil. Patients suffering from this disease show a severe reaction to the anticancer drug 5-fluorouracil.
See also OMIM:274270
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00517329C → R in DPYDD; allele DPYD*9A and allele DPYD*9B; loss of activity. 5 PublicationsCorresponds to variant rs1801265dbSNPEnsembl.1
Natural variantiVAR_005174235R → W in DPYDD; allele DPYD*8; loss of activity. 2 PublicationsCorresponds to variant rs1801266dbSNPEnsembl.1
Natural variantiVAR_005177886R → H in DPYDD; allele DPYD*9B; 25% of activity. 2 PublicationsCorresponds to variant rs1801267dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi1806.
MalaCardsiDPYD.
MIMi274270. phenotype.
OpenTargetsiENSG00000188641.
Orphaneti293948. 1p21.3 microdeletion syndrome.
240839. 5-fluorouracil toxicity.
1675. Dihydropyrimidine dehydrogenase deficiency.
PharmGKBiPA145.

Chemistry databases

ChEMBLiCHEMBL3172.
DrugBankiDB01101. Capecitabine.
DB03147. Flavin adenine dinucleotide.
DB00544. Fluorouracil.

Polymorphism and mutation databases

BioMutaiDPYD.
DMDMi160332325.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000211141 – 33
ChainiPRO_00000211154 – 1025Dihydropyrimidine dehydrogenase [NADP(+)]Add BLAST1022

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei384N6-acetyllysineCombined sources1
Modified residuei905PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ12882.
MaxQBiQ12882.
PaxDbiQ12882.
PeptideAtlasiQ12882.
PRIDEiQ12882.

PTM databases

iPTMnetiQ12882.
PhosphoSitePlusiQ12882.

Expressioni

Tissue specificityi

Found in most tissues with greatest activity found in liver and peripheral blood mononuclear cells.

Gene expression databases

BgeeiENSG00000188641.
CleanExiHS_DPYD.
GenevisibleiQ12882. HS.

Organism-specific databases

HPAiCAB033241.
HPA045210.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
GOPCQ9HD263EBI-2839838,EBI-349832
LXNQ9BS403EBI-2839838,EBI-1044504

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi108140. 9 interactors.
IntActiQ12882. 20 interactors.
STRINGi9606.ENSP00000359211.

Chemistry databases

BindingDBiQ12882.

Structurei

3D structure databases

ProteinModelPortaliQ12882.
SMRiQ12882.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini69 – 1004Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST32
Domaini944 – 9764Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST33
Domaini978 – 10074Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni668 – 670Substrate bindingBy similarity3
Regioni736 – 737Substrate bindingBy similarity2

Sequence similaritiesi

Contains 3 4Fe-4S ferredoxin-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0399. Eukaryota.
COG0167. LUCA.
COG0493. LUCA.
COG1146. LUCA.
GeneTreeiENSGT00500000044896.
HOGENOMiHOG000169491.
HOVERGENiHBG004351.
InParanoidiQ12882.
KOiK00207.
OMAiYQAIEFD.
OrthoDBiEOG091G00YL.
PhylomeDBiQ12882.
TreeFamiTF105791.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.50.50.60. 3 hits.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR013785. Aldolase_TIM.
IPR005720. Dihydroorotate_DH.
IPR028261. DPD_II.
IPR023753. FAD/NAD-binding_dom.
IPR009051. Helical_ferredxn.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
PF14691. Fer4_20. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
TIGRFAMsiTIGR01037. pyrD_sub1_fam. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 3 hits.
[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: Q12882-1) [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
MAPVLSKDSA DIESILALNP RTQTHATLCS TSAKKLDKKH WKRNPDKNCF
60 70 80 90 100
NCEKLENNFD DIKHTTLGER GALREAMRCL KCADAPCQKS CPTNLDIKSF
110 120 130 140 150
ITSIANKNYY GAAKMIFSDN PLGLTCGMVC PTSDLCVGGC NLYATEEGPI
160 170 180 190 200
NIGGLQQFAT EVFKAMSIPQ IRNPSLPPPE KMSEAYSAKI ALFGAGPASI
210 220 230 240 250
SCASFLARLG YSDITIFEKQ EYVGGLSTSE IPQFRLPYDV VNFEIELMKD
260 270 280 290 300
LGVKIICGKS LSVNEMTLST LKEKGYKAAF IGIGLPEPNK DAIFQGLTQD
310 320 330 340 350
QGFYTSKDFL PLVAKGSKAG MCACHSPLPS IRGVVIVLGA GDTAFDCATS
360 370 380 390 400
ALRCGARRVF IVFRKGFVNI RAVPEEMELA KEEKCEFLPF LSPRKVIVKG
410 420 430 440 450
GRIVAMQFVR TEQDETGKWN EDEDQMVHLK ADVVISAFGS VLSDPKVKEA
460 470 480 490 500
LSPIKFNRWG LPEVDPETMQ TSEAWVFAGG DVVGLANTTV ESVNDGKQAS
510 520 530 540 550
WYIHKYVQSQ YGASVSAKPE LPLFYTPIDL VDISVEMAGL KFINPFGLAS
560 570 580 590 600
ATPATSTSMI RRAFEAGWGF ALTKTFSLDK DIVTNVSPRI IRGTTSGPMY
610 620 630 640 650
GPGQSSFLNI ELISEKTAAY WCQSVTELKA DFPDNIVIAS IMCSYNKNDW
660 670 680 690 700
TELAKKSEDS GADALELNLS CPHGMGERGM GLACGQDPEL VRNICRWVRQ
710 720 730 740 750
AVQIPFFAKL TPNVTDIVSI ARAAKEGGAN GVTATNTVSG LMGLKSDGTP
760 770 780 790 800
WPAVGIAKRT TYGGVSGTAI RPIALRAVTS IARALPGFPI LATGGIDSAE
810 820 830 840 850
SGLQFLHSGA SVLQVCSAIQ NQDFTVIEDY CTGLKALLYL KSIEELQDWD
860 870 880 890 900
GQSPATVSHQ KGKPVPRIAE LMDKKLPSFG PYLEQRKKII AENKIRLKEQ
910 920 930 940 950
NVAFSPLKRN CFIPKRPIPT IKDVIGKALQ YLGTFGELSN VEQVVAMIDE
960 970 980 990 1000
EMCINCGKCY MTCNDSGYQA IQFDPETHLP TITDTCTGCT LCLSVCPIVD
1010 1020
CIKMVSRTTP YEPKRGVPLS VNPVC
Length:1,025
Mass (Da):111,401
Last modified:November 13, 2007 - v2
Checksum:i0201943955AB2C21
GO
Isoform 2 (identifier: Q12882-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     162-173: VFKAMSIPQIRN → TLILAFSLMNHL
     174-1025: Missing.

Note: No experimental confirmation available.
Show »
Length:173
Mass (Da):18,936
Checksum:i94D241E912F29B6B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti131P → S in AAI08743 (PubMed:16710414).Curated1
Sequence conflicti845E → G in BAF83906 (PubMed:14702039).Curated1
Sequence conflicti910N → S in AAA57474 (PubMed:8083224).Curated1
Sequence conflicti1024V → G in AAI31779 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00517329C → R in DPYDD; allele DPYD*9A and allele DPYD*9B; loss of activity. 5 PublicationsCorresponds to variant rs1801265dbSNPEnsembl.1
Natural variantiVAR_054034166M → V.Corresponds to variant rs2297595dbSNPEnsembl.1
Natural variantiVAR_005174235R → W in DPYDD; allele DPYD*8; loss of activity. 2 PublicationsCorresponds to variant rs1801266dbSNPEnsembl.1
Natural variantiVAR_005175534S → N in allele DPYD*4. 2 PublicationsCorresponds to variant rs1801158dbSNPEnsembl.1
Natural variantiVAR_005176543I → V in allele DPYD*5. 3 PublicationsCorresponds to variant rs1801159dbSNPEnsembl.1
Natural variantiVAR_014760732V → I.2 PublicationsCorresponds to variant rs1801160dbSNPEnsembl.1
Natural variantiVAR_005177886R → H in DPYDD; allele DPYD*9B; 25% of activity. 2 PublicationsCorresponds to variant rs1801267dbSNPEnsembl.1
Natural variantiVAR_005178995V → F in allele DPYD*10; low activity. Corresponds to variant rs1801268dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_044929162 – 173VFKAM…PQIRN → TLILAFSLMNHL in isoform 2. 2 PublicationsAdd BLAST12
Alternative sequenceiVSP_044930174 – 1025Missing in isoform 2. 2 PublicationsAdd BLAST852

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09178 mRNA. Translation: AAA57474.1.
U20938 mRNA. Translation: AAB51366.1.
AB003063 mRNA. Translation: BAA89789.1.
BT006740 mRNA. Translation: AAP35386.1.
AK291217 mRNA. Translation: BAF83906.1.
AL356457
, AC091608, AC093576, AC099787, AC114878, AC138135, BX908805 Genomic DNA. Translation: CAH70570.1.
BX908805
, AC091608, AC093576, AC099787, AC114878, AC138135, AL356457 Genomic DNA. Translation: CAI15125.1.
CH471097 Genomic DNA. Translation: EAW73002.1.
BC008379 mRNA. Translation: AAH08379.1.
BC064027 mRNA. Translation: AAH64027.1.
BC108742 mRNA. Translation: AAI08743.1.
BC131777 mRNA. Translation: AAI31778.1.
BC131778 mRNA. Translation: AAI31779.1.
X95670 Genomic DNA. Translation: CAA64973.1.
U57655 Genomic DNA. Translation: AAB07049.1.
CCDSiCCDS30777.1. [Q12882-1]
CCDS53346.1. [Q12882-2]
PIRiA54718.
RefSeqiNP_000101.2. NM_000110.3. [Q12882-1]
NP_001153773.1. NM_001160301.1. [Q12882-2]
UniGeneiHs.335034.

Genome annotation databases

EnsembliENST00000306031; ENSP00000307107; ENSG00000188641. [Q12882-2]
ENST00000370192; ENSP00000359211; ENSG00000188641. [Q12882-1]
GeneIDi1806.
KEGGihsa:1806.
UCSCiuc001drv.4. human. [Q12882-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09178 mRNA. Translation: AAA57474.1.
U20938 mRNA. Translation: AAB51366.1.
AB003063 mRNA. Translation: BAA89789.1.
BT006740 mRNA. Translation: AAP35386.1.
AK291217 mRNA. Translation: BAF83906.1.
AL356457
, AC091608, AC093576, AC099787, AC114878, AC138135, BX908805 Genomic DNA. Translation: CAH70570.1.
BX908805
, AC091608, AC093576, AC099787, AC114878, AC138135, AL356457 Genomic DNA. Translation: CAI15125.1.
CH471097 Genomic DNA. Translation: EAW73002.1.
BC008379 mRNA. Translation: AAH08379.1.
BC064027 mRNA. Translation: AAH64027.1.
BC108742 mRNA. Translation: AAI08743.1.
BC131777 mRNA. Translation: AAI31778.1.
BC131778 mRNA. Translation: AAI31779.1.
X95670 Genomic DNA. Translation: CAA64973.1.
U57655 Genomic DNA. Translation: AAB07049.1.
CCDSiCCDS30777.1. [Q12882-1]
CCDS53346.1. [Q12882-2]
PIRiA54718.
RefSeqiNP_000101.2. NM_000110.3. [Q12882-1]
NP_001153773.1. NM_001160301.1. [Q12882-2]
UniGeneiHs.335034.

3D structure databases

ProteinModelPortaliQ12882.
SMRiQ12882.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108140. 9 interactors.
IntActiQ12882. 20 interactors.
STRINGi9606.ENSP00000359211.

Chemistry databases

BindingDBiQ12882.
ChEMBLiCHEMBL3172.
DrugBankiDB01101. Capecitabine.
DB03147. Flavin adenine dinucleotide.
DB00544. Fluorouracil.

PTM databases

iPTMnetiQ12882.
PhosphoSitePlusiQ12882.

Polymorphism and mutation databases

BioMutaiDPYD.
DMDMi160332325.

Proteomic databases

EPDiQ12882.
MaxQBiQ12882.
PaxDbiQ12882.
PeptideAtlasiQ12882.
PRIDEiQ12882.

Protocols and materials databases

DNASUi1806.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306031; ENSP00000307107; ENSG00000188641. [Q12882-2]
ENST00000370192; ENSP00000359211; ENSG00000188641. [Q12882-1]
GeneIDi1806.
KEGGihsa:1806.
UCSCiuc001drv.4. human. [Q12882-1]

Organism-specific databases

CTDi1806.
DisGeNETi1806.
GeneCardsiDPYD.
H-InvDBHIX0000804.
HGNCiHGNC:3012. DPYD.
HPAiCAB033241.
HPA045210.
MalaCardsiDPYD.
MIMi274270. phenotype.
612779. gene.
neXtProtiNX_Q12882.
OpenTargetsiENSG00000188641.
Orphaneti293948. 1p21.3 microdeletion syndrome.
240839. 5-fluorouracil toxicity.
1675. Dihydropyrimidine dehydrogenase deficiency.
PharmGKBiPA145.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0399. Eukaryota.
COG0167. LUCA.
COG0493. LUCA.
COG1146. LUCA.
GeneTreeiENSGT00500000044896.
HOGENOMiHOG000169491.
HOVERGENiHBG004351.
InParanoidiQ12882.
KOiK00207.
OMAiYQAIEFD.
OrthoDBiEOG091G00YL.
PhylomeDBiQ12882.
TreeFamiTF105791.

Enzyme and pathway databases

UniPathwayiUPA00131.
BioCyciMetaCyc:HS06975-MONOMER.
ZFISH:HS06975-MONOMER.
BRENDAi1.3.1.2. 2681.
ReactomeiR-HSA-73621. Pyrimidine catabolism.

Miscellaneous databases

ChiTaRSiDPYD. human.
GeneWikiiDPYD.
GenomeRNAii1806.
PROiQ12882.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000188641.
CleanExiHS_DPYD.
GenevisibleiQ12882. HS.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.50.50.60. 3 hits.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR013785. Aldolase_TIM.
IPR005720. Dihydroorotate_DH.
IPR028261. DPD_II.
IPR023753. FAD/NAD-binding_dom.
IPR009051. Helical_ferredxn.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
PF14691. Fer4_20. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
TIGRFAMsiTIGR01037. pyrD_sub1_fam. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDPYD_HUMAN
AccessioniPrimary (citable) accession number: Q12882
Secondary accession number(s): A2RRQ2
, A2RRQ3, A8K5A2, A8MWG9, B1AN21, E9PFN1, Q16694, Q16761, Q32NB0, Q96HL6, Q96TH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 13, 2007
Last modified: November 2, 2016
This is version 175 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.