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Protein

Nicotinamide phosphoribosyltransferase

Gene

NAMPT

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

Functioni

Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway. The secreted form behaves both as a cytokine with immunomodulating properties and an adipokine with anti-diabetic properties, it has no enzymatic activity, partly because of lack of activation by ATP, which has a low level in extracellular space and plasma. Plays a role in the modulation of circadian clock function. NAMPT-dependent oscillatory production of NAD regulates oscillation of clock target gene expression by releasing the core clock component: CLOCK-ARNTL/BMAL1 heterodimer from NAD-dependent SIRT1-mediated suppression (By similarity).By similarity1 Publication

Catalytic activityi

Nicotinamide D-ribonucleotide + diphosphate = nicotinamide + 5-phospho-alpha-D-ribose 1-diphosphate.

Enzyme regulationi

Inhibited by FK866. FK866 competes for the same binding site as nicotinamide, but due to its very low dissociation rate, it is essentially an irreversible inhibitor.1 Publication

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes nicotinamide D-ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and nicotinamide.
Proteins known to be involved in this subpathway in this organism are:
  1. Nicotinamide phosphoribosyltransferase (NAMPT)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes nicotinamide D-ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and nicotinamide, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei196Diphosphate1
Binding sitei219Nicotinamide ribonucleotide1
Binding sitei247Diphosphate1
Binding sitei311Diphosphate1
Binding sitei384Nicotinamide ribonucleotide; via amide nitrogen1
Binding sitei392Nicotinamide ribonucleotide1

GO - Molecular functioni

GO - Biological processi

  • cell-cell signaling Source: ProtInc
  • circadian regulation of gene expression Source: UniProtKB
  • circadian rhythm Source: Reactome
  • female pregnancy Source: Ensembl
  • NAD biosynthetic process Source: UniProtKB-UniPathway
  • nicotinamide metabolic process Source: Reactome
  • positive regulation of cell proliferation Source: ProtInc
  • positive regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
  • positive regulation of smooth muscle cell proliferation Source: Ensembl
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • response to organic cyclic compound Source: Ensembl
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Glycosyltransferase, Transferase

Keywords - Biological processi

Biological rhythms, Pyridine nucleotide biosynthesis

Enzyme and pathway databases

BioCyciZFISH:HS02817-MONOMER.
BRENDAi2.4.2.12. 2681.
ReactomeiR-HSA-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-HSA-197264. Nicotinamide salvaging.
SABIO-RKP43490.
SIGNORiP43490.
UniPathwayiUPA00253; UER00890.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinamide phosphoribosyltransferase (EC:2.4.2.12)
Short name:
NAmPRTase
Short name:
Nampt
Alternative name(s):
Pre-B-cell colony-enhancing factor 1
Short name:
Pre-B cell-enhancing factor
Visfatin
Gene namesi
Name:NAMPT
Synonyms:PBEF, PBEF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:30092. NAMPT.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB-KW
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi219D → N or S: No effect on activity towards nicotinamide. Alters specificity, so that the enzyme acquires activity towards nicotinic acid. 1 Publication1
Mutagenesisi247H → A: Reduces activity towards nicotinamide. 1 Publication1
Mutagenesisi311R → D: Reduces activity towards nicotinamide. 1 Publication1

Organism-specific databases

DisGeNETi10135.
OpenTargetsiENSG00000105835.
PharmGKBiPA162396933.

Chemistry databases

ChEMBLiCHEMBL1744525.

Polymorphism and mutation databases

BioMutaiNAMPT.
DMDMi1172027.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002058631 – 491Nicotinamide phosphoribosyltransferaseAdd BLAST491

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei188PhosphotyrosineCombined sources1
Modified residuei472PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP43490.
MaxQBiP43490.
PaxDbiP43490.
PeptideAtlasiP43490.
PRIDEiP43490.

PTM databases

iPTMnetiP43490.
PhosphoSitePlusiP43490.
SwissPalmiP43490.

Expressioni

Tissue specificityi

Expressed in large amounts in bone marrow, liver tissue, and muscle. Also present in heart, placenta, lung, and kidney tissues.

Gene expression databases

BgeeiENSG00000105835.
CleanExiHS_NAMPT.
ExpressionAtlasiP43490. baseline and differential.
GenevisibleiP43490. HS.

Organism-specific databases

HPAiCAB034349.
HPA047776.
HPA057722.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FTLP027923EBI-2829310,EBI-713279
IFITM3Q016283EBI-2829310,EBI-7932862
MT-ND1P038863EBI-2829310,EBI-1246156

GO - Molecular functioni

  • cytokine activity Source: ProtInc

Protein-protein interaction databases

BioGridi115438. 30 interactors.
DIPiDIP-29218N.
IntActiP43490. 11 interactors.
MINTiMINT-4530953.
STRINGi9606.ENSP00000222553.

Chemistry databases

BindingDBiP43490.

Structurei

Secondary structure

1491
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 13Combined sources3
Beta strandi14 – 16Combined sources3
Helixi17 – 24Combined sources8
Beta strandi30 – 39Combined sources10
Beta strandi56 – 58Combined sources3
Helixi62 – 69Combined sources8
Helixi77 – 91Combined sources15
Helixi98 – 108Combined sources11
Beta strandi114 – 118Combined sources5
Beta strandi124 – 126Combined sources3
Beta strandi129 – 138Combined sources10
Helixi139 – 141Combined sources3
Helixi144 – 147Combined sources4
Helixi149 – 153Combined sources5
Helixi156 – 180Combined sources25
Helixi186 – 188Combined sources3
Beta strandi189 – 192Combined sources4
Helixi195 – 197Combined sources3
Helixi201 – 211Combined sources11
Turni212 – 214Combined sources3
Beta strandi216 – 220Combined sources5
Helixi222 – 230Combined sources9
Beta strandi234 – 236Combined sources3
Helixi247 – 251Combined sources5
Helixi255 – 257Combined sources3
Helixi258 – 268Combined sources11
Beta strandi270 – 272Combined sources3
Beta strandi274 – 277Combined sources4
Helixi283 – 288Combined sources6
Helixi289 – 294Combined sources6
Helixi296 – 299Combined sources4
Beta strandi308 – 311Combined sources4
Helixi317 – 331Combined sources15
Beta strandi338 – 340Combined sources3
Beta strandi348 – 352Combined sources5
Helixi358 – 370Combined sources13
Helixi375 – 377Combined sources3
Beta strandi378 – 383Combined sources6
Helixi384 – 387Combined sources4
Turni392 – 396Combined sources5
Beta strandi397 – 406Combined sources10
Beta strandi409 – 412Combined sources4
Helixi421 – 423Combined sources3
Beta strandi431 – 434Combined sources4
Beta strandi440 – 443Combined sources4
Helixi447 – 450Combined sources4
Beta strandi453 – 455Combined sources3
Beta strandi459 – 463Combined sources5
Helixi473 – 479Combined sources7
Turni483 – 485Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E5BX-ray2.00A/B1-491[»]
2E5CX-ray2.20A/B1-491[»]
2E5DX-ray2.00A/B1-491[»]
2GVGX-ray2.20A/B/C/D/E/F1-491[»]
2GVJX-ray2.10A/B1-491[»]
3DGRX-ray2.10A/B1-484[»]
3DHDX-ray2.00A/B1-484[»]
3DHFX-ray1.80A/B1-484[»]
3DKJX-ray2.00A/B1-484[»]
3DKLX-ray1.89A/B1-484[»]
4JNMX-ray2.20A/B1-491[»]
4JR5X-ray1.91A/B1-491[»]
4KFNX-ray1.60A/B1-491[»]
4KFOX-ray1.60A/B1-491[»]
4KFPX-ray1.84A/B1-491[»]
4L4LX-ray2.12A/B1-491[»]
4L4MX-ray2.44A/B1-491[»]
4LTSX-ray1.69A/B1-491[»]
4LV9X-ray1.81A/B1-491[»]
4LVAX-ray1.55A/B1-491[»]
4LVBX-ray1.84A/B1-491[»]
4LVDX-ray1.75A/B1-491[»]
4LVFX-ray1.50A/B1-491[»]
4LVGX-ray1.70A/B1-491[»]
4LWWX-ray1.64A/B1-491[»]
4M6PX-ray1.75A/B1-491[»]
4M6QX-ray2.41A/B1-491[»]
4N9BX-ray2.86A/B1-491[»]
4N9CX-ray1.75A/B1-491[»]
4N9DX-ray1.70A/B1-491[»]
4N9EX-ray1.72A/B1-491[»]
4O0ZX-ray2.05A/B1-491[»]
4O10X-ray1.55A/B1-491[»]
4O12X-ray2.50A/B1-491[»]
4O13X-ray1.75A/B1-491[»]
4O14X-ray1.87A/B1-491[»]
4O15X-ray1.80A/B1-491[»]
4O16X-ray1.78A1-491[»]
4O17X-ray1.82A/B1-491[»]
4O18X-ray1.92A/B1-491[»]
4O19X-ray1.75A/B1-491[»]
4O1AX-ray1.87A/B1-491[»]
4O1BX-ray1.65A/B1-491[»]
4O1CX-ray2.09A/B1-491[»]
4O1DX-ray1.70A/B1-491[»]
4O28X-ray2.00A/B1-491[»]
4WQ6X-ray1.72A/B1-491[»]
5KITX-ray1.60A/B1-491[»]
ProteinModelPortaliP43490.
SMRiP43490.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43490.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni311 – 313Nicotinamide ribonucleotide binding3
Regioni353 – 354Nicotinamide ribonucleotide binding2

Sequence similaritiesi

Belongs to the NAPRTase family.Curated

Phylogenomic databases

eggNOGiENOG410IEB2. Eukaryota.
COG1488. LUCA.
GeneTreeiENSGT00390000006647.
HOGENOMiHOG000216546.
HOVERGENiHBG000336.
InParanoidiP43490.
KOiK03462.
OMAiKKFPITE.
OrthoDBiEOG091G04ZB.
PhylomeDBiP43490.
TreeFamiTF333530.

Family and domain databases

CDDicd01569. PBEF_like. 1 hit.
InterProiIPR007229. Nic_PRibTrfase-Fam.
IPR016471. Nicotinamide_PRibTrfase.
IPR002638. Quinolinate_PRibosylTrfase_C.
[Graphical view]
PANTHERiPTHR11098. PTHR11098. 1 hit.
PTHR11098:SF15. PTHR11098:SF15. 1 hit.
PfamiPF04095. NAPRTase. 1 hit.
[Graphical view]
PIRSFiPIRSF005943. NMPRT. 1 hit.
SUPFAMiSSF51690. SSF51690. 1 hit.

Sequencei

Sequence statusi: Complete.

P43490-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKLR
60 70 80 90 100
KVKYEETVFY GLQYILNKYL KGKVVTKEKI QEAKDVYKEH FQDDVFNEKG
110 120 130 140 150
WNYILEKYDG HLPIEIKAVP EGFVIPRGNV LFTVENTDPE CYWLTNWIET
160 170 180 190 200
ILVQSWYPIT VATNSREQKK ILAKYLLETS GNLDGLEYKL HDFGYRGVSS
210 220 230 240 250
QETAGIGASA HLVNFKGTDT VAGLALIKKY YGTKDPVPGY SVPAAEHSTI
260 270 280 290 300
TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV
310 320 330 340 350
SRSTQAPLII RPDSGNPLDT VLKVLEILGK KFPVTENSKG YKLLPPYLRV
360 370 380 390 400
IQGDGVDINT LQEIVEGMKQ KMWSIENIAF GSGGGLLQKL TRDLLNCSFK
410 420 430 440 450
CSYVVTNGLG INVFKDPVAD PNKRSKKGRL SLHRTPAGNF VTLEEGKGDL
460 470 480 490
EEYGQDLLHT VFKNGKVTKS YSFDEIRKNA QLNIELEAAH H
Length:491
Mass (Da):55,521
Last modified:November 1, 1995 - v1
Checksum:i6BF07B631B589AC0
GO

Sequence cautioni

The sequence AAQ96862 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAL24400 differs from that shown. Reason: Erroneous gene model prediction.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036614176L → S in a colorectal cancer sample; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02020 mRNA. Translation: AAA17884.1.
AK292851 mRNA. Translation: BAF85540.1.
AC007032 Genomic DNA. Translation: AAF19249.1.
AC007032 Genomic DNA. Translation: AAQ96862.1. Sequence problems.
CH236947 Genomic DNA. Translation: EAL24399.1.
CH236947 Genomic DNA. Translation: EAL24400.1. Sequence problems.
CH471070 Genomic DNA. Translation: EAW83382.1.
BC072439 mRNA. Translation: AAH72439.1.
BC106046 mRNA. Translation: AAI06047.1.
CCDSiCCDS5737.1.
PIRiA55927.
RefSeqiNP_005737.1. NM_005746.2.
XP_005250157.1. XM_005250100.2.
UniGeneiHs.489615.

Genome annotation databases

EnsembliENST00000222553; ENSP00000222553; ENSG00000105835.
GeneIDi10135.
KEGGihsa:10135.
UCSCiuc003vdq.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02020 mRNA. Translation: AAA17884.1.
AK292851 mRNA. Translation: BAF85540.1.
AC007032 Genomic DNA. Translation: AAF19249.1.
AC007032 Genomic DNA. Translation: AAQ96862.1. Sequence problems.
CH236947 Genomic DNA. Translation: EAL24399.1.
CH236947 Genomic DNA. Translation: EAL24400.1. Sequence problems.
CH471070 Genomic DNA. Translation: EAW83382.1.
BC072439 mRNA. Translation: AAH72439.1.
BC106046 mRNA. Translation: AAI06047.1.
CCDSiCCDS5737.1.
PIRiA55927.
RefSeqiNP_005737.1. NM_005746.2.
XP_005250157.1. XM_005250100.2.
UniGeneiHs.489615.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E5BX-ray2.00A/B1-491[»]
2E5CX-ray2.20A/B1-491[»]
2E5DX-ray2.00A/B1-491[»]
2GVGX-ray2.20A/B/C/D/E/F1-491[»]
2GVJX-ray2.10A/B1-491[»]
3DGRX-ray2.10A/B1-484[»]
3DHDX-ray2.00A/B1-484[»]
3DHFX-ray1.80A/B1-484[»]
3DKJX-ray2.00A/B1-484[»]
3DKLX-ray1.89A/B1-484[»]
4JNMX-ray2.20A/B1-491[»]
4JR5X-ray1.91A/B1-491[»]
4KFNX-ray1.60A/B1-491[»]
4KFOX-ray1.60A/B1-491[»]
4KFPX-ray1.84A/B1-491[»]
4L4LX-ray2.12A/B1-491[»]
4L4MX-ray2.44A/B1-491[»]
4LTSX-ray1.69A/B1-491[»]
4LV9X-ray1.81A/B1-491[»]
4LVAX-ray1.55A/B1-491[»]
4LVBX-ray1.84A/B1-491[»]
4LVDX-ray1.75A/B1-491[»]
4LVFX-ray1.50A/B1-491[»]
4LVGX-ray1.70A/B1-491[»]
4LWWX-ray1.64A/B1-491[»]
4M6PX-ray1.75A/B1-491[»]
4M6QX-ray2.41A/B1-491[»]
4N9BX-ray2.86A/B1-491[»]
4N9CX-ray1.75A/B1-491[»]
4N9DX-ray1.70A/B1-491[»]
4N9EX-ray1.72A/B1-491[»]
4O0ZX-ray2.05A/B1-491[»]
4O10X-ray1.55A/B1-491[»]
4O12X-ray2.50A/B1-491[»]
4O13X-ray1.75A/B1-491[»]
4O14X-ray1.87A/B1-491[»]
4O15X-ray1.80A/B1-491[»]
4O16X-ray1.78A1-491[»]
4O17X-ray1.82A/B1-491[»]
4O18X-ray1.92A/B1-491[»]
4O19X-ray1.75A/B1-491[»]
4O1AX-ray1.87A/B1-491[»]
4O1BX-ray1.65A/B1-491[»]
4O1CX-ray2.09A/B1-491[»]
4O1DX-ray1.70A/B1-491[»]
4O28X-ray2.00A/B1-491[»]
4WQ6X-ray1.72A/B1-491[»]
5KITX-ray1.60A/B1-491[»]
ProteinModelPortaliP43490.
SMRiP43490.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115438. 30 interactors.
DIPiDIP-29218N.
IntActiP43490. 11 interactors.
MINTiMINT-4530953.
STRINGi9606.ENSP00000222553.

Chemistry databases

BindingDBiP43490.
ChEMBLiCHEMBL1744525.

PTM databases

iPTMnetiP43490.
PhosphoSitePlusiP43490.
SwissPalmiP43490.

Polymorphism and mutation databases

BioMutaiNAMPT.
DMDMi1172027.

Proteomic databases

EPDiP43490.
MaxQBiP43490.
PaxDbiP43490.
PeptideAtlasiP43490.
PRIDEiP43490.

Protocols and materials databases

DNASUi10135.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000222553; ENSP00000222553; ENSG00000105835.
GeneIDi10135.
KEGGihsa:10135.
UCSCiuc003vdq.4. human.

Organism-specific databases

CTDi10135.
DisGeNETi10135.
GeneCardsiNAMPT.
HGNCiHGNC:30092. NAMPT.
HPAiCAB034349.
HPA047776.
HPA057722.
MIMi608764. gene.
neXtProtiNX_P43490.
OpenTargetsiENSG00000105835.
PharmGKBiPA162396933.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEB2. Eukaryota.
COG1488. LUCA.
GeneTreeiENSGT00390000006647.
HOGENOMiHOG000216546.
HOVERGENiHBG000336.
InParanoidiP43490.
KOiK03462.
OMAiKKFPITE.
OrthoDBiEOG091G04ZB.
PhylomeDBiP43490.
TreeFamiTF333530.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00890.
BioCyciZFISH:HS02817-MONOMER.
BRENDAi2.4.2.12. 2681.
ReactomeiR-HSA-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-HSA-197264. Nicotinamide salvaging.
SABIO-RKP43490.
SIGNORiP43490.

Miscellaneous databases

ChiTaRSiNAMPT. human.
EvolutionaryTraceiP43490.
GeneWikiiNicotinamide_phosphoribosyltransferase.
GenomeRNAii10135.
PROiP43490.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000105835.
CleanExiHS_NAMPT.
ExpressionAtlasiP43490. baseline and differential.
GenevisibleiP43490. HS.

Family and domain databases

CDDicd01569. PBEF_like. 1 hit.
InterProiIPR007229. Nic_PRibTrfase-Fam.
IPR016471. Nicotinamide_PRibTrfase.
IPR002638. Quinolinate_PRibosylTrfase_C.
[Graphical view]
PANTHERiPTHR11098. PTHR11098. 1 hit.
PTHR11098:SF15. PTHR11098:SF15. 1 hit.
PfamiPF04095. NAPRTase. 1 hit.
[Graphical view]
PIRSFiPIRSF005943. NMPRT. 1 hit.
SUPFAMiSSF51690. SSF51690. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNAMPT_HUMAN
AccessioniPrimary (citable) accession number: P43490
Secondary accession number(s): A4D0Q9
, A4D0R0, Q3KQV0, Q8WW95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 159 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.