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UniProtKB - P14324 (FPPS_HUMAN)

Protein

Farnesyl pyrophosphate synthase

Gene

FDPS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+Note: Binds 3 Mg2+ ions per subunit.

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inactivated by interferon-induced RSAD2. This inactivation may result of disruption of lipid rafts at the plasma membrane, and thus have an antiviral effect since many enveloped viruses need lipid rafts to bud efficiently out of the cell.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: farnesyl diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Farnesyl pyrophosphate synthase (FDPS), Geranylgeranyl pyrophosphate synthase (GGPS1)
This subpathway is part of the pathway farnesyl diphosphate biosynthesis, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate, the pathway farnesyl diphosphate biosynthesis and in Isoprenoid biosynthesis.

Pathwayi: geranyl diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Farnesyl pyrophosphate synthase (FDPS), Geranylgeranyl pyrophosphate synthase (GGPS1)
This subpathway is part of the pathway geranyl diphosphate biosynthesis, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate, the pathway geranyl diphosphate biosynthesis and in Isoprenoid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei123Isopentenyl diphosphate1
Binding sitei126Isopentenyl diphosphate1
Binding sitei162Isopentenyl diphosphate1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei164Important for determining product chain lengthBy similarity1
Sitei165Important for determining product chain lengthBy similarity1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi169Magnesium 11
Metal bindingi169Magnesium 21
Metal bindingi173Magnesium 11
Metal bindingi173Magnesium 21
Binding sitei178Dimethylallyl diphosphate1
Binding sitei179Isopentenyl diphosphate1
Binding sitei266Dimethylallyl diphosphate1
Binding sitei267Dimethylallyl diphosphate1
Binding sitei306Dimethylallyl diphosphate1
Metal bindingi309Magnesium 31
Binding sitei323Dimethylallyl diphosphate1
Binding sitei332Dimethylallyl diphosphateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • dimethylallyltranstransferase activity Source: GO_Central
  • geranyltranstransferase activity Source: GO_Central
  • metal ion binding Source: UniProtKB-KW
  • RNA binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransferase
Biological processCholesterol biosynthesis, Cholesterol metabolism, Host-virus interaction, Isoprene biosynthesis, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:ENSG00000160752-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.5.1.10 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-191273 Cholesterol biosynthesis
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P14324

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi
UPA00259;UER00368

UPA00260;UER00369

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000001248
SLP:000001252 [P14324-2]

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Farnesyl pyrophosphate synthase (EC:2.5.1.10)
Short name:
FPP synthase
Short name:
FPS
Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase
Dimethylallyltranstransferase (EC:2.5.1.1)
Farnesyl diphosphate synthase
Geranyltranstransferase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FDPS
Synonyms:FPS, KIAA1293
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000160752.14

Human Gene Nomenclature Database

More...HGNCi		HGNC:3631 FDPS

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		134629 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P14324

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Porokeratosis 9, multiple types (POROK9)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of porokeratosis, a disorder of faulty keratinization characterized by one or more atrophic patches surrounded by a distinctive hyperkeratotic ridgelike border called the cornoid lamella. The keratotic lesions can progress to overt cutaneous neoplasms, typically squamous cell carcinomas. Multiple clinical variants of porokeratosis are recognized, including porokeratosis of Mibelli, linear porokeratosis, disseminated superficial actinic porokeratosis, palmoplantar porokeratosis, and punctate porokeratosis. Different clinical presentations can be observed among members of the same family. Individuals expressing more than one variant have also been reported.
See also OMIM:616631
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_075062179R → Q in POROK9. 1 PublicationCorresponds to variant dbSNP:rs863225241EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		2224

MalaCards human disease database

More...MalaCardsi		FDPS
MIMi616631 phenotype

Open Targets

More...OpenTargetsi		ENSG00000160752

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		79152 Disseminated superficial actinic porokeratosis

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA28075

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1782

Drug and drug target database

More...DrugBanki		DB00630 Alendronic acid
DB01785 Dimethylallyl Diphosphate
DB07780 FARNESYL DIPHOSPHATE
DB02552 Geranyl Diphosphate
DB07841 GERANYLGERANYL DIPHOSPHATE
DB00710 Ibandronate
DB04714 ISOPENTENYL PYROPHOSPHATE
DB02508 Isopentyl Pyrophosphate
DB00282 Pamidronate
DB00884 Risedronate
DB00399 Zoledronic acid

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		644

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		FDPS

Domain mapping of disease mutations (DMDM)

More...DMDMi		215274250

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001239441 – 419Farnesyl pyrophosphate synthaseAdd BLAST419

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei123N6-acetyllysineCombined sources1
Modified residuei353N6-acetyllysineCombined sources1
Isoform 2 (identifier: P14324-2)
Modified residuei1N-acetylmethionine1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P14324

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P14324

MaxQB - The MaxQuant DataBase

More...MaxQBi		P14324

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P14324

PeptideAtlas

More...PeptideAtlasi		P14324

PRoteomics IDEntifications database

More...PRIDEi		P14324

ProteomicsDB human proteome resource

More...ProteomicsDBi		53046

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P14324-1 [P14324-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P14324

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P14324

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P14324

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000160752 Expressed in 231 organ(s), highest expression level in right adrenal gland

CleanEx database of gene expression profiles

More...CleanExi		HS_FDPS

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P14324 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P14324 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA028200

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. Interacts with RSAD2.3 Publications
(Microbial infection) Interacts with HTLV-1 protein p13(II).1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108517, 85 interactors

Database of interacting proteins

More...DIPi		DIP-50059N

Protein interaction database and analysis system

More...IntActi		P14324, 12 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000349078

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P14324

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1419
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YQ7X-ray2.20A67-419[»]
1YV5X-ray2.00A67-419[»]
1ZW5X-ray2.30A67-419[»]
2F7MX-ray2.30F72-419[»]
2F89X-ray2.60F72-419[»]
2F8CX-ray2.20F72-419[»]
2F8ZX-ray2.60F72-419[»]
2F92X-ray2.15F72-419[»]
2F94X-ray1.94F72-419[»]
2F9KX-ray2.06F72-419[»]
2OPMX-ray2.40A67-419[»]
2OPNX-ray2.70A67-419[»]
2QISX-ray1.80A67-419[»]
2RAHX-ray2.00A67-419[»]
2VF6X-ray2.10A67-419[»]
3B7LX-ray1.95A67-419[»]
3CP6X-ray1.95A67-419[»]
3N1VX-ray2.18F72-419[»]
3N1WX-ray2.56F72-419[»]
3N3LX-ray2.74F72-419[»]
3N45X-ray1.88F72-419[»]
3N46X-ray2.35F72-419[»]
3N49X-ray2.50F72-419[»]
3N5HX-ray2.20F72-419[»]
3N5JX-ray2.35F72-419[»]
3N6KX-ray2.25F72-419[»]
3RYEX-ray2.10A71-419[»]
3S4JX-ray1.95A71-419[»]
4DEMX-ray1.85F67-419[»]
4GA3X-ray2.39A72-419[»]
4H5CX-ray2.02F67-419[»]
4H5DX-ray2.02F67-419[»]
4H5EX-ray2.04F67-419[»]
4JVJX-ray2.80F67-419[»]
4KFAX-ray1.98A67-419[»]
4KPDX-ray1.96A67-419[»]
4KPJX-ray1.95A67-419[»]
4KQ5X-ray2.40A67-419[»]
4KQSX-ray1.97A67-419[»]
4KQUX-ray2.07A67-419[»]
4L2XX-ray2.55F67-419[»]
4LFVX-ray2.00F67-419[»]
4LPGX-ray2.35F67-419[»]
4LPHX-ray2.30F67-419[»]
4N1ZX-ray2.35F72-419[»]
4N9UX-ray2.11A67-419[»]
4NFIX-ray1.85F67-419[»]
4NFJX-ray2.05F67-419[»]
4NFKX-ray1.85F67-419[»]
4NG6X-ray2.35A67-419[»]
4NKEX-ray1.46A67-419[»]
4NKFX-ray2.00A67-419[»]
4NUAX-ray1.43A67-419[»]
4OGUX-ray2.10A67-419[»]
4P0VX-ray2.40A73-419[»]
4P0WX-ray2.41A72-419[»]
4P0XX-ray2.50A72-419[»]
4PVXX-ray2.18F67-419[»]
4PVYX-ray2.05F67-419[»]
4Q23X-ray1.98A67-419[»]
4QPFX-ray1.59A67-419[»]
4QXSX-ray1.90F67-419[»]
4RXAX-ray2.20A72-419[»]
4XQRX-ray2.15F67-419[»]
4XQSX-ray2.30F67-419[»]
4XQTX-ray2.10F67-419[»]
5CG5Other1.40A74-419[»]
5CG6Other1.70A74-419[»]
5DGMX-ray2.86F72-419[»]
5DGNX-ray2.08F72-419[»]
5DGSX-ray2.62F72-419[»]
5DIQX-ray2.10F72-419[»]
5DJPX-ray2.40F72-419[»]
5DJRX-ray2.40F72-419[»]
5DJVX-ray2.30F72-419[»]
5JA0X-ray1.90F67-419[»]
5JUZX-ray2.40F67-419[»]
5JV0X-ray2.40F67-419[»]
5JV1X-ray2.30F67-419[»]
5JV2X-ray2.30F67-419[»]
5KSXX-ray2.65F67-419[»]
5YGIX-ray2.18A72-419[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P14324

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P14324

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P14324

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the FPP/GGPP synthase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0711 Eukaryota
COG0142 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00900000141074

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000160912

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG005741

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P14324

KEGG Orthology (KO)

More...KOi		K00787

Identification of Orthologs from Complete Genome Data

More...OMAi		KHSFIVI

Database of Orthologous Groups

More...OrthoDBi		1066656at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P14324

TreeFam database of animal gene trees

More...TreeFami		TF300897

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.600.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR008949 Isoprenoid_synthase_dom_sf
IPR000092 Polyprenyl_synt
IPR033749 Polyprenyl_synt_CS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00348 polyprenyl_synt, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48576 SSF48576, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00723 POLYPRENYL_SYNTHASE_1, 1 hit
PS00444 POLYPRENYL_SYNTHASE_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P14324-1) [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
MPLSRWLRSV GVFLLPAPYW APRERWLGSL RRPSLVHGYP VLAWHSARCW 
        60         70         80         90        100
CQAWTEEPRA LCSSLRMNGD QNSDVYAQEK QDFVQHFSQI VRVLTEDEMG 
       110        120        130        140        150
HPEIGDAIAR LKEVLEYNAI GGKYNRGLTV VVAFRELVEP RKQDADSLQR 
       160        170        180        190        200
AWTVGWCVEL LQAFFLVADD IMDSSLTRRG QICWYQKPGV GLDAINDANL 
       210        220        230        240        250
LEACIYRLLK LYCREQPYYL NLIELFLQSS YQTEIGQTLD LLTAPQGNVD 
       260        270        280        290        300
LVRFTEKRYK SIVKYKTAFY SFYLPIAAAM YMAGIDGEKE HANAKKILLE 
       310        320        330        340        350
MGEFFQIQDD YLDLFGDPSV TGKIGTDIQD NKCSWLVVQC LQRATPEQYQ 
       360        370        380        390        400
ILKENYGQKE AEKVARVKAL YEELDLPAVF LQYEEDSYSH IMALIEQYAA 
       410 
PLPPAVFLGL ARKIYKRRK
Length:419
Mass (Da):48,275
Last modified:November 25, 2008 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i52934B80A808FB67
GO
Isoform 2 (identifier: P14324-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.

Show »
Length:353
Mass (Da):40,532
Checksum:i15B19F2A5C51B166
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WVN4A0A087WVN4_HUMAN
Farnesyl pyrophosphate synthase
FDPS
274Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087X1D8A0A087X1D8_HUMAN
Farnesyl pyrophosphate synthase
FDPS
174Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087X090A0A087X090_HUMAN
Farnesyl diphosphate synthase (Farn...
FDPS hCG_1997329
248Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WTP2A0A087WTP2_HUMAN
Farnesyl pyrophosphate synthase
FDPS
80Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA03523 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti141R → K in BQ062616 (Ref. 7) Curated1
Sequence conflicti182I → T in AAA52423 (PubMed:1968462).Curated1
Sequence conflicti284G → R in BQ062616 (Ref. 7) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075062179R → Q in POROK9. 1 PublicationCorresponds to variant dbSNP:rs863225241EnsemblClinVar.1
Natural variantiVAR_061274364V → A. Corresponds to variant dbSNP:rs41314549Ensembl.1
Natural variantiVAR_049644391I → V. Corresponds to variant dbSNP:rs17456Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0469581 – 66Missing in isoform 2. 2 PublicationsAdd BLAST66

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
J05262 mRNA Translation: AAA52423.1
D14697 mRNA Translation: BAA03523.2 Different initiation.
AK291084 mRNA Translation: BAF83773.1
AL139410 Genomic DNA No translation available.
CH471121 Genomic DNA Translation: EAW53076.1
CH471121 Genomic DNA Translation: EAW53077.1
CH471121 Genomic DNA Translation: EAW53078.1
BC010004 mRNA Translation: AAH10004.1
BQ062616 mRNA No translation available.
M29863 mRNA Translation: AAA35820.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS1110.1 [P14324-1]
CCDS44241.1 [P14324-2]

Protein sequence database of the Protein Information Resource

More...PIRi		A35726

NCBI Reference Sequences

More...RefSeqi		NP_001129293.1, NM_001135821.1 [P14324-1]
NP_001129294.1, NM_001135822.1 [P14324-2]
NP_001229753.1, NM_001242824.1 [P14324-2]
NP_001229754.1, NM_001242825.1
NP_001995.1, NM_002004.3 [P14324-1]
XP_005245019.1, XM_005244962.1 [P14324-2]
XP_005245020.1, XM_005244963.1 [P14324-2]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.335918

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000356657; ENSP00000349078; ENSG00000160752 [P14324-1]
ENST00000368356; ENSP00000357340; ENSG00000160752 [P14324-1]
ENST00000447866; ENSP00000391755; ENSG00000160752 [P14324-2]
ENST00000467076; ENSP00000480142; ENSG00000160752 [P14324-2]
ENST00000612683; ENSP00000478235; ENSG00000160752 [P14324-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2224

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2224

UCSC genome browser

More...UCSCi		uc001fkc.3 human [P14324-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05262 mRNA Translation: AAA52423.1
D14697 mRNA Translation: BAA03523.2 Different initiation.
AK291084 mRNA Translation: BAF83773.1
AL139410 Genomic DNA No translation available.
CH471121 Genomic DNA Translation: EAW53076.1
CH471121 Genomic DNA Translation: EAW53077.1
CH471121 Genomic DNA Translation: EAW53078.1
BC010004 mRNA Translation: AAH10004.1
BQ062616 mRNA No translation available.
M29863 mRNA Translation: AAA35820.1
CCDSiCCDS1110.1 [P14324-1]
CCDS44241.1 [P14324-2]
PIRiA35726
RefSeqiNP_001129293.1, NM_001135821.1 [P14324-1]
NP_001129294.1, NM_001135822.1 [P14324-2]
NP_001229753.1, NM_001242824.1 [P14324-2]
NP_001229754.1, NM_001242825.1
NP_001995.1, NM_002004.3 [P14324-1]
XP_005245019.1, XM_005244962.1 [P14324-2]
XP_005245020.1, XM_005244963.1 [P14324-2]
UniGeneiHs.335918

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YQ7X-ray2.20A67-419[»]
1YV5X-ray2.00A67-419[»]
1ZW5X-ray2.30A67-419[»]
2F7MX-ray2.30F72-419[»]
2F89X-ray2.60F72-419[»]
2F8CX-ray2.20F72-419[»]
2F8ZX-ray2.60F72-419[»]
2F92X-ray2.15F72-419[»]
2F94X-ray1.94F72-419[»]
2F9KX-ray2.06F72-419[»]
2OPMX-ray2.40A67-419[»]
2OPNX-ray2.70A67-419[»]
2QISX-ray1.80A67-419[»]
2RAHX-ray2.00A67-419[»]
2VF6X-ray2.10A67-419[»]
3B7LX-ray1.95A67-419[»]
3CP6X-ray1.95A67-419[»]
3N1VX-ray2.18F72-419[»]
3N1WX-ray2.56F72-419[»]
3N3LX-ray2.74F72-419[»]
3N45X-ray1.88F72-419[»]
3N46X-ray2.35F72-419[»]
3N49X-ray2.50F72-419[»]
3N5HX-ray2.20F72-419[»]
3N5JX-ray2.35F72-419[»]
3N6KX-ray2.25F72-419[»]
3RYEX-ray2.10A71-419[»]
3S4JX-ray1.95A71-419[»]
4DEMX-ray1.85F67-419[»]
4GA3X-ray2.39A72-419[»]
4H5CX-ray2.02F67-419[»]
4H5DX-ray2.02F67-419[»]
4H5EX-ray2.04F67-419[»]
4JVJX-ray2.80F67-419[»]
4KFAX-ray1.98A67-419[»]
4KPDX-ray1.96A67-419[»]
4KPJX-ray1.95A67-419[»]
4KQ5X-ray2.40A67-419[»]
4KQSX-ray1.97A67-419[»]
4KQUX-ray2.07A67-419[»]
4L2XX-ray2.55F67-419[»]
4LFVX-ray2.00F67-419[»]
4LPGX-ray2.35F67-419[»]
4LPHX-ray2.30F67-419[»]
4N1ZX-ray2.35F72-419[»]
4N9UX-ray2.11A67-419[»]
4NFIX-ray1.85F67-419[»]
4NFJX-ray2.05F67-419[»]
4NFKX-ray1.85F67-419[»]
4NG6X-ray2.35A67-419[»]
4NKEX-ray1.46A67-419[»]
4NKFX-ray2.00A67-419[»]
4NUAX-ray1.43A67-419[»]
4OGUX-ray2.10A67-419[»]
4P0VX-ray2.40A73-419[»]
4P0WX-ray2.41A72-419[»]
4P0XX-ray2.50A72-419[»]
4PVXX-ray2.18F67-419[»]
4PVYX-ray2.05F67-419[»]
4Q23X-ray1.98A67-419[»]
4QPFX-ray1.59A67-419[»]
4QXSX-ray1.90F67-419[»]
4RXAX-ray2.20A72-419[»]
4XQRX-ray2.15F67-419[»]
4XQSX-ray2.30F67-419[»]
4XQTX-ray2.10F67-419[»]
5CG5Other1.40A74-419[»]
5CG6Other1.70A74-419[»]
5DGMX-ray2.86F72-419[»]
5DGNX-ray2.08F72-419[»]
5DGSX-ray2.62F72-419[»]
5DIQX-ray2.10F72-419[»]
5DJPX-ray2.40F72-419[»]
5DJRX-ray2.40F72-419[»]
5DJVX-ray2.30F72-419[»]
5JA0X-ray1.90F67-419[»]
5JUZX-ray2.40F67-419[»]
5JV0X-ray2.40F67-419[»]
5JV1X-ray2.30F67-419[»]
5JV2X-ray2.30F67-419[»]
5KSXX-ray2.65F67-419[»]
5YGIX-ray2.18A72-419[»]
ProteinModelPortaliP14324
SMRiP14324
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108517, 85 interactors
DIPiDIP-50059N
IntActiP14324, 12 interactors
STRINGi9606.ENSP00000349078

Chemistry databases

BindingDBiP14324
ChEMBLiCHEMBL1782
DrugBankiDB00630 Alendronic acid
DB01785 Dimethylallyl Diphosphate
DB07780 FARNESYL DIPHOSPHATE
DB02552 Geranyl Diphosphate
DB07841 GERANYLGERANYL DIPHOSPHATE
DB00710 Ibandronate
DB04714 ISOPENTENYL PYROPHOSPHATE
DB02508 Isopentyl Pyrophosphate
DB00282 Pamidronate
DB00884 Risedronate
DB00399 Zoledronic acid
GuidetoPHARMACOLOGYi644
SwissLipidsiSLP:000001248
SLP:000001252 [P14324-2]

PTM databases

iPTMnetiP14324
PhosphoSitePlusiP14324
SwissPalmiP14324

Polymorphism and mutation databases

BioMutaiFDPS
DMDMi215274250

Proteomic databases

EPDiP14324
jPOSTiP14324
MaxQBiP14324
PaxDbiP14324
PeptideAtlasiP14324
PRIDEiP14324
ProteomicsDBi53046
TopDownProteomicsiP14324-1 [P14324-1]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		2224
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356657; ENSP00000349078; ENSG00000160752 [P14324-1]
ENST00000368356; ENSP00000357340; ENSG00000160752 [P14324-1]
ENST00000447866; ENSP00000391755; ENSG00000160752 [P14324-2]
ENST00000467076; ENSP00000480142; ENSG00000160752 [P14324-2]
ENST00000612683; ENSP00000478235; ENSG00000160752 [P14324-2]
GeneIDi2224
KEGGihsa:2224
UCSCiuc001fkc.3 human [P14324-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2224
DisGeNETi2224
EuPathDBiHostDB:ENSG00000160752.14

GeneCards: human genes, protein and diseases

More...GeneCardsi		FDPS

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0025342
HGNCiHGNC:3631 FDPS
HPAiHPA028200
MalaCardsiFDPS
MIMi134629 gene
616631 phenotype
neXtProtiNX_P14324
OpenTargetsiENSG00000160752
Orphaneti79152 Disseminated superficial actinic porokeratosis
PharmGKBiPA28075

Human Unidentified Gene-Encoded large proteins database

More...HUGEi		Search...

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0711 Eukaryota
COG0142 LUCA
GeneTreeiENSGT00900000141074
HOGENOMiHOG000160912
HOVERGENiHBG005741
InParanoidiP14324
KOiK00787
OMAiKHSFIVI
OrthoDBi1066656at2759
PhylomeDBiP14324
TreeFamiTF300897

Enzyme and pathway databases

UniPathwayi
UPA00259;UER00368

UPA00260;UER00369

BioCyciMetaCyc:ENSG00000160752-MONOMER
BRENDAi2.5.1.10 2681
ReactomeiR-HSA-191273 Cholesterol biosynthesis
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
SABIO-RKiP14324

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		FDPS human
EvolutionaryTraceiP14324

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		2224

Protein Ontology

More...PROi		PR:P14324

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000160752 Expressed in 231 organ(s), highest expression level in right adrenal gland
CleanExiHS_FDPS
ExpressionAtlasiP14324 baseline and differential
GenevisibleiP14324 HS

Family and domain databases

Gene3Di1.10.600.10, 1 hit
InterProiView protein in InterPro
IPR008949 Isoprenoid_synthase_dom_sf
IPR000092 Polyprenyl_synt
IPR033749 Polyprenyl_synt_CS
PfamiView protein in Pfam
PF00348 polyprenyl_synt, 1 hit
SUPFAMiSSF48576 SSF48576, 1 hit
PROSITEiView protein in PROSITE
PS00723 POLYPRENYL_SYNTHASE_1, 1 hit
PS00444 POLYPRENYL_SYNTHASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFPPS_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P14324
Secondary accession number(s): D3DV91, E9PCI9, Q96G29
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 25, 2008
Last modified: January 16, 2019
This is version 211 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
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