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Protein

Peroxisomal biogenesis factor 3

Gene

PEX3

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

Functioni

Involved in peroxisome biosynthesis and integrity. Assembles membrane vesicles before the matrix proteins are translocated. As a docking factor for PEX19, is necessary for the import of peroxisomal membrane proteins in the peroxisomes.2 Publications

GO - Molecular functioni

  1. amino acid transmembrane transporter activity Source: GO_Central
  2. lipid binding Source: UniProtKB
  3. protein dimerization activity Source: UniProtKB

GO - Biological processi

  1. amino acid transmembrane transport Source: GO_Central
  2. peroxisome membrane biogenesis Source: Ensembl
  3. peroxisome organization Source: UniProtKB
  4. protein import into peroxisome membrane Source: UniProtKB
  5. regulation of mitochondrion degradation Source: ParkinsonsUK-UCL
  6. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Peroxisome biogenesis

Enzyme and pathway databases

ReactomeiREACT_111158. ABCA transporters in lipid homeostasis.

Protein family/group databases

TCDBi9.A.17.1.2. the integral membrane peroxisomal protein importer-2 (ppi2) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal biogenesis factor 3
Alternative name(s):
Peroxin-3
Peroxisomal assembly protein PEX3
Gene namesi
Name:PEX3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:8858. PEX3.

Subcellular locationi

  1. Peroxisome membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei16 – 3621HelicalSequence AnalysisAdd
BLAST
Topological domaini37 – 11680PeroxisomalSequence AnalysisAdd
BLAST
Transmembranei117 – 14024HelicalSequence AnalysisAdd
BLAST
Topological domaini141 – 373233CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. endoplasmic reticulum Source: UniProtKB
  3. integral component of peroxisomal membrane Source: UniProtKB
  4. intracellular membrane-bounded organelle Source: HPA
  5. membrane Source: UniProtKB
  6. nucleoplasm Source: HPA
  7. peroxisomal membrane Source: UniProtKB
  8. peroxisome Source: UniProtKB
  9. protein complex Source: UniProtKB
  10. protein-lipid complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Peroxisome

Pathology & Biotechi

Involvement in diseasei

Peroxisome biogenesis disorder complementation group 12 (PBD-CG12)

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA peroxisomal disorder arising from a failure of protein import into the peroxisomal membrane or matrix. The peroxisome biogenesis disorders (PBD group) are genetically heterogeneous with at least 14 distinct genetic groups as concluded from complementation studies. Include disorders are: Zellweger syndrome (ZWS), neonatal adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and IRD are distinct from RCDP and constitute a clinical continuum of overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS).

See also OMIM:614882
Peroxisome biogenesis disorder 10A (PBD10A)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and clinically characterized by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life.

See also OMIM:614882
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti138 – 1381G → E in PBD10A. 1 Publication
VAR_009304

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi125 – 1251L → P: Abolishes binding to PEX19 without affecting targeting to peroxisomes; when associated with D-134. 1 Publication
Mutagenesisi134 – 1341N → D: Abolishes binding to PEX19 without affecting targeting to peroxisomes; when associated with P-125. 1 Publication

Keywords - Diseasei

Disease mutation, Peroxisome biogenesis disorder, Zellweger syndrome

Organism-specific databases

MIMi614882. phenotype.
Orphaneti772. Infantile Refsum disease.
44. Neonatal adrenoleukodystrophy.
912. Zellweger syndrome.
PharmGKBiPA33200.

Polymorphism and mutation databases

BioMutaiPEX3.
DMDMi3914303.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 373373Peroxisomal biogenesis factor 3PRO_0000208737Add
BLAST

Proteomic databases

MaxQBiP56589.
PaxDbiP56589.
PeptideAtlasiP56589.
PRIDEiP56589.

PTM databases

PhosphoSiteiP56589.

Expressioni

Tissue specificityi

Found in all examined tissues.

Gene expression databases

BgeeiP56589.
CleanExiHS_PEX3.
ExpressionAtlasiP56589. baseline and differential.
GenevestigatoriP56589.

Organism-specific databases

HPAiHPA042830.
HPA058006.

Interactioni

Subunit structurei

Interacts with PEX19.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PEX19P4085523EBI-594885,EBI-594747

Protein-protein interaction databases

BioGridi114076. 9 interactions.
IntActiP56589. 4 interactions.
MINTiMINT-241504.
STRINGi9606.ENSP00000356563.

Structurei

Secondary structure

1
373
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi41 – 8343Combined sources
Helixi86 – 938Combined sources
Helixi100 – 14243Combined sources
Beta strandi147 – 1515Combined sources
Helixi158 – 1658Combined sources
Helixi166 – 1683Combined sources
Helixi169 – 1724Combined sources
Helixi174 – 19118Combined sources
Beta strandi199 – 2013Combined sources
Helixi202 – 21716Combined sources
Helixi234 – 2374Combined sources
Helixi246 – 2483Combined sources
Helixi255 – 27117Combined sources
Helixi274 – 29623Combined sources
Beta strandi319 – 3213Combined sources
Helixi322 – 3309Combined sources
Helixi333 – 3364Combined sources
Turni339 – 3413Combined sources
Helixi344 – 3496Combined sources
Helixi352 – 36615Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AJBX-ray2.50A49-373[»]
3MK4X-ray2.42A41-373[»]
ProteinModelPortaliP56589.
SMRiP56589. Positions 52-368.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56589.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4545Targeting to peroxisomesAdd
BLAST
Regioni120 – 13617Interaction with PEX19Add
BLAST

Sequence similaritiesi

Belongs to the peroxin-3 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG259038.
GeneTreeiENSGT00390000008481.
HOGENOMiHOG000007212.
HOVERGENiHBG000467.
InParanoidiP56589.
KOiK13336.
OMAiARRQFHF.
OrthoDBiEOG71ZP1Q.
PhylomeDBiP56589.
TreeFamiTF352826.

Family and domain databases

InterProiIPR006966. Peroxin-3.
[Graphical view]
PfamiPF04882. Peroxin-3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56589-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRSVWNFLK RHKKKCIFLG TVLGGVYILG KYGQKKIREI QEREAAEYIA
60 70 80 90 100
QARRQYHFES NQRTCNMTVL SMLPTLREAL MQQLNSESLT ALLKNRPSNK
110 120 130 140 150
LEIWEDLKII SFTRSTVAVY STCMLVVLLR VQLNIIGGYI YLDNAAVGKN
160 170 180 190 200
GTTILAPPDV QQQYLSSIQH LLGDGLTELI TVIKQAVQKV LGSVSLKHSL
210 220 230 240 250
SLLDLEQKLK EIRNLVEQHK SSSWINKDGS KPLLCHYMMP DEETPLAVQA
260 270 280 290 300
CGLSPRDITT IKLLNETRDM LESPDFSTVL NTCLNRGFSR LLDNMAEFFR
310 320 330 340 350
PTEQDLQHGN SMNSLSSVSL PLAKIIPIVN GQIHSVCSET PSHFVQDLLT
360 370
MEQVKDFAAN VYEAFSTPQQ LEK
Length:373
Mass (Da):42,140
Last modified:December 15, 1998 - v1
Checksum:i3515A1F29656B7CC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti82 – 821Q → R.
Corresponds to variant rs35220041 [ dbSNP | Ensembl ].
VAR_053572
Natural varianti138 – 1381G → E in PBD10A. 1 Publication
VAR_009304

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001625 mRNA. Translation: CAA04879.1.
AJ131389 mRNA. Translation: CAA10362.1.
AJ009866
, AJ009867, AJ009868, AJ009869, AJ009870, AJ009871, AJ009872, AJ009873, AJ009874 Genomic DNA. Translation: CAA08904.1.
AB035307 mRNA. Translation: BAA97993.1.
AY277600 mRNA. Translation: AAQ18039.1.
CR542062 mRNA. Translation: CAG46859.1.
AL031320 Genomic DNA. Translation: CAB53744.1.
CH471051 Genomic DNA. Translation: EAW47866.1.
BC014551 mRNA. Translation: AAH14551.1.
BC015506 mRNA. Translation: AAH15506.1.
CCDSiCCDS5199.1.
RefSeqiNP_003621.1. NM_003630.2.
UniGeneiHs.592832.
Hs.7277.

Genome annotation databases

EnsembliENST00000367591; ENSP00000356563; ENSG00000034693.
GeneIDi8504.
KEGGihsa:8504.
UCSCiuc003qjl.3. human.

Polymorphism and mutation databases

BioMutaiPEX3.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001625 mRNA. Translation: CAA04879.1.
AJ131389 mRNA. Translation: CAA10362.1.
AJ009866
, AJ009867, AJ009868, AJ009869, AJ009870, AJ009871, AJ009872, AJ009873, AJ009874 Genomic DNA. Translation: CAA08904.1.
AB035307 mRNA. Translation: BAA97993.1.
AY277600 mRNA. Translation: AAQ18039.1.
CR542062 mRNA. Translation: CAG46859.1.
AL031320 Genomic DNA. Translation: CAB53744.1.
CH471051 Genomic DNA. Translation: EAW47866.1.
BC014551 mRNA. Translation: AAH14551.1.
BC015506 mRNA. Translation: AAH15506.1.
CCDSiCCDS5199.1.
RefSeqiNP_003621.1. NM_003630.2.
UniGeneiHs.592832.
Hs.7277.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AJBX-ray2.50A49-373[»]
3MK4X-ray2.42A41-373[»]
ProteinModelPortaliP56589.
SMRiP56589. Positions 52-368.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114076. 9 interactions.
IntActiP56589. 4 interactions.
MINTiMINT-241504.
STRINGi9606.ENSP00000356563.

Protein family/group databases

TCDBi9.A.17.1.2. the integral membrane peroxisomal protein importer-2 (ppi2) family.

PTM databases

PhosphoSiteiP56589.

Polymorphism and mutation databases

BioMutaiPEX3.
DMDMi3914303.

Proteomic databases

MaxQBiP56589.
PaxDbiP56589.
PeptideAtlasiP56589.
PRIDEiP56589.

Protocols and materials databases

DNASUi8504.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367591; ENSP00000356563; ENSG00000034693.
GeneIDi8504.
KEGGihsa:8504.
UCSCiuc003qjl.3. human.

Organism-specific databases

CTDi8504.
GeneCardsiGC06P143772.
GeneReviewsiPEX3.
HGNCiHGNC:8858. PEX3.
HPAiHPA042830.
HPA058006.
MIMi603164. gene.
614882. phenotype.
neXtProtiNX_P56589.
Orphaneti772. Infantile Refsum disease.
44. Neonatal adrenoleukodystrophy.
912. Zellweger syndrome.
PharmGKBiPA33200.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG259038.
GeneTreeiENSGT00390000008481.
HOGENOMiHOG000007212.
HOVERGENiHBG000467.
InParanoidiP56589.
KOiK13336.
OMAiARRQFHF.
OrthoDBiEOG71ZP1Q.
PhylomeDBiP56589.
TreeFamiTF352826.

Enzyme and pathway databases

ReactomeiREACT_111158. ABCA transporters in lipid homeostasis.

Miscellaneous databases

EvolutionaryTraceiP56589.
GeneWikiiPEX3.
GenomeRNAii8504.
NextBioi31825.
PROiP56589.
SOURCEiSearch...

Gene expression databases

BgeeiP56589.
CleanExiHS_PEX3.
ExpressionAtlasiP56589. baseline and differential.
GenevestigatoriP56589.

Family and domain databases

InterProiIPR006966. Peroxin-3.
[Graphical view]
PfamiPF04882. Peroxin-3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the gene encoding the human peroxisomal assembly protein Pex3p."
    Kammerer S., Holzinger A., Welsch U., Roscher A.A.
    FEBS Lett. 429:53-60(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Identification and characterization of the human peroxin PEX3."
    Soukupova M., Sprenger C., Gorgas K., Kunau W.H., Dodt G.
    Eur. J. Cell Biol. 78:357-374(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The human PEX3 gene encoding a peroxisomal assembly protein: genomic organization, positional mapping, and mutation analysis in candidate phenotypes."
    Muntau A.C., Holzinger A., Mayerhofer P.U., Gartner J., Roscher A.A., Kammerer S.
    Biochem. Biophys. Res. Commun. 268:704-710(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The peroxin pex3p initiates membrane assembly in peroxisome biogenesis."
    Ghaedi K., Tamura S., Okumoto K., Matsuzono Y., Fujiki Y.
    Mol. Biol. Cell 11:2085-2102(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CHARACTERIZATION, VARIANT PBD10A GLU-138.
    Tissue: Liver.
  5. "Identification of a human transforming gene."
    Kim J.W.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skin and Uterus.
  10. "PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis."
    Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., Gould S.J.
    J. Cell Biol. 148:931-944(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PEX19.
  11. "Human pex19p binds peroxisomal integral membrane proteins at regions distinct from their sorting sequences."
    Fransen M., Wylin T., Brees C., Mannaerts G.P., Van Veldhoven P.P.
    Mol. Cell. Biol. 21:4413-4424(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PEX19, SUBCELLULAR LOCATION.
  12. "PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins."
    Fang Y., Morrell J.C., Jones J.M., Gould S.J.
    J. Cell Biol. 164:863-875(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LEU-125 AND ASN-134.
  13. "Defective peroxisome membrane synthesis due to mutations in human PEX3 causes Zellweger syndrome, complementation group G."
    Muntau A.C., Mayerhofer P.U., Paton B.C., Kammerer S., Roscher A.A.
    Am. J. Hum. Genet. 67:967-975(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN PBD-CG12 AND PBD10A.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Structural basis for docking of peroxisomal membrane protein carrier Pex19p onto its receptor Pex3p."
    Sato Y., Shibata H., Nakatsu T., Nakano H., Kashiwayama Y., Imanaka T., Kato H.
    EMBO J. 29:4083-4093(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 49-373 IN COMPLEX WITH PEX19, SUBUNIT.
  16. "Insights into peroxisome function from the structure of PEX3 in complex with a soluble fragment of PEX19."
    Schmidt F., Treiber N., Zocher G., Bjelic S., Steinmetz M.O., Kalbacher H., Stehle T., Dodt G.
    J. Biol. Chem. 285:25410-25417(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 41-373 IN COMPLEX WITH PEX19, SUBUNIT.

Entry informationi

Entry nameiPEX3_HUMAN
AccessioniPrimary (citable) accession number: P56589
Secondary accession number(s): Q6FGP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: April 29, 2015
This is version 134 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 6
    Human chromosome 6: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.