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F5H830 (F5H830_HUMAN) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein names
Gene names
Name:PPARD Ensembl ENSP00000443759
OrganismHomo sapiens (Human) [Reference proteome] Ensembl ENSP00000443759
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Sequence similarities

Contains nuclear receptor DNA-binding domain. SAAS SAAS008946

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data. Ensembl ENSP00000443759

Ontologies

Keywords
   Biological processTranscription
Transcription regulation SAAS SAAS008946
   Cellular componentNucleus SAAS SAAS008946
   DomainZinc-finger SAAS SAAS008946
   LigandDNA-binding SAAS SAAS008946
Metal-binding
Zinc
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadipose tissue development

Inferred from electronic annotation. Source: Ensembl

anagen

Inferred from electronic annotation. Source: Ensembl

axon ensheathment

Inferred from electronic annotation. Source: Ensembl

cell differentiation

Inferred from electronic annotation. Source: Ensembl

cell-substrate adhesion

Inferred from electronic annotation. Source: Ensembl

decidualization

Inferred from electronic annotation. Source: Ensembl

embryo implantation

Inferred from electronic annotation. Source: Ensembl

fatty acid beta-oxidation

Inferred from electronic annotation. Source: Ensembl

fatty acid transport

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

keratinocyte migration

Inferred from electronic annotation. Source: Ensembl

keratinocyte proliferation

Inferred from electronic annotation. Source: Ensembl

mRNA transcription

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of collagen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

phospholipid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of epidermis development

Inferred from electronic annotation. Source: Ensembl

positive regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasodilation

Inferred from electronic annotation. Source: Ensembl

proteoglycan metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

response to activity

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to vitamin A

Inferred from electronic annotation. Source: Ensembl

vitamin A metabolic process

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionfatty acid binding

Inferred from electronic annotation. Source: Ensembl

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
F5H830 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: 824202A9F773E0FC

FASTA33838,786
        10         20         30         40         50         60 
MKLEYEKCER SCKIQKKNRN KCQYCRFQKC LALGMSHNAI RFGRMPEAEK RKLVAGLTAN 

        70         80         90        100        110        120 
EGSQYNPQVA DLKAFSKHIY NAYLKNFNMT KKKARSILTG KASHTAPFVI HDIETLWQAE 

       130        140        150        160        170        180 
KGLVWKQLVN GLPPYKEISV HVFYRCQCTT VETVRELTEF AKSIPSFSSL FLNDQVTLLK 

       190        200        210        220        230        240 
YGVHEAIFAM LASIVNKDGL LVANGSGFVT REFLRSLRKP FSDIIEPKFE FAVKFNALEL 

       250        260        270        280        290        300 
DDSDLALFIA AIILCGDRPG LMNVPRVEAI QDTILRALEF HLQANHPDAQ YLFPKLLQKM 

       310        320        330 
ADLRQLVTEH AQMMQRIKKT ETETSLHPLL QEIYKDMY 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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., 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].
[2]Ensembl
Submitted (JUL-2011) to UniProtKB
Cited for: IDENTIFICATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL022721 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortalF5H830.
SMRF5H830. Positions 1-338.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000540939; ENSP00000443759; ENSG00000112033.

Organism-specific databases

HGNCHGNC:9235. PPARD.
GenAtlasSearch...

Gene expression databases

ArrayExpressF5H830.
BgeeF5H830.

Family and domain databases

Gene3D1.10.565.10. 2 hits.
InterProIPR003074. 1Cnucl_rcpt.
IPR003075. 1Cnucl_rcpt_B.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR01288. PROXISOMEPAR.
PR01290. PROXISOMPABR.
PR00398. STRDHORMONER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPARD. human.
NextBio35509498.

Entry information

Entry nameF5H830_HUMAN
AccessionPrimary (citable) accession number: F5H830
Entry history
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: April 16, 2014
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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.