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Q6NT89 (TRNP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TMF-regulated nuclear protein 1
Gene names
Name:TRNP1
Synonyms:C1orf225, TRNP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

DNA-binding factor that regulates the expression of a subset of genes and plays a key role in tangential, radial, and lateral expansion of the brain neocortex. Regulates neural stem cells proliferation and the production of intermediate neural progenitors and basal radial glial cells affecting the process of cerebral cortex gyrification. May control the proliferation rate of cells by regulating their progression through key cell-cycle transition points By similarity.

Subunit structure

Interacts with TMF1; may regulate TRNP1 proteasomal degradation By similarity.

Subcellular location

Nucleus By similarity.

Developmental stage

Expression is detected in the ventricular zone and neuronal layers of the developing cerebral cortex at 12, 18 and 21 gestation weeks. Differences in regional expression seem to correlate with the process of gyrification of the cortex. Highly expressed in germinal layers of the precentral and parahippocampal gyri, that exhibit little radial expansion and folding, and weakly expressed in germinal layers of the occipital and temporal lobes, that undergo greater expansion and folding. Ref.3

Post-translational modification

Ubiquitinated, leading to its degradation by the proteasome By similarity.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 227227TMF-regulated nuclear protein 1
PRO_0000336088

Regions

Compositional bias23 – 5533Pro-rich

Natural variations

Natural variant271W → R. Ref.2
Corresponds to variant rs6689941 [ dbSNP | Ensembl ].
VAR_043545

Sequences

Sequence LengthMass (Da)Tools
Q6NT89 [UniParc].

Last modified March 3, 2009. Version 2.
Checksum: 01FBA6DC86CCD7CA

FASTA22723,482
        10         20         30         40         50         60 
MPGCRISACG PGAQEGTAEQ RSPPPPWDPM PSSQPPPPTP TLTPTPTPGQ SPPLPDAAGA 

        70         80         90        100        110        120 
SAGAAEDQEL QRWRQGASGI AGLAGPGGGS GAAAGAGGRA LELAEARRRL LEVEGRRRLV 

       130        140        150        160        170        180 
SELESRVLQL HRVFLAAELR LAHRAESLSR LSGGVAQAEL YLAAHGSRLK KGPRRGRRGR 

       190        200        210        220 
PPALLASALG LGGCVPWGAG RLRRGHGPEP DSPFRRSPPR GPASPQR 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"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], VARIANT ARG-27.
Tissue: Eye.
[3]"Trnp1 regulates expansion and folding of the mammalian cerebral cortex by control of radial glial fate."
Stahl R., Walcher T., De Juan Romero C., Pilz G.A., Cappello S., Irmler M., Sanz-Aquela J.M., Beckers J., Blum R., Borrell V., Goetz M.
Cell 153:535-549(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.

Web resources

Protein Spotlight

the geometry of intelligence - Issue 152 of August 2013

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL356390 Genomic DNA. No translation available.
BC069216 mRNA. Translation: AAH69216.1.
RefSeqNP_001013664.1. NM_001013642.2.
XP_005245924.1. XM_005245867.1.
UniGeneHs.355747.

3D structure databases

ProteinModelPortalQ6NT89.
SMRQ6NT89. Positions 96-174.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ6NT89.

Polymorphism databases

DMDM224471860.

Proteomic databases

PRIDEQ6NT89.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000522111; ENSP00000429216; ENSG00000253368.
GeneID388610.
KEGGhsa:388610.
UCSCuc001bnj.4. human.

Organism-specific databases

CTD388610.
GeneCardsGC01P027320.
HGNCHGNC:34348. TRNP1.
neXtProtNX_Q6NT89.
PharmGKBPA164727311.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000154686.
InParanoidQ6NT89.
OMACVPWGAG.
OrthoDBEOG7FZ024.
PhylomeDBQ6NT89.
TreeFamTF338814.

Gene expression databases

BgeeQ6NT89.
CleanExHS_C1orf225.
GenevestigatorQ6NT89.

Family and domain databases

ProtoNetSearch...

Other

NextBio102215.
PROQ6NT89.

Entry information

Entry nameTRNP1_HUMAN
AccessionPrimary (citable) accession number: Q6NT89
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 3, 2009
Last modified: April 16, 2014
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM