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Protein

TMF-regulated nuclear protein 1

Gene

TRNP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. DNA binding Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cerebellar cortex morphogenesis Source: UniProtKB
  3. neural precursor cell proliferation Source: UniProtKB
  4. regulation of cell cycle Source: UniProtKB
  5. regulation of cell proliferation Source: UniProtKB
  6. regulation of transcription, DNA-templated Source: UniProtKB-KW
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell cycle, Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
TMF-regulated nuclear protein 1
Gene namesi
Name:TRNP1
Synonyms:C1orf225, TRNP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:34348. TRNP1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nuclear euchromatin Source: Ensembl
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164727311.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 227227TMF-regulated nuclear protein 1PRO_0000336088Add
BLAST

Post-translational modificationi

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

Keywords - PTMi

Ubl conjugation

Proteomic databases

PRIDEiQ6NT89.

PTM databases

PhosphoSiteiQ6NT89.

Expressioni

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiQ6NT89.
CleanExiHS_C1orf225.
GenevestigatoriQ6NT89.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ6NT89.
SMRiQ6NT89. Positions 96-174.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi23 – 5533Pro-richAdd
BLAST

Phylogenomic databases

GeneTreeiENSGT00390000017418.
HOGENOMiHOG000154686.
InParanoidiQ6NT89.
OMAiCVPWGAG.
OrthoDBiEOG7FZ024.
PhylomeDBiQ6NT89.
TreeFamiTF338814.

Sequencei

Sequence statusi: Complete.

Q6NT89-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPGCRISACG PGAQEGTAEQ RSPPPPWDPM PSSQPPPPTP TLTPTPTPGQ
60 70 80 90 100
SPPLPDAAGA SAGAAEDQEL QRWRQGASGI AGLAGPGGGS GAAAGAGGRA
110 120 130 140 150
LELAEARRRL LEVEGRRRLV SELESRVLQL HRVFLAAELR LAHRAESLSR
160 170 180 190 200
LSGGVAQAEL YLAAHGSRLK KGPRRGRRGR PPALLASALG LGGCVPWGAG
210 220
RLRRGHGPEP DSPFRRSPPR GPASPQR
Length:227
Mass (Da):23,482
Last modified:March 3, 2009 - v2
Checksum:i01FBA6DC86CCD7CA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271W → R.1 Publication
Corresponds to variant rs6689941 [ dbSNP | Ensembl ].
VAR_043545

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL356390 Genomic DNA. No translation available.
BC069216 mRNA. Translation: AAH69216.1.
CCDSiCCDS41289.1.
RefSeqiNP_001013664.1. NM_001013642.2.
XP_005245924.1. XM_005245867.1.
UniGeneiHs.355747.

Genome annotation databases

EnsembliENST00000522111; ENSP00000429216; ENSG00000253368.
GeneIDi388610.
KEGGihsa:388610.
UCSCiuc001bnj.4. human.

Polymorphism databases

DMDMi224471860.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Protein Spotlight

the geometry of intelligence - Issue 152 of August 2013

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL356390 Genomic DNA. No translation available.
BC069216 mRNA. Translation: AAH69216.1.
CCDSiCCDS41289.1.
RefSeqiNP_001013664.1. NM_001013642.2.
XP_005245924.1. XM_005245867.1.
UniGeneiHs.355747.

3D structure databases

ProteinModelPortaliQ6NT89.
SMRiQ6NT89. Positions 96-174.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ6NT89.

Polymorphism databases

DMDMi224471860.

Proteomic databases

PRIDEiQ6NT89.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000522111; ENSP00000429216; ENSG00000253368.
GeneIDi388610.
KEGGihsa:388610.
UCSCiuc001bnj.4. human.

Organism-specific databases

CTDi388610.
GeneCardsiGC01P027320.
HGNCiHGNC:34348. TRNP1.
neXtProtiNX_Q6NT89.
PharmGKBiPA164727311.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000017418.
HOGENOMiHOG000154686.
InParanoidiQ6NT89.
OMAiCVPWGAG.
OrthoDBiEOG7FZ024.
PhylomeDBiQ6NT89.
TreeFamiTF338814.

Miscellaneous databases

GenomeRNAii388610.
NextBioi102215.
PROiQ6NT89.

Gene expression databases

BgeeiQ6NT89.
CleanExiHS_C1orf225.
GenevestigatoriQ6NT89.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiTRNP1_HUMAN
AccessioniPrimary (citable) accession number: Q6NT89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 3, 2009
Last modified: January 7, 2015
This is version 73 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

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.