ID   TRNP1_HUMAN             Reviewed;         227 AA.
AC   Q6NT89;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=TMF-regulated nuclear protein 1;
GN   Name=TRNP1; Synonyms=C1orf225, TRNP;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-27.
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=23622239; DOI=10.1016/j.cell.2013.03.027;
RA   Stahl R., Walcher T., De Juan Romero C., Pilz G.A., Cappello S., Irmler M.,
RA   Sanz-Aquela J.M., Beckers J., Blum R., Borrell V., Goetz M.;
RT   "Trnp1 regulates expansion and folding of the mammalian cerebral cortex by
RT   control of radial glial fate.";
RL   Cell 153:535-549(2013).
CC   -!- FUNCTION: DNA-binding factor that regulates the expression of a subset
CC       of genes and plays a key role in tangential, radial, and lateral
CC       expansion of the brain neocortex. Regulates neural stem cells
CC       proliferation and the production of intermediate neural progenitors and
CC       basal radial glial cells affecting the process of cerebral cortex
CC       gyrification. May control the proliferation rate of cells by regulating
CC       their progression through key cell-cycle transition points (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with TMF1; may regulate TRNP1 proteasomal
CC       degradation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expression is detected in the ventricular zone and
CC       neuronal layers of the developing cerebral cortex at 12, 18 and 21
CC       gestation weeks. Differences in regional expression seem to correlate
CC       with the process of gyrification of the cortex. Highly expressed in
CC       germinal layers of the precentral and parahippocampal gyri, that
CC       exhibit little radial expansion and folding, and weakly expressed in
CC       germinal layers of the occipital and temporal lobes, that undergo
CC       greater expansion and folding. {ECO:0000269|PubMed:23622239}.
CC   -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC       {ECO:0000250}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=the geometry of intelligence
CC       - Issue 152 of August 2013;
CC       URL="https://web.expasy.org/spotlight/back_issues/152/";
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DR   EMBL; AL356390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC069216; AAH69216.1; -; mRNA.
DR   CCDS; CCDS41289.1; -.
DR   RefSeq; NP_001013664.1; NM_001013642.2.
DR   RefSeq; XP_005245924.1; XM_005245867.3.
DR   AlphaFoldDB; Q6NT89; -.
DR   SMR; Q6NT89; -.
DR   BioGRID; 132770; 6.
DR   IntAct; Q6NT89; 1.
DR   STRING; 9606.ENSP00000429216; -.
DR   iPTMnet; Q6NT89; -.
DR   PhosphoSitePlus; Q6NT89; -.
DR   BioMuta; TRNP1; -.
DR   DMDM; 224471860; -.
DR   MassIVE; Q6NT89; -.
DR   PaxDb; 9606-ENSP00000429216; -.
DR   PeptideAtlas; Q6NT89; -.
DR   ProteomicsDB; 66667; -.
DR   Antibodypedia; 68540; 50 antibodies from 9 providers.
DR   DNASU; 388610; -.
DR   Ensembl; ENST00000522111.3; ENSP00000429216.2; ENSG00000253368.4.
DR   GeneID; 388610; -.
DR   KEGG; hsa:388610; -.
DR   MANE-Select; ENST00000522111.3; ENSP00000429216.2; NM_001013642.3; NP_001013664.2.
DR   UCSC; uc001bnj.5; human.
DR   AGR; HGNC:34348; -.
DR   CTD; 388610; -.
DR   DisGeNET; 388610; -.
DR   GeneCards; TRNP1; -.
DR   HGNC; HGNC:34348; TRNP1.
DR   HPA; ENSG00000253368; Tissue enhanced (esophagus, retina, stomach).
DR   neXtProt; NX_Q6NT89; -.
DR   OpenTargets; ENSG00000253368; -.
DR   PharmGKB; PA164727311; -.
DR   VEuPathDB; HostDB:ENSG00000253368; -.
DR   eggNOG; ENOG502S7AN; Eukaryota.
DR   GeneTree; ENSGT00390000017418; -.
DR   HOGENOM; CLU_106336_0_0_1; -.
DR   InParanoid; Q6NT89; -.
DR   OMA; CLPWPVN; -.
DR   OrthoDB; 4616497at2759; -.
DR   PhylomeDB; Q6NT89; -.
DR   TreeFam; TF338814; -.
DR   PathwayCommons; Q6NT89; -.
DR   SignaLink; Q6NT89; -.
DR   BioGRID-ORCS; 388610; 70 hits in 1152 CRISPR screens.
DR   GenomeRNAi; 388610; -.
DR   Pharos; Q6NT89; Tdark.
DR   PRO; PR:Q6NT89; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q6NT89; Protein.
DR   Bgee; ENSG00000253368; Expressed in cardiac muscle of right atrium and 173 other cell types or tissues.
DR   ExpressionAtlas; Q6NT89; baseline and differential.
DR   GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0021696; P:cerebellar cortex morphogenesis; ISS:UniProtKB.
DR   GO; GO:0061351; P:neural precursor cell proliferation; ISS:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR   InterPro; IPR040266; TRNP1.
DR   PANTHER; PTHR40714; TMF-REGULATED NUCLEAR PROTEIN 1; 1.
DR   PANTHER; PTHR40714:SF1; TMF-REGULATED NUCLEAR PROTEIN 1; 1.
DR   Genevisible; Q6NT89; HS.
PE   2: Evidence at transcript level;
KW   Cell cycle; Developmental protein; DNA-binding; Neurogenesis; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..227
FT                   /note="TMF-regulated nuclear protein 1"
FT                   /id="PRO_0000336088"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..53
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         27
FT                   /note="W -> R (in dbSNP:rs6689941)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_043545"
SQ   SEQUENCE   227 AA;  23482 MW;  01FBA6DC86CCD7CA CRC64;
     MPGCRISACG PGAQEGTAEQ RSPPPPWDPM PSSQPPPPTP TLTPTPTPGQ SPPLPDAAGA
     SAGAAEDQEL QRWRQGASGI AGLAGPGGGS GAAAGAGGRA LELAEARRRL LEVEGRRRLV
     SELESRVLQL HRVFLAAELR LAHRAESLSR LSGGVAQAEL YLAAHGSRLK KGPRRGRRGR
     PPALLASALG LGGCVPWGAG RLRRGHGPEP DSPFRRSPPR GPASPQR
//