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Protein

Transcriptional-regulating factor 1

Gene

TRERF1

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

Functioni

Binds DNA and activates transcription of CYP11A1. Interaction with CREBBP and EP300 results in a synergistic transcriptional activation of CYP11A1.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri512 – 53423C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1013 – 103725C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1086 – 110823C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding, bending Source: UniProtKB
  • ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • RNA polymerase II transcription cofactor activity Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: GO_Central

GO - Biological processi

  • cholesterol catabolic process Source: UniProtKB
  • homeostatic process Source: UniProtKB
  • multicellular organism development Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of hormone biosynthetic process Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: GO_Central
  • steroid biosynthetic process Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional-regulating factor 1
Alternative name(s):
Breast cancer anti-estrogen resistance 2
Transcriptional-regulating protein 132
Zinc finger protein rapa
Zinc finger transcription factor TReP-132
Gene namesi
Name:TRERF1
Synonyms:BCAR2, RAPA, TREP132
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:18273. TRERF1.

Subcellular locationi

GO - Cellular componenti

  • histone deacetylase complex Source: GO_Central
  • nucleus Source: UniProtKB
  • transcription factor complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134923539.

Polymorphism and mutation databases

BioMutaiTRERF1.
DMDMi74762683.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12001200Transcriptional-regulating factor 1PRO_0000197134Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei491 – 4911PhosphoserineCombined sources
Modified residuei633 – 6331N6-acetyllysineBy similarity
Modified residuei640 – 6401N6-acetyllysineBy similarity
Modified residuei767 – 7671PhosphothreonineCombined sources
Modified residuei954 – 9541PhosphothreonineCombined sources
Modified residuei955 – 9551PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ96PN7.
MaxQBiQ96PN7.
PaxDbiQ96PN7.
PeptideAtlasiQ96PN7.
PRIDEiQ96PN7.

PTM databases

iPTMnetiQ96PN7.
PhosphoSiteiQ96PN7.

Expressioni

Tissue specificityi

Highest expression was seen in thymus, testis and adrenal cortex, expressed also in the adrenal medulla, thyroid, and stomach. Highly expressed in steroidogenic JEG-3 and MCF-7 cells, low expression was seen in non-steroidogenic Hep-G2 and HEK293 cells.1 Publication

Gene expression databases

BgeeiQ96PN7.
CleanExiHS_TRERF1.
ExpressionAtlasiQ96PN7. baseline and differential.
GenevisibleiQ96PN7. HS.

Organism-specific databases

HPAiHPA051273.
HPA059943.

Interactioni

Subunit structurei

Interacts with CREBBP and EP300 (PubMed:11349124). Interacts with DNTTIP1 (PubMed:16371131, PubMed:21573134). Interacts with DNTT (PubMed:16371131).3 Publications

GO - Molecular functioni

  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120919. 10 interactions.
IntActiQ96PN7. 3 interactions.
STRINGi9606.ENSP00000362013.

Structurei

3D structure databases

ProteinModelPortaliQ96PN7.
SMRiQ96PN7. Positions 780-934, 1010-1110.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini779 – 87092ELM2PROSITE-ProRule annotationAdd
BLAST
Domaini885 – 93652SANTPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni439 – 1200762Interacts with CREBBPAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi202 – 417216Gln-richAdd
BLAST
Compositional biasi553 – 749197Pro-richAdd
BLAST
Compositional biasi956 – 98227Glu-richAdd
BLAST

Sequence similaritiesi

Contains 3 C2H2-type zinc fingers.PROSITE-ProRule annotation
Contains 1 ELM2 domain.PROSITE-ProRule annotation
Contains 1 SANT domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri512 – 53423C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1013 – 103725C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1086 – 110823C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG4167. Eukaryota.
ENOG4110BKZ. LUCA.
GeneTreeiENSGT00530000063277.
HOVERGENiHBG082398.
InParanoidiQ96PN7.
OrthoDBiEOG7QVM1T.
PhylomeDBiQ96PN7.
TreeFamiTF106431.

Family and domain databases

InterProiIPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF01448. ELM2. 1 hit.
PF13912. zf-C2H2_6. 3 hits.
[Graphical view]
SMARTiSM01189. ELM2. 1 hit.
SM00717. SANT. 1 hit.
SM00355. ZnF_C2H2. 3 hits.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS51156. ELM2. 1 hit.
PS51293. SANT. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96PN7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGDQQLYKTN HVAHGSENLF YQQPPLGVHS GLNHNYGNAV TGGGMDAPQA
60 70 80 90 100
SPISPHFPQD TRDGLGLPVG SKNLGQMDTS RQGGWGSHAG PGNHVQLRGN
110 120 130 140 150
LANSNMMWGA PAQAEPTDGY QYTYSQASEI RTQKLTSGVL HKLDSFTQVF
160 170 180 190 200
ANQNLRIQVN NMAQVLHTQS AVMDGAPDSA LRQLLSQKPM EPPAPAIPSR
210 220 230 240 250
YQQVPQQPHP GFTGGLSKPA LQVGQHPTQG HLYYDYQQPL AQVPVQGGQP
260 270 280 290 300
LQAPQMLSQH MQQMQQHQYY PPQQQQQAGQ QRISMQEIQT QPQQIRPSQP
310 320 330 340 350
QPPPQQQQPQ QLQLQQRQGS MQIPQYYQPQ PMMQHLQEQQ QQQMHLQPPS
360 370 380 390 400
YHRDPHQYTP EQAHTVQLIP LGSMSQYYYQ EPQQPYSHPL YQQSHLSQHQ
410 420 430 440 450
QREDSQLKTY SSDRQAQAML SSHGDLGPPD TGMGDPASSD LTRVSSTLPH
460 470 480 490 500
RPLLSPSGIH LNNMGPQHQQ LSPSAMWPQM HLPDGRAQPG SPESSGQPKG
510 520 530 540 550
AFGEQFDAKN KLTCSICLKE FKNLPALNGH MRSHGGMRAS PNLKQEEGEK
560 570 580 590 600
VLPPQPQPPL PPPPPPPPPP QLPPEAESLT PMVMPVSVPV KLLPPKPSSQ
610 620 630 640 650
GFTNSTVAAP SARDKPASSM SDDEMPVLEI PRKHQPSVPK AEEPLKTVQE
660 670 680 690 700
KKKFRHRPEP LFIPPPPSYN PNPAASYSGA TLYQSQLRSP RVLGDHLLLD
710 720 730 740 750
PTHELPPYTP PPMLSPVRQG SGLFSNVLIS GHGPGAHPQL PLTPLTPTPR
760 770 780 790 800
VLLCRSNSID GSNVTVTPGP GEQTVDVEPR INIGLRFQAE IPELQDISAL
810 820 830 840 850
AQDTHKATLV WKPWPELENH DLQQRVENLL NLCCSSALPG GGTNSEFALH
860 870 880 890 900
SLFEAKGDVM VALEMLLLRK PVRLKCHPLA NYHYAGSDKW TSLERKLFNK
910 920 930 940 950
ALATYSKDFI FVQKMVKSKT VAQCVEYYYT WKKIMRLGRK HRTRLAEIID
960 970 980 990 1000
DCVTSEEEEE LEEEEEEDPE EDRKSTKEEE SEVPKSPEPP PVPVLAPTEG
1010 1020 1030 1040 1050
PPLQALGQPS GSFICEMPNC GAVFSSRQAL NGHARIHGGT NQVTKARGAI
1060 1070 1080 1090 1100
PSGKQKPGGT QSGYCSVKSS PSHSTTSGET DPTTIFPCKE CGKVFFKIKS
1110 1120 1130 1140 1150
RNAHMKTHRQ QEEQQRQKAQ KAAFAAEMAA TIERTTGPVG APGLLPLDQL
1160 1170 1180 1190 1200
SLIKPIKDVD ILDDDVVQQL GGVMEEAEVV DTDLLLDDQD SVLLQGDAEL
Length:1,200
Mass (Da):132,256
Last modified:December 1, 2001 - v1
Checksum:iB77057F46A73404F
GO
Isoform 2 (identifier: Q96PN7-2) [UniParc]FASTAAdd to basket

Also known as: Rapa-1

The sequence of this isoform differs from the canonical sequence as follows:
     1-161: Missing.
     546-628: Missing.

Show »
Length:956
Mass (Da):106,264
Checksum:i7BE77C8D7B10CCF9
GO
Isoform 3 (identifier: Q96PN7-3) [UniParc]FASTAAdd to basket

Also known as: Rapa-2

The sequence of this isoform differs from the canonical sequence as follows:
     1-161: Missing.
     546-628: Missing.
     1022-1022: A → ADCRCHVTPFLPQ

Show »
Length:968
Mass (Da):107,662
Checksum:iAC9777B930C5BD82
GO
Isoform 4 (identifier: Q96PN7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     546-628: Missing.

Note: Gene prediction based on EST data.
Show »
Length:1,117
Mass (Da):123,601
Checksum:iF0325B9D6F297BBB
GO
Isoform 5 (identifier: Q96PN7-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     546-628: Missing.
     1022-1022: A → ADCRCHVTPFLPQ

Note: Gene prediction based on EST data.
Show »
Length:1,129
Mass (Da):124,999
Checksum:iBDE472412D3DFF89
GO

Sequence cautioni

The sequence BAA92082.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti658 – 6581P → S in CAB88206 (Ref. 2) Curated
Sequence conflicti658 – 6581P → S in CAB88207 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti431 – 4311T → A.
Corresponds to variant rs35162277 [ dbSNP | Ensembl ].
VAR_050197
Natural varianti766 – 7661V → I.
Corresponds to variant rs59159203 [ dbSNP | Ensembl ].
VAR_061362
Natural varianti834 – 8341C → S.
Corresponds to variant rs2295275 [ dbSNP | Ensembl ].
VAR_050198
Natural varianti1019 – 10191N → T.
Corresponds to variant rs35978318 [ dbSNP | Ensembl ].
VAR_050199
Natural varianti1187 – 11871D → N.
Corresponds to variant rs11751765 [ dbSNP | Ensembl ].
VAR_050200

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 161161Missing in isoform 2 and isoform 3. 1 PublicationVSP_015644Add
BLAST
Alternative sequencei546 – 62883Missing in isoform 2, isoform 3, isoform 4 and isoform 5. 1 PublicationVSP_015645Add
BLAST
Alternative sequencei1022 – 10221A → ADCRCHVTPFLPQ in isoform 3 and isoform 5. 1 PublicationVSP_015646

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF297872 mRNA. Translation: AAL01653.1.
AJ277275 mRNA. Translation: CAB88206.1.
AJ277276 mRNA. Translation: CAB88207.1.
AM404259 mRNA. Translation: CAL49295.1.
AM404183 mRNA. Translation: CAL49297.1.
AL096814 Genomic DNA. Translation: CAD92526.1.
AL096814 Genomic DNA. Translation: CAD92527.2.
AL096814 Genomic DNA. Translation: CAD92528.2.
AK002096 mRNA. Translation: BAA92082.1. Different initiation.
CCDSiCCDS4867.1. [Q96PN7-1]
RefSeqiNP_001284502.1. NM_001297573.1.
NP_277037.1. NM_033502.3. [Q96PN7-1]
XP_006715208.1. XM_006715145.2. [Q96PN7-1]
XP_006715210.1. XM_006715147.2. [Q96PN7-5]
XP_006715211.1. XM_006715148.2. [Q96PN7-4]
UniGeneiHs.485392.

Genome annotation databases

EnsembliENST00000340840; ENSP00000339438; ENSG00000124496. [Q96PN7-5]
ENST00000354325; ENSP00000346285; ENSG00000124496. [Q96PN7-4]
ENST00000372917; ENSP00000362008; ENSG00000124496. [Q96PN7-2]
ENST00000372922; ENSP00000362013; ENSG00000124496. [Q96PN7-1]
GeneIDi55809.
KEGGihsa:55809.
UCSCiuc003osc.3. human. [Q96PN7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF297872 mRNA. Translation: AAL01653.1.
AJ277275 mRNA. Translation: CAB88206.1.
AJ277276 mRNA. Translation: CAB88207.1.
AM404259 mRNA. Translation: CAL49295.1.
AM404183 mRNA. Translation: CAL49297.1.
AL096814 Genomic DNA. Translation: CAD92526.1.
AL096814 Genomic DNA. Translation: CAD92527.2.
AL096814 Genomic DNA. Translation: CAD92528.2.
AK002096 mRNA. Translation: BAA92082.1. Different initiation.
CCDSiCCDS4867.1. [Q96PN7-1]
RefSeqiNP_001284502.1. NM_001297573.1.
NP_277037.1. NM_033502.3. [Q96PN7-1]
XP_006715208.1. XM_006715145.2. [Q96PN7-1]
XP_006715210.1. XM_006715147.2. [Q96PN7-5]
XP_006715211.1. XM_006715148.2. [Q96PN7-4]
UniGeneiHs.485392.

3D structure databases

ProteinModelPortaliQ96PN7.
SMRiQ96PN7. Positions 780-934, 1010-1110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120919. 10 interactions.
IntActiQ96PN7. 3 interactions.
STRINGi9606.ENSP00000362013.

PTM databases

iPTMnetiQ96PN7.
PhosphoSiteiQ96PN7.

Polymorphism and mutation databases

BioMutaiTRERF1.
DMDMi74762683.

Proteomic databases

EPDiQ96PN7.
MaxQBiQ96PN7.
PaxDbiQ96PN7.
PeptideAtlasiQ96PN7.
PRIDEiQ96PN7.

Protocols and materials databases

DNASUi55809.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340840; ENSP00000339438; ENSG00000124496. [Q96PN7-5]
ENST00000354325; ENSP00000346285; ENSG00000124496. [Q96PN7-4]
ENST00000372917; ENSP00000362008; ENSG00000124496. [Q96PN7-2]
ENST00000372922; ENSP00000362013; ENSG00000124496. [Q96PN7-1]
GeneIDi55809.
KEGGihsa:55809.
UCSCiuc003osc.3. human. [Q96PN7-1]

Organism-specific databases

CTDi55809.
GeneCardsiTRERF1.
HGNCiHGNC:18273. TRERF1.
HPAiHPA051273.
HPA059943.
MIMi610322. gene.
neXtProtiNX_Q96PN7.
PharmGKBiPA134923539.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4167. Eukaryota.
ENOG4110BKZ. LUCA.
GeneTreeiENSGT00530000063277.
HOVERGENiHBG082398.
InParanoidiQ96PN7.
OrthoDBiEOG7QVM1T.
PhylomeDBiQ96PN7.
TreeFamiTF106431.

Miscellaneous databases

ChiTaRSiTRERF1. human.
GeneWikiiTRERF1.
GenomeRNAii55809.
PROiQ96PN7.
SOURCEiSearch...

Gene expression databases

BgeeiQ96PN7.
CleanExiHS_TRERF1.
ExpressionAtlasiQ96PN7. baseline and differential.
GenevisibleiQ96PN7. HS.

Family and domain databases

InterProiIPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF01448. ELM2. 1 hit.
PF13912. zf-C2H2_6. 3 hits.
[Graphical view]
SMARTiSM01189. ELM2. 1 hit.
SM00717. SANT. 1 hit.
SM00355. ZnF_C2H2. 3 hits.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS51156. ELM2. 1 hit.
PS51293. SANT. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression."
    Gizard F., Lavallee B., DeWitte F., Hum D.W.
    J. Biol. Chem. 276:33881-33892(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH CREBBP AND EP300.
    Tissue: Adrenal gland.
  2. "The cDNA sequences of rapa-1 and -2, two zinc finger proteins with unique structural characteristics."
    Mauch S., Sedlacek R., Krawinkel U.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "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].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 900-1200 (ISOFORMS 1/2/4).
    Tissue: Placenta.
  6. "Direct binding of TReP-132 with TdT results in reduction of TdT activity."
    Fujisaki S., Sato A., Toyomoto T., Hayano T., Sugai M., Kubota T., Koiwai O.
    Genes Cells 11:47-57(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNTTIP1 AND DNTT, SUBCELLULAR LOCATION, FUNCTION IN DNA-BINDING.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-767, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Nuclear cGMP-dependent kinase regulates gene expression via activity-dependent recruitment of a conserved histone deacetylase complex."
    Hao Y., Xu N., Box A.C., Schaefer L., Kannan K., Zhang Y., Florens L., Seidel C., Washburn M.P., Wiegraebe W., Mak H.Y.
    PLoS Genet. 7:E1002065-E1002065(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNTTIP1, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-954 AND SER-955, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiTREF1_HUMAN
AccessioniPrimary (citable) accession number: Q96PN7
Secondary accession number(s): Q05GC6
, Q7Z6T2, Q7Z6T3, Q9NQ72, Q9NQ73, Q9NUN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 130 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

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. SIMILARITY comments
    Index of protein domains and families

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 one 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.