Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

TCF3 fusion partner homolog

Gene

Tfpt

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Appears to promote apoptosis in a p53/TP53-independent manner.
Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.By similarity

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • protein heterodimerization activity Source: RGD
  • protein kinase binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • DNA recombination Source: UniProtKB-KW
  • DNA repair Source: UniProtKB-KW
  • male gonad development Source: RGD
  • positive regulation of apoptotic process Source: RGD
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Apoptosis, DNA damage, DNA recombination, DNA repair, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
TCF3 fusion partner homolog
Alternative name(s):
Protein amida
Gene namesi
Name:Tfpt
Synonyms:Amida
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620839. Tfpt.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 259259TCF3 fusion partner homologPRO_0000254583Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei167 – 1671PhosphoserineBy similarity
Modified residuei172 – 1721PhosphothreonineBy similarity
Modified residuei180 – 1801PhosphoserineCombined sources
Modified residuei188 – 1881PhosphoserineBy similarity
Modified residuei203 – 2031PhosphothreonineBy similarity
Modified residuei255 – 2551PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9JMG6.

PTM databases

iPTMnetiQ9JMG6.
PhosphoSiteiQ9JMG6.

Expressioni

Tissue specificityi

Ubiquitously expressed. Abundant in the brain.1 Publication

Interactioni

Subunit structurei

Interacts with NOL3; translocates NOL3 into the nucleus and negatively regulated TFPT-induced cell death. Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the N-terminus of INO80 (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PawrQ626278EBI-1767101,EBI-1187240

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi250095. 2 interactions.
IntActiQ9JMG6. 1 interaction.
STRINGi10116.ENSRNOP00000018913.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG410IXD0. Eukaryota.
ENOG4111UBX. LUCA.
HOGENOMiHOG000139148.
HOVERGENiHBG056588.
InParanoidiQ9JMG6.
KOiK11670.
OMAiMRVLDAY.
OrthoDBiEOG76T9SH.
PhylomeDBiQ9JMG6.
TreeFamiTF338152.

Family and domain databases

InterProiIPR033555. TFPT.
[Graphical view]
PANTHERiPTHR35084. PTHR35084. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9JMG6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELEQREGTM AAVGFEEFSA PPGSELALPP LFGGHILESE LETEVEFVSG
60 70 80 90 100
GLGDSGLRER DEEEEAARGR RRRQRELNRR KYQALGRRCR EIEQVNERVL
110 120 130 140 150
NRLHQVQRIT RRLQQERRFL MRVLDSYGDD YRDSQFTIVL EDDGSQGTDV
160 170 180 190 200
PTPGNVENEP PEKEGLSPPQ RTTATLDPSS PAPGEGPSGR KRRRAPRAAS
210 220 230 240 250
SLTPELAPVQ VGAEGWGQGV IKVEEDFGFE ADEALDSSWV SRGPDKLLPY

PTLASPPFD
Length:259
Mass (Da):28,908
Last modified:October 31, 2006 - v2
Checksum:i674408B3F3FB6863
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC103574 Genomic DNA. No translation available.
AB029495 mRNA. Translation: BAA90702.1.
RefSeqiNP_620225.1. NM_138870.1.
XP_006228098.1. XM_006228036.2.
UniGeneiRn.12922.

Genome annotation databases

GeneIDi85423.
KEGGirno:85423.
UCSCiRGD:620839. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC103574 Genomic DNA. No translation available.
AB029495 mRNA. Translation: BAA90702.1.
RefSeqiNP_620225.1. NM_138870.1.
XP_006228098.1. XM_006228036.2.
UniGeneiRn.12922.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250095. 2 interactions.
IntActiQ9JMG6. 1 interaction.
STRINGi10116.ENSRNOP00000018913.

PTM databases

iPTMnetiQ9JMG6.
PhosphoSiteiQ9JMG6.

Proteomic databases

PaxDbiQ9JMG6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi85423.
KEGGirno:85423.
UCSCiRGD:620839. rat.

Organism-specific databases

CTDi29844.
RGDi620839. Tfpt.

Phylogenomic databases

eggNOGiENOG410IXD0. Eukaryota.
ENOG4111UBX. LUCA.
HOGENOMiHOG000139148.
HOVERGENiHBG056588.
InParanoidiQ9JMG6.
KOiK11670.
OMAiMRVLDAY.
OrthoDBiEOG76T9SH.
PhylomeDBiQ9JMG6.
TreeFamiTF338152.

Miscellaneous databases

PROiQ9JMG6.

Family and domain databases

InterProiIPR033555. TFPT.
[Graphical view]
PANTHERiPTHR35084. PTHR35084. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Molecular cloning and characterization of Amida, a novel protein which interacts with a neuron-specific immediate early gene product arc, contains novel nuclear localization signals, and causes cell death in cultured cells."
    Irie Y., Yamagata K., Gan Y., Miyamoto K., Do E., Kuo C.H., Taira E., Miki N.
    J. Biol. Chem. 275:2647-2653(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-259, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, POSSIBLE FUNCTION IN APOPTOSIS, INTERACTION WITH NOL3.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTFPT_RAT
AccessioniPrimary (citable) accession number: Q9JMG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: July 6, 2016
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.