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Protein

Tetratricopeptide repeat protein 5

Gene

Ttc5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adapter protein involved in p53/TP53 response that acts by regulating and mediating the assembly of multi-protein complexes. Required to facilitate the interaction between JMY and p300/EP300 and increase p53/TP53-dependent transcription and apoptosis. Prevents p53/TP53 degradation by MDM2.2 Publications

GO - Molecular functioni

  • chromatin binding Source: MGI
  • DNA binding Source: MGI

GO - Biological processi

  • DNA repair Source: UniProtKB-KW
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiR-MMU-6804760. Regulation of TP53 Activity through Methylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Tetratricopeptide repeat protein 5
Short name:
TPR repeat protein 5
Alternative name(s):
Stress-responsive activator of p300
Gene namesi
Name:Ttc5
Synonyms:Strap
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:2683584. Ttc5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Tetratricopeptide repeat protein 5PRO_0000106382Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031Phosphoserine; by ATM2 Publications
Modified residuei221 – 2211Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation at Ser-203 enhances protein stability, regulates nuclear accumulation and association with p300/EP300.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ99LG4.
MaxQBiQ99LG4.
PaxDbiQ99LG4.
PRIDEiQ99LG4.

PTM databases

iPTMnetiQ99LG4.
PhosphoSiteiQ99LG4.

Expressioni

Inductioni

Sress-responsive protein. Induced upon UV or ionizing irradiation (at protein level).1 Publication

Gene expression databases

BgeeiQ99LG4.
CleanExiMM_TTC5.
GenevisibleiQ99LG4. MM.

Interactioni

Subunit structurei

Interacts with JMY and p300/EP300.1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000006451.

Structurei

Secondary structure

1
440
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2824Combined sources
Helixi30 – 334Combined sources
Helixi36 – 416Combined sources
Helixi42 – 6120Combined sources
Helixi68 – 7811Combined sources
Beta strandi80 – 834Combined sources
Helixi86 – 9813Combined sources
Helixi103 – 11614Combined sources
Helixi119 – 13012Combined sources
Helixi136 – 14611Combined sources
Helixi154 – 17421Combined sources
Helixi179 – 19517Combined sources
Helixi200 – 21617Combined sources
Helixi218 – 2225Combined sources
Helixi224 – 23613Combined sources
Helixi240 – 25314Combined sources
Helixi258 – 28023Combined sources
Turni281 – 2833Combined sources
Helixi286 – 2949Combined sources
Helixi299 – 3013Combined sources
Turni304 – 3074Combined sources
Helixi324 – 3263Combined sources
Beta strandi329 – 3313Combined sources
Beta strandi335 – 34511Combined sources
Beta strandi352 – 36211Combined sources
Beta strandi365 – 3695Combined sources
Beta strandi383 – 3886Combined sources
Beta strandi390 – 3989Combined sources
Beta strandi401 – 41111Combined sources
Helixi413 – 4153Combined sources
Helixi425 – 4273Combined sources
Beta strandi428 – 4303Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ABNX-ray2.05A/B1-440[»]
ProteinModelPortaliQ99LG4.
SMRiQ99LG4. Positions 1-429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati7 – 6155TPR 11 PublicationAdd
BLAST
Repeati68 – 9831TPR 21 PublicationAdd
BLAST
Repeati103 – 13028TPR 31 PublicationAdd
BLAST
Repeati136 – 17439TPR 41 PublicationAdd
BLAST
Repeati179 – 21638TPR 51 PublicationAdd
BLAST
Repeati224 – 25330TPR 61 PublicationAdd
BLAST

Sequence similaritiesi

Contains 6 TPR repeats.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiENOG410IEK9. Eukaryota.
ENOG410XP1F. LUCA.
GeneTreeiENSGT00390000006227.
HOGENOMiHOG000006922.
HOVERGENiHBG054388.
InParanoidiQ99LG4.
OMAiAVMVYNM.
OrthoDBiEOG79SDXP.
TreeFamiTF316804.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
IPR032076. TTC5_OB.
[Graphical view]
PfamiPF16669. TTC5_OB. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
PROSITEiPS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99LG4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMADEEEEAK HVLQKLQGLV DRLYCFRDSY FETHSVEDAG RKQQDVQEEM
60 70 80 90 100
EKTLQQMEEV LGSAQVEAQA LMLKGKALNV TPDYSPEAEV LLSKAVKLEP
110 120 130 140 150
ELVEAWNQLG EVYWKKGDVA SAHTCFSGAL THCKNKVSLQ NLSMVLRQLQ
160 170 180 190 200
TDSGDEHSRH VMDSVRQAKL AVQMDVLDGR SWYILGNAYL SLYFNTGQNP
210 220 230 240 250
KISQQALSAY AQAEKVDRKA SSNPDLHLNR ATLHKYEESY GEALEGFSQA
260 270 280 290 300
AALDPVWPEP QQREQQLLEF LSRLTSLLES KGKTKPKKLQ SMLGSLRPAH
310 320 330 340 350
LGPCGDGRYQ SASGQKMTLE LKPLSTLQPG VNSGTVVLGK VVFSLTTEEK
360 370 380 390 400
VPFTFGLVDS DGPCYAVMVY NVVQSWGVLI GDSVAIPEPN LRHHQIRHKG
410 420 430 440
KDYSFSSVRV ETPLLLVVNG KPQNSSSQAS ATVASRPQCE
Length:440
Mass (Da):48,795
Last modified:July 27, 2011 - v2
Checksum:i07CB475AD1CEA370
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti120 – 1201A → T in AAH03272 (PubMed:15489334).Curated
Sequence conflicti120 – 1201A → T in AAH25610 (PubMed:15489334).Curated
Sequence conflicti120 – 1201A → T in AAH92074 (PubMed:15489334).Curated
Sequence conflicti256 – 2561V → A in AAH03272 (PubMed:15489334).Curated
Sequence conflicti256 – 2561V → A in AAH25610 (PubMed:15489334).Curated
Sequence conflicti256 – 2561V → A in AAH92074 (PubMed:15489334).Curated
Sequence conflicti430 – 4301S → Y in BAE34192 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK157777 mRNA. Translation: BAE34192.1.
AK161279 mRNA. Translation: BAE36290.1.
BC003272 mRNA. Translation: AAH03272.1.
BC025610 mRNA. Translation: AAH25610.1.
BC092074 mRNA. Translation: AAH92074.1.
CCDSiCCDS36905.1.
RefSeqiNP_001074418.1. NM_001080949.2.
UniGeneiMm.276362.

Genome annotation databases

EnsembliENSMUST00000006451; ENSMUSP00000006451; ENSMUSG00000006288.
GeneIDi219022.
KEGGimmu:219022.
UCSCiuc007tlm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK157777 mRNA. Translation: BAE34192.1.
AK161279 mRNA. Translation: BAE36290.1.
BC003272 mRNA. Translation: AAH03272.1.
BC025610 mRNA. Translation: AAH25610.1.
BC092074 mRNA. Translation: AAH92074.1.
CCDSiCCDS36905.1.
RefSeqiNP_001074418.1. NM_001080949.2.
UniGeneiMm.276362.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ABNX-ray2.05A/B1-440[»]
ProteinModelPortaliQ99LG4.
SMRiQ99LG4. Positions 1-429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000006451.

PTM databases

iPTMnetiQ99LG4.
PhosphoSiteiQ99LG4.

Proteomic databases

EPDiQ99LG4.
MaxQBiQ99LG4.
PaxDbiQ99LG4.
PRIDEiQ99LG4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006451; ENSMUSP00000006451; ENSMUSG00000006288.
GeneIDi219022.
KEGGimmu:219022.
UCSCiuc007tlm.2. mouse.

Organism-specific databases

CTDi91875.
MGIiMGI:2683584. Ttc5.

Phylogenomic databases

eggNOGiENOG410IEK9. Eukaryota.
ENOG410XP1F. LUCA.
GeneTreeiENSGT00390000006227.
HOGENOMiHOG000006922.
HOVERGENiHBG054388.
InParanoidiQ99LG4.
OMAiAVMVYNM.
OrthoDBiEOG79SDXP.
TreeFamiTF316804.

Enzyme and pathway databases

ReactomeiR-MMU-6804760. Regulation of TP53 Activity through Methylation.

Miscellaneous databases

PROiQ99LG4.
SOURCEiSearch...

Gene expression databases

BgeeiQ99LG4.
CleanExiMM_TTC5.
GenevisibleiQ99LG4. MM.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
IPR032076. TTC5_OB.
[Graphical view]
PfamiPF16669. TTC5_OB. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
PROSITEiPS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  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].
    Strain: FVB/N.
    Tissue: Mammary tumor and Salivary gland.
  3. Cited for: FUNCTION, INTERACTION WITH JMY, INDUCTION.
  4. "A new effector pathway links ATM kinase with the DNA damage response."
    Demonacos C., Krstic-Demonacos M., Smith L., Xu D., O'Connor D.P., Jansson M., La Thangue N.B.
    Nat. Cell Biol. 6:968-976(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-203.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Spleen and Testis.
  6. "The p53 cofactor Strap exhibits an unexpected TPR motif and oligonucleotide-binding (OB)-fold structure."
    Adams C.J., Pike A.C., Maniam S., Sharpe T.D., Coutts A.S., Knapp S., La Thangue N.B., Bullock A.N.
    Proc. Natl. Acad. Sci. U.S.A. 109:3778-3783(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), PHOSPHORYLATION AT SER-203 AND SER-221, TPR REPEATS.

Entry informationi

Entry nameiTTC5_MOUSE
AccessioniPrimary (citable) accession number: Q99LG4
Secondary accession number(s): Q3TTN5, Q3TZL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 106 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.