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Protein

SERTA domain-containing protein 2

Gene

Sertad2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acts at E2F-responsive promoters as coregulator to integrate signals provided by PHD- and/or bromodomain-containing transcription factors. May act as coactivator as well as corepressor of E2F1-TFDP1 and E2F4-TFDP1 complexes on E2F consensus binding sites, which would activate or inhibit E2F-target genes expression. Modulates fat storage by down-regulating the expression of key genes involved in adipocyte lipolysis, thermogenesis and oxidative metabolism.1 Publication

GO - Molecular functioni

  • transcription coactivator activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
SERTA domain-containing protein 2
Alternative name(s):
Transcriptional regulator interacting with the PHD-bromodomain 2
Short name:
TRIP-Br2
Gene namesi
Name:Sertad2
Synonyms:Kiaa0127
ORF Names:MNCb-1504
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1931026. Sertad2.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: Exported out of the nucleus via its NES in a XPO1-dependent manner. Once in the cytoplasm, is degraded by the proteasome (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Resist development of obesity because of enhanced lipolysis and thermogenesis due, in part, to an increase in brown adipocytes number. On high fat diet (HFD), show reduced white adipose tissue (WAT) weight with smaller adipocyte size, improved glucose tolerance and insulin sensitivity with lower fasting glucose and insulin concentrations. Animals on HFD have higher and lower concentrations of adiponectin and leptin, respectively, compared to wild type. They don't develop liver steatosis and have 57% less adipose tissue macrophage infiltration.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309SERTA domain-containing protein 2PRO_0000191614Add
BLAST

Post-translational modificationi

Polyubiquitinated, which promotes proteasomal degradation.By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ9JJG5.
PRIDEiQ9JJG5.

PTM databases

PhosphoSiteiQ9JJG5.

Expressioni

Tissue specificityi

Expressed in white and brown adipose tissue.1 Publication

Inductioni

Up-regulated by high fat diet in adipose tissue.1 Publication

Gene expression databases

BgeeiQ9JJG5.
CleanExiMM_SERTAD2.
ExpressionAtlasiQ9JJG5. baseline and differential.
GenevisibleiQ9JJG5. MM.

Interactioni

Subunit structurei

Interacts with XPO1; which mediates nuclear export. Interacts with TFDP1; modulates transactivation activity of TFDP1/E2F complexes (By similarity).By similarity

Protein-protein interaction databases

BioGridi208368. 2 interactions.
STRINGi10090.ENSMUSP00000090981.

Structurei

3D structure databases

ProteinModelPortaliQ9JJG5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 8048SERTAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni230 – 30677Required for transactivation activityBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi233 – 2386Nuclear export signal (NES)By similarity

Sequence similaritiesi

Contains 1 SERTA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IEG3. Eukaryota.
ENOG4110A16. LUCA.
GeneTreeiENSGT00530000063867.
HOGENOMiHOG000111497.
HOVERGENiHBG097654.
InParanoidiQ9JJG5.
OMAiPCDLGST.
OrthoDBiEOG7VTDNP.
PhylomeDBiQ9JJG5.
TreeFamiTF331620.

Family and domain databases

InterProiIPR009263. SERTA_dom.
[Graphical view]
PfamiPF06031. SERTA. 1 hit.
[Graphical view]
PROSITEiPS51053. SERTA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JJG5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGKGGKRKF DEHEDGLEGK IVSPSDGPSR VSYTLQRQTI FNISLMKLYN
60 70 80 90 100
HRPLTEPSLQ KTVLINNMLR RIQEELKQEG SLRPAFTPSS QPSNSLSDSY
110 120 130 140 150
QEAPPPAPHP CDLGSTTPLE ACLTPASLLE DDNDDTFCTL QAVHPAAPTR
160 170 180 190 200
LSSAALPAEK DSFSSALDEI EELCPTSTST EAAHTAAPEG PKGTSSESSV
210 220 230 240 250
QKPEGPEEGR TDDSRFMDSL PGNFEITTST GFLTDLTLDD ILFADIDTSM
260 270 280 290 300
YDFDPCTSAS GTASKMAPVS ADDLLKTLAP YSNQPVAPSQ PFKMDLTELD

HIMEVLVGS
Length:309
Mass (Da):33,312
Last modified:July 11, 2003 - v2
Checksum:iD4178688F0DF8F00
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1403CTL → FTF in AAK52832 (PubMed:11331592).Curated
Sequence conflicti142 – 1421A → S in AAH14726 (PubMed:15489334).Curated
Sequence conflicti145 – 1451P → S in AAK52832 (PubMed:11331592).Curated
Sequence conflicti234 – 2341T → A in BAA95026 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041541 mRNA. Translation: BAA95026.1.
AK076787 mRNA. Translation: BAC36480.1.
BC014726 mRNA. Translation: AAH14726.1.
AF366403 mRNA. Translation: AAK52832.1.
CCDSiCCDS24458.1.
RefSeqiNP_001033714.1. NM_001038625.1.
NP_067347.2. NM_021372.2.
XP_006514829.1. XM_006514766.2.
UniGeneiMm.339676.

Genome annotation databases

EnsembliENSMUST00000093292; ENSMUSP00000090981; ENSMUSG00000049800.
ENSMUST00000109585; ENSMUSP00000105214; ENSMUSG00000049800.
ENSMUST00000109586; ENSMUSP00000105215; ENSMUSG00000049800.
GeneIDi58172.
KEGGimmu:58172.
UCSCiuc007idc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041541 mRNA. Translation: BAA95026.1.
AK076787 mRNA. Translation: BAC36480.1.
BC014726 mRNA. Translation: AAH14726.1.
AF366403 mRNA. Translation: AAK52832.1.
CCDSiCCDS24458.1.
RefSeqiNP_001033714.1. NM_001038625.1.
NP_067347.2. NM_021372.2.
XP_006514829.1. XM_006514766.2.
UniGeneiMm.339676.

3D structure databases

ProteinModelPortaliQ9JJG5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208368. 2 interactions.
STRINGi10090.ENSMUSP00000090981.

PTM databases

PhosphoSiteiQ9JJG5.

Proteomic databases

PaxDbiQ9JJG5.
PRIDEiQ9JJG5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000093292; ENSMUSP00000090981; ENSMUSG00000049800.
ENSMUST00000109585; ENSMUSP00000105214; ENSMUSG00000049800.
ENSMUST00000109586; ENSMUSP00000105215; ENSMUSG00000049800.
GeneIDi58172.
KEGGimmu:58172.
UCSCiuc007idc.1. mouse.

Organism-specific databases

CTDi9792.
MGIiMGI:1931026. Sertad2.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IEG3. Eukaryota.
ENOG4110A16. LUCA.
GeneTreeiENSGT00530000063867.
HOGENOMiHOG000111497.
HOVERGENiHBG097654.
InParanoidiQ9JJG5.
OMAiPCDLGST.
OrthoDBiEOG7VTDNP.
PhylomeDBiQ9JJG5.
TreeFamiTF331620.

Miscellaneous databases

ChiTaRSiSertad2. mouse.
PROiQ9JJG5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JJG5.
CleanExiMM_SERTAD2.
ExpressionAtlasiQ9JJG5. baseline and differential.
GenevisibleiQ9JJG5. MM.

Family and domain databases

InterProiIPR009263. SERTA_dom.
[Graphical view]
PfamiPF06031. SERTA. 1 hit.
[Graphical view]
PROSITEiPS51053. SERTA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
    Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  2. "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: Testis.
  3. "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].
    Tissue: Kidney.
  4. "TRIP-Br: a novel family of PHD zinc finger- and bromodomain-interacting proteins that regulate the transcriptional activity of E2F-1/DP-1."
    Hsu S.-I., Yang C.M., Sim K.G., Hentschel D.M., O'Leary E., Bonventre J.V.
    EMBO J. 20:2273-2285(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 129-309.
  5. "Ablation of TRIP-Br2, a regulator of fat lipolysis, thermogenesis and oxidative metabolism, prevents diet-induced obesity and insulin resistance."
    Liew C.W., Boucher J., Cheong J.K., Vernochet C., Koh H.J., Mallol C., Townsend K., Langin D., Kawamori D., Hu J., Tseng Y.H., Hellerstein M.K., Farmer S.R., Goodyear L., Doria A., Blueher M., Hsu S.I., Kulkarni R.N.
    Nat. Med. 19:217-226(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ADIPOGENESIS, INDUCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.

Entry informationi

Entry nameiSRTD2_MOUSE
AccessioniPrimary (citable) accession number: Q9JJG5
Secondary accession number(s): Q8C609, Q91WL3, Q925E5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: July 11, 2003
Last modified: June 8, 2016
This is version 103 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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.