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Q14140 (SRTD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SERTA domain-containing protein 2
Alternative name(s):
Transcriptional regulator interacting with the PHD-bromodomain 2
Short name=TRIP-Br2
Gene names
Name:SERTAD2
Synonyms:KIAA0127
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4

Subunit structure

Interacts with XPO1; which mediates nuclear export. Interacts with TFDP1; modulates transactivation activity of TFDP1/E2F complexes. Ref.4 Ref.5

Subcellular location

Nucleus. Cytoplasm. Note: Exported out of the nucleus via its NES in a XPO1-dependent manner. Once in the cytoplasm, is degraded by the proteasome. Ref.5

Tissue specificity

Expressed in adipose tissue. Ref.6

Developmental stage

Transcript levels remain constant in all phases of the cell cycle. In contrast, protein levels accumulate at the G1/S phase boundary and decrease progressively through S phase until G2/M phase is reached, residual expression is observed in the G2/M and early G1 phases. Ref.5

Post-translational modification

Polyubiquitinated, which promotes proteasomal degradation.

Sequence similarities

Contains 1 SERTA domain.

Sequence caution

The sequence BAA09476.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314SERTA domain-containing protein 2
PRO_0000191613

Regions

Domain33 – 8048SERTA
Region235 – 31177Required for transactivation activity
Region238 – 2436Nuclear export signal (NES)

Experimental info

Mutagenesis2381L → A: Abolishes the interaction with XPO1 as well as the nuclear export and the subsequent proteasomal degradation. Ref.5
Mutagenesis2411L → A: Slight resistance to proteasomal degradation, no effect on the interaction with XPO1 neither on nuclear export. Ref.5
Mutagenesis2431L → A: Slight decrease of interaction with XPO1 and resistance to proteasomal degradation, no effect on nuclear export. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q14140 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E43107FC565AAC31

FASTA31433,897
        10         20         30         40         50         60 
MLGKGGKRKF DEHEDGLEGK IVSPCDGPSK VSYTLQRQTI FNISLMKLYN HRPLTEPSLQ 

        70         80         90        100        110        120 
KTVLINNMLR RIQEELKQEG SLRPMFTPSS QPTTEPSDSY REAPPAFSHL ASPSSHPCDL 

       130        140        150        160        170        180 
GSTTPLEACL TPASLLEDDD DTFCTSQAMQ PTAPTKLSPP ALLPEKDSFS SALDEIEELC 

       190        200        210        220        230        240 
PTSTSTEAAT AATDSVKGTS SEAGTQKLDG PQESRADDSK LMDSLPGNFE ITTSTGFLTD 

       250        260        270        280        290        300 
LTLDDILFAD IDTSMYDFDP CTSSSGTASK MAPVSADDLL KTLAPYSSQP VTPSQPFKMD 

       310 
LTELDHIMEV LVGS 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Bone marrow.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: Brain and Brain cortex.
[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: FUNCTION AS COREGULATOR, INTERACTION WITH TFDP1.
[5]"CRM1-mediated nuclear export is required for 26 S proteasome-dependent degradation of the TRIP-Br2 proto-oncoprotein."
Cheong J.K., Gunaratnam L., Hsu S.I.
J. Biol. Chem. 283:11661-11676(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH XPO1, DEVELOPMENTAL STAGE, NUCLEAR EXPORT SIGNAL, UBIQUITINATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-238; LEU-241 AND LEU-243.
[6]"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: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D50917 mRNA. Translation: BAA09476.2. Different initiation.
AC007365 Genomic DNA. Translation: AAY14766.1.
BC074788 mRNA. Translation: AAH74788.1.
BC074789 mRNA. Translation: AAH74789.1.
BC101639 mRNA. Translation: AAI01640.1.
BC101641 mRNA. Translation: AAI01642.1.
RefSeqNP_055570.1. NM_014755.2.
XP_005264726.1. XM_005264669.1.
UniGeneHs.591569.

3D structure databases

ProteinModelPortalQ14140.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115136. 9 interactions.
IntActQ14140. 1 interaction.
STRING9606.ENSP00000326933.

PTM databases

PhosphoSiteQ14140.

Polymorphism databases

DMDM3123047.

Proteomic databases

PaxDbQ14140.
PRIDEQ14140.

Protocols and materials databases

DNASU9792.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313349; ENSP00000326933; ENSG00000179833.
GeneID9792.
KEGGhsa:9792.
UCSCuc002sde.2. human.

Organism-specific databases

CTD9792.
GeneCardsGC02M064770.
HGNCHGNC:30784. SERTAD2.
HPAHPA019021.
HPA020904.
neXtProtNX_Q14140.
PharmGKBPA134948884.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47551.
HOGENOMHOG000111497.
HOVERGENHBG097654.
InParanoidQ14140.
OMAPCDLGST.
OrthoDBEOG7VTDNP.
PhylomeDBQ14140.
TreeFamTF331620.

Gene expression databases

BgeeQ14140.
CleanExHS_SERTAD2.
GenevestigatorQ14140.

Family and domain databases

InterProIPR009263. SERTA.
[Graphical view]
PANTHERPTHR16277. PTHR16277. 1 hit.
PfamPF06031. SERTA. 1 hit.
[Graphical view]
PROSITEPS51053. SERTA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi9792.
NextBio36874.
PROQ14140.

Entry information

Entry nameSRTD2_HUMAN
AccessionPrimary (citable) accession number: Q14140
Secondary accession number(s): Q53TS2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM