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Q9QXN3 (TRIP4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Activating signal cointegrator 1

Short name=ASC-1
Alternative name(s):
Thyroid receptor-interacting protein 4
Short name=TR-interacting protein 4
Short name=TRIP-4
Gene names
Name:Trip4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length581 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription coactivator of nuclear receptors which functions in conjunction with CBP-p300 and SRC-1 and may play an important role in establishing distinct coactivator complexes under different cellular conditions. Plays a pivotal role in the transactivation of NF-kappa-B, SRF and AP1. Acts as a mediator of transrepression between nuclear receptor and either AP1 or NF-kappa-B By similarity. Plays a role in androgen receptor transactivation and testicular function. Ref.2

Subunit structure

Specifically interacts with the ligand binding domain of the thyroid receptor (TR). This interaction requires the presence of thyroid hormone. Exists as a steady-state complex associated with ASCC1, ASCC2 and HELIC1 By similarity. Interacts with the androgen receptor androgen (AR) in an androgen, testosterone and dihydrotestosterone-dependent manner. Interacts with NEK6 By similarity. Ref.1

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Note: Cytoplasmic under conditions of serum deprivation. Co- localizes with NEK6 in the centrosome By similarity.

Tissue specificity

Ubiquitously expressed. Ref.2

Post-translational modification

Phosphorylated by NEK6 By similarity.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9QXN3-1)

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.
Isoform 2 (identifier: Q9QXN3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     526-539: FPDISQESDSSFVF → GNWIPRSIKEQRRG
     540-581: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 581580Activating signal cointegrator 1
PRO_0000065632

Regions

Zinc finger167 – 21953C4-type

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue2891Phosphotyrosine Ref.7

Natural variations

Alternative sequence526 – 53914FPDIS…SSFVF → GNWIPRSIKEQRRG in isoform 2.
VSP_011109
Alternative sequence540 – 58142Missing in isoform 2.
VSP_011110

Experimental info

Sequence conflict71A → G in BAC30209. Ref.3
Sequence conflict3881S → P in AAF18440. Ref.1
Sequence conflict3881S → P in AAN23117. Ref.2
Sequence conflict3881S → P in AAH21316. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 2CAB3512E3CEDDA7

FASTA58166,197
        10         20         30         40         50         60 
MAVAGAAYRE PLVHWCTQQL QKTFALDVSE EIIQYVLSIE NAEEIREYVT DLLQGNEGKK 

        70         80         90        100        110        120 
GQFIEDLITK WQKNDQEFIS DSFQQCLRKD EILDGQRSVD QLKRSRRKGR NKQEVPAFPE 

       130        140        150        160        170        180 
PDVAVEVKTP LDLAKAQESN NSVKKKTRFV NLYTREGQDK LAVLLPGRHP CDCLGQKHKL 

       190        200        210        220        230        240 
INNCLVCGRI VCEQEGSGPC LFCGSLVCTN EEQDILQRDS NKSQKLLKKL MSGAETSGKV 

       250        260        270        280        290        300 
DVSTKDLLPH QESRMKSGLE KAIKHKEKLL EFDRTSIRRT QVIDDESDYF ASDSNQWLSK 

       310        320        330        340        350        360 
VEREMLQKRE EELRELRHAS RLSKKVTIDF AGRKILEDEN PLAEYHSRLD ETIQAIASGT 

       370        380        390        400        410        420 
LNQSLVTLDR SCEEPLGVLV NPNMYQASPQ WVDNTGSTPQ KKTSLSAGPR LEPSLHQHQL 

       430        440        450        460        470        480 
RIQDQEFQEG FDGGWCLSMH QPWASLLVRG IKRVEGRSWY TPHRGRLWIA ATGKRPSPQE 

       490        500        510        520        530        540 
VSELQATYRL LRGKDVEFPN DYPSGCLLGC VDLIDCLSQK QFQEQFPDIS QESDSSFVFI 

       550        560        570        580 
CKNPQEMVVK FPIKGNPKIW KLDSKIHQGA KKGLMKQNKA V 

« Hide

Isoform 2 [UniParc].

Checksum: FF965B4855F43891
Show »

FASTA53961,533

References

« Hide 'large scale' references
[1]"Novel transcription coactivator complex containing activating signal cointegrator 1."
Jung D.-J., Sung H.-S., Goo Y.-W., Lee H.M., Park O.K., Jung S.-Y., Lim J., Kim H.-J., Lee S.-K., Kim T.S., Lee J.W., Lee Y.C.
Mol. Cell. Biol. 22:5203-5211(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ASCC1; ASCC2 AND HELIC1.
Tissue: Liver.
[2]"Activating signal cointegrator 1 is highly expressed in murine testicular Leydig cells and enhances the ligand-dependent transactivation of androgen receptor."
Lee Y.S., Kim H.-J., Lee H.J., Lee J.W., Chun S.-Y., Ko S.-K., Lee K.
Biol. Reprod. 67:1580-1587(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
Strain: CD-1.
Tissue: Testis.
[3]"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. expand/collapse author list , 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] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Hypothalamus.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"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] (ISOFORM 1).
Strain: FVB/N.
Tissue: Mammary tumor.
[6]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 89-97, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[7]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF197574 mRNA. Translation: AAF18440.1.
AF539614 mRNA. Translation: AAN23117.1.
AK039024 mRNA. Translation: BAC30209.1.
AC151906 Genomic DNA. No translation available.
BC021316 mRNA. Translation: AAH21316.1.
CCDSCCDS23298.1. [Q9QXN3-1]
CCDS52838.1. [Q9QXN3-2]
RefSeqNP_001164378.1. NM_001170907.1. [Q9QXN3-2]
NP_062771.2. NM_019797.4. [Q9QXN3-1]
XP_006511359.1. XM_006511296.1. [Q9QXN3-1]
XP_006511360.1. XM_006511297.1. [Q9QXN3-1]
XP_006511361.1. XM_006511298.1. [Q9QXN3-1]
XP_006511362.1. XM_006511299.1. [Q9QXN3-1]
XP_006511363.1. XM_006511300.1. [Q9QXN3-2]
UniGeneMm.208379.

3D structure databases

ProteinModelPortalQ9QXN3.
SMRQ9QXN3. Positions 434-581.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207956. 3 interactions.

PTM databases

PhosphoSiteQ9QXN3.

Proteomic databases

MaxQBQ9QXN3.
PRIDEQ9QXN3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000117083; ENSMUSP00000113949; ENSMUSG00000032386. [Q9QXN3-1]
ENSMUST00000119245; ENSMUSP00000112385; ENSMUSG00000032386. [Q9QXN3-1]
ENSMUST00000122410; ENSMUSP00000112866; ENSMUSG00000032386. [Q9QXN3-2]
ENSMUST00000179395; ENSMUSP00000137304; ENSMUSG00000032386. [Q9QXN3-2]
GeneID56404.
KEGGmmu:56404.
UCSCuc009qdz.2. mouse. [Q9QXN3-2]
uc012gvn.1. mouse. [Q9QXN3-1]

Organism-specific databases

CTD9325.
MGIMGI:1928469. Trip4.

Phylogenomic databases

eggNOGNOG248556.
GeneTreeENSGT00390000005300.
HOGENOMHOG000006873.
HOVERGENHBG061618.
InParanoidQ9QXN3.
OMAMSGTENS.
OrthoDBEOG7RZ5PP.
TreeFamTF314842.

Gene expression databases

ArrayExpressQ9QXN3.
BgeeQ9QXN3.
CleanExMM_TRIP4.
GenevestigatorQ9QXN3.

Family and domain databases

InterProIPR007374. ASCH_domain.
IPR015947. PUA-like_domain.
IPR009349. Znf_C2HC5.
[Graphical view]
PfamPF04266. ASCH. 1 hit.
PF06221. zf-C2HC5. 1 hit.
[Graphical view]
SMARTSM01022. ASCH. 1 hit.
[Graphical view]
SUPFAMSSF88697. SSF88697. 2 hits.
ProtoNetSearch...

Other

ChiTaRSTRIP4. mouse.
NextBio312526.
PROQ9QXN3.
SOURCESearch...

Entry information

Entry nameTRIP4_MOUSE
AccessionPrimary (citable) accession number: Q9QXN3
Secondary accession number(s): E9QK64, Q8CAD5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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