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Protein

Activating signal cointegrator 1

Gene

Trip4

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

Functioni

Transcription coactivator which associates with nuclear receptors, transcriptional coactivators including EP300, CREBBP and NCOA1, and basal transcription factors like TBP and TFIIA to facilitate nuclear receptors-mediated transcription. May thereby play an important role in establishing distinct coactivator complexes under different cellular conditions. Plays a role in thyroid hormone receptor and estrogen receptor transactivation (By similarity). Also involved in androgen receptor transactivation (PubMed:12077347). 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).By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri167 – 21953C4-typeAdd
BLAST

GO - Molecular functioni

  1. estrogen receptor binding Source: UniProtKB
  2. histone acetyltransferase binding Source: UniProtKB
  3. ligand-dependent nuclear receptor binding Source: UniProtKB
  4. protease binding Source: MGI
  5. transcription coactivator activity Source: UniProtKB
  6. ubiquitin-like protein ligase binding Source: UniProtKB
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. intracellular estrogen receptor signaling pathway Source: UniProtKB
  2. positive regulation of transcription, DNA-templated Source: UniProtKB
  3. toxin transport Source: MGI
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Activating signal cointegrator 11 Publication
Short name:
ASC-11 Publication
Alternative name(s):
Thyroid receptor-interacting protein 4Curated
Short name:
TR-interacting protein 4Curated
Short name:
TRIP-4Curated
Gene namesi
Name:Trip4Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1928469. Trip4.

Subcellular locationi

Nucleus By similarity. Cytoplasmcytosol By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
Note: Cytoplasmic under conditions of serum deprivation. Colocalizes with NEK6 in the centrosome.By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: UniProtKB-SubCell
  3. microtubule organizing center Source: UniProtKB-SubCell
  4. nucleoplasm Source: MGI
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 581580Activating signal cointegrator 1PRO_0000065632Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei289 – 2891Phosphotyrosine1 Publication
Cross-linki324 – 324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1)By similarity
Cross-linki334 – 334Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1)By similarity

Post-translational modificationi

Phosphorylated by NEK6.By similarity
Polyufmylated by the UFM1-conjugating system composed of the enzymes UBA5, UFC1 and UFL1. Deufmylated by the protease UFSP2. Ufmylation of TRIP4 is promoted by ligand-bound nuclear receptors that compete with UFSP2 for interaction with TRIP4. Nuclear receptors-induced ufmylation promotes the recruitment of additional transcriptional coactivators like EP300 and NCOA1 and therefore the assembly of a coactivator complex facilitating nuclear receptor-mediated transcription.By similarity1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9QXN3.
PRIDEiQ9QXN3.

PTM databases

PhosphoSiteiQ9QXN3.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ9QXN3.
CleanExiMM_TRIP4.
ExpressionAtlasiQ9QXN3. baseline and differential.
GenevestigatoriQ9QXN3.

Interactioni

Subunit structurei

Interacts with the thyroid hormone receptor/TR (via the ligand-binding domain); this interaction requires the presence of thyroid hormone (By similarity). Interacts with the androgen receptor/AR; in an androgen, testosterone and dihydrotestosterone-dependent manner (By similarity). Interacts with ESR1 (estrogen ligand-bound); competes with UFSP2 (By similarity). Interacts with UFSP2; competes with ligand-bound ESR1 (By similarity). Interacts with DDRGK1 and UFL1; the interaction with DDRGK1 is direct (By similarity). Interacts with NCOA1 (By similarity). Interacts with EP300 (By similarity). Exists as a steady-state complex associated with ASCC1, ASCC2 and HELIC1 (PubMed:12077347). Interacts with NEK6 (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi207956. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9QXN3.
SMRiQ9QXN3. Positions 434-581.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni200 – 300101Mediates interaction with DDRGK1By similarityAdd
BLAST
Regioni300 – 400101Mediates interaction with UFL1By similarityAdd
BLAST

Domaini

The C4-type zinc finger mediates a competitive interaction with UFSP2 and ligand-bound nuclear receptors. It also mediates interaction with the transcriptional coactivators and the basal transcription machinery.By similarity

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri167 – 21953C4-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG248556.
GeneTreeiENSGT00390000005300.
HOGENOMiHOG000006873.
HOVERGENiHBG061618.
InParanoidiQ9QXN3.
OMAiDCLSQEQ.
OrthoDBiEOG7RZ5PP.
TreeFamiTF314842.

Family and domain databases

InterProiIPR007374. ASCH_domain.
IPR015947. PUA-like_domain.
IPR009349. Znf_C2HC5.
[Graphical view]
PfamiPF04266. ASCH. 1 hit.
PF06221. zf-C2HC5. 1 hit.
[Graphical view]
SMARTiSM01022. ASCH. 1 hit.
[Graphical view]
SUPFAMiSSF88697. SSF88697. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9QXN3-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAVAGAAYRE PLVHWCTQQL QKTFALDVSE EIIQYVLSIE NAEEIREYVT
60 70 80 90 100
DLLQGNEGKK GQFIEDLITK WQKNDQEFIS DSFQQCLRKD EILDGQRSVD
110 120 130 140 150
QLKRSRRKGR NKQEVPAFPE PDVAVEVKTP LDLAKAQESN NSVKKKTRFV
160 170 180 190 200
NLYTREGQDK LAVLLPGRHP CDCLGQKHKL INNCLVCGRI VCEQEGSGPC
210 220 230 240 250
LFCGSLVCTN EEQDILQRDS NKSQKLLKKL MSGAETSGKV DVSTKDLLPH
260 270 280 290 300
QESRMKSGLE KAIKHKEKLL EFDRTSIRRT QVIDDESDYF ASDSNQWLSK
310 320 330 340 350
VEREMLQKRE EELRELRHAS RLSKKVTIDF AGRKILEDEN PLAEYHSRLD
360 370 380 390 400
ETIQAIASGT LNQSLVTLDR SCEEPLGVLV NPNMYQASPQ WVDNTGSTPQ
410 420 430 440 450
KKTSLSAGPR LEPSLHQHQL RIQDQEFQEG FDGGWCLSMH QPWASLLVRG
460 470 480 490 500
IKRVEGRSWY TPHRGRLWIA ATGKRPSPQE VSELQATYRL LRGKDVEFPN
510 520 530 540 550
DYPSGCLLGC VDLIDCLSQK QFQEQFPDIS QESDSSFVFI CKNPQEMVVK
560 570 580
FPIKGNPKIW KLDSKIHQGA KKGLMKQNKA V
Length:581
Mass (Da):66,197
Last modified:July 27, 2011 - v2
Checksum:i2CAB3512E3CEDDA7
GO
Isoform 2 (identifier: Q9QXN3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     526-539: FPDISQESDSSFVF → GNWIPRSIKEQRRG
     540-581: Missing.

Note: No experimental confirmation available.

Show »
Length:539
Mass (Da):61,533
Checksum:iFF965B4855F43891
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71A → G in BAC30209 (PubMed:16141072).Curated
Sequence conflicti388 – 3881S → P in AAF18440 (PubMed:12077347).Curated
Sequence conflicti388 – 3881S → P in AAN23117 (PubMed:12390891).Curated
Sequence conflicti388 – 3881S → P in AAH21316 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei526 – 53914FPDIS…SSFVF → GNWIPRSIKEQRRG in isoform 2. 1 PublicationVSP_011109Add
BLAST
Alternative sequencei540 – 58142Missing in isoform 2. 1 PublicationVSP_011110Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23298.1. [Q9QXN3-1]
CCDS52838.1. [Q9QXN3-2]
RefSeqiNP_001164378.1. NM_001170907.1. [Q9QXN3-2]
NP_062771.2. NM_019797.4. [Q9QXN3-1]
XP_006511359.1. XM_006511296.2. [Q9QXN3-1]
XP_006511361.1. XM_006511298.2. [Q9QXN3-1]
XP_006511362.1. XM_006511299.2. [Q9QXN3-1]
UniGeneiMm.208379.

Genome annotation databases

EnsembliENSMUST00000117083; ENSMUSP00000113949; ENSMUSG00000032386. [Q9QXN3-1]
ENSMUST00000119245; ENSMUSP00000112385; ENSMUSG00000032386. [Q9QXN3-1]
ENSMUST00000122410; ENSMUSP00000112866; ENSMUSG00000032386. [Q9QXN3-2]
ENSMUST00000179395; ENSMUSP00000137304; ENSMUSG00000032386. [Q9QXN3-2]
GeneIDi56404.
KEGGimmu:56404.
UCSCiuc009qdz.2. mouse. [Q9QXN3-2]
uc012gvn.1. mouse. [Q9QXN3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23298.1. [Q9QXN3-1]
CCDS52838.1. [Q9QXN3-2]
RefSeqiNP_001164378.1. NM_001170907.1. [Q9QXN3-2]
NP_062771.2. NM_019797.4. [Q9QXN3-1]
XP_006511359.1. XM_006511296.2. [Q9QXN3-1]
XP_006511361.1. XM_006511298.2. [Q9QXN3-1]
XP_006511362.1. XM_006511299.2. [Q9QXN3-1]
UniGeneiMm.208379.

3D structure databases

ProteinModelPortaliQ9QXN3.
SMRiQ9QXN3. Positions 434-581.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207956. 3 interactions.

PTM databases

PhosphoSiteiQ9QXN3.

Proteomic databases

MaxQBiQ9QXN3.
PRIDEiQ9QXN3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000117083; ENSMUSP00000113949; ENSMUSG00000032386. [Q9QXN3-1]
ENSMUST00000119245; ENSMUSP00000112385; ENSMUSG00000032386. [Q9QXN3-1]
ENSMUST00000122410; ENSMUSP00000112866; ENSMUSG00000032386. [Q9QXN3-2]
ENSMUST00000179395; ENSMUSP00000137304; ENSMUSG00000032386. [Q9QXN3-2]
GeneIDi56404.
KEGGimmu:56404.
UCSCiuc009qdz.2. mouse. [Q9QXN3-2]
uc012gvn.1. mouse. [Q9QXN3-1]

Organism-specific databases

CTDi9325.
MGIiMGI:1928469. Trip4.

Phylogenomic databases

eggNOGiNOG248556.
GeneTreeiENSGT00390000005300.
HOGENOMiHOG000006873.
HOVERGENiHBG061618.
InParanoidiQ9QXN3.
OMAiDCLSQEQ.
OrthoDBiEOG7RZ5PP.
TreeFamiTF314842.

Miscellaneous databases

ChiTaRSiTrip4. mouse.
NextBioi312526.
PROiQ9QXN3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QXN3.
CleanExiMM_TRIP4.
ExpressionAtlasiQ9QXN3. baseline and differential.
GenevestigatoriQ9QXN3.

Family and domain databases

InterProiIPR007374. ASCH_domain.
IPR015947. PUA-like_domain.
IPR009349. Znf_C2HC5.
[Graphical view]
PfamiPF04266. ASCH. 1 hit.
PF06221. zf-C2HC5. 1 hit.
[Graphical view]
SMARTiSM01022. ASCH. 1 hit.
[Graphical view]
SUPFAMiSSF88697. SSF88697. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2001) [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(2001) [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.
    , 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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Hypothalamus.
  4. 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(2003) [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 (MAR-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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  8. "Ubiquitin fold modifier 1 (UFM1) and its target UFBP1 protect pancreatic beta cells from ER stress-induced apoptosis."
    Lemaire K., Moura R.F., Granvik M., Igoillo-Esteve M., Hohmeier H.E., Hendrickx N., Newgard C.B., Waelkens E., Cnop M., Schuit F.
    PLoS ONE 6:E18517-E18517(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UFMYLATION.

Entry informationi

Entry nameiTRIP4_MOUSE
AccessioniPrimary (citable) accession number: Q9QXN3
Secondary accession number(s): E9QK64, Q8CAD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 116 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, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

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 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.