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Q15650 (TRIP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Plays a role in androgen receptor transactivation and in testicular function By similarity. Ref.6

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. Interacts with the androgen receptor androgen (AR) in an androgen, testosterone and dihydrotestosterone-dependent manner By similarity. Interacts with NEK6. Ref.6 Ref.10

Subcellular location

Nucleus. Cytoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Cytoplasmic under conditions of serum deprivation. Colocalizes with NEK6 in the centrosome. Ref.10

Post-translational modification

Phosphorylated by NEK6. Ref.10

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 581580Activating signal cointegrator 1
PRO_0000065631

Regions

Zinc finger171 – 18717C4-type

Amino acid modifications

Modified residue21N-acetylalanine Ref.9
Modified residue2891Phosphotyrosine By similarity

Experimental info

Sequence conflict1571G → R in AAF01278. Ref.1
Sequence conflict1571G → R in AAC41738. Ref.5
Sequence conflict1641L → A in AAF01278. Ref.1
Sequence conflict392 – 41019VDHTG…SSGFG → LTTQVQPHRRRLSVLQDLD Ref.5

Secondary structure

........................ 581
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15650 [UniParc].

Last modified October 17, 2006. Version 4.
Checksum: DADD3994533A808E

FASTA58166,146
        10         20         30         40         50         60 
MAVAGAVSGE PLVHWCTQQL RKTFGLDVSE EIIQYVLSIE SAEEIREYVT DLLQGNEGKK 

        70         80         90        100        110        120 
GQFIEELITK WQKNDQELIS DPLQQCFKKD EILDGQKSGD HLKRGRKKGR NRQEVPAFTE 

       130        140        150        160        170        180 
PDTTAEVKTP FDLAKAQENS NSVKKKTKFV NLYTREGQDR LAVLLPGRHP CDCLGQKHKL 

       190        200        210        220        230        240 
INNCLICGRI VCEQEGSGPC LFCGTLVCTH EEQDILQRDS NKSQKLLKKL MSGVENSGKV 

       250        260        270        280        290        300 
DISTKDLLPH QELRIKSGLE KAIKHKDKLL EFDRTSIRRT QVIDDESDYF ASDSNQWLSK 

       310        320        330        340        350        360 
LERETLQKRE EELRELRHAS RLSKKVTIDF AGRKILEEEN SLAEYHSRLD ETIQAIANGT 

       370        380        390        400        410        420 
LNQPLTKLDR SSEEPLGVLV NPNMYQSPPQ WVDHTGAASQ KKAFRSSGFG LEFNSFQHQL 

       430        440        450        460        470        480 
RIQDQEFQEG FDGGWCLSVH QPWASLLVRG IKRVEGRSWY TPHRGRLWIA ATAKKPSPQE 

       490        500        510        520        530        540 
VSELQATYRL LRGKDVEFPN DYPSGCLLGC VDLIDCLSQK QFKEQFPDIS QESDSPFVFI 

       550        560        570        580 
CKNPQEMVVK FPIKGNPKIW KLDSKIHQGA KKGLMKQNKA V 

« Hide

References

« Hide 'large scale' references
[1]"Activating signal cointegrator 1, a novel transcription coactivator of nuclear receptors, and its cytosolic localization under conditions of serum deprivation."
Kim H.J., Yi J.Y., Sung H.S., Moore D.D., Jhun B.H., Lee Y.C., Lee J.W.
Mol. Cell. Biol. 19:6323-6332(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Lung.
[5]"Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor."
Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.
Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 125-410.
[6]"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: FUNCTION, INTERACTION WITH ASCC1; ASCC2 AND HELIC1.
[7]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome."
Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J.
J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK6, PHOSPHORYLATION BY NEK6.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF168418 mRNA. Translation: AAF01278.1.
AK314319 mRNA. Translation: BAG36967.1.
CH471082 Genomic DNA. Translation: EAW77685.1.
BC012448 mRNA. Translation: AAH12448.1.
L40371 mRNA. Translation: AAC41738.1.
CCDSCCDS10194.1.
RefSeqNP_057297.2. NM_016213.4.
UniGeneHs.500340.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5ONMR-A435-581[»]
ProteinModelPortalQ15650.
SMRQ15650. Positions 434-581.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114735. 33 interactions.
IntActQ15650. 4 interactions.
STRING9606.ENSP00000261884.

PTM databases

PhosphoSiteQ15650.

Polymorphism databases

DMDM116242828.

Proteomic databases

MaxQBQ15650.
PaxDbQ15650.
PeptideAtlasQ15650.
PRIDEQ15650.

Protocols and materials databases

DNASU9325.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261884; ENSP00000261884; ENSG00000103671.
GeneID9325.
KEGGhsa:9325.
UCSCuc002anm.3. human.

Organism-specific databases

CTD9325.
GeneCardsGC15P064876.
HGNCHGNC:12310. TRIP4.
HPAHPA016605.
HPA050666.
MIM604501. gene.
neXtProtNX_Q15650.
PharmGKBPA36988.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG248556.
HOGENOMHOG000006873.
HOVERGENHBG061618.
InParanoidQ15650.
OMAMSGTENS.
OrthoDBEOG7RZ5PP.
PhylomeDBQ15650.
TreeFamTF314842.

Gene expression databases

ArrayExpressQ15650.
BgeeQ15650.
CleanExHS_TRIP4.
GenevestigatorQ15650.

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

EvolutionaryTraceQ15650.
GeneWikiTRIP4.
GenomeRNAi9325.
NextBio34931.
PROQ15650.
SOURCESearch...

Entry information

Entry nameTRIP4_HUMAN
AccessionPrimary (citable) accession number: Q15650
Secondary accession number(s): B2RAS0, Q96ED7, Q9UKH0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 126 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM