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Q15650

- TRIP4_HUMAN

UniProt

Q15650 - TRIP4_HUMAN

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Protein
Activating signal cointegrator 1
Gene
TRIP4
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri171 – 18717C4-type
Add
BLAST

GO - Molecular functioni

  1. ligand-dependent nuclear receptor binding Source: UniProtKB
  2. transcription coactivator activity Source: ProtInc
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. positive regulation of transcription, DNA-templated Source: UniProtKB
  2. transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:TRIP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:12310. TRIP4.

Subcellular locationi

Nucleus. Cytoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
Note: Cytoplasmic under conditions of serum deprivation. Colocalizes with NEK6 in the centrosome.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. microtubule organizing center Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36988.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 581580Activating signal cointegrator 1
PRO_0000065631Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei289 – 2891Phosphotyrosine By similarity

Post-translational modificationi

Phosphorylated by NEK6.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15650.
PaxDbiQ15650.
PeptideAtlasiQ15650.
PRIDEiQ15650.

PTM databases

PhosphoSiteiQ15650.

Expressioni

Gene expression databases

ArrayExpressiQ15650.
BgeeiQ15650.
CleanExiHS_TRIP4.
GenevestigatoriQ15650.

Organism-specific databases

HPAiHPA016605.
HPA050666.

Interactioni

Subunit structurei

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 NEK6.2 Publications

Protein-protein interaction databases

BioGridi114735. 33 interactions.
IntActiQ15650. 4 interactions.
STRINGi9606.ENSP00000261884.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi435 – 4395
Helixi443 – 4486
Beta strandi454 – 4596
Beta strandi465 – 4717
Helixi478 – 49215
Beta strandi504 – 51815
Helixi521 – 5255
Turni530 – 5323
Beta strandi535 – 54612
Beta strandi557 – 5615
Helixi564 – 5729
Helixi573 – 5753

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5ONMR-A435-581[»]
ProteinModelPortaliQ15650.
SMRiQ15650. Positions 434-581.

Miscellaneous databases

EvolutionaryTraceiQ15650.

Family & Domainsi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG248556.
HOGENOMiHOG000006873.
HOVERGENiHBG061618.
InParanoidiQ15650.
OMAiMSGTENS.
OrthoDBiEOG7RZ5PP.
PhylomeDBiQ15650.
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.

Sequencei

Sequence statusi: Complete.

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

Q15650-1 [UniParc]FASTAAdd to Basket

« Hide

MAVAGAVSGE PLVHWCTQQL RKTFGLDVSE EIIQYVLSIE SAEEIREYVT    50
DLLQGNEGKK GQFIEELITK WQKNDQELIS DPLQQCFKKD EILDGQKSGD 100
HLKRGRKKGR NRQEVPAFTE PDTTAEVKTP FDLAKAQENS NSVKKKTKFV 150
NLYTREGQDR LAVLLPGRHP CDCLGQKHKL INNCLICGRI VCEQEGSGPC 200
LFCGTLVCTH EEQDILQRDS NKSQKLLKKL MSGVENSGKV DISTKDLLPH 250
QELRIKSGLE KAIKHKDKLL EFDRTSIRRT QVIDDESDYF ASDSNQWLSK 300
LERETLQKRE EELRELRHAS RLSKKVTIDF AGRKILEEEN SLAEYHSRLD 350
ETIQAIANGT LNQPLTKLDR SSEEPLGVLV NPNMYQSPPQ WVDHTGAASQ 400
KKAFRSSGFG LEFNSFQHQL RIQDQEFQEG FDGGWCLSVH QPWASLLVRG 450
IKRVEGRSWY TPHRGRLWIA ATAKKPSPQE VSELQATYRL LRGKDVEFPN 500
DYPSGCLLGC VDLIDCLSQK QFKEQFPDIS QESDSPFVFI CKNPQEMVVK 550
FPIKGNPKIW KLDSKIHQGA KKGLMKQNKA V 581
Length:581
Mass (Da):66,146
Last modified:October 17, 2006 - v4
Checksum:iDADD3994533A808E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1571G → R in AAF01278. 1 Publication
Sequence conflicti157 – 1571G → R in AAC41738. 1 Publication
Sequence conflicti164 – 1641L → A in AAF01278. 1 Publication
Sequence conflicti392 – 41019VDHTG…SSGFG → LTTQVQPHRRRLSVLQDLD1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS10194.1.
RefSeqiNP_057297.2. NM_016213.4.
UniGeneiHs.500340.

Genome annotation databases

EnsembliENST00000261884; ENSP00000261884; ENSG00000103671.
GeneIDi9325.
KEGGihsa:9325.
UCSCiuc002anm.3. human.

Polymorphism databases

DMDMi116242828.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS10194.1.
RefSeqi NP_057297.2. NM_016213.4.
UniGenei Hs.500340.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2E5O NMR - A 435-581 [» ]
ProteinModelPortali Q15650.
SMRi Q15650. Positions 434-581.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114735. 33 interactions.
IntActi Q15650. 4 interactions.
STRINGi 9606.ENSP00000261884.

PTM databases

PhosphoSitei Q15650.

Polymorphism databases

DMDMi 116242828.

Proteomic databases

MaxQBi Q15650.
PaxDbi Q15650.
PeptideAtlasi Q15650.
PRIDEi Q15650.

Protocols and materials databases

DNASUi 9325.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261884 ; ENSP00000261884 ; ENSG00000103671 .
GeneIDi 9325.
KEGGi hsa:9325.
UCSCi uc002anm.3. human.

Organism-specific databases

CTDi 9325.
GeneCardsi GC15P064876.
HGNCi HGNC:12310. TRIP4.
HPAi HPA016605.
HPA050666.
MIMi 604501. gene.
neXtProti NX_Q15650.
PharmGKBi PA36988.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG248556.
HOGENOMi HOG000006873.
HOVERGENi HBG061618.
InParanoidi Q15650.
OMAi MSGTENS.
OrthoDBi EOG7RZ5PP.
PhylomeDBi Q15650.
TreeFami TF314842.

Miscellaneous databases

EvolutionaryTracei Q15650.
GeneWikii TRIP4.
GenomeRNAii 9325.
NextBioi 34931.
PROi Q15650.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q15650.
Bgeei Q15650.
CleanExi HS_TRIP4.
Genevestigatori Q15650.

Family and domain databases

InterProi IPR007374. ASCH_domain.
IPR015947. PUA-like_domain.
IPR009349. Znf_C2HC5.
[Graphical view ]
Pfami PF04266. ASCH. 1 hit.
PF06221. zf-C2HC5. 1 hit.
[Graphical view ]
SMARTi SM01022. ASCH. 1 hit.
[Graphical view ]
SUPFAMi SSF88697. SSF88697. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTRIP4_HUMAN
AccessioniPrimary (citable) accession number: Q15650
Secondary accession number(s): B2RAS0, Q96ED7, Q9UKH0
Entry historyi
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 statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

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