Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q15650

- TRIP4_HUMAN

UniProt

Q15650 - TRIP4_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri171 – 18717C4-typeAdd
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 1 Publication. Cytoplasm 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
Note: Cytoplasmic under conditions of serum deprivation. Colocalizes with NEK6 in the centrosome.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-KW
  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 1PRO_0000065631Add
BLAST

Amino acid modifications

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

BgeeiQ15650.
CleanExiHS_TRIP4.
ExpressionAtlasiQ15650. baseline and differential.
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.By similarity2 Publications

Protein-protein interaction databases

BioGridi114735. 35 interactions.
IntActiQ15650. 4 interactions.
STRINGi9606.ENSP00000261884.

Structurei

Secondary structure

1
581
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi435 – 4395Combined sources
Helixi443 – 4486Combined sources
Beta strandi454 – 4596Combined sources
Beta strandi465 – 4717Combined sources
Helixi478 – 49215Combined sources
Beta strandi504 – 51815Combined sources
Helixi521 – 5255Combined sources
Turni530 – 5323Combined sources
Beta strandi535 – 54612Combined sources
Beta strandi557 – 5615Combined sources
Helixi564 – 5729Combined sources
Helixi573 – 5753Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5ONMR-A435-581[»]
ProteinModelPortaliQ15650.
SMRiQ15650. Positions 434-581.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15650.

Family & Domainsi

Zinc finger

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

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG248556.
GeneTreeiENSGT00390000005300.
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

        10         20         30         40         50
MAVAGAVSGE PLVHWCTQQL RKTFGLDVSE EIIQYVLSIE SAEEIREYVT
60 70 80 90 100
DLLQGNEGKK GQFIEELITK WQKNDQELIS DPLQQCFKKD EILDGQKSGD
110 120 130 140 150
HLKRGRKKGR NRQEVPAFTE PDTTAEVKTP FDLAKAQENS NSVKKKTKFV
160 170 180 190 200
NLYTREGQDR LAVLLPGRHP CDCLGQKHKL INNCLICGRI VCEQEGSGPC
210 220 230 240 250
LFCGTLVCTH EEQDILQRDS NKSQKLLKKL MSGVENSGKV DISTKDLLPH
260 270 280 290 300
QELRIKSGLE KAIKHKDKLL EFDRTSIRRT QVIDDESDYF ASDSNQWLSK
310 320 330 340 350
LERETLQKRE EELRELRHAS RLSKKVTIDF AGRKILEEEN SLAEYHSRLD
360 370 380 390 400
ETIQAIANGT LNQPLTKLDR SSEEPLGVLV NPNMYQSPPQ WVDHTGAASQ
410 420 430 440 450
KKAFRSSGFG LEFNSFQHQL RIQDQEFQEG FDGGWCLSVH QPWASLLVRG
460 470 480 490 500
IKRVEGRSWY TPHRGRLWIA ATAKKPSPQE VSELQATYRL LRGKDVEFPN
510 520 530 540 550
DYPSGCLLGC VDLIDCLSQK QFKEQFPDIS QESDSPFVFI CKNPQEMVVK
560 570 580
FPIKGNPKIW KLDSKIHQGA KKGLMKQNKA V
Length:581
Mass (Da):66,146
Last modified:October 17, 2006 - v4
Checksum:iDADD3994533A808E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1571G → R in AAF01278. (PubMed:10454579)Curated
Sequence conflicti157 – 1571G → R in AAC41738. (PubMed:7776974)Curated
Sequence conflicti164 – 1641L → A in AAF01278. (PubMed:10454579)Curated
Sequence conflicti392 – 41019VDHTG…SSGFG → LTTQVQPHRRRLSVLQDLD(PubMed:7776974)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 35 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 GC15P065758.
HGNCi HGNC:12310. TRIP4.
HPAi HPA016605.
HPA050666.
MIMi 604501. gene.
neXtProti NX_Q15650.
PharmGKBi PA36988.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG248556.
GeneTreei ENSGT00390000005300.
HOGENOMi HOG000006873.
HOVERGENi HBG061618.
InParanoidi Q15650.
OMAi MSGTENS.
OrthoDBi EOG7RZ5PP.
PhylomeDBi Q15650.
TreeFami TF314842.

Miscellaneous databases

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

Gene expression databases

Bgeei Q15650.
CleanExi HS_TRIP4.
ExpressionAtlasi Q15650. baseline and differential.
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: November 26, 2014
This is version 129 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