Q15654 (TRIP6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thyroid receptor-interacting protein 6
Short name=TR-interacting protein 6
Short name=TRIP-6

Alternative name(s):
Opa-interacting protein 1
Short name=OIP-1
Zyxin-related protein 1
Short name=ZRP-1

Gene names

Name:	TRIP6
Synonyms:	OIP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	476 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Relays signals from the cell surface to the nucleus to weaken adherens junction and promote actin cytoskeleton reorganization and cell invasiveness. Involved in lysophosphatidic acid-induced cell adhesion and migration. Acts as a transcriptional coactivator for NF-kappa-B and JUN, and mediates the transrepression of these transcription factors induced by glucocorticoid receptor. Ref.9 Ref.10 Ref.14 Ref.19
Subunit structure	Specifically interacts with the ligand binding domain of the thyroid receptor (TR) in the presence of thyroid hormone. Interacts with PTPN13. Interacts with SVIL isoform 2. Interacts with LPAR2 but not other LPA receptors. Interacts with PRKAA2. Interacts with MAGI1. Interacts with SCRIB By similarity. Binds to S.typhimurium protein sseI. Ref.2 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19
Subcellular location	Cytoplasm › cytoskeleton. Cell junction › focal adhesion. Nucleus. Cytoplasm. Note: Shuttles between nucleus and cytoplasm. Ref.14
Tissue specificity	Abundantly expressed in kidney, liver and lung. Lower levels in heart, placenta and pancreas. Expressed in colonic epithelial cells. Up-regulated in colonic tumors. Ref.19
Domain	The LIM zinc-binding domains mediate interaction with LPAR2 and with S.typhimurium protein sseI.
Post-translational modification	Phosphorylation at Tyr-55 by SRC is required for enhancement of lysophosphatidic acid-induced cell migration. Tyr-55 is dephosphorylated by PTPN13. Ref.12 Ref.17
Sequence similarities	Belongs to the zyxin/ajuba family. Contains 3 LIM zinc-binding domains.
Sequence caution	The sequence AAC41740.1 differs from that shown. Reason: Frameshift at position 461.

Ontologies

Keywords
Biological process	Cell adhesion Transcription Transcription regulation
Cellular component	Cell junction Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Polymorphism
Domain	LIM domain Repeat
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	focal adhesion assembly Non-traceable author statement Ref.10. Source: UniProtKB positive regulation of cell migration Inferred from mutant phenotype Ref.10. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW release of cytoplasmic sequestered NF-kappaB Inferred from direct assay PubMed 15657077. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell focal adhesion Inferred from direct assay Ref.10. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	interleukin-1 receptor binding Inferred from direct assay PubMed 15657077. Source: UniProtKB thyroid hormone receptor binding Non-traceable author statement Ref.1. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATN1	P54259	2	EBI-742327,EBI-945980
Hoxa1	P09022	3	EBI-742327,EBI-3957603	From a different organism.
HOXA9	P31269	4	EBI-742327,EBI-742314
PPP1R16A	Q96I34	3	EBI-742327,EBI-710402

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 476

476

Thyroid receptor-interacting protein 6

PRO_0000075908

Regions

Domain

279 – 316

38

LIM zinc-binding 1

Domain

339 – 398

60

LIM zinc-binding 2

Domain

399 – 467

69

LIM zinc-binding 3

Region

469 – 476

8

Interaction with MAGI1 and PTPN13

Amino acid modifications

Modified residue

55

1

Phosphotyrosine; by SRC Ref.12 Ref.17

Modified residue

92

1

Phosphoserine Ref.13 Ref.20

Modified residue

142

1

Phosphoserine Ref.18

Natural variations

Natural variant

111

1

R → Q. Ref.7
Corresponds to variant rs2437100 [ dbSNP | Ensembl ].

VAR_062262

Natural variant

230

1

V → I. Ref.7
Corresponds to variant rs2075756 [ dbSNP | Ensembl ].

VAR_050171

Natural variant

296

1

L → F. Ref.7
Corresponds to variant rs17855370 [ dbSNP | Ensembl ].

VAR_013309

Experimental info

Mutagenesis

101

1

S → A: Exclusively located in nucleus. Ref.14

Mutagenesis

102

1

S → A: Exclusively located in nucleus. Ref.14

Mutagenesis

474

1

T → A: Reduces interaction with MAGI1. Ref.19

Sequence conflict

39 – 40

2

Missing in AAH02680. Ref.7

Sequence conflict

102

1

S → T in AAB62222. Ref.2

Sequence conflict

106

1

E → K in AAB62222. Ref.2

Sequence conflict

135

1

S → C in CAA05080. Ref.1

Sequence conflict

310 – 313

4

CRAQ → MPGP in AAC41740. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

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.

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476

Helix Strand Turn

Details...

Beta strand

280 – 282

3

Beta strand

288 – 290

3

Beta strand

296 – 300

5

Turn

302 – 304

3

Beta strand

308 – 310

3

Beta strand

319 – 324

6

Beta strand

326 – 328

3

Helix

329 – 337

9

Turn

340 – 342

3

Beta strand

351 – 353

3

Beta strand

356 – 358

3

Turn

360 – 362

3

Beta strand

366 – 368

3

Helix

388 – 394

7

Sequences

	Sequence		Length	Mass (Da)
	Q15654 [UniParc]. Last modified May 15, 2002. Version 3. Checksum: 2BA7C747DF30A8FD	FASTA	476	50,288
	10 20 30 40 50 60 MSGPTWLPPK QPEPARAPQG RAIPRGTPGP PPAHGAALQP HPRVNFCPLP SEQCYQAPGG 70 80 90 100 110 120 PEDRGPAWVG SHGVLQHTQG LPADRGGLRP GSLDAEIDLL SSTLAELNGG RGHASRRPDR 130 140 150 160 170 180 QAYEPPPPPA YRTGSLKPNP ASPLPASPYG GPTPASYTTA STPAGPAFPV QVKVAQPVRG 190 200 210 220 230 240 CGPPRRGASQ ASGPLPGPHF PLPGRGEVWG PGYRSQREPG PGAKEEAAGV SGPAGRGRGG 250 260 270 280 290 300 EHGPQVPLSQ PPEDELDRLT KKLVHDMNHP PSGEYFGQCG GCGEDVVGDG AGVVALDRVF 310 320 330 340 350 360 HVGCFVCSTC RAQLRGQHFY AVERRAYCEG CYVATLEKCA TCSQPILDRI LRAMGKAYHP 370 380 390 400 410 420 GCFTCVVCHR GLDGIPFTVD ATSQIHCIED FHRKFAPRCS VCGGAIMPEP GQEETVRIVA 430 440 450 460 470 LDRSFHIGCY KCEECGLLLS SEGECQGCYP LDGHILCKAC SAWRIQELSA TVTTDC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human TRIP6 gene encodes a LIM domain protein and maps to chromosome 7q22, a region associated with tumorigenesis." Yi J., Beckerle M.C. Genomics 49:314-316(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"ZRP-1, a zyxin-related protein, interacts with the second PDZ domain of the cytosolic protein tyrosine phosphatase hPTP1E." Murthy K.K., Clark K., Fortin Y., Shen S.-H., Banville D. J. Biol. Chem. 274:20679-20687(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INTERACTION WITH PTPN13.
[3]	"Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5." Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P., Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W., Koop B.F. Nucleic Acids Res. 29:1352-1365(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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].
[5]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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. , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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], VARIANTS GLN-111; ILE-230 AND PHE-296. Tissue: Cervix, Kidney and Pancreas.
[8]	"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 310-476.
[9]	"A nuclear isoform of the focal adhesion LIM-domain protein Trip6 integrates activating and repressing signals at AP-1- and NF-kappaB-regulated promoters." Kassel O., Schneider S., Heilbock C., Litfin M., Goettlicher M., Herrlich P. Genes Dev. 18:2518-2528(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"TRIP6 enhances lysophosphatidic acid-induced cell migration by interacting with the lysophosphatidic acid 2 receptor." Xu J., Lai Y.-J., Lin W.-C., Lin F.-T. J. Biol. Chem. 279:10459-10468(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LPAR2, FUNCTION.
[11]	"The tumor suppressor Scrib selectively interacts with specific members of the zyxin family of proteins." Petit M.M.R., Crombez K.R.M.O., Vervenne H.B.V.K., Weyns N., Van de Ven W.J.M. FEBS Lett. 579:5061-5068(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SCRIB.
[12]	"c-Src-mediated phosphorylation of TRIP6 regulates its function in lysophosphatidic acid-induced cell migration." Lai Y.-J., Chen C.-S., Lin W.-C., Lin F.-T. Mol. Cell. Biol. 25:5859-5868(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-55.
[13]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"TRIP6 transcriptional co-activator is a novel substrate of AMP-activated protein kinase." Solaz-Fuster M.C., Gimeno-Alcaniz J.V., Casado M., Sanz P. Cell. Signal. 18:1702-1712(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRKAA2, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-101 AND SER-102, FUNCTION.
[15]	"Supervillin modulation of focal adhesions involving TRIP6/ZRP-1." Takizawa N., Smith T.C., Nebl T., Crowley J.L., Palmieri S.J., Lifshitz L.M., Ehrhardt A.G., Hoffman L.M., Beckerle M.C., Luna E.J. J. Cell Biol. 174:447-458(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SVIL.
[16]	"Salmonella typhimurium disseminates within its host by manipulating the motility of infected cells." Worley M.J., Nieman G.S., Geddes K., Heffron F. Proc. Natl. Acad. Sci. U.S.A. 103:17915-17920(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SALMONELLA TYPHIMURIUM SSEI.
[17]	"PTPL1/FAP-1 negatively regulates TRIP6 function in lysophosphatidic acid-induced cell migration." Lai Y.-J., Lin W.-C., Lin F.-T. J. Biol. Chem. 282:24381-24387(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTPN13, PHOSPHORYLATION AT TYR-55.
[18]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"TRIP6, a novel molecular partner of the MAGI-1 scaffolding molecule, promotes invasiveness." Chastre E., Abdessamad M., Kruglov A., Bruyneel E., Bracke M., Di Gioia Y., Beckerle M.C., van Roy F., Kotelevets L. FASEB J. 23:916-928(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAGI1 AND PTPN13, MUTAGENESIS OF THR-474, TISSUE SPECIFICITY, FUNCTION.
[20]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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].
[22]	"Solution structure of the first and second LIM domain of thyroid receptor interacting protein 6 (TRIP6)." RIKEN structural genomics initiative (RSGI) Submitted (OCT-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 279-396.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ001902 mRNA. Translation: CAA05080.1.
AF000974 mRNA. Translation: AAB62222.1.
AF093836, AF093834, AF093835 Genomic DNA. Translation: AAD03037.1.
AF312032 Genomic DNA. Translation: AAK21007.1.
AK291906 mRNA. Translation: BAF84595.1.
CH236956 Genomic DNA. Translation: EAL23817.1.
CH471091 Genomic DNA. Translation: EAW76472.1.
BC002680 mRNA. Translation: AAH02680.1.
BC004249 mRNA. Translation: AAH04249.1.
BC004999 mRNA. Translation: AAH04999.1.
BC021540 mRNA. Translation: AAH21540.1.
BC028985 mRNA. Translation: AAH28985.1.
L40374 mRNA. Translation: AAC41740.1. Frameshift.

IPI

IPI00301561.

RefSeq

NP_003293.2. NM_003302.2.

UniGene

Hs.534360.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X61	NMR	-	A	279-337	[»]
2DLO	NMR	-	A	329-396	[»]

ProteinModelPortal

Q15654.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15654. 34 interactions.

MINT

MINT-1366827.

STRING

9606.ENSP00000200457.

PTM databases

PhosphoSite

Q15654.

Polymorphism databases

DMDM

20981729.

Proteomic databases

PaxDb

Q15654.

PeptideAtlas

Q15654.

PRIDE

Q15654.

Protocols and materials databases

DNASU

7205.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000200457; ENSP00000200457; ENSG00000087077.

GeneID

7205.

KEGG

hsa:7205.

UCSC

uc003uww.3. human.

Organism-specific databases

CTD

7205.

GeneCards

GC07P100464.

H-InvDB

HIX0167828.

HGNC

HGNC:12311. TRIP6.

HPA

CAB046454.
CAB046460.

MIM

602933. gene.

neXtProt

NX_Q15654.

PharmGKB

PA36989.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG279196.

HOVERGEN

HBG093602.

InParanoid

Q15654.

KO

K12792.

OrthoDB

EOG44J2J8.

PhylomeDB

Q15654.

Enzyme and pathway databases

Pathway_Interaction_DB

lysophospholipid_pathway. LPA receptor mediated events.

Gene expression databases

ArrayExpress

Q15654.

Bgee

Q15654.

CleanEx

HS_TRIP6.

Genevestigator

Q15654.

GermOnline

ENSG00000087077. Homo sapiens.

Family and domain databases

Gene3D

2.10.110.10. 3 hits.

InterPro

IPR001781. Znf_LIM.
[Graphical view]

Pfam

PF00412. LIM. 3 hits.
[Graphical view]

SMART

SM00132. LIM. 3 hits.
[Graphical view]

PROSITE

PS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TRIP6. human.

EvolutionaryTrace

Q15654.

GenomeRNAi

7205.

NextBio

28238.

SOURCE

Search...

Entry information

Entry name

TRIP6_HUMAN

Accession

Primary (citable) accession number: Q15654
Secondary accession number(s): A4D2E7 , O15170, O15275, Q9BTB2, Q9BUE5, Q9BXP3, Q9UNT4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 15, 2002
Last modified:	May 1, 2013
This is version 123 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.