TRIOBP

Protein-coding gene in the species Homo sapiens

TRIOBP

Identifiers

Aliases

TRIOBP, DFNB28, TAP68, TARA, dJ37E16.4, HRIHFB2122, TRIO and F-actin binding protein

External IDs

OMIM: 609761; MGI: 1349410; HomoloGene: 5104; GeneCards: TRIOBP; OMA:TRIOBP - orthologs

Gene location (Human)

Chr.	Chromosome 22 (human)^[1]

Band	22q13.1	Start	37,697,048 bp^[1]
Band	22q13.1	End	37,776,556 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 15 (mouse)^[2]

Band	15 E1\|15 37.7 cM	Start	78,831,924 bp^[2]
Band	15 E1\|15 37.7 cM	End	78,890,069 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

lower lobe of lung

apex of heart

right ventricle

stromal cell of endometrium

tail of epididymis

tendon of biceps brachii

left uterine tube

ectocervix

canal of the cervix

right coronary artery

Top expressed in

zygote

granulocyte

genital tubercle

tail of embryo

tibiofemoral joint

secondary oocyte

triceps brachii muscle

external carotid artery

ventricular zone

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	actin filament binding actin binding ubiquitin protein ligase binding myosin II binding
Cellular component	focal adhesion microtubule organizing center nucleus cytoskeleton midbody actin cytoskeleton cytoplasm
Biological process	barbed-end actin filament capping regulation of actin cytoskeleton organization cell cycle cell division positive regulation of substrate adhesion-dependent cell spreading actin modification hearing auditory receptor cell stereocilium organization
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


11078


110253

Ensembl


ENSG00000100106


ENSMUSG00000033088

UniProt


Q9H2D6


Q99KW3

RefSeq (mRNA)


NM_138632 NM_001039141 NM_007032


NM_001024716 NM_001039155 NM_001039156 NM_138579

RefSeq (protein)


NP_001034230 NP_008963 NP_619538


NP_001019887 NP_001034244 NP_001034245 NP_613045

Location (UCSC)

Chr 22: 37.7 – 37.78 Mb

Chr 15: 78.83 – 78.89 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

TRIO and F-actin-binding protein is a protein that in humans is encoded by the TRIOBP gene.^[5]^[6]^[7]^[8]

This gene encodes a protein that interacts with Trio, which is involved with neural tissue development and in controlling actin cytoskeleton organization, cell motility, and cell growth. This trio-binding protein also associates with F-actin and stabilizes F-actin structures. Domains contained in this encoded protein are an N-terminal pleckstrin homology domain and a C-terminal coiled-coil region. Mutations in this gene have been associated with a form of autosomal-recessive nonsyndromic deafness. Multiple alternatively-spliced transcript variants that would encode different isoforms have been found for this gene, though some transcripts may be subject to nonsense-mediated decay (NMD).^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000100106 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000033088 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Seipel K, O'Brien SP, Iannotti E, Medley QG, Streuli M (Jan 2001). "Tara, a novel F-actin binding protein, associates with the Trio guanine nucleotide exchange factor and regulates actin cytoskeletal organization". J Cell Sci. 114 (Pt 2): 389–99. doi:10.1242/jcs.114.2.389. PMID 11148140.
^ Riazuddin S, Khan SN, Ahmed ZM, Ghosh M, Caution K, Nazli S, Kabra M, Zafar AU, Chen K, Naz S, Antonellis A, Pavan WJ, Green ED, Wilcox ER, Friedman PL, Morell RJ, Riazuddin S, Friedman TB (Dec 2005). "Mutations in TRIOBP, which encodes a putative cytoskeletal-organizing protein, are associated with nonsyndromic recessive deafness". Am J Hum Genet. 78 (1): 137–43. doi:10.1086/499164. PMC 1380211. PMID 16385457.
^ Shahin H, Walsh T, Sobe T, Abu Sa'ed J, Abu Rayan A, Lynch ED, Lee MK, Avraham KB, King MC, Kanaan M (Dec 2005). "Mutations in a novel isoform of TRIOBP that encodes a filamentous-actin binding protein are responsible for DFNB28 recessive nonsyndromic hearing loss". Am J Hum Genet. 78 (1): 144–52. doi:10.1086/499495. PMC 1380212. PMID 16385458.
^ ^a ^b "Entrez Gene: TRIOBP TRIO and F-actin binding protein".

Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. doi:10.1093/dnares/9.3.99. PMID 12168954.
Mayer BJ, Ren R, Clark KL, Baltimore D (1993). "A putative modular domain present in diverse signaling proteins". Cell. 73 (4): 629–30. doi:10.1016/0092-8674(93)90244-K. PMID 8500161. S2CID 44282241.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Ueki N, Oda T, Kondo M, et al. (1999). "Selection system for genes encoding nuclear-targeted proteins". Nat. Biotechnol. 16 (13): 1338–42. doi:10.1038/4315. PMID 9853615. S2CID 20001769.
Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi:10.1038/990031. PMID 10591208.
Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Hirosawa M, Nagase T, Murahashi Y, et al. (2001). "Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping". DNA Res. 8 (1): 1–9. doi:10.1093/dnares/8.1.1. PMID 11258795.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
Li X, Lan J, Zhu Y, et al. (2007). "Expression, purification, and characterization of Tara, a novel telomere repeat-binding factor 1 (TRF1)-binding protein". Protein Expr. Purif. 55 (1): 84–92. doi:10.1016/j.pep.2007.05.004. PMID 17629495.

Proteins of the cytoskeleton

Human

Microfilaments
and ABPs

Myofilament

Actins	A1 A2 B C1 G1 G2
Myosins	I MYO1A MYO1B MYO1C MYO1D MYO1E MYO1F MYO1G MYO1H) II MYH1 MYH2 MYH3 MYH4 MYH6 MYH7 MYH7B MYH8 MYH9 MYH10 MYH11 MYH13 MYH14 MYH15 MYH16 III MYO3A MYO3B V MYO5A MYO5B MYO5C VI MYO6 VII MYO7A MYO7B IX MYO9A MYO9B X MYO10 XV MYO15A XVIII MYO18A MYO18B LC MYL1 MYL2 MYL3 MYL4 MYL5 MYL6 MYL6B MYL7 MYL9 MYLIP MYLK MYLK2 MYLL1
Other	Tropomodulin 1 2 3 4 Troponin T 1 2 3 C 1 2 I 1 2 3 Tropomyosin 1 2 3 4 Actinin 1 2 3 4 Arp2/3 complex actin depolymerizing factors Cofilin 1 2 Destrin Gelsolin Profilin 1 2 Titin

Other

Intermediate
filaments

Type 1/2
(Keratin,
Cytokeratin)

Epithelial keratins (soft alpha-keratins)	type I/chromosome 17 9 10 12 13 14 15 16 17 19 20 chromosome 12 18 none 21 type II/chromosome 12 1 2A 3 4 5 6A 6B 6C 7 8
Hair keratins (hard alpha-keratins)	type I/chromosome 17 31 32 33A 33B 34 35 36 37 38 type II/chromosome 12 81 82 83 84 85 86
Ungrouped alpha	chromosome 17 23 24 25 26 27 28 39 40 chromosome 12 71 72 73 74 75 76 77 78 79 80
Not alpha	Beta-keratin

Type 3

Type 4

Type 5

Microtubules
and MAPs

Tubulins	TUBA1A TUBA1B TUBA1C TUBA3C TUBA3D TUBA3E TUBA4A TUBA8 TUBB TUBB1 TUBB2A TUBB2B TUBB2C TUBB3 TUBB4 TUBB4Q TUBB6 TUBB8 TUBG1 TUBG2 TUBGCP2 TUBGCP3 TUBGCP4 TUBGCP5 TUBGCP6 TUBD1 TUBE1
MAPs	EB1 EB2 EB3 MAP1A MAP1B MAP2 MAP4
Kinesins	KIF1A KIF1B KIF2A KIF2C KIF3B KIF3C KIF4A KIF4B KIF5A KIF5B KIF5C KIF6 KIF7 KIF9 KIF11 KIF12 KIF13A KIF13B KIF14 KIF15 KIF16B KIF17 KIF18A KIF18B KIF19 KIF20A KIF20B KIF21A KIF21B KIF22 KIF23 KIF24 KIF25 KIF26A KIF26B KIF27 KIFC1 KIFC2 KIFC3
Dyneins	axonemal: DNAH1 DNAH2 DNAH3 DNAH5 DNAH6 DNAH7 DNAH8 DNAH9 DNAH10 DNAH11 DNAH12 DNAH13 DNAH14 DNAH17 DNAI1 DNAI2 DNALI1 DNAL1 DNAL4 cytoplasmic: DYNC1H1 DYNC2H1 DYNC1I1 DYNC1I2 DYNC1LI1 DYNC1LI2 DYNC2LI1 DYNLL1 DYNLL2 DYNLRB1 DYNLRB2 DYNLT1 DYNLT3
Microtubule organising proteins	CAMSAP1 CAMSAP2 CAMSAP3 Centrin 1 Centrin 2 Centrin 3 PCM1
Microtubule severing proteins	Katanin Spastin
Other	Tau protein Dynactin DCTN1 Stathmin Tektin TEKT1 TEKT2 TEKT3 TEKT4 TEKT5 Dynamin DNM1 DNM2 DNM3