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Q9H2D6

- TARA_HUMAN

UniProt

Q9H2D6 - TARA_HUMAN

Protein

TRIO and F-actin-binding protein

Gene

TRIOBP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 3 (21 Mar 2006)
      Previous versions | rss
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    Functioni

    May regulate actin cytoskeletal organization, cell spreading and cell contraction by directly binding and stabilizing filamentous F-actin. The localized formation of TARA and TRIO complexes coordinates the amount of F-actin present in stress fibers. May also serve as a linker protein to recruit proteins required for F-actin formation and turnover.1 Publication

    GO - Molecular functioni

    1. actin filament binding Source: MGI
    2. GTP-Rho binding Source: UniProtKB
    3. myosin II binding Source: UniProtKB
    4. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. actin modification Source: UniProtKB
    2. barbed-end actin filament capping Source: UniProtKB
    3. mitotic nuclear division Source: UniProtKB-KW
    4. positive regulation of substrate adhesion-dependent cell spreading Source: MGI

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TRIO and F-actin-binding protein
    Alternative name(s):
    Protein Tara
    Trio-associated repeat on actin
    Gene namesi
    Name:TRIOBP
    Synonyms:KIAA1662, TARA
    ORF Names:HRIHFB2122
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:17009. TRIOBP.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasmcytoskeleton 1 Publication
    Note: Localized to F-actin in a periodic pattern.
    Isoform 1 : Nucleus 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication. Midbody 1 Publication
    Note: Centrosomal localization occurs upon phosphorylation by PLK1 at Thr-457 and lasts from prophase to anaphase. At telophase, relocalizes to midbody.

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. cytoplasm Source: HPA
    3. microtubule organizing center Source: UniProtKB-SubCell
    4. midbody Source: UniProtKB-SubCell
    5. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Deafness, autosomal recessive, 28 (DFNB28) [MIM:609823]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1019 – 10191G → R in DFNB28. 1 Publication
    VAR_025719

    Keywords - Diseasei

    Deafness, Disease mutation, Non-syndromic deafness

    Organism-specific databases

    MIMi609823. phenotype.
    Orphaneti90636. Autosomal recessive nonsyndromic sensorineural deafness type DFNB.
    PharmGKBiPA142670699.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 23652365TRIO and F-actin-binding proteinPRO_0000072433Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1949 – 19491Phosphoserine2 Publications
    Modified residuei1955 – 19551Phosphoserine3 Publications
    Modified residuei2229 – 22291Phosphothreonine; by PLK11 Publication

    Post-translational modificationi

    Ubiquitinated by HECTD3, leading to its degradation by the proteasome.1 Publication
    Isoform 1: Phosphorylation at Thr-457 by PLK1 ensures mitotic progression and is essential for accurate chromosome segregation.4 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9H2D6.
    PaxDbiQ9H2D6.
    PRIDEiQ9H2D6.

    PTM databases

    PhosphoSiteiQ9H2D6.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in heart and placenta. Isoform 3 is expressed in fetal brain, retina and cochlea but is not detectable in the other tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ9H2D6.
    BgeeiQ9H2D6.
    GenevestigatoriQ9H2D6.

    Organism-specific databases

    HPAiHPA003747.
    HPA019769.

    Interactioni

    Subunit structurei

    Binds to TRIO and F-actin. May also interact with myosin II. Interacts with HECTD3.1 Publication

    Protein-protein interaction databases

    BioGridi116261. 9 interactions.
    IntActiQ9H2D6. 9 interactions.
    MINTiMINT-1397991.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H2D6.
    SMRiQ9H2D6. Positions 1781-1886.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1778 – 1887110PHPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili2062 – 2247186Sequence AnalysisAdd
    BLAST
    Coiled coili2281 – 236181Sequence AnalysisAdd
    BLAST

    Domaini

    Sequence similaritiesi

    Contains 1 PH domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG094025.
    InParanoidiQ9H2D6.
    OMAiPYCDLPR.
    OrthoDBiEOG773XKP.
    PhylomeDBiQ9H2D6.
    TreeFamiTF343361.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PfamiPF00169. PH. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    [Graphical view]
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: Q9H2D6-1) [UniParc]FASTAAdd to Basket

    Also known as: TRIOBP-6

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEEVPGDALC EHFEANILTQ NRCQNCFHPE EAHGARYQEL RSPSGAEVPY     50
    CDLPRCPPAP EDPLSASTSG CQSVVDPGLR PGPKRGPSPS AGLPEEGPTA 100
    APRSRSRELE AVPYLEGLTT SLCGSCNEDP GSDPTSSPDS ATPDDTSNSS 150
    SVDWDTVERQ EEEAPSWDEL AVMIPRRPRE GPRADSSQRA PSLLTRSPVG 200
    GDAAGQKKED TGGGGRSAGQ HWARLRGESG LSLERHRSTL TQASSMTPHS 250
    GPRSTTSQAS PAQRDTAQAA STREIPRASS PHRITQRDTS RASSTQQEIS 300
    RASSTQQETS RASSTQEDTP RASSTQEDTP RASSTQWNTP RASSPSRSTQ 350
    LDNPRTSSTQ QDNPQTSFPT CTPQRENPRT PCVQQDDPRA SSPNRTTQRE 400
    NSRTSCAQRD NPKASRTSSP NRATRDNPRT SCAQRDNPRA SSPSRATRDN 450
    PTTSCAQRDN PRASRTSSPN RATRDNPRTS CAQRDNPRAS SPSRATRDNP 500
    TTSCAQRDNP RASRTSSPNR ATRDNPRTSC AQRDNPRASS PNRAARDNPT 550
    TSCAQRDNPR ASRTSSPNRA TRDNPRTSCA QRDNPRASSP NRATRDNPTT 600
    SCAQRDNPRA SRTSSPNRAT RDNPRTSCAQ RDNPRASSPN RTTQQDSPRT 650
    SCARRDDPRA SSPNRTIQQE NPRTSCALRD NPRASSPSRT IQQENPRTSC 700
    AQRDDPRASS PNRTTQQENP RTSCARRDNP RASSRNRTIQ RDNPRTSCAQ 750
    RDNPRASSPN RTIQQENLRT SCTRQDNPRT SSPNRATRDN PRTSCAQRDN 800
    LRASSPIRAT QQDNPRTCIQ QNIPRSSSTQ QDNPKTSCTK RDNLRPTCTQ 850
    RDRTQSFSFQ RDNPGTSSSQ CCTQKENLRP SSPHRSTQWN NPRNSSPHRT 900
    NKDIPWASFP LRPTQSDGPR TSSPSRSKQS EVPWASIALR PTQGDRPQTS 950
    SPSRPAQHDP PQSSFGPTQY NLPSRATSSS HNPGHQSTSR TSSPVYPAAY 1000
    GAPLTSPEPS QPPCAVCIGH RDAPRASSPP RYLQHDPFPF FPEPRAPESE 1050
    PPHHEPPYIP PAVCIGHRDA PRASSPPRHT QFDPFPFLPD TSDAEHQCQS 1100
    PQHEPLQLPA PVCIGYRDAP RASSPPRQAP EPSLLFQDLP RASTESLVPS 1150
    MDSLHECPHI PTPVCIGHRD APSFSSPPRQ APEPSLFFQD PPGTSMESLA 1200
    PSTDSLHGSP VLIPQVCIGH RDAPRASSPP RHPPSDLAFL APSPSPGSSG 1250
    GSRGSAPPGE TRHNLEREEY TVLADLPPPR RLAQRQPGPQ AQCSSGGRTH 1300
    SPGRAEVERL FGQERRKSEA AGAFQAQDEG RSQQPSQGQS QLLRRQSSPA 1350
    PSRQVTMLPA KQAELTRRSQ AEPPHPWSPE KRPEGDRQLQ GSPLPPRTSA 1400
    RTPERELRTQ RPLESGQAGP RQPLGVWQSQ EEPPGSQGPH RHLERSWSSQ 1450
    EGGLGPGGWW GCGEPSLGAA KAPEGAWGGT SREYKESWGQ PEAWEEKPTH 1500
    ELPRELGKRS PLTSPPENWG GPAESSQSWH SGTPTAVGWG AEGACPYPRG 1550
    SERRPELDWR DLLGLLRAPG EGVWARVPSL DWEGLLELLQ ARLPRKDPAG 1600
    HRDDLARALG PELGPPGTND VPEQESHSQP EGWAEATPVN GHSPALQSQS 1650
    PVQLPSPACT STQWPKIKVT RGPATATLAG LEQTGPLGSR STAKGPSLPE 1700
    LQFQPEEPEE SEPSRGQDPL TDQKQADSAD KRPAEGKAGS PLKGRLVTSW 1750
    RMPGDRPTLF NPFLLSLGVL RWRRPDLLNF KKGWMSILDE PGEPPSPSLT 1800
    TTSTSQWKKH WFVLTDSSLK YYRDSTAEEA DELDGEIDLR SCTDVTEYAV 1850
    QRNYGFQIHT KDAVYTLSAM TSGIRRNWIE ALRKTVRPTS APDVTKLSDS 1900
    NKENALHSYS TQKGPLKAGE QRAGSEVISR GGPRKADGQR QALDYVELSP 1950
    LTQASPQRAR TPARTPDRLA KQEELERDLA QRSEERRKWF EATDSRTPEV 2000
    PAGEGPRRGL GAPLTEDQQN RLSEEIEKKW QELEKLPLRE NKRVPLTALL 2050
    NQSRGERRGP PSDGHEALEK EVQALRAQLE AWRLQGEAPQ SALRSQEDGH 2100
    IPPGYISQEA CERSLAEMES SHQQVMEELQ RHHERELQRL QQEKEWLLAE 2150
    ETAATASAIE AMKKAYQEEL SRELSKTRSL QQGPDGLRKQ HQSDVEALKR 2200
    ELQVLSEQYS QKCLEIGALM RQAEEREHTL RRCQQEGQEL LRHNQELHGR 2250
    LSEEIDQLRG FIASQGMGNG CGRSNERSSC ELEVLLRVKE NELQYLKKEV 2300
    QCLRDELQMM QKDKRFTSGK YQDVYVELSH IKTRSEREIE QLKEHLRLAM 2350
    AALQEKESMR NSLAE 2365
    Length:2,365
    Mass (Da):261,376
    Last modified:March 21, 2006 - v3
    Checksum:iB2CF9AD57E930283
    GO
    Isoform 3 (identifier: Q9H2D6-2) [UniParc]FASTAAdd to Basket

    Also known as: Long isoform

    The sequence of this isoform differs from the canonical sequence as follows:
         1317-1355: Missing.
         1729-1774: Missing.
         1794-1806: Missing.

    Show »
    Length:2,267
    Mass (Da):250,724
    Checksum:iA0055359F5C3D655
    GO
    Isoform 4 (identifier: Q9H2D6-3) [UniParc]FASTAAdd to Basket

    Also known as: TRIOBP-3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-172: Missing.

    Show »
    Length:2,193
    Mass (Da):243,071
    Checksum:i2056F789C0E11E01
    GO
    Isoform 5 (identifier: Q9H2D6-4) [UniParc]FASTAAdd to Basket

    Also known as: TRIOBP-4

    The sequence of this isoform differs from the canonical sequence as follows:
         1-172: Missing.
         1317-2365: Missing.

    Show »
    Length:1,144
    Mass (Da):125,524
    Checksum:i90E403C1C0B946FD
    GO
    Isoform 1 (identifier: Q9H2D6-5) [UniParc]FASTAAdd to Basket

    Also known as: TRIOBP-1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1772: Missing.
         1773-1774: RR → MT

    Show »
    Length:593
    Mass (Da):68,041
    Checksum:i109AA7D9CC10B21A
    GO
    Isoform 6 (identifier: Q9H2D6-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-61: MEEVPGDALC...DLPRCPPAPE → MGGWKGPGQR...LPPPWGAAMT
         62-1774: Missing.
         2109-2144: EACERSLAEMESSHQQVMEELQRHHERELQRLQQEK → LVGVITVPVLQTRPLSSERLCDLPKVTPPAGLKGGI
         2145-2365: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:431
    Mass (Da):47,624
    Checksum:i499617230FA5DAC3
    GO
    Isoform 7 (identifier: Q9H2D6-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-61: MEEVPGDALC...DLPRCPPAPE → MGGWKGPGQR...LPPPWGAAMT
         62-1774: Missing.

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:652
    Mass (Da):74,048
    Checksum:i2B3B90A23A047212
    GO

    Sequence cautioni

    The sequence BAA34800.1 differs from that shown. Reason: Frameshift at position 478.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti713 – 7197RTTQQEN → KSTFGCL in BAB33332. (PubMed:11258795)Curated
    Sequence conflicti1421 – 14211R → S in ABB77204. (PubMed:16385458)Curated
    Sequence conflicti1689 – 16891S → G in ABB77204. (PubMed:16385458)Curated
    Sequence conflicti1896 – 18961Missing in ABB77204. (PubMed:16385458)Curated
    Sequence conflicti1904 – 19041N → D in ABB77204. (PubMed:16385458)Curated
    Sequence conflicti2114 – 21141S → T in AAG44841. (PubMed:11148140)Curated
    Sequence conflicti2141 – 21411Q → L in AAH04303. (PubMed:15489334)Curated
    Sequence conflicti2274 – 22741S → T in AAG44841. (PubMed:11148140)Curated
    Sequence conflicti2283 – 22831E → EHLYPQ in AAH04303. (PubMed:15489334)Curated
    Sequence conflicti2359 – 23591M → I in AAG44841. (PubMed:11148140)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti217 – 2171S → N.
    Corresponds to variant rs12628603 [ dbSNP | Ensembl ].
    VAR_059725
    Natural varianti493 – 4931S → N.
    Corresponds to variant rs4821700 [ dbSNP | Ensembl ].
    VAR_059726
    Natural varianti817 – 8171T → S.
    Corresponds to variant rs41302575 [ dbSNP | Ensembl ].
    VAR_061708
    Natural varianti863 – 8631N → K.
    Corresponds to variant rs9610841 [ dbSNP | Ensembl ].
    VAR_051412
    Natural varianti1019 – 10191G → R in DFNB28. 1 Publication
    VAR_025719
    Natural varianti1187 – 11871F → L.
    Corresponds to variant rs5756795 [ dbSNP | Ensembl ].
    VAR_059727
    Natural varianti1300 – 13001H → R.
    Corresponds to variant rs739138 [ dbSNP | Ensembl ].
    VAR_059728
    Natural varianti1372 – 13721E → D.
    Corresponds to variant rs8140207 [ dbSNP | Ensembl ].
    VAR_051413
    Natural varianti1377 – 13771W → R.2 Publications
    Corresponds to variant rs8140958 [ dbSNP | Ensembl ].
    VAR_051414

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 17721772Missing in isoform 1. 2 PublicationsVSP_017711Add
    BLAST
    Alternative sequencei1 – 172172Missing in isoform 4 and isoform 5. 1 PublicationVSP_017712Add
    BLAST
    Alternative sequencei1 – 6161MEEVP…PPAPE → MGGWKGPGQRRGKEGPEARR RAAERGGGGGGGGVPAPRSP AREPRPRSCLLLPPPWGAAM T in isoform 6 and isoform 7. 1 PublicationVSP_047498Add
    BLAST
    Alternative sequencei62 – 17741713Missing in isoform 6 and isoform 7. 1 PublicationVSP_047499Add
    BLAST
    Alternative sequencei1317 – 23651049Missing in isoform 5. 1 PublicationVSP_017713Add
    BLAST
    Alternative sequencei1317 – 135539Missing in isoform 3. 1 PublicationVSP_017714Add
    BLAST
    Alternative sequencei1729 – 177446Missing in isoform 3. 1 PublicationVSP_017715Add
    BLAST
    Alternative sequencei1773 – 17742RR → MT in isoform 1. 2 PublicationsVSP_017716
    Alternative sequencei1794 – 180613Missing in isoform 3. 1 PublicationVSP_017717Add
    BLAST
    Alternative sequencei2109 – 214436EACER…LQQEK → LVGVITVPVLQTRPLSSERL CDLPKVTPPAGLKGGI in isoform 6. 1 PublicationVSP_047500Add
    BLAST
    Alternative sequencei2145 – 2365221Missing in isoform 6. 1 PublicationVSP_047501Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF281030 mRNA. Translation: AAG44841.1.
    DQ228003 mRNA. Translation: ABB59559.1.
    DQ228004 mRNA. Translation: ABB59560.1.
    DQ228005 mRNA. Translation: ABB59561.1.
    DQ278603 mRNA. Translation: ABB77204.1.
    Z83844 Genomic DNA. No translation available.
    BC003618 mRNA. Translation: AAH03618.1.
    BC004303 mRNA. Translation: AAH04303.1.
    BC013278 mRNA. Translation: AAH13278.2.
    BC022200 mRNA. No translation available.
    AB015343 mRNA. Translation: BAA34800.1. Frameshift.
    AB051449 mRNA. Translation: BAB33332.2.
    CCDSiCCDS33644.1. [Q9H2D6-6]
    CCDS43015.1. [Q9H2D6-1]
    CCDS43016.1. [Q9H2D6-7]
    RefSeqiNP_001034230.1. NM_001039141.2. [Q9H2D6-1]
    NP_008963.3. NM_007032.5. [Q9H2D6-7]
    NP_619538.2. NM_138632.2. [Q9H2D6-6]
    UniGeneiHs.533030.

    Genome annotation databases

    EnsembliENST00000403663; ENSP00000386026; ENSG00000100106. [Q9H2D6-7]
    ENST00000406386; ENSP00000384312; ENSG00000100106. [Q9H2D6-1]
    ENST00000407319; ENSP00000383913; ENSG00000100106. [Q9H2D6-6]
    GeneIDi11078.
    KEGGihsa:11078.
    UCSCiuc003atq.1. human. [Q9H2D6-1]
    uc003ats.1. human. [Q9H2D6-4]

    Polymorphism databases

    DMDMi90110075.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF281030 mRNA. Translation: AAG44841.1 .
    DQ228003 mRNA. Translation: ABB59559.1 .
    DQ228004 mRNA. Translation: ABB59560.1 .
    DQ228005 mRNA. Translation: ABB59561.1 .
    DQ278603 mRNA. Translation: ABB77204.1 .
    Z83844 Genomic DNA. No translation available.
    BC003618 mRNA. Translation: AAH03618.1 .
    BC004303 mRNA. Translation: AAH04303.1 .
    BC013278 mRNA. Translation: AAH13278.2 .
    BC022200 mRNA. No translation available.
    AB015343 mRNA. Translation: BAA34800.1 . Frameshift.
    AB051449 mRNA. Translation: BAB33332.2 .
    CCDSi CCDS33644.1. [Q9H2D6-6 ]
    CCDS43015.1. [Q9H2D6-1 ]
    CCDS43016.1. [Q9H2D6-7 ]
    RefSeqi NP_001034230.1. NM_001039141.2. [Q9H2D6-1 ]
    NP_008963.3. NM_007032.5. [Q9H2D6-7 ]
    NP_619538.2. NM_138632.2. [Q9H2D6-6 ]
    UniGenei Hs.533030.

    3D structure databases

    ProteinModelPortali Q9H2D6.
    SMRi Q9H2D6. Positions 1781-1886.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116261. 9 interactions.
    IntActi Q9H2D6. 9 interactions.
    MINTi MINT-1397991.

    PTM databases

    PhosphoSitei Q9H2D6.

    Polymorphism databases

    DMDMi 90110075.

    Proteomic databases

    MaxQBi Q9H2D6.
    PaxDbi Q9H2D6.
    PRIDEi Q9H2D6.

    Protocols and materials databases

    DNASUi 11078.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000403663 ; ENSP00000386026 ; ENSG00000100106 . [Q9H2D6-7 ]
    ENST00000406386 ; ENSP00000384312 ; ENSG00000100106 . [Q9H2D6-1 ]
    ENST00000407319 ; ENSP00000383913 ; ENSG00000100106 . [Q9H2D6-6 ]
    GeneIDi 11078.
    KEGGi hsa:11078.
    UCSCi uc003atq.1. human. [Q9H2D6-1 ]
    uc003ats.1. human. [Q9H2D6-4 ]

    Organism-specific databases

    CTDi 11078.
    GeneCardsi GC22P038092.
    GeneReviewsi TRIOBP.
    HGNCi HGNC:17009. TRIOBP.
    HPAi HPA003747.
    HPA019769.
    MIMi 609761. gene.
    609823. phenotype.
    neXtProti NX_Q9H2D6.
    Orphaneti 90636. Autosomal recessive nonsyndromic sensorineural deafness type DFNB.
    PharmGKBi PA142670699.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG094025.
    InParanoidi Q9H2D6.
    OMAi PYCDLPR.
    OrthoDBi EOG773XKP.
    PhylomeDBi Q9H2D6.
    TreeFami TF343361.

    Miscellaneous databases

    ChiTaRSi TRIOBP. human.
    GeneWikii TRIOBP.
    GenomeRNAii 11078.
    NextBioi 42114.
    PROi Q9H2D6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H2D6.
    Bgeei Q9H2D6.
    Genevestigatori Q9H2D6.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    Pfami PF00169. PH. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    [Graphical view ]
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Tara, a novel F-actin binding protein, associates with the Trio guanine nucleotide exchange factor and regulates actin cytoskeletal organization."
      Seipel K., O'Brien S.P., Iannotti E., Medley Q.G., Streuli M.
      J. Cell Sci. 114:389-399(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Mutations in TRIOBP, which encodes a putative cytoskeletal-organizing protein, are associated with nonsyndromic recessive deafness."
      Riazuddin S., Khan S.N., Ahmed Z.M., Ghosh M., Caution K., Nazli S., Kabra M., Zafar A.U., Chen K., Naz S., Antonellis A., Pavan W.J., Green E.D., Wilcox E.R., Friedman P.L., Morell R.J., Riazuddin S., Friedman T.B.
      Am. J. Hum. Genet. 78:137-143(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4 AND 5), INVOLVEMENT IN DFNB28.
      Tissue: Inner ear.
    3. "Mutations in a novel isoform of TRIOBP that encodes a filamentous-actin binding protein are responsible for DFNB28 recessive nonsyndromic hearing loss."
      Shahin H., Walsh T., Sobe T., Abu Sa'ed J., Abu Rayan A., Lynch E.D., Lee M.K., Avraham K.B., King M.-C., Kanaan M.
      Am. J. Hum. Genet. 78:144-152(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, VARIANTS DFNB28 ARG-1019 AND ARG-1377.
      Tissue: Brain.
    4. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-431 (ISOFORM 6).
      Tissue: Colon and Pancreas.
    6. "Selection system for genes encoding nuclear-targeted proteins."
      Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.
      Nat. Biotechnol. 16:1338-1342(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 340-563, SUBCELLULAR LOCATION.
      Tissue: Fetal brain.
    7. "Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping."
      Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.
      DNA Res. 8:1-9(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 713-2365, VARIANT ARG-1377.
      Tissue: Brain.
    8. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    9. "The E3 ubiquitin ligase HECTD3 regulates ubiquitination and degradation of Tara."
      Yu J., Lan J., Zhu Y., Li X., Lai X., Xue Y., Jin C., Huang H.
      Biochem. Biophys. Res. Commun. 367:805-812(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HECTD3, UBIQUITINATION.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1949 AND SER-1955, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1955, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-1949 AND SER-1955, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Phosphorylation of Tara by Plk1 is essential for faithful chromosome segregation in mitosis."
      Zhu Y., Wang C., Lan J., Yu J., Jin C., Huang H.
      Exp. Cell Res. 318:2344-2352(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-2229, SUBCELLULAR LOCATION (ISOFORM 1).

    Entry informationi

    Entry nameiTARA_HUMAN
    AccessioniPrimary (citable) accession number: Q9H2D6
    Secondary accession number(s): B1AHD4
    , B1AHD7, F2Z2W0, F8W6V6, O94797, Q2PZW8, Q2Q3Z9, Q2Q400, Q5R3M6, Q96DW1, Q9BT77, Q9BTL7, Q9BY98, Q9Y3L4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: March 21, 2006
    Last modified: October 1, 2014
    This is version 132 of the entry and version 3 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

    Miscellaneous

    Has been identified in PubMed:9853615 by a selection system for genes encoding nuclear-targeted protein.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3