TRIPB_HUMAN
ID TRIPB_HUMAN Reviewed; 1979 AA.
AC Q15643; B2RUT2; O14689; O15154; O95949; Q6MZL5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Thyroid receptor-interacting protein 11;
DE Short=TR-interacting protein 11;
DE Short=TRIP-11;
DE AltName: Full=Clonal evolution-related gene on chromosome 14 protein;
DE AltName: Full=Golgi-associated microtubule-binding protein 210;
DE Short=GMAP-210;
DE AltName: Full=Trip230;
GN Name=TRIP11; Synonyms=CEV14;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH RB1 AND THRB.
RC TISSUE=Fibroblast;
RX PubMed=9256431; DOI=10.1073/pnas.94.17.9040;
RA Chang K.-H., Chen Y., Chen T.-T., Chou W.-H., Chen P.-L., Ma Y.-T.,
RA Yang-Feng T.L., Leng L., Tsai M.-J., O'Malley B.W., Lee W.-H.;
RT "A thyroid hormone receptor coactivator negatively regulated by the
RT retinoblastoma protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9040-9045(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, INTERACTION WITH MICROTUBULES, AND VARIANT SER-1827.
RC TISSUE=Cervix carcinoma;
RX PubMed=10189370; DOI=10.1083/jcb.145.1.83;
RA Infante C., Ramos-Morales F., Fedriani F., Bornens M., Rios R.M.;
RT "GMAP-210, a cis-Golgi network-associated protein, is a minus end
RT microtubule-binding protein.";
RL J. Cell Biol. 145:83-98(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-39 AND SER-1827.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 257-1950 (ISOFORM 2).
RC TISSUE=Salivary gland;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1188-1979, CHROMOSOMAL TRANSLOCATION WITH
RP PDGFRB, TISSUE SPECIFICITY, AND VARIANT SER-1827.
RC TISSUE=Leukemia;
RX PubMed=9373237;
RA Abe A., Emi N., Tanimoto M., Terasaki H., Marunouchi T., Saito H.;
RT "Fusion of the platelet-derived growth factor receptor beta to a novel gene
RT CEV14 in acute myelogenous leukemia after clonal evolution.";
RL Blood 90:4271-4277(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1757-1944, INTERACTION WITH THRB, AND VARIANT
RP SER-1827.
RC TISSUE=Cervix carcinoma;
RX PubMed=7776974; DOI=10.1210/mend.9.2.7776974;
RA Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
RT "Two classes of proteins dependent on either the presence or absence of
RT thyroid hormone for interaction with the thyroid hormone receptor.";
RL Mol. Endocrinol. 9:243-254(1995).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1891, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP INTERACTION WITH IFT20.
RX PubMed=19112494; DOI=10.1371/journal.pgen.1000315;
RA Follit J.A., San Agustin J.T., Xu F., Jonassen J.A., Samtani R., Lo C.W.,
RA Pazour G.J.;
RT "The Golgin GMAP210/TRIP11 anchors IFT20 to the Golgi complex.";
RL PLoS Genet. 4:E1000315-E1000315(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-1842 AND THR-1846,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1842 AND THR-1846, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP INVOLVEMENT IN ACG1A, AND VARIANT ACG1A 264-ARG--GLN-1979 DEL.
RX PubMed=20089971; DOI=10.1056/nejmoa0900158;
RA Smits P., Bolton A.D., Funari V., Hong M., Boyden E.D., Lu L.,
RA Manning D.K., Dwyer N.D., Moran J.L., Prysak M., Merriman B., Nelson S.F.,
RA Bonafe L., Superti-Furga A., Ikegawa S., Krakow D., Cohn D.H.,
RA Kirchhausen T., Warman M.L., Beier D.R.;
RT "Lethal skeletal dysplasia in mice and humans lacking the golgin GMAP-
RT 210.";
RL N. Engl. J. Med. 362:206-216(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464 AND SER-1842, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464 AND SER-1891, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP FUNCTION.
RX PubMed=25717001; DOI=10.1242/jcs.166710;
RA Roboti P., Sato K., Lowe M.;
RT "The golgin GMAP-210 is required for efficient membrane trafficking in the
RT early secretory pathway.";
RL J. Cell Sci. 128:1595-1606(2015).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH RAB2A, AND
RP MUTAGENESIS OF 2-MET--LEU-38 AND 1113-SER--LEU-1423.
RX PubMed=25473115; DOI=10.1091/mbc.e14-10-1450;
RA Sato K., Roboti P., Mironov A.A., Lowe M.;
RT "Coupling of vesicle tethering and Rab binding is required for in vivo
RT functionality of the golgin GMAP-210.";
RL Mol. Biol. Cell 26:537-553(2015).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORM 2), TISSUE SPECIFICITY, INVOLVEMENT
RP IN ODCD1, VARIANTS ACG1A 264-ARG--GLN-1979 DEL; 1160-GLN--GLN-1979 DEL;
RP 1167-ARG--GLN-1979 DEL; 1224-TRP--GLN-1979 DEL; 1321-LEU--GLN-1979 DEL AND
RP 1376-SER--GLN-1979 DEL, CHARACTERIZATION OF VARIANT ACG1A
RP 1224-TRP--GLN-1979 DEL, AND VARIANTS ODCD1 105-VAL--GLN-196 DEL;
RP 196-GLN--GLN-1979 DEL; 264-ARG--GLN-1979 DEL; TYR-410; 1512-GLN--GLN-1979
RP DEL AND VAL-1806.
RX PubMed=30728324; DOI=10.1172/jci.insight.124701;
RA Wehrle A., Witkos T.M., Unger S., Schneider J., Follit J.A., Hermann J.,
RA Welting T., Fano V., Hietala M., Vatanavicharn N., Schoner K., Spranger J.,
RA Schmidts M., Zabel B., Pazour G.J., Bloch-Zupan A., Nishimura G.,
RA Superti-Furga A., Lowe M., Lausch E.;
RT "Hypomorphic mutations of TRIP11 cause odontochondrodysplasia.";
RL JCI Insight 4:0-0(2019).
RN [21]
RP VARIANT [LARGE SCALE ANALYSIS] ILE-1846.
RX PubMed=18987736; DOI=10.1038/nature07485;
RA Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
RA Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
RA Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
RA Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
RA Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
RA Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
RA Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S.,
RA Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A.,
RA DiPersio J.F., Wilson R.K.;
RT "DNA sequencing of a cytogenetically normal acute myeloid leukaemia
RT genome.";
RL Nature 456:66-72(2008).
RN [22]
RP VARIANT ALA-559.
RX PubMed=27717682; DOI=10.1016/j.jstrokecerebrovasdis.2016.09.003;
RA Mukawa M., Nariai T., Onda H., Yoneyama T., Aihara Y., Hirota K., Kudo T.,
RA Sumita K., Maehara T., Kawamata T., Kasuya H., Akagawa H.;
RT "Exome sequencing identified CCER2 as a novel candidate gene for Moyamoya
RT disease.";
RL J. Stroke Cerebrovasc. Dis. 26:150-161(2017).
CC -!- FUNCTION: Is a membrane tether required for vesicle tethering to Golgi.
CC Has an essential role in the maintenance of Golgi structure and
CC function (PubMed:25473115, PubMed:30728324). It is required for
CC efficient anterograde and retrograde trafficking in the early secretory
CC pathway, functioning at both the ER-to-Golgi intermediate compartment
CC (ERGIC) and Golgi complex (PubMed:25717001). Binds the ligand binding
CC domain of the thyroid receptor (THRB) in the presence of
CC triiodothyronine and enhances THRB-modulated transcription.
CC {ECO:0000269|PubMed:10189370, ECO:0000269|PubMed:25473115,
CC ECO:0000269|PubMed:25717001, ECO:0000269|PubMed:30728324,
CC ECO:0000269|PubMed:9256431}.
CC -!- SUBUNIT: Interacts with the active form of RAB2A (PubMed:25473115).
CC Interacts with IFT20 (PubMed:19112494). Binds RB1.
CC {ECO:0000269|PubMed:19112494, ECO:0000269|PubMed:25473115}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000269|PubMed:10189370, ECO:0000269|PubMed:25473115}; Peripheral
CC membrane protein {ECO:0000269|PubMed:10189370}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10189370}. Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000269|PubMed:25473115}. Note=Associates
CC with the ends of centrosome-nucleated microtubules.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15643-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15643-2; Sequence=VSP_060242;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas, muscle, heart,
CC testis, peripheral blood leukocytes, and in several leukemia cell
CC lines. Detected at intermediate levels in placenta and kidney, and at
CC low levels in brain and lung. Isoform 1 and isoform 2 are expressed in
CC articular chondrocytes (PubMed:30728324). {ECO:0000269|PubMed:10189370,
CC ECO:0000269|PubMed:30728324, ECO:0000269|PubMed:9373237}.
CC -!- DOMAIN: Extended rod-like protein with coiled-coil domains.
CC -!- DOMAIN: The C-terminus is required for recruitment to the Golgi
CC apparatus and endoplasmic reticulum-Golgi intermediate compartment.
CC {ECO:0000269|PubMed:25473115}.
CC -!- DISEASE: Note=A chromosomal aberration involving TRIP11 may be a cause
CC of acute myelogenous leukemia. Translocation t(5;14)(q33;q32) with
CC PDGFRB. The fusion protein may be involved in clonal evolution of
CC leukemia and eosinophilia. {ECO:0000269|PubMed:9373237}.
CC -!- DISEASE: Achondrogenesis 1A (ACG1A) [MIM:200600]: A form of
CC achondrogenesis type 1, a lethal form of chondrodysplasia characterized
CC by deficient ossification in the lumbar vertebrae and absent
CC ossification in the sacral, pubic and ischial bones and clinically by
CC stillbirth or early death. In addition to severe micromelia, there is a
CC disproportionately large cranium due to marked edema of soft tissues.
CC {ECO:0000269|PubMed:20089971, ECO:0000269|PubMed:30728324}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Odontochondrodysplasia 1 (ODCD1) [MIM:184260]: An autosomal
CC recessive disorder of skeletal and dental development characterized by
CC mesomelic shortening of tubular bones, ligamentous laxity, scoliosis,
CC and dentinogenesis imperfecta involving both primary and secondary
CC dentition. Radiologic features include trident pelvis, posteriorly
CC flattened vertebrae, and brachydactyly with cone-shaped epiphyses.
CC {ECO:0000269|PubMed:30728324}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB84386.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CEV14ID96.html";
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DR EMBL; AF007217; AAD09135.1; -; mRNA.
DR EMBL; Y12490; CAA73095.1; -; mRNA.
DR EMBL; AL049872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC146845; AAI46846.1; -; mRNA.
DR EMBL; BX641024; CAE46015.1; -; mRNA.
DR EMBL; AF011368; AAB84386.1; ALT_FRAME; mRNA.
DR EMBL; L40380; AAC41730.1; ALT_SEQ; mRNA.
DR CCDS; CCDS9899.1; -. [Q15643-1]
DR PIR; T03719; T03719.
DR RefSeq; NP_004230.2; NM_004239.4. [Q15643-1]
DR AlphaFoldDB; Q15643; -.
DR SMR; Q15643; -.
DR BioGRID; 114732; 145.
DR DIP; DIP-40357N; -.
DR IntAct; Q15643; 45.
DR MINT; Q15643; -.
DR STRING; 9606.ENSP00000267622; -.
DR GlyGen; Q15643; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15643; -.
DR PhosphoSitePlus; Q15643; -.
DR BioMuta; TRIP11; -.
DR DMDM; 292495059; -.
DR EPD; Q15643; -.
DR jPOST; Q15643; -.
DR MassIVE; Q15643; -.
DR MaxQB; Q15643; -.
DR PaxDb; Q15643; -.
DR PeptideAtlas; Q15643; -.
DR PRIDE; Q15643; -.
DR ProteomicsDB; 60680; -.
DR Antibodypedia; 121; 98 antibodies from 17 providers.
DR DNASU; 9321; -.
DR Ensembl; ENST00000267622.8; ENSP00000267622.4; ENSG00000100815.12. [Q15643-1]
DR GeneID; 9321; -.
DR KEGG; hsa:9321; -.
DR MANE-Select; ENST00000267622.8; ENSP00000267622.4; NM_004239.4; NP_004230.2.
DR UCSC; uc001xzy.4; human. [Q15643-1]
DR CTD; 9321; -.
DR DisGeNET; 9321; -.
DR GeneCards; TRIP11; -.
DR HGNC; HGNC:12305; TRIP11.
DR HPA; ENSG00000100815; Low tissue specificity.
DR MalaCards; TRIP11; -.
DR MIM; 184260; phenotype.
DR MIM; 200600; phenotype.
DR MIM; 604505; gene.
DR neXtProt; NX_Q15643; -.
DR OpenTargets; ENSG00000100815; -.
DR Orphanet; 93299; Achondrogenesis type 1A.
DR Orphanet; 166272; Odontochondrodysplasia.
DR PharmGKB; PA36984; -.
DR VEuPathDB; HostDB:ENSG00000100815; -.
DR eggNOG; ENOG502QRXC; Eukaryota.
DR GeneTree; ENSGT00710000106769; -.
DR HOGENOM; CLU_001835_0_0_1; -.
DR InParanoid; Q15643; -.
DR OMA; MHIEVLE; -.
DR OrthoDB; 153176at2759; -.
DR PhylomeDB; Q15643; -.
DR TreeFam; TF351148; -.
DR PathwayCommons; Q15643; -.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR Reactome; R-HSA-9703465; Signaling by FLT3 fusion proteins.
DR SignaLink; Q15643; -.
DR SIGNOR; Q15643; -.
DR BioGRID-ORCS; 9321; 11 hits in 1085 CRISPR screens.
DR ChiTaRS; TRIP11; human.
DR GeneWiki; TRIP11; -.
DR GenomeRNAi; 9321; -.
DR Pharos; Q15643; Tbio.
DR PRO; PR:Q15643; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q15643; protein.
DR Bgee; ENSG00000100815; Expressed in calcaneal tendon and 180 other tissues.
DR ExpressionAtlas; Q15643; baseline and differential.
DR Genevisible; Q15643; HS.
DR GO; GO:0005801; C:cis-Golgi network; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0002079; C:inner acrosomal membrane; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0002081; C:outer acrosomal membrane; IEA:Ensembl.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
DR GO; GO:0051216; P:cartilage development; IMP:UniProtKB.
DR GO; GO:0003413; P:chondrocyte differentiation involved in endochondral bone morphogenesis; IEA:Ensembl.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0090161; P:Golgi ribbon formation; IMP:UniProtKB.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IEA:Ensembl.
DR GO; GO:0006486; P:protein glycosylation; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
DR GO; GO:0099041; P:vesicle tethering to Golgi; IMP:UniProtKB.
DR InterPro; IPR000237; GRIP_dom.
DR PROSITE; PS50913; GRIP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosomal rearrangement; Coiled coil;
KW Cytoplasm; Cytoskeleton; Disease variant; Dwarfism; Golgi apparatus;
KW Membrane; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..1979
FT /note="Thyroid receptor-interacting protein 11"
FT /id="PRO_0000190076"
FT DOMAIN 1774..1823
FT /note="GRIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00250"
FT REGION 2..38
FT /note="Amphipathic lipid-packing sensor required for
FT tethering of intra-Golgi vesicles"
FT /evidence="ECO:0000269|PubMed:25473115"
FT REGION 1017..1195
FT /note="Involved in RAB2A binding"
FT /evidence="ECO:0000269|PubMed:25473115"
FT REGION 1325..1599
FT /note="Involved in RAB2A binding"
FT /evidence="ECO:0000269|PubMed:25473115"
FT REGION 1873..1920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 52..1773
FT /evidence="ECO:0000255"
FT COMPBIAS 1887..1914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1754..1755
FT /note="Breakpoint for translocation to form TRIP11-PDGFRB"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1842
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 1846
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 1891
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 410..438
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:30728324"
FT /id="VSP_060242"
FT VARIANT 39
FT /note="M -> L (in dbSNP:rs17127898)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_055861"
FT VARIANT 105..196
FT /note="Missing (in ODCD1; in-frame exon 4 skipping; due to
FT a nucleotide substitution that may also cause protein
FT truncation)"
FT /evidence="ECO:0000269|PubMed:30728324"
FT /id="VAR_082008"
FT VARIANT 196..1979
FT /note="Missing (in ODCD1; due to a nucleotide substitution
FT that causes protein truncation or in-frame exon 4
FT skipping)"
FT /evidence="ECO:0000269|PubMed:30728324"
FT /id="VAR_082009"
FT VARIANT 264..1979
FT /note="Missing (in ACG1A and ODCD1)"
FT /evidence="ECO:0000269|PubMed:20089971,
FT ECO:0000269|PubMed:30728324"
FT /id="VAR_082010"
FT VARIANT 410
FT /note="D -> Y (in ODCD1; due to a nucleotide substitution
FT that causes in-frame exon 9 skipping or results in missense
FT variant Y-410; patient cells contain both type of
FT transcripts; the transcript lacking exon 9 is the most
FT abundant; dbSNP:rs1566863801)"
FT /evidence="ECO:0000269|PubMed:30728324"
FT /id="VAR_082011"
FT VARIANT 506
FT /note="E -> A (in dbSNP:rs2273186)"
FT /id="VAR_055862"
FT VARIANT 559
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:27717682"
FT /id="VAR_079175"
FT VARIANT 795
FT /note="V -> L (in dbSNP:rs34699762)"
FT /id="VAR_055863"
FT VARIANT 884
FT /note="D -> G (in dbSNP:rs34967261)"
FT /id="VAR_055864"
FT VARIANT 1040
FT /note="I -> V (in dbSNP:rs34805848)"
FT /id="VAR_055865"
FT VARIANT 1107
FT /note="E -> D (in dbSNP:rs4619320)"
FT /id="VAR_060344"
FT VARIANT 1160..1979
FT /note="Missing (in ACG1A)"
FT /evidence="ECO:0000269|PubMed:30728324"
FT /id="VAR_082012"
FT VARIANT 1167..1979
FT /note="Missing (in ACG1A)"
FT /evidence="ECO:0000269|PubMed:30728324"
FT /id="VAR_082285"
FT VARIANT 1224..1979
FT /note="Missing (in ACG1A; does not localize to cis-Golgi;
FT results in disruption of Golgi cisternal stack
FT architecture)"
FT /evidence="ECO:0000269|PubMed:30728324"
FT /id="VAR_082013"
FT VARIANT 1321..1979
FT /note="Missing (in ACG1A)"
FT /evidence="ECO:0000269|PubMed:30728324"
FT /id="VAR_082014"
FT VARIANT 1376..1979
FT /note="Missing (in ACG1A)"
FT /evidence="ECO:0000269|PubMed:30728324"
FT /id="VAR_082015"
FT VARIANT 1413
FT /note="D -> A (in dbSNP:rs12884523)"
FT /id="VAR_060345"
FT VARIANT 1503
FT /note="M -> V (in dbSNP:rs34839498)"
FT /id="VAR_055866"
FT VARIANT 1512..1979
FT /note="Missing (in ODCD1)"
FT /evidence="ECO:0000269|PubMed:30728324"
FT /id="VAR_082016"
FT VARIANT 1576
FT /note="R -> H (in dbSNP:rs35007347)"
FT /id="VAR_055867"
FT VARIANT 1749
FT /note="E -> A (in dbSNP:rs2273183)"
FT /id="VAR_055868"
FT VARIANT 1752
FT /note="R -> K (in dbSNP:rs11851376)"
FT /id="VAR_055869"
FT VARIANT 1806
FT /note="M -> V (in ODCD1; due to a nucleotide substitution
FT that causes missplicing of exon 18 or results in missense
FT variant V-1806; patient cells contain both type of
FT transcripts; the transcript with the missense variant is
FT the most abundant; dbSNP:rs1566843321)"
FT /evidence="ECO:0000269|PubMed:30728324"
FT /id="VAR_082017"
FT VARIANT 1827
FT /note="G -> S (in dbSNP:rs1051340)"
FT /evidence="ECO:0000269|PubMed:10189370,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7776974,
FT ECO:0000269|PubMed:9373237"
FT /id="VAR_060346"
FT VARIANT 1846
FT /note="T -> I (in dbSNP:rs141259390)"
FT /evidence="ECO:0000269|PubMed:18987736"
FT /id="VAR_054151"
FT MUTAGEN 2..38
FT /note="Missing: Abolishes tethering of intra-Golgi
FT vesicles."
FT /evidence="ECO:0000269|PubMed:25473115"
FT MUTAGEN 1113..1423
FT /note="Missing: Abolishes interaction with RAB2A."
FT /evidence="ECO:0000269|PubMed:25473115"
FT CONFLICT 121
FT /note="L -> F (in Ref. 1; AAD09135)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="A -> G (in Ref. 1; AAD09135)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="Q -> R (in Ref. 1; AAD09135)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="D -> A (in Ref. 1; AAD09135)"
FT /evidence="ECO:0000305"
FT CONFLICT 561..563
FT /note="KEK -> FVL (in Ref. 1; AAD09135)"
FT /evidence="ECO:0000305"
FT CONFLICT 1202
FT /note="N -> H (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1213
FT /note="K -> T (in Ref. 5; CAE46015)"
FT /evidence="ECO:0000305"
FT CONFLICT 1237
FT /note="H -> R (in Ref. 6; AAB84386)"
FT /evidence="ECO:0000305"
FT CONFLICT 1346..1347
FT /note="QQ -> HE (in Ref. 6; AAB84386)"
FT /evidence="ECO:0000305"
FT CONFLICT 1566
FT /note="E -> V (in Ref. 5; CAE46015)"
FT /evidence="ECO:0000305"
FT CONFLICT 1658..1665
FT /note="QLSVSQEQ -> RFCLSGT (in Ref. 1; AAD09135)"
FT /evidence="ECO:0000305"
FT CONFLICT 1670
FT /note="A -> R (in Ref. 1; AAD09135)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1979 AA; 227586 MW; 437EB5F5966BB1AE CRC64;
MSSWLGGLGS GLGQSLGQVG GSLASLTGQI SNFTKDMLME GTEEVEAELP DSRTKEIEAI
HAILRSENER LKKLCTDLEE KHEASEIQIK QQSTSYRNQL QQKEVEISHL KARQIALQDQ
LLKLQSAAQS VPSGAGVPAT TASSSFAYGI SHHPSAFHDD DMDFGDIISS QQEINRLSNE
VSRLESEVGH WRHIAQTSKA QGTDNSDQSE ICKLQNIIKE LKQNRSQEID DHQHEMSVLQ
NAHQQKLTEI SRRHREELSD YEERIEELEN LLQQGGSGVI ETDLSKIYEM QKTIQVLQIE
KVESTKKMEQ LEDKIKDINK KLSSAENDRD ILRREQEQLN VEKRQIMEEC ENLKLECSKL
QPSAVKQSDT MTEKERILAQ SASVEEVFRL QQALSDAENE IMRLSSLNQD NSLAEDNLKL
KMRIEVLEKE KSLLSQEKEE LQMSLLKLNN EYEVIKSTAT RDISLDSELH DLRLNLEAKE
QELNQSISEK ETLIAEIEEL DRQNQEATKH MILIKDQLSK QQNEGDSIIS KLKQDLNDEK
KRVHQLEDDK MDITKELDVQ KEKLIQSEVA LNDLHLTKQK LEDKVENLVD QLNKSQESNV
SIQKENLELK EHIRQNEEEL SRIRNELMQS LNQDSNSNFK DTLLKEREAE VRNLKQNLSE
LEQLNENLKK VAFDVKMENE KLVLACEDVR HQLEECLAGN NQLSLEKNTI VETLKMEKGE
IEAELCWAKK RLLEEANKYE KTIEELSNAR NLNTSALQLE HEHLIKLNQK KDMEIAELKK
NIEQMDTDHK ETKDVLSSSL EEQKQLTQLI NKKEIFIEKL KERSSKLQEE LDKYSQALRK
NEILRQTIEE KDRSLGSMKE ENNHLQEELE RLREEQSRTA PVADPKTLDS VTELASEVSQ
LNTIKEHLEE EIKHHQKIIE DQNQSKMQLL QSLQEQKKEM DEFRYQHEQM NATHTQLFLE
KDEEIKSLQK TIEQIKTQLH EERQDIQTDN SDIFQETKVQ SLNIENGSEK HDLSKAETER
LVKGIKEREL EIKLLNEKNI SLTKQIDQLS KDEVGKLTQI IQQKDLEIQA LHARISSTSH
TQDVVYLQQQ LQAYAMEREK VFAVLNEKTR ENSHLKTEYH KMMDIVAAKE AALIKLQDEN
KKLSTRFESS GQDMFRETIQ NLSRIIREKD IEIDALSQKC QTLLAVLQTS STGNEAGGVN
SNQFEELLQE RDKLKQQVKK MEEWKQQVMT TVQNMQHESA QLQEELHQLQ AQVLVDSDNN
SKLQVDYTGL IQSYEQNETK LKNFGQELAQ VQHSIGQLCN TKDLLLGKLD IISPQLSSAS
LLTPQSAECL RASKSEVLSE SSELLQQELE ELRKSLQEKD ATIRTLQENN HRLSDSIAAT
SELERKEHEQ TDSEIKQLKE KQDVLQKLLK EKDLLIKAKS DQLLSSNENF TNKVNENELL
RQAVTNLKER ILILEMDIGK LKGENEKIVE TYRGKETEYQ ALQETNMKFS MMLREKEFEC
HSMKEKALAF EQLLKEKEQG KTGELNQLLN AVKSMQEKTV VFQQERDQVM LALKQKQMEN
TALQNEVQRL RDKEFRSNQE LERLRNHLLE SEDSYTREAL AAEDREAKLR KKVTVLEEKL
VSSSNAMENA SHQASVQVES LQEQLNVVSK QRDETALQLS VSQEQVKQYA LSLANLQMVL
EHFQQEEKAM YSAELEKQKQ LIAEWKKNAE NLEGKVISLQ ECLDEANAAL DSASRLTEQL
DVKEEQIEEL KRQNELRQEM LDDVQKKLMS LANSSEGKVD KVLMRNLFIG HFHTPKNQRH
EVLRLMGSIL GVRREEMEQL FHDDQGGVTR WMTGWLGGGS KSVPNTPLRP NQQSVVNSSF
SELFVKFLET ESHPSIPPPK LSVHDMKPLD SPGRRKRDTN APESFKDTAE SRSGRRTDVN
PFLAPRSAAV PLINPAGLGP GGPGHLLLKP ISDVLPTFTP LPALPDNSAG VVLKDLLKQ
