Full text data of TRAK1
TRAK1
(KIAA1042, OIP106)
[Confidence: low (only semi-automatic identification from reviews)]
Trafficking kinesin-binding protein 1 (106 kDa O-GlcNAc transferase-interacting protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Trafficking kinesin-binding protein 1 (106 kDa O-GlcNAc transferase-interacting protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UPV9
ID TRAK1_HUMAN Reviewed; 953 AA.
AC Q9UPV9; E9PDS2; Q63HR0; Q659B5; Q96B69;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=Trafficking kinesin-binding protein 1;
DE AltName: Full=106 kDa O-GlcNAc transferase-interacting protein;
GN Name=TRAK1; Synonyms=KIAA1042, OIP106;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-508 (ISOFORM 3).
RC TISSUE=Kidney, and 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH O-GLCNAC TRANSFERASE, AND
RP GLYCOSYLATION.
RX PubMed=12435728; DOI=10.1074/jbc.M209384200;
RA Iyer S.P.N., Akimoto Y., Hart G.W.;
RT "Identification and cloning of a novel family of coiled-coil domain
RT proteins that interact with O-GlcNAc transferase.";
RL J. Biol. Chem. 278:5399-5409(2003).
RN [6]
RP INTERACTION WITH KIF5C, AND SUBCELLULAR LOCATION.
RX PubMed=15644324; DOI=10.1074/jbc.M409095200;
RA Brickley K., Smith M.J., Beck M., Stephenson F.A.;
RT "GRIF-1 and OIP106, members of a novel gene family of coiled-coil
RT domain proteins: association in vivo and in vitro with kinesin.";
RL J. Biol. Chem. 280:14723-14732(2005).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RHOT1 AND RHOT2.
RX PubMed=16630562; DOI=10.1016/j.bbrc.2006.03.163;
RA Fransson S., Ruusala A., Aspenstroem P.;
RT "The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in
RT mitochondrial trafficking.";
RL Biochem. Biophys. Res. Commun. 344:500-510(2006).
RN [8]
RP 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 [9]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND MARKER FOR GASTRIC
RP CANCER.
RX PubMed=18986759; DOI=10.1016/j.canlet.2008.09.031;
RA Zhang F., Ren G., Lu Y., Jin B., Wang J., Chen X., Liu Z., Li K.,
RA Nie Y., Wang X., Fan D.;
RT "Identification of TRAK1 (Trafficking protein, kinesin-binding 1) as
RT MGb2-Ag: a novel cancer biomarker.";
RL Cancer Lett. 274:250-258(2009).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HGS.
RX PubMed=18675823; DOI=10.1016/j.jmb.2008.07.045;
RA Webber E., Li L., Chin L.S.;
RT "Hypertonia-associated protein Trak1 is a novel regulator of endosome-
RT to-lysosome trafficking.";
RL J. Mol. Biol. 382:638-651(2008).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=19528298; DOI=10.1083/jcb.200811033;
RA Li Y., Lim S., Hoffman D., Aspenstrom P., Federoff H.J., Rempe D.A.;
RT "HUMMR, a hypoxia- and HIF-1alpha-inducible protein, alters
RT mitochondrial distribution and transport.";
RL J. Cell Biol. 185:1065-1081(2009).
CC -!- FUNCTION: Involved in the regulation of endosome-to-lysosome
CC trafficking, including endocytic trafficking of EGF-EGFR complexes
CC and GABA-A receptors.
CC -!- SUBUNIT: Interacts with O-GlcNAc transferase. Interacts with
CC RHOT1/Miro-1 and RHOT2/Miro-2. Interacts with HGS. Interacts with
CC GABRA1 (By similarity). Interacts with KIF5C.
CC -!- INTERACTION:
CC Q8IXI2:RHOT1; NbExp=3; IntAct=EBI-1105048, EBI-1396430;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion. Early
CC endosome. Endosome. Note=Predominantly associated with early
CC endosome. The localization to early endosomes depends on its
CC interaction with HRS. Colocalizes with MGARP at the mitochondria.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UPV9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPV9-2; Sequence=VSP_010839, VSP_010840, VSP_010841;
CC Note=Ref.2 (CAH56169) sequence is in conflict in positions:
CC 630:TE->T;
CC Name=3;
CC IsoId=Q9UPV9-3; Sequence=VSP_045558, VSP_045559, VSP_045560;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: High expression in spinal cord and moderate
CC expression in all other tissues and specific brain regions
CC examined. Expressed in all cell lines examined.
CC -!- DOMAIN: The C-terminal region is required for the early endosomal
CC and mitochondrial localization.
CC -!- PTM: O-glycosylated.
CC -!- MISCELLANEOUS: Over-expressed in all investigated carcinomas,
CC especially in gastric adenocarcinoma and signet-ring carcinoma and
CC may serve as a marker of gastric cancer.
CC -!- SIMILARITY: Contains 1 HAP1 N-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA82994.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
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DR EMBL; AB028965; BAA82994.2; ALT_INIT; mRNA.
DR EMBL; BX647199; CAH56169.1; -; mRNA.
DR EMBL; AL713787; CAH56394.1; -; mRNA.
DR EMBL; AC018358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC137935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015922; AAH15922.1; -; mRNA.
DR RefSeq; NP_001036111.1; NM_001042646.2.
DR RefSeq; NP_001252537.1; NM_001265608.1.
DR RefSeq; NP_001252539.1; NM_001265610.1.
DR RefSeq; NP_055780.2; NM_014965.4.
DR UniGene; Hs.535711; -.
DR ProteinModelPortal; Q9UPV9; -.
DR SMR; Q9UPV9; 309-349.
DR IntAct; Q9UPV9; 8.
DR MINT; MINT-1195439; -.
DR STRING; 9606.ENSP00000328998; -.
DR PhosphoSite; Q9UPV9; -.
DR DMDM; 13124654; -.
DR PaxDb; Q9UPV9; -.
DR PRIDE; Q9UPV9; -.
DR DNASU; 22906; -.
DR Ensembl; ENST00000327628; ENSP00000328998; ENSG00000182606.
DR Ensembl; ENST00000449246; ENSP00000410717; ENSG00000182606.
DR GeneID; 22906; -.
DR KEGG; hsa:22906; -.
DR UCSC; uc003ckz.5; human.
DR CTD; 22906; -.
DR GeneCards; GC03P042108; -.
DR HGNC; HGNC:29947; TRAK1.
DR HPA; HPA005853; -.
DR MIM; 608112; gene.
DR neXtProt; NX_Q9UPV9; -.
DR PharmGKB; PA128394593; -.
DR eggNOG; NOG246318; -.
DR HOGENOM; HOG000143414; -.
DR HOVERGEN; HBG069248; -.
DR InParanoid; Q9UPV9; -.
DR KO; K15369; -.
DR OMA; NSCDVCN; -.
DR OrthoDB; EOG7CRTSM; -.
DR PhylomeDB; Q9UPV9; -.
DR ChiTaRS; TRAK1; human.
DR GeneWiki; TRAK1; -.
DR GenomeRNAi; 22906; -.
DR NextBio; 43565; -.
DR PRO; PR:Q9UPV9; -.
DR ArrayExpress; Q9UPV9; -.
DR Bgee; Q9UPV9; -.
DR CleanEx; HS_TRAK1; -.
DR Genevestigator; Q9UPV9; -.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IDA:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0006605; P:protein targeting; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR InterPro; IPR006933; HAP1_N.
DR InterPro; IPR022154; Traffickng_kinesin-bd_prot_dom.
DR Pfam; PF04849; HAP1_N; 1.
DR Pfam; PF12448; Milton; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW Endosome; Glycoprotein; Mitochondrion; Nucleus; Reference proteome.
FT CHAIN 1 953 Trafficking kinesin-binding protein 1.
FT /FTId=PRO_0000058037.
FT DOMAIN 47 354 HAP1 N-terminal.
FT REGION 359 509 Interaction with HGS.
FT COILED 104 356 Potential.
FT COILED 492 532 Potential.
FT COMPBIAS 200 203 Poly-Ser.
FT VAR_SEQ 1 97 MALVFQFGQPVRAQPLPGLCHGKLIRTNACDVCNSTDLPEV
FT EIISLLEEQLPHYKLRADTIYGYDHDDWLHTPLISPDANID
FT LTTEQIEETLKYFLL -> MQKFIEADYYELDWYYEECSDV
FT L (in isoform 3).
FT /FTId=VSP_045558.
FT VAR_SEQ 1 96 MALVFQFGQPVRAQPLPGLCHGKLIRTNACDVCNSTDLPEV
FT EIISLLEEQLPHYKLRADTIYGYDHDDWLHTPLISPDANID
FT LTTEQIEETLKYFL -> MSLRDKGGEEECFEYDCQDEERK
FT PTHRQHDTQDLLEEV (in isoform 2).
FT /FTId=VSP_010839.
FT VAR_SEQ 583 630 SATLHHWQQLAQPHLGGILDPRPGVVTKGFRTLDVDLDEVY
FT CLNDFEE -> DHAGPRPLSVLLGDSLWSLIHLRKAGHLCH
FT AYSFFFRDSHPRCWFEFL (in isoform 3).
FT /FTId=VSP_045559.
FT VAR_SEQ 631 953 Missing (in isoform 3).
FT /FTId=VSP_045560.
FT VAR_SEQ 655 746 AHHPGKCMSQTNSTFTFTTCRILHPSDELTRVTPSLNSAPT
FT PACGSTSHLKSTPVATPCTPRRLSLAESFTNTRESTTTMST
FT SLGLVWLLKE -> GERSQARVTVSGSRSYPSRPQASPEEM
FT QEPPAATEEEEEEEEEEEEGSGEGTTISPVNLAPFPEAEFW
FT AILTSVPGTIRSGSLSVASARLCG (in isoform 2).
FT /FTId=VSP_010840.
FT VAR_SEQ 747 953 Missing (in isoform 2).
FT /FTId=VSP_010841.
FT CONFLICT 503 503 S -> P (in Ref. 2; CAH56169).
FT CONFLICT 638 638 S -> F (in Ref. 2; CAH56169).
SQ SEQUENCE 953 AA; 106040 MW; E834BE07CF41D9A4 CRC64;
MALVFQFGQP VRAQPLPGLC HGKLIRTNAC DVCNSTDLPE VEIISLLEEQ LPHYKLRADT
IYGYDHDDWL HTPLISPDAN IDLTTEQIEE TLKYFLLCAE RVGQMTKTYN DIDAVTRLLE
EKERDLELAA RIGQSLLKKN KTLTERNELL EEQVEHIREE VSQLRHELSM KDELLQFYTS
AAEESEPESV CSTPLKRNES SSSVQNYFHL DSLQKKLKDL EEENVVLRSE ASQLKTETIT
YEEKEQQLVN DCVKELRDAN VQIASISEEL AKKTEDAARQ QEEITHLLSQ IVDLQKKAKA
CAVENEELVQ HLGAAKDAQR QLTAELRELE DKYAECMEML HEAQEELKNL RNKTMPNTTS
RRYHSLGLFP MDSLAAEIEG TMRKELQLEE AESPDITHQK RVFETVRNIN QVVKQRSLTP
SPMNIPGSNQ SSAMNSLLSS CVSTPRSSFY GSDIGNVVLD NKTNSIILET EAADLGNDER
SKKPGTPGTP GSHDLETALR RLSLRRENYL SERRFFEEEQ ERKLQELAEK GELRSGSLTP
TESIMSLGTH SRFSEFTGFS GMSFSSRSYL PEKLQIVKPL EGSATLHHWQ QLAQPHLGGI
LDPRPGVVTK GFRTLDVDLD EVYCLNDFEE DDTGDHISLP RLATSTPVQH PETSAHHPGK
CMSQTNSTFT FTTCRILHPS DELTRVTPSL NSAPTPACGS TSHLKSTPVA TPCTPRRLSL
AESFTNTRES TTTMSTSLGL VWLLKERGIS AAVYDPQSWD RAGRGSLLHS YTPKMAVIPS
TPPNSPMQTP TSSPPSFEFK CTSPPYDNFL ASKPASSILR EVREKNVRSS ESQTDVSVSN
LNLVDKVRRF GVAKVVNSGR AHVPTLTEEQ GPLLCGPPGP APALVPRGLV PEGLPLRCPT
VTSAIGGLQL NSGIRRNRSF PTMVGSSMQM KAPVTLTSGI LMGAKLSKQT SLR
//
ID TRAK1_HUMAN Reviewed; 953 AA.
AC Q9UPV9; E9PDS2; Q63HR0; Q659B5; Q96B69;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=Trafficking kinesin-binding protein 1;
DE AltName: Full=106 kDa O-GlcNAc transferase-interacting protein;
GN Name=TRAK1; Synonyms=KIAA1042, OIP106;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-508 (ISOFORM 3).
RC TISSUE=Kidney, and 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH O-GLCNAC TRANSFERASE, AND
RP GLYCOSYLATION.
RX PubMed=12435728; DOI=10.1074/jbc.M209384200;
RA Iyer S.P.N., Akimoto Y., Hart G.W.;
RT "Identification and cloning of a novel family of coiled-coil domain
RT proteins that interact with O-GlcNAc transferase.";
RL J. Biol. Chem. 278:5399-5409(2003).
RN [6]
RP INTERACTION WITH KIF5C, AND SUBCELLULAR LOCATION.
RX PubMed=15644324; DOI=10.1074/jbc.M409095200;
RA Brickley K., Smith M.J., Beck M., Stephenson F.A.;
RT "GRIF-1 and OIP106, members of a novel gene family of coiled-coil
RT domain proteins: association in vivo and in vitro with kinesin.";
RL J. Biol. Chem. 280:14723-14732(2005).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RHOT1 AND RHOT2.
RX PubMed=16630562; DOI=10.1016/j.bbrc.2006.03.163;
RA Fransson S., Ruusala A., Aspenstroem P.;
RT "The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in
RT mitochondrial trafficking.";
RL Biochem. Biophys. Res. Commun. 344:500-510(2006).
RN [8]
RP 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 [9]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND MARKER FOR GASTRIC
RP CANCER.
RX PubMed=18986759; DOI=10.1016/j.canlet.2008.09.031;
RA Zhang F., Ren G., Lu Y., Jin B., Wang J., Chen X., Liu Z., Li K.,
RA Nie Y., Wang X., Fan D.;
RT "Identification of TRAK1 (Trafficking protein, kinesin-binding 1) as
RT MGb2-Ag: a novel cancer biomarker.";
RL Cancer Lett. 274:250-258(2009).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HGS.
RX PubMed=18675823; DOI=10.1016/j.jmb.2008.07.045;
RA Webber E., Li L., Chin L.S.;
RT "Hypertonia-associated protein Trak1 is a novel regulator of endosome-
RT to-lysosome trafficking.";
RL J. Mol. Biol. 382:638-651(2008).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=19528298; DOI=10.1083/jcb.200811033;
RA Li Y., Lim S., Hoffman D., Aspenstrom P., Federoff H.J., Rempe D.A.;
RT "HUMMR, a hypoxia- and HIF-1alpha-inducible protein, alters
RT mitochondrial distribution and transport.";
RL J. Cell Biol. 185:1065-1081(2009).
CC -!- FUNCTION: Involved in the regulation of endosome-to-lysosome
CC trafficking, including endocytic trafficking of EGF-EGFR complexes
CC and GABA-A receptors.
CC -!- SUBUNIT: Interacts with O-GlcNAc transferase. Interacts with
CC RHOT1/Miro-1 and RHOT2/Miro-2. Interacts with HGS. Interacts with
CC GABRA1 (By similarity). Interacts with KIF5C.
CC -!- INTERACTION:
CC Q8IXI2:RHOT1; NbExp=3; IntAct=EBI-1105048, EBI-1396430;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion. Early
CC endosome. Endosome. Note=Predominantly associated with early
CC endosome. The localization to early endosomes depends on its
CC interaction with HRS. Colocalizes with MGARP at the mitochondria.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UPV9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPV9-2; Sequence=VSP_010839, VSP_010840, VSP_010841;
CC Note=Ref.2 (CAH56169) sequence is in conflict in positions:
CC 630:TE->T;
CC Name=3;
CC IsoId=Q9UPV9-3; Sequence=VSP_045558, VSP_045559, VSP_045560;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: High expression in spinal cord and moderate
CC expression in all other tissues and specific brain regions
CC examined. Expressed in all cell lines examined.
CC -!- DOMAIN: The C-terminal region is required for the early endosomal
CC and mitochondrial localization.
CC -!- PTM: O-glycosylated.
CC -!- MISCELLANEOUS: Over-expressed in all investigated carcinomas,
CC especially in gastric adenocarcinoma and signet-ring carcinoma and
CC may serve as a marker of gastric cancer.
CC -!- SIMILARITY: Contains 1 HAP1 N-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA82994.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; AB028965; BAA82994.2; ALT_INIT; mRNA.
DR EMBL; BX647199; CAH56169.1; -; mRNA.
DR EMBL; AL713787; CAH56394.1; -; mRNA.
DR EMBL; AC018358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC137935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015922; AAH15922.1; -; mRNA.
DR RefSeq; NP_001036111.1; NM_001042646.2.
DR RefSeq; NP_001252537.1; NM_001265608.1.
DR RefSeq; NP_001252539.1; NM_001265610.1.
DR RefSeq; NP_055780.2; NM_014965.4.
DR UniGene; Hs.535711; -.
DR ProteinModelPortal; Q9UPV9; -.
DR SMR; Q9UPV9; 309-349.
DR IntAct; Q9UPV9; 8.
DR MINT; MINT-1195439; -.
DR STRING; 9606.ENSP00000328998; -.
DR PhosphoSite; Q9UPV9; -.
DR DMDM; 13124654; -.
DR PaxDb; Q9UPV9; -.
DR PRIDE; Q9UPV9; -.
DR DNASU; 22906; -.
DR Ensembl; ENST00000327628; ENSP00000328998; ENSG00000182606.
DR Ensembl; ENST00000449246; ENSP00000410717; ENSG00000182606.
DR GeneID; 22906; -.
DR KEGG; hsa:22906; -.
DR UCSC; uc003ckz.5; human.
DR CTD; 22906; -.
DR GeneCards; GC03P042108; -.
DR HGNC; HGNC:29947; TRAK1.
DR HPA; HPA005853; -.
DR MIM; 608112; gene.
DR neXtProt; NX_Q9UPV9; -.
DR PharmGKB; PA128394593; -.
DR eggNOG; NOG246318; -.
DR HOGENOM; HOG000143414; -.
DR HOVERGEN; HBG069248; -.
DR InParanoid; Q9UPV9; -.
DR KO; K15369; -.
DR OMA; NSCDVCN; -.
DR OrthoDB; EOG7CRTSM; -.
DR PhylomeDB; Q9UPV9; -.
DR ChiTaRS; TRAK1; human.
DR GeneWiki; TRAK1; -.
DR GenomeRNAi; 22906; -.
DR NextBio; 43565; -.
DR PRO; PR:Q9UPV9; -.
DR ArrayExpress; Q9UPV9; -.
DR Bgee; Q9UPV9; -.
DR CleanEx; HS_TRAK1; -.
DR Genevestigator; Q9UPV9; -.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IDA:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0006605; P:protein targeting; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR InterPro; IPR006933; HAP1_N.
DR InterPro; IPR022154; Traffickng_kinesin-bd_prot_dom.
DR Pfam; PF04849; HAP1_N; 1.
DR Pfam; PF12448; Milton; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW Endosome; Glycoprotein; Mitochondrion; Nucleus; Reference proteome.
FT CHAIN 1 953 Trafficking kinesin-binding protein 1.
FT /FTId=PRO_0000058037.
FT DOMAIN 47 354 HAP1 N-terminal.
FT REGION 359 509 Interaction with HGS.
FT COILED 104 356 Potential.
FT COILED 492 532 Potential.
FT COMPBIAS 200 203 Poly-Ser.
FT VAR_SEQ 1 97 MALVFQFGQPVRAQPLPGLCHGKLIRTNACDVCNSTDLPEV
FT EIISLLEEQLPHYKLRADTIYGYDHDDWLHTPLISPDANID
FT LTTEQIEETLKYFLL -> MQKFIEADYYELDWYYEECSDV
FT L (in isoform 3).
FT /FTId=VSP_045558.
FT VAR_SEQ 1 96 MALVFQFGQPVRAQPLPGLCHGKLIRTNACDVCNSTDLPEV
FT EIISLLEEQLPHYKLRADTIYGYDHDDWLHTPLISPDANID
FT LTTEQIEETLKYFL -> MSLRDKGGEEECFEYDCQDEERK
FT PTHRQHDTQDLLEEV (in isoform 2).
FT /FTId=VSP_010839.
FT VAR_SEQ 583 630 SATLHHWQQLAQPHLGGILDPRPGVVTKGFRTLDVDLDEVY
FT CLNDFEE -> DHAGPRPLSVLLGDSLWSLIHLRKAGHLCH
FT AYSFFFRDSHPRCWFEFL (in isoform 3).
FT /FTId=VSP_045559.
FT VAR_SEQ 631 953 Missing (in isoform 3).
FT /FTId=VSP_045560.
FT VAR_SEQ 655 746 AHHPGKCMSQTNSTFTFTTCRILHPSDELTRVTPSLNSAPT
FT PACGSTSHLKSTPVATPCTPRRLSLAESFTNTRESTTTMST
FT SLGLVWLLKE -> GERSQARVTVSGSRSYPSRPQASPEEM
FT QEPPAATEEEEEEEEEEEEGSGEGTTISPVNLAPFPEAEFW
FT AILTSVPGTIRSGSLSVASARLCG (in isoform 2).
FT /FTId=VSP_010840.
FT VAR_SEQ 747 953 Missing (in isoform 2).
FT /FTId=VSP_010841.
FT CONFLICT 503 503 S -> P (in Ref. 2; CAH56169).
FT CONFLICT 638 638 S -> F (in Ref. 2; CAH56169).
SQ SEQUENCE 953 AA; 106040 MW; E834BE07CF41D9A4 CRC64;
MALVFQFGQP VRAQPLPGLC HGKLIRTNAC DVCNSTDLPE VEIISLLEEQ LPHYKLRADT
IYGYDHDDWL HTPLISPDAN IDLTTEQIEE TLKYFLLCAE RVGQMTKTYN DIDAVTRLLE
EKERDLELAA RIGQSLLKKN KTLTERNELL EEQVEHIREE VSQLRHELSM KDELLQFYTS
AAEESEPESV CSTPLKRNES SSSVQNYFHL DSLQKKLKDL EEENVVLRSE ASQLKTETIT
YEEKEQQLVN DCVKELRDAN VQIASISEEL AKKTEDAARQ QEEITHLLSQ IVDLQKKAKA
CAVENEELVQ HLGAAKDAQR QLTAELRELE DKYAECMEML HEAQEELKNL RNKTMPNTTS
RRYHSLGLFP MDSLAAEIEG TMRKELQLEE AESPDITHQK RVFETVRNIN QVVKQRSLTP
SPMNIPGSNQ SSAMNSLLSS CVSTPRSSFY GSDIGNVVLD NKTNSIILET EAADLGNDER
SKKPGTPGTP GSHDLETALR RLSLRRENYL SERRFFEEEQ ERKLQELAEK GELRSGSLTP
TESIMSLGTH SRFSEFTGFS GMSFSSRSYL PEKLQIVKPL EGSATLHHWQ QLAQPHLGGI
LDPRPGVVTK GFRTLDVDLD EVYCLNDFEE DDTGDHISLP RLATSTPVQH PETSAHHPGK
CMSQTNSTFT FTTCRILHPS DELTRVTPSL NSAPTPACGS TSHLKSTPVA TPCTPRRLSL
AESFTNTRES TTTMSTSLGL VWLLKERGIS AAVYDPQSWD RAGRGSLLHS YTPKMAVIPS
TPPNSPMQTP TSSPPSFEFK CTSPPYDNFL ASKPASSILR EVREKNVRSS ESQTDVSVSN
LNLVDKVRRF GVAKVVNSGR AHVPTLTEEQ GPLLCGPPGP APALVPRGLV PEGLPLRCPT
VTSAIGGLQL NSGIRRNRSF PTMVGSSMQM KAPVTLTSGI LMGAKLSKQT SLR
//
MIM
608112
*RECORD*
*FIELD* NO
608112
*FIELD* TI
*608112 TRAFFICKING PROTEIN, KINESIN-BINDING 1; TRAK1
;;OGT-INTERACTING PROTEIN, 106-KD; OIP106;;
read moreKIAA1042;;
MILTON, DROSOPHILA, HOMOLOG OF
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated fetal brain cDNA
library, Kikuno et al. (1999) cloned KIAA1042. The deduced protein
contains 953 amino acids. RT-PCR ELISA detected high expression of
OIP106 in spinal cord and moderate expression in all other tissues and
specific brain regions examined.
By searching a sequence database for homologs of rat Oip98 (ALS2CR3;
607334), Iyer et al. (2003) identified KIAA1042, which they designated
OIP106. OIP106 contains coiled-coil domains. Confocal and electron
microscopy showed that OIP106 colocalized with RNA polymerase II (see
180660) in nuclear puncta in HeLa cells. In vitro translation
synthesized a protein with an apparent molecular mass of about 115 kD by
SDS/PAGE. Western blot analysis detected a 115-kD OIP106 protein in HeLa
cell lysates. Further analysis revealed expression of OIP106 in all cell
lines examined.
GENE FUNCTION
Iyer et al. (2003) found that OIP106 interacted with the
tetratricopeptide repeats of OGT (300255) and was O-glycosylated by OGT.
However, unlike other O-glycosylation substrates, OIP106 formed stable
in vitro and in vivo associations with OGT. Coimmunoprecipitations
confirmed that OIP106 interacts with RNA polymerase II and with OGT in
vivo.
Numerous studies have shown that neuroreceptors, including
gamma-aminobutyric acid type A, or GABA(A), receptors, are not
stationary structures on the cell surface. Instead, they undergo a
constant flux whereby surface-bound receptors are endocytosed to form an
intracellular pool, and receptors in this pool are either recycled back
onto the cell surface or shunted toward lysosome-mediated degradation.
Several pieces of evidence suggest that TRAK1, and perhaps TRAK2
(ALS2CR3; 607334), is involved in this trafficking process. Both TRAK1
and TRAK2 are associated with the motor protein kinesin (see 602809)
(Brickley et al., 2005), and TRAK2 can bind to the beta-2 subunit of
GABA(A) receptors (Beck et al., 2002). Based on these observations,
Gilbert et al. (2006) hypothesized that TRAK1 has a crucial role in
regulating the endocytic trafficking of GABA(A) receptors. TRAK1 may
facilitate the targeting of endocytosed GABA(A) receptors back to the
cell surface or block them from degradation. TRAK1 may also be involved
in directing newly synthesized GABA(A) receptors to the cell surface.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the OIP106
gene to chromosome 3 (TMAP stSG4620). Gilbert et al. (2006) stated that
this gene, which they referred to as TRAK1, is located on 3p.
ANIMAL MODEL
Hypertonia, which results from motor pathway defects in the central
nervous system (CNS), is observed in numerous neurologic disorders,
including cerebral palsy, stroke, spinal cord injury, stiff-person
syndrome (184850), spastic paraplegia, dystonia, and Parkinson disease.
Mice with mutation in the 'hypertonic' gene (hyrt) exhibit severe
hypertonia as their primary symptom. Gilbert et al. (2006) showed that
Hyrt mutant mice have much lower levels of gamma-aminobutyric acid type
A, or GABA(A), receptors in their CNS, particularly the lower motor
neurons, than do wildtype mice, indicating that the hypertonicity of the
mutants is likely to be caused by deficits in GABA-mediated motor neuron
inhibition. By linkage analysis they localized the mutant gene
responsible for the hyrt phenotype to mouse chromosome 9 in a region
containing the KIAA1042 gene. Mouse KIAA1042 contains 16 exons and
predicts a protein of 939 amino acids. Sequencing of KIAA1042 in hyrt
homozygotes revealed a 20-bp deletion in the last exon of KIAA1042 that
results in a frameshift after amino acid position 824. Given that the
deletion disrupts only the final 12% of the protein, it may result in
partial loss of function.
NOMENCLATURE
Gilbert et al. (2006) noted that the TRAK1 gene was also referred to as
mammalian Milton (Stowers et al., 2002).
*FIELD* RF
1. Beck, M.; Brickley, K.; Wilkinson, H. L.; Sharma, S.; Smith, M.;
Chazot, P. L.; Pollard, S.; Stephenson, F. A.: Identification, molecular
cloning, and characterization of a novel GABA-A receptor-associated
protein, GRIF-1. J. Biol. Chem. 277: 30079-30090, 2002.
2. Brickley, K.; Smith, M. J.; Beck M.; Stephenson, F. A.: GRIF-1
and OIP106, members of a novel gene family of coiled-coil domain proteins:
association in vivo and in vitro with kinesin. J. Biol. Chem. 280:
14723-14732, 2005.
3. Gilbert, S. L.; Zhang, L.; Forster, M. L.; Iwase, T.; Soliven,
B.; Donahue, L. R.; Sweet, H. O.; Bronson, R. T.; Davisson, M. T.;
Wollmann, R. L.; Lahn, B. T.: Trak1 mutation disrupts GABA(A) receptor
homeostasis in hypertonic mice. Nature Genet. 38: 245-250, 2006.
Note: Erratum: Nature Genet. 38: 389 only, 2006.
4. Iyer, S. P. N.; Akimoto, Y.; Hart, G. W.: Identification and cloning
of a novel family of coiled-coil domain proteins that interact with
O-GlcNAc transferase. J. Biol. Chem. 278: 5399-5409, 2003.
5. Kikuno, R.; Nagase, T.; Ishikawa, K.; Hirosawa, M.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XIV. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 6: 197-205, 1999.
6. Stowers, R. S.; Megeath, L. J.; Gorska-Andrzejak, J.; Meinertzhagen,
I. A.; Schwarz, T. L.: Axonal transport of mitochondria to synapses
depends on milton, a novel Drosophila protein. Neuron 36: 1063-1077,
2002.
*FIELD* CN
Victor A. McKusick - updated: 2/7/2006
Victor A. McKusick - updated: 1/4/2006
*FIELD* CD
Patricia A. Hartz: 9/24/2003
*FIELD* ED
alopez: 06/12/2006
alopez: 2/10/2006
terry: 2/7/2006
alopez: 1/9/2006
terry: 1/4/2006
mgross: 9/24/2003
*RECORD*
*FIELD* NO
608112
*FIELD* TI
*608112 TRAFFICKING PROTEIN, KINESIN-BINDING 1; TRAK1
;;OGT-INTERACTING PROTEIN, 106-KD; OIP106;;
read moreKIAA1042;;
MILTON, DROSOPHILA, HOMOLOG OF
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated fetal brain cDNA
library, Kikuno et al. (1999) cloned KIAA1042. The deduced protein
contains 953 amino acids. RT-PCR ELISA detected high expression of
OIP106 in spinal cord and moderate expression in all other tissues and
specific brain regions examined.
By searching a sequence database for homologs of rat Oip98 (ALS2CR3;
607334), Iyer et al. (2003) identified KIAA1042, which they designated
OIP106. OIP106 contains coiled-coil domains. Confocal and electron
microscopy showed that OIP106 colocalized with RNA polymerase II (see
180660) in nuclear puncta in HeLa cells. In vitro translation
synthesized a protein with an apparent molecular mass of about 115 kD by
SDS/PAGE. Western blot analysis detected a 115-kD OIP106 protein in HeLa
cell lysates. Further analysis revealed expression of OIP106 in all cell
lines examined.
GENE FUNCTION
Iyer et al. (2003) found that OIP106 interacted with the
tetratricopeptide repeats of OGT (300255) and was O-glycosylated by OGT.
However, unlike other O-glycosylation substrates, OIP106 formed stable
in vitro and in vivo associations with OGT. Coimmunoprecipitations
confirmed that OIP106 interacts with RNA polymerase II and with OGT in
vivo.
Numerous studies have shown that neuroreceptors, including
gamma-aminobutyric acid type A, or GABA(A), receptors, are not
stationary structures on the cell surface. Instead, they undergo a
constant flux whereby surface-bound receptors are endocytosed to form an
intracellular pool, and receptors in this pool are either recycled back
onto the cell surface or shunted toward lysosome-mediated degradation.
Several pieces of evidence suggest that TRAK1, and perhaps TRAK2
(ALS2CR3; 607334), is involved in this trafficking process. Both TRAK1
and TRAK2 are associated with the motor protein kinesin (see 602809)
(Brickley et al., 2005), and TRAK2 can bind to the beta-2 subunit of
GABA(A) receptors (Beck et al., 2002). Based on these observations,
Gilbert et al. (2006) hypothesized that TRAK1 has a crucial role in
regulating the endocytic trafficking of GABA(A) receptors. TRAK1 may
facilitate the targeting of endocytosed GABA(A) receptors back to the
cell surface or block them from degradation. TRAK1 may also be involved
in directing newly synthesized GABA(A) receptors to the cell surface.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the OIP106
gene to chromosome 3 (TMAP stSG4620). Gilbert et al. (2006) stated that
this gene, which they referred to as TRAK1, is located on 3p.
ANIMAL MODEL
Hypertonia, which results from motor pathway defects in the central
nervous system (CNS), is observed in numerous neurologic disorders,
including cerebral palsy, stroke, spinal cord injury, stiff-person
syndrome (184850), spastic paraplegia, dystonia, and Parkinson disease.
Mice with mutation in the 'hypertonic' gene (hyrt) exhibit severe
hypertonia as their primary symptom. Gilbert et al. (2006) showed that
Hyrt mutant mice have much lower levels of gamma-aminobutyric acid type
A, or GABA(A), receptors in their CNS, particularly the lower motor
neurons, than do wildtype mice, indicating that the hypertonicity of the
mutants is likely to be caused by deficits in GABA-mediated motor neuron
inhibition. By linkage analysis they localized the mutant gene
responsible for the hyrt phenotype to mouse chromosome 9 in a region
containing the KIAA1042 gene. Mouse KIAA1042 contains 16 exons and
predicts a protein of 939 amino acids. Sequencing of KIAA1042 in hyrt
homozygotes revealed a 20-bp deletion in the last exon of KIAA1042 that
results in a frameshift after amino acid position 824. Given that the
deletion disrupts only the final 12% of the protein, it may result in
partial loss of function.
NOMENCLATURE
Gilbert et al. (2006) noted that the TRAK1 gene was also referred to as
mammalian Milton (Stowers et al., 2002).
*FIELD* RF
1. Beck, M.; Brickley, K.; Wilkinson, H. L.; Sharma, S.; Smith, M.;
Chazot, P. L.; Pollard, S.; Stephenson, F. A.: Identification, molecular
cloning, and characterization of a novel GABA-A receptor-associated
protein, GRIF-1. J. Biol. Chem. 277: 30079-30090, 2002.
2. Brickley, K.; Smith, M. J.; Beck M.; Stephenson, F. A.: GRIF-1
and OIP106, members of a novel gene family of coiled-coil domain proteins:
association in vivo and in vitro with kinesin. J. Biol. Chem. 280:
14723-14732, 2005.
3. Gilbert, S. L.; Zhang, L.; Forster, M. L.; Iwase, T.; Soliven,
B.; Donahue, L. R.; Sweet, H. O.; Bronson, R. T.; Davisson, M. T.;
Wollmann, R. L.; Lahn, B. T.: Trak1 mutation disrupts GABA(A) receptor
homeostasis in hypertonic mice. Nature Genet. 38: 245-250, 2006.
Note: Erratum: Nature Genet. 38: 389 only, 2006.
4. Iyer, S. P. N.; Akimoto, Y.; Hart, G. W.: Identification and cloning
of a novel family of coiled-coil domain proteins that interact with
O-GlcNAc transferase. J. Biol. Chem. 278: 5399-5409, 2003.
5. Kikuno, R.; Nagase, T.; Ishikawa, K.; Hirosawa, M.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XIV. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 6: 197-205, 1999.
6. Stowers, R. S.; Megeath, L. J.; Gorska-Andrzejak, J.; Meinertzhagen,
I. A.; Schwarz, T. L.: Axonal transport of mitochondria to synapses
depends on milton, a novel Drosophila protein. Neuron 36: 1063-1077,
2002.
*FIELD* CN
Victor A. McKusick - updated: 2/7/2006
Victor A. McKusick - updated: 1/4/2006
*FIELD* CD
Patricia A. Hartz: 9/24/2003
*FIELD* ED
alopez: 06/12/2006
alopez: 2/10/2006
terry: 2/7/2006
alopez: 1/9/2006
terry: 1/4/2006
mgross: 9/24/2003