Full text data of TDRD6
TDRD6
[Confidence: low (only semi-automatic identification from reviews)]
Tudor domain-containing protein 6 (Antigen NY-CO-45; Cancer/testis antigen 41.2; CT41.2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Tudor domain-containing protein 6 (Antigen NY-CO-45; Cancer/testis antigen 41.2; CT41.2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O60522
ID TDRD6_HUMAN Reviewed; 2096 AA.
AC O60522; B3KWU2; F5H5M3; Q5HYB1; Q5VTS4; Q6ZMX5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 28-NOV-2006, sequence version 2.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Tudor domain-containing protein 6;
DE AltName: Full=Antigen NY-CO-45;
DE AltName: Full=Cancer/testis antigen 41.2;
DE Short=CT41.2;
GN Name=TDRD6;
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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1161 (ISOFORM 1),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 887-2066 (ISOFORM 2), AND
RP VARIANT GLU-1014.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1073-2096 (ISOFORM 1).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1271-2096 (ISOFORM 1).
RC TISSUE=Colon tumor;
RX PubMed=9610721;
RX DOI=10.1002/(SICI)1097-0215(19980529)76:5<652::AID-IJC7>3.0.CO;2-P;
RA Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E.,
RA Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
RT "Characterization of human colon cancer antigens recognized by
RT autologous antibodies.";
RL Int. J. Cancer 76:652-658(1998).
CC -!- FUNCTION: Involved in spermiogenesis, chromatoid body formation
CC and for proper precursor and mature miRNA expression (By
CC similarity).
CC -!- SUBUNIT: Found in a mRNP complex, at least composed of TDRD1,
CC TDRD6, TDRD7 and DDX4. Found in a complex, at least composed of
CC PIWIL1, PIWIL2 and TDRD6. Interacts with DDX4 and PIWIL1 (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Present in
CC chromatoid body (CB) of spermatids (mammalian counterpart of
CC germplasm, pole plasm or polar granules in Drosophila germ cells),
CC also named processing bodies (P-bodies) in somatic cells. Detected
CC in the multilobular cytoplasmic CBs (also called
CC intermitochondrial cementin) in pachytene spermatocytes and as a
CC single perinuclear CB in haploid round spermatids. Colocalizes in
CC CB with DDX4, PIWIL1, PIWIL2, TDRD1 and TDRD7 (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60522-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60522-2; Sequence=VSP_044801;
CC Note=No experimental confirmation available;
CC -!- PTM: Undergoes proteolytic cleavage near the C-terminal by an
CC unknown protease during the transition from meiosis I to meiosis
CC II in primary spermatocytes (By similarity).
CC -!- SIMILARITY: Contains 8 Tudor domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC18034.1; Type=Frameshift; Positions=1994;
CC Sequence=CAI45997.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AL591242; CAH73905.1; -; Genomic_DNA.
DR EMBL; AK125838; BAG54254.1; -; mRNA.
DR EMBL; AK131455; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX648686; CAI45997.1; ALT_INIT; mRNA.
DR EMBL; AF039442; AAC18034.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001010870.1; NM_001010870.2.
DR RefSeq; NP_001161831.1; NM_001168359.1.
DR UniGene; Hs.656983; -.
DR ProteinModelPortal; O60522; -.
DR SMR; O60522; 314-409, 498-660, 783-944, 998-1135, 1309-1477, 1531-1670.
DR STRING; 9606.ENSP00000346065; -.
DR PaxDb; O60522; -.
DR PRIDE; O60522; -.
DR Ensembl; ENST00000316081; ENSP00000346065; ENSG00000180113.
DR Ensembl; ENST00000544460; ENSP00000443299; ENSG00000180113.
DR GeneID; 221400; -.
DR KEGG; hsa:221400; -.
DR UCSC; uc003oyj.3; human.
DR CTD; 221400; -.
DR GeneCards; GC06P046702; -.
DR H-InvDB; HIX0025021; -.
DR HGNC; HGNC:21339; TDRD6.
DR HPA; HPA035710; -.
DR MIM; 611200; gene.
DR neXtProt; NX_O60522; -.
DR PharmGKB; PA134945900; -.
DR eggNOG; NOG327358; -.
DR HOGENOM; HOG000154540; -.
DR HOVERGEN; HBG059095; -.
DR InParanoid; O60522; -.
DR OMA; WTFYCQL; -.
DR OrthoDB; EOG7XWPMP; -.
DR GenomeRNAi; 221400; -.
DR NextBio; 91317; -.
DR PRO; PR:O60522; -.
DR Bgee; O60522; -.
DR CleanEx; HS_TDRD6; -.
DR Genevestigator; O60522; -.
DR GO; GO:0033391; C:chromatoid body; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0043186; C:P granule; IEA:Ensembl.
DR GO; GO:0007281; P:germ cell development; IEA:Ensembl.
DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00567; TUDOR; 7.
DR SMART; SM00333; TUDOR; 8.
DR PROSITE; PS50304; TUDOR; 6.
PE 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Developmental protein; Differentiation; Polymorphism;
KW Reference proteome; Repeat; Spermatogenesis.
FT CHAIN 1 2096 Tudor domain-containing protein 6.
FT /FTId=PRO_0000183167.
FT DOMAIN 65 120 Tudor 1.
FT DOMAIN 310 369 Tudor 2.
FT DOMAIN 536 593 Tudor 3.
FT DOMAIN 816 875 Tudor 4.
FT DOMAIN 1033 1088 Tudor 5.
FT DOMAIN 1352 1411 Tudor 6.
FT DOMAIN 1567 1626 Tudor 7.
FT DOMAIN 2026 2084 Tudor 8.
FT COMPBIAS 453 458 Poly-Glu.
FT VAR_SEQ 2058 2087 Missing (in isoform 2).
FT /FTId=VSP_044801.
FT VARIANT 192 192 R -> Q (in dbSNP:rs7750596).
FT /FTId=VAR_029050.
FT VARIANT 398 398 T -> A (in dbSNP:rs3799277).
FT /FTId=VAR_029051.
FT VARIANT 795 795 I -> M (in dbSNP:rs9463234).
FT /FTId=VAR_052423.
FT VARIANT 1014 1014 Q -> E (in dbSNP:rs9381472).
FT /FTId=VAR_029052.
FT CONFLICT 1273 1273 E -> K (in Ref. 4; AAC18034).
FT CONFLICT 1455 1455 Q -> R (in Ref. 3; CAI45997).
FT CONFLICT 1955 1955 M -> V (in Ref. 3; CAI45997).
FT CONFLICT 2016 2016 A -> D (in Ref. 4; AAC18034).
SQ SEQUENCE 2096 AA; 236517 MW; 19FED65D6FE68E44 CRC64;
MCSTPGMPAP GASLALRVSF VDVHPDVIPV QLWGLVGERR GEYLRLSREI QEAAATRGQW
ALGSASASPG ELCLVQVGLL WHRCRVVSRQ AQESRVFLLD EGRTITAGAG SLAPGRREFF
NLPSEVLGCV LAGLVPAGCG AGSGEPPQHW PADAVDFLSN LQGKEVHGCV LDVLLLHRLV
LLEVPDVFQQ MRELGLARRV PDSLFRSLLE RYLTAATASV GSGVPVLSRV PLKQKQPGLD
YFYPQLQLGV TEAVVITQVC HPHRIHCQLR SVSQEIHRLS ESMAQVYRGS TGTGDENSTS
ATWEEREESP DKPGSPCASC GLDGHWYRAL LLETFRPQRC AQVLHVDYGR KELVSCSSLR
YLLPEYFRMP VVTYPCALYG LWDGGRGWSR SQVGDLKTLI LGKAVNAKIE FYCSFEHVYY
VSLYGEDGIN LNRVFGVQSC CLADRVLQSQ ATEEEEPETS QSQSPAEEVD EEISLPALRS
IRLKMNAFYD AQVEFVKNPS EFWIRLRKHN VTFSKLMRRM CGFYSSASKL DGVVLKPEPD
DLCCVKWKEN GYYRAIVTKL DDKSVDVFLV DRGNSENVDW YDVRMLLPQF RQLPILAVKC
TLADIWPLGK TWSQEAVSFF KKTVLHKELV IHILDKQDHQ YVIEILDESR TGEENISKVI
AQAGYAKYQE FETKENILVN AHSPGHVSNH FTTESNKIPF AKTGEGEQKA KRENKTTSVS
KALSDTTVVT NGSTELVVQE KVKRASVYFP LMQNCLEIKP GSSSKGELEV GSTVEVRVSY
VENPGYFWCQ LTRNIQGLKT LMSDIQYYCK NTAAPHQRNT LACLAKRTVN RQWSRALISG
IQSVEHVNVT FVDYGDREMV SVKNIYSISE EFLKVKAQAF RCSLYNLIQP VGQNPFVWDV
KAIQAFNEFI DNAWQKNLEL KCTIFALASI NEELFNIVDL LTPFQSACHF LVEKRLARPV
KLQKPLESSV QLHSYFYSTH DMKIGSEELV YITHIDDPWT FYCQLARNAN ILEQLSCSIT
QLSKVLLNLK TSPLNPGTLC LAKYTDGNWY RGIVIEKEPK KVFFVDFGNI YVVTSDDLLP
IPSDAYDVLL LPMQAVRCSL SDIPDHIPEE VVVWFQETIL DKSLKALVVA KDPDGTLIIE
LYGDNIQISA SINKKLGLLS YKDRIRKKES EVLCSTTETL EEKNENMKLP CTEYLSKSVG
YKLPNKEILE ESYKPQINSS YKELKLLQSL TKTNLVTQYQ DSVGNKNSQV FPLTTEKKEE
ISAETPLKTA RVEATLSERK IGDSCDKDLP LKFCEFPQKT IMPGFKTTVY VSHINDLSDF
YVQLIEDEAE ISHLSERLNS VKTRPEYYVG PPLQRGDMIC AVFPEDNLWY RAVIKEQQPN
DLLSVQFIDY GNVSVVHTNK IGRLDLVNAI LPGLCIHCSL QGFEVPDNKN SKKMMHYFSQ
RTSEAAIRCE FVKFQDRWEV ILADEHGIIA DDMISRYALS EKSQVELSTQ VIKSASSKSV
NKSDIDTSVF LNWYNPEKKM IRAYATVIDG PEYFWCQFAD TEKLQCLEVE VQTAGEQVAD
RRNCIPCPYI GDPCIVRYRE DGHYYRALIT NICEDYLVSV RLVDFGNIED CVDPKALWAI
PSELLSVPMQ AFPCCLSGFN ISEGLCSQEG NDYFYEIITE DVLEITILEI RRDVCDIPLA
IVDLKSKGKS INEKMEKYSK TGIKSALPYE NIDSEIKQTL GSYNLDVGLK KLSNKAVQNK
IYMEQQTDEL AEITEKDVNI IGTKPSNFRD PKTDNICEGF ENPCKDKIDT EELEGELECH
LVDKAEFDDK YLITGFNTLL PHANETKEIL ELNSLEVPLS PDDESKEFLE LESIELQNSL
VVDEEKGELS PVPPNVPLSQ ECVTKGAMEL FTLQLPLSCE AEKQPELELP TAQLPLDDKM
DPLSLGVSQK AQESMCTEDM RKSSCVESFD DQRRMSLHLH GADCDPKTQN EMNICEEEFV
EYKNRDAISA LMPLFSEEES SDGSKHNNGL PDHISAQLQN TYTLKAFTVG SKCVVWSSLR
NTWSKCEILE TAEEGTRVLN LSNGMEEIVN PENVWNGIPK LDKSPPEKRG LEVMEI
//
ID TDRD6_HUMAN Reviewed; 2096 AA.
AC O60522; B3KWU2; F5H5M3; Q5HYB1; Q5VTS4; Q6ZMX5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 28-NOV-2006, sequence version 2.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Tudor domain-containing protein 6;
DE AltName: Full=Antigen NY-CO-45;
DE AltName: Full=Cancer/testis antigen 41.2;
DE Short=CT41.2;
GN Name=TDRD6;
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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1161 (ISOFORM 1),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 887-2066 (ISOFORM 2), AND
RP VARIANT GLU-1014.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1073-2096 (ISOFORM 1).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1271-2096 (ISOFORM 1).
RC TISSUE=Colon tumor;
RX PubMed=9610721;
RX DOI=10.1002/(SICI)1097-0215(19980529)76:5<652::AID-IJC7>3.0.CO;2-P;
RA Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E.,
RA Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
RT "Characterization of human colon cancer antigens recognized by
RT autologous antibodies.";
RL Int. J. Cancer 76:652-658(1998).
CC -!- FUNCTION: Involved in spermiogenesis, chromatoid body formation
CC and for proper precursor and mature miRNA expression (By
CC similarity).
CC -!- SUBUNIT: Found in a mRNP complex, at least composed of TDRD1,
CC TDRD6, TDRD7 and DDX4. Found in a complex, at least composed of
CC PIWIL1, PIWIL2 and TDRD6. Interacts with DDX4 and PIWIL1 (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Present in
CC chromatoid body (CB) of spermatids (mammalian counterpart of
CC germplasm, pole plasm or polar granules in Drosophila germ cells),
CC also named processing bodies (P-bodies) in somatic cells. Detected
CC in the multilobular cytoplasmic CBs (also called
CC intermitochondrial cementin) in pachytene spermatocytes and as a
CC single perinuclear CB in haploid round spermatids. Colocalizes in
CC CB with DDX4, PIWIL1, PIWIL2, TDRD1 and TDRD7 (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60522-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60522-2; Sequence=VSP_044801;
CC Note=No experimental confirmation available;
CC -!- PTM: Undergoes proteolytic cleavage near the C-terminal by an
CC unknown protease during the transition from meiosis I to meiosis
CC II in primary spermatocytes (By similarity).
CC -!- SIMILARITY: Contains 8 Tudor domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC18034.1; Type=Frameshift; Positions=1994;
CC Sequence=CAI45997.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AL591242; CAH73905.1; -; Genomic_DNA.
DR EMBL; AK125838; BAG54254.1; -; mRNA.
DR EMBL; AK131455; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX648686; CAI45997.1; ALT_INIT; mRNA.
DR EMBL; AF039442; AAC18034.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001010870.1; NM_001010870.2.
DR RefSeq; NP_001161831.1; NM_001168359.1.
DR UniGene; Hs.656983; -.
DR ProteinModelPortal; O60522; -.
DR SMR; O60522; 314-409, 498-660, 783-944, 998-1135, 1309-1477, 1531-1670.
DR STRING; 9606.ENSP00000346065; -.
DR PaxDb; O60522; -.
DR PRIDE; O60522; -.
DR Ensembl; ENST00000316081; ENSP00000346065; ENSG00000180113.
DR Ensembl; ENST00000544460; ENSP00000443299; ENSG00000180113.
DR GeneID; 221400; -.
DR KEGG; hsa:221400; -.
DR UCSC; uc003oyj.3; human.
DR CTD; 221400; -.
DR GeneCards; GC06P046702; -.
DR H-InvDB; HIX0025021; -.
DR HGNC; HGNC:21339; TDRD6.
DR HPA; HPA035710; -.
DR MIM; 611200; gene.
DR neXtProt; NX_O60522; -.
DR PharmGKB; PA134945900; -.
DR eggNOG; NOG327358; -.
DR HOGENOM; HOG000154540; -.
DR HOVERGEN; HBG059095; -.
DR InParanoid; O60522; -.
DR OMA; WTFYCQL; -.
DR OrthoDB; EOG7XWPMP; -.
DR GenomeRNAi; 221400; -.
DR NextBio; 91317; -.
DR PRO; PR:O60522; -.
DR Bgee; O60522; -.
DR CleanEx; HS_TDRD6; -.
DR Genevestigator; O60522; -.
DR GO; GO:0033391; C:chromatoid body; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0043186; C:P granule; IEA:Ensembl.
DR GO; GO:0007281; P:germ cell development; IEA:Ensembl.
DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00567; TUDOR; 7.
DR SMART; SM00333; TUDOR; 8.
DR PROSITE; PS50304; TUDOR; 6.
PE 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Developmental protein; Differentiation; Polymorphism;
KW Reference proteome; Repeat; Spermatogenesis.
FT CHAIN 1 2096 Tudor domain-containing protein 6.
FT /FTId=PRO_0000183167.
FT DOMAIN 65 120 Tudor 1.
FT DOMAIN 310 369 Tudor 2.
FT DOMAIN 536 593 Tudor 3.
FT DOMAIN 816 875 Tudor 4.
FT DOMAIN 1033 1088 Tudor 5.
FT DOMAIN 1352 1411 Tudor 6.
FT DOMAIN 1567 1626 Tudor 7.
FT DOMAIN 2026 2084 Tudor 8.
FT COMPBIAS 453 458 Poly-Glu.
FT VAR_SEQ 2058 2087 Missing (in isoform 2).
FT /FTId=VSP_044801.
FT VARIANT 192 192 R -> Q (in dbSNP:rs7750596).
FT /FTId=VAR_029050.
FT VARIANT 398 398 T -> A (in dbSNP:rs3799277).
FT /FTId=VAR_029051.
FT VARIANT 795 795 I -> M (in dbSNP:rs9463234).
FT /FTId=VAR_052423.
FT VARIANT 1014 1014 Q -> E (in dbSNP:rs9381472).
FT /FTId=VAR_029052.
FT CONFLICT 1273 1273 E -> K (in Ref. 4; AAC18034).
FT CONFLICT 1455 1455 Q -> R (in Ref. 3; CAI45997).
FT CONFLICT 1955 1955 M -> V (in Ref. 3; CAI45997).
FT CONFLICT 2016 2016 A -> D (in Ref. 4; AAC18034).
SQ SEQUENCE 2096 AA; 236517 MW; 19FED65D6FE68E44 CRC64;
MCSTPGMPAP GASLALRVSF VDVHPDVIPV QLWGLVGERR GEYLRLSREI QEAAATRGQW
ALGSASASPG ELCLVQVGLL WHRCRVVSRQ AQESRVFLLD EGRTITAGAG SLAPGRREFF
NLPSEVLGCV LAGLVPAGCG AGSGEPPQHW PADAVDFLSN LQGKEVHGCV LDVLLLHRLV
LLEVPDVFQQ MRELGLARRV PDSLFRSLLE RYLTAATASV GSGVPVLSRV PLKQKQPGLD
YFYPQLQLGV TEAVVITQVC HPHRIHCQLR SVSQEIHRLS ESMAQVYRGS TGTGDENSTS
ATWEEREESP DKPGSPCASC GLDGHWYRAL LLETFRPQRC AQVLHVDYGR KELVSCSSLR
YLLPEYFRMP VVTYPCALYG LWDGGRGWSR SQVGDLKTLI LGKAVNAKIE FYCSFEHVYY
VSLYGEDGIN LNRVFGVQSC CLADRVLQSQ ATEEEEPETS QSQSPAEEVD EEISLPALRS
IRLKMNAFYD AQVEFVKNPS EFWIRLRKHN VTFSKLMRRM CGFYSSASKL DGVVLKPEPD
DLCCVKWKEN GYYRAIVTKL DDKSVDVFLV DRGNSENVDW YDVRMLLPQF RQLPILAVKC
TLADIWPLGK TWSQEAVSFF KKTVLHKELV IHILDKQDHQ YVIEILDESR TGEENISKVI
AQAGYAKYQE FETKENILVN AHSPGHVSNH FTTESNKIPF AKTGEGEQKA KRENKTTSVS
KALSDTTVVT NGSTELVVQE KVKRASVYFP LMQNCLEIKP GSSSKGELEV GSTVEVRVSY
VENPGYFWCQ LTRNIQGLKT LMSDIQYYCK NTAAPHQRNT LACLAKRTVN RQWSRALISG
IQSVEHVNVT FVDYGDREMV SVKNIYSISE EFLKVKAQAF RCSLYNLIQP VGQNPFVWDV
KAIQAFNEFI DNAWQKNLEL KCTIFALASI NEELFNIVDL LTPFQSACHF LVEKRLARPV
KLQKPLESSV QLHSYFYSTH DMKIGSEELV YITHIDDPWT FYCQLARNAN ILEQLSCSIT
QLSKVLLNLK TSPLNPGTLC LAKYTDGNWY RGIVIEKEPK KVFFVDFGNI YVVTSDDLLP
IPSDAYDVLL LPMQAVRCSL SDIPDHIPEE VVVWFQETIL DKSLKALVVA KDPDGTLIIE
LYGDNIQISA SINKKLGLLS YKDRIRKKES EVLCSTTETL EEKNENMKLP CTEYLSKSVG
YKLPNKEILE ESYKPQINSS YKELKLLQSL TKTNLVTQYQ DSVGNKNSQV FPLTTEKKEE
ISAETPLKTA RVEATLSERK IGDSCDKDLP LKFCEFPQKT IMPGFKTTVY VSHINDLSDF
YVQLIEDEAE ISHLSERLNS VKTRPEYYVG PPLQRGDMIC AVFPEDNLWY RAVIKEQQPN
DLLSVQFIDY GNVSVVHTNK IGRLDLVNAI LPGLCIHCSL QGFEVPDNKN SKKMMHYFSQ
RTSEAAIRCE FVKFQDRWEV ILADEHGIIA DDMISRYALS EKSQVELSTQ VIKSASSKSV
NKSDIDTSVF LNWYNPEKKM IRAYATVIDG PEYFWCQFAD TEKLQCLEVE VQTAGEQVAD
RRNCIPCPYI GDPCIVRYRE DGHYYRALIT NICEDYLVSV RLVDFGNIED CVDPKALWAI
PSELLSVPMQ AFPCCLSGFN ISEGLCSQEG NDYFYEIITE DVLEITILEI RRDVCDIPLA
IVDLKSKGKS INEKMEKYSK TGIKSALPYE NIDSEIKQTL GSYNLDVGLK KLSNKAVQNK
IYMEQQTDEL AEITEKDVNI IGTKPSNFRD PKTDNICEGF ENPCKDKIDT EELEGELECH
LVDKAEFDDK YLITGFNTLL PHANETKEIL ELNSLEVPLS PDDESKEFLE LESIELQNSL
VVDEEKGELS PVPPNVPLSQ ECVTKGAMEL FTLQLPLSCE AEKQPELELP TAQLPLDDKM
DPLSLGVSQK AQESMCTEDM RKSSCVESFD DQRRMSLHLH GADCDPKTQN EMNICEEEFV
EYKNRDAISA LMPLFSEEES SDGSKHNNGL PDHISAQLQN TYTLKAFTVG SKCVVWSSLR
NTWSKCEILE TAEEGTRVLN LSNGMEEIVN PENVWNGIPK LDKSPPEKRG LEVMEI
//
MIM
611200
*RECORD*
*FIELD* NO
611200
*FIELD* TI
*611200 TUDOR DOMAIN-CONTAINING PROTEIN 6; TDRD6
*FIELD* TX
CLONING
By immunoscreening a pituitary cDNA library with sera from patients with
read moreautoimmune polyendocrine syndrome-1 (APS1; 240300), Bensing et al.
(2007) cloned TDRD6. Database analysis revealed several TDRD6 variants
with different putative transcriptional start sites and alternative
splicing. The longest protein contains 2,096 amino acids and has 7 tudor
domains. Database analysis suggested that TDRD6 is primarily expressed
in testis, with low levels in other endocrine tissues, such as
pituitary, adrenal gland, and pancreas.
GENE FUNCTION
Bensing et al. (2007) found that sera from 42 (49%) of 86 APS1 patients
reacted with in vitro-translated TDRD6 fragments. Sera from patients
with other autoimmune diseases and from healthy controls showed no
immunoreactivity. Immunohistochemical analysis revealed that sera from 3
of 6 APS1 patients with growth hormone deficiency (see 262400) stained
specific cell populations and nerves in guinea pig pituitary gland.
GENE STRUCTURE
Bensing et al. (2007) determined that the TDRD6 gene contains 4 exons
and spans 14 kb.
MAPPING
By genomic sequence analysis, Bensing et al. (2007) mapped the TDRD6
gene to chromosome 6p12.3.
*FIELD* RF
1. Bensing, S.; Fetissov, S. O.; Mulder, J.; Perheentupa, J.; Gustafsson,
J.; Husebye, E. S.; Oscarson, M.; Ekwall, O.; Crock, P. A.; Hokfelt,
T.; Hulting, A.-L.; Kampe, O.: Pituitary autoantibodies in autoimmune
polyendocrine syndrome type 1. Proc. Nat. Acad. Sci. 104: 949-954,
2007.
*FIELD* CD
Patricia A. Hartz: 7/12/2007
*FIELD* ED
alopez: 06/02/2009
mgross: 7/12/2007
*RECORD*
*FIELD* NO
611200
*FIELD* TI
*611200 TUDOR DOMAIN-CONTAINING PROTEIN 6; TDRD6
*FIELD* TX
CLONING
By immunoscreening a pituitary cDNA library with sera from patients with
read moreautoimmune polyendocrine syndrome-1 (APS1; 240300), Bensing et al.
(2007) cloned TDRD6. Database analysis revealed several TDRD6 variants
with different putative transcriptional start sites and alternative
splicing. The longest protein contains 2,096 amino acids and has 7 tudor
domains. Database analysis suggested that TDRD6 is primarily expressed
in testis, with low levels in other endocrine tissues, such as
pituitary, adrenal gland, and pancreas.
GENE FUNCTION
Bensing et al. (2007) found that sera from 42 (49%) of 86 APS1 patients
reacted with in vitro-translated TDRD6 fragments. Sera from patients
with other autoimmune diseases and from healthy controls showed no
immunoreactivity. Immunohistochemical analysis revealed that sera from 3
of 6 APS1 patients with growth hormone deficiency (see 262400) stained
specific cell populations and nerves in guinea pig pituitary gland.
GENE STRUCTURE
Bensing et al. (2007) determined that the TDRD6 gene contains 4 exons
and spans 14 kb.
MAPPING
By genomic sequence analysis, Bensing et al. (2007) mapped the TDRD6
gene to chromosome 6p12.3.
*FIELD* RF
1. Bensing, S.; Fetissov, S. O.; Mulder, J.; Perheentupa, J.; Gustafsson,
J.; Husebye, E. S.; Oscarson, M.; Ekwall, O.; Crock, P. A.; Hokfelt,
T.; Hulting, A.-L.; Kampe, O.: Pituitary autoantibodies in autoimmune
polyendocrine syndrome type 1. Proc. Nat. Acad. Sci. 104: 949-954,
2007.
*FIELD* CD
Patricia A. Hartz: 7/12/2007
*FIELD* ED
alopez: 06/02/2009
mgross: 7/12/2007