Full text data of TXNDC9
TXNDC9
(APACD)
[Confidence: low (only semi-automatic identification from reviews)]
Thioredoxin domain-containing protein 9 (ATP-binding protein associated with cell differentiation; Protein 1-4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Thioredoxin domain-containing protein 9 (ATP-binding protein associated with cell differentiation; Protein 1-4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O14530
ID TXND9_HUMAN Reviewed; 226 AA.
AC O14530; B2R9G8; D3DVI4; Q53HG4; Q53RV8; Q6NSF5; Q9BRU6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 19-SEP-2002, sequence version 2.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Thioredoxin domain-containing protein 9;
DE AltName: Full=ATP-binding protein associated with cell differentiation;
DE AltName: Full=Protein 1-4;
GN Name=TXNDC9; Synonyms=APACD;
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 [MRNA].
RC TISSUE=Leukemia;
RA Shiosaka T.;
RT "Differential expression of 1-4 gene in functionally distinct ME-1
RT subclones.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Brain, and 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 [9]
RP FUNCTION, AND INTERACTION WITH TCP1 COMPLEX.
RX PubMed=16415341; DOI=10.1074/jbc.M513235200;
RA Stirling P.C., Cuellar J., Alfaro G.A., El Khadali F., Beh C.T.,
RA Valpuesta J.M., Melki R., Leroux M.R.;
RT "PhLP3 modulates CCT-mediated actin and tubulin folding via ternary
RT complexes with substrates.";
RL J. Biol. Chem. 281:7012-7021(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASS
RP SPECTROMETRY.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASS
RP SPECTROMETRY.
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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.,
RA Buerckstuemmer T., 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221 AND SER-223, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Significantly diminishes the chaperonin TCP1 complex
CC ATPase activity, thus negatively impacts protein folding,
CC including that of actin or tubulin.
CC -!- SUBUNIT: Forms ternary complexes with the chaperonin TCP1 complex,
CC spanning the cylindrical chaperonin cavity and contacting at least
CC 2 subunits.
CC -!- INTERACTION:
CC Q99689:FEZ1; NbExp=2; IntAct=EBI-707554, EBI-396435;
CC -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR EMBL; AB006679; BAA21881.1; -; mRNA.
DR EMBL; AK313777; BAG36515.1; -; mRNA.
DR EMBL; CR456935; CAG33216.1; -; mRNA.
DR EMBL; AK222616; BAD96336.1; -; mRNA.
DR EMBL; AB451403; BAG70217.1; -; mRNA.
DR EMBL; AC079447; AAX93257.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01869.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01870.1; -; Genomic_DNA.
DR EMBL; BC005968; AAH05968.1; -; mRNA.
DR EMBL; BC022864; AAH22864.1; -; mRNA.
DR EMBL; BC070183; AAH70183.2; -; mRNA.
DR RefSeq; NP_005774.2; NM_005783.3.
DR UniGene; Hs.536122; -.
DR ProteinModelPortal; O14530; -.
DR SMR; O14530; 71-189.
DR IntAct; O14530; 9.
DR MINT; MINT-1374838; -.
DR STRING; 9606.ENSP00000264255; -.
DR PhosphoSite; O14530; -.
DR PaxDb; O14530; -.
DR PeptideAtlas; O14530; -.
DR PRIDE; O14530; -.
DR DNASU; 10190; -.
DR Ensembl; ENST00000264255; ENSP00000264255; ENSG00000115514.
DR GeneID; 10190; -.
DR KEGG; hsa:10190; -.
DR UCSC; uc002szz.3; human.
DR CTD; 10190; -.
DR GeneCards; GC02M099921; -.
DR HGNC; HGNC:24110; TXNDC9.
DR HPA; HPA031844; -.
DR HPA; HPA031845; -.
DR HPA; HPA031846; -.
DR MIM; 612564; gene.
DR neXtProt; NX_O14530; -.
DR PharmGKB; PA134957934; -.
DR eggNOG; COG0526; -.
DR HOVERGEN; HBG054120; -.
DR InParanoid; O14530; -.
DR OMA; STEMLEW; -.
DR PhylomeDB; O14530; -.
DR GeneWiki; TXNDC9; -.
DR GenomeRNAi; 10190; -.
DR NextBio; 38568; -.
DR PRO; PR:O14530; -.
DR ArrayExpress; O14530; -.
DR Bgee; O14530; -.
DR CleanEx; HS_TXNDC9; -.
DR Genevestigator; O14530; -.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW Complete proteome; Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 226 Thioredoxin domain-containing protein 9.
FT /FTId=PRO_0000120166.
FT DOMAIN 74 180 Thioredoxin.
FT MOD_RES 188 188 Phosphoserine.
FT MOD_RES 221 221 Phosphoserine.
FT MOD_RES 223 223 Phosphoserine.
FT VARIANT 2 2 E -> G (in dbSNP:rs11542366).
FT /FTId=VAR_058327.
FT VARIANT 14 14 L -> Q (in dbSNP:rs11542369).
FT /FTId=VAR_058328.
FT VARIANT 38 38 Q -> R (in dbSNP:rs11542371).
FT /FTId=VAR_058329.
FT CONFLICT 122 122 K -> N (in Ref. 1; BAA21881).
FT CONFLICT 190 190 N -> D (in Ref. 4; BAD96336).
FT CONFLICT 214 214 I -> M (in Ref. 1; BAA21881).
SQ SEQUENCE 226 AA; 26534 MW; 2735A2562D1143C3 CRC64;
MEADASVDMF SKVLEHQLLQ TTKLVEEHLD SEIQKLDQMD EDELERLKEK RLQALRKAQQ
QKQEWLSKGH GEYREIPSER DFFQEVKESE NVVCHFYRDS TFRCKILDRH LAILSKKHLE
TKFLKLNVEK APFLCERLHI KVIPTLALLK DGKTQDYVVG FTDLGNTDDF TTETLEWRLG
SSDILNYSGN LMEPPFQNQK KFGTNFTKLE KKTIRGKKYD SDSDDD
//
ID TXND9_HUMAN Reviewed; 226 AA.
AC O14530; B2R9G8; D3DVI4; Q53HG4; Q53RV8; Q6NSF5; Q9BRU6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 19-SEP-2002, sequence version 2.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Thioredoxin domain-containing protein 9;
DE AltName: Full=ATP-binding protein associated with cell differentiation;
DE AltName: Full=Protein 1-4;
GN Name=TXNDC9; Synonyms=APACD;
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 [MRNA].
RC TISSUE=Leukemia;
RA Shiosaka T.;
RT "Differential expression of 1-4 gene in functionally distinct ME-1
RT subclones.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Brain, and 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 [9]
RP FUNCTION, AND INTERACTION WITH TCP1 COMPLEX.
RX PubMed=16415341; DOI=10.1074/jbc.M513235200;
RA Stirling P.C., Cuellar J., Alfaro G.A., El Khadali F., Beh C.T.,
RA Valpuesta J.M., Melki R., Leroux M.R.;
RT "PhLP3 modulates CCT-mediated actin and tubulin folding via ternary
RT complexes with substrates.";
RL J. Biol. Chem. 281:7012-7021(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASS
RP SPECTROMETRY.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASS
RP SPECTROMETRY.
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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.,
RA Buerckstuemmer T., 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221 AND SER-223, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Significantly diminishes the chaperonin TCP1 complex
CC ATPase activity, thus negatively impacts protein folding,
CC including that of actin or tubulin.
CC -!- SUBUNIT: Forms ternary complexes with the chaperonin TCP1 complex,
CC spanning the cylindrical chaperonin cavity and contacting at least
CC 2 subunits.
CC -!- INTERACTION:
CC Q99689:FEZ1; NbExp=2; IntAct=EBI-707554, EBI-396435;
CC -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR EMBL; AB006679; BAA21881.1; -; mRNA.
DR EMBL; AK313777; BAG36515.1; -; mRNA.
DR EMBL; CR456935; CAG33216.1; -; mRNA.
DR EMBL; AK222616; BAD96336.1; -; mRNA.
DR EMBL; AB451403; BAG70217.1; -; mRNA.
DR EMBL; AC079447; AAX93257.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01869.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01870.1; -; Genomic_DNA.
DR EMBL; BC005968; AAH05968.1; -; mRNA.
DR EMBL; BC022864; AAH22864.1; -; mRNA.
DR EMBL; BC070183; AAH70183.2; -; mRNA.
DR RefSeq; NP_005774.2; NM_005783.3.
DR UniGene; Hs.536122; -.
DR ProteinModelPortal; O14530; -.
DR SMR; O14530; 71-189.
DR IntAct; O14530; 9.
DR MINT; MINT-1374838; -.
DR STRING; 9606.ENSP00000264255; -.
DR PhosphoSite; O14530; -.
DR PaxDb; O14530; -.
DR PeptideAtlas; O14530; -.
DR PRIDE; O14530; -.
DR DNASU; 10190; -.
DR Ensembl; ENST00000264255; ENSP00000264255; ENSG00000115514.
DR GeneID; 10190; -.
DR KEGG; hsa:10190; -.
DR UCSC; uc002szz.3; human.
DR CTD; 10190; -.
DR GeneCards; GC02M099921; -.
DR HGNC; HGNC:24110; TXNDC9.
DR HPA; HPA031844; -.
DR HPA; HPA031845; -.
DR HPA; HPA031846; -.
DR MIM; 612564; gene.
DR neXtProt; NX_O14530; -.
DR PharmGKB; PA134957934; -.
DR eggNOG; COG0526; -.
DR HOVERGEN; HBG054120; -.
DR InParanoid; O14530; -.
DR OMA; STEMLEW; -.
DR PhylomeDB; O14530; -.
DR GeneWiki; TXNDC9; -.
DR GenomeRNAi; 10190; -.
DR NextBio; 38568; -.
DR PRO; PR:O14530; -.
DR ArrayExpress; O14530; -.
DR Bgee; O14530; -.
DR CleanEx; HS_TXNDC9; -.
DR Genevestigator; O14530; -.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW Complete proteome; Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 226 Thioredoxin domain-containing protein 9.
FT /FTId=PRO_0000120166.
FT DOMAIN 74 180 Thioredoxin.
FT MOD_RES 188 188 Phosphoserine.
FT MOD_RES 221 221 Phosphoserine.
FT MOD_RES 223 223 Phosphoserine.
FT VARIANT 2 2 E -> G (in dbSNP:rs11542366).
FT /FTId=VAR_058327.
FT VARIANT 14 14 L -> Q (in dbSNP:rs11542369).
FT /FTId=VAR_058328.
FT VARIANT 38 38 Q -> R (in dbSNP:rs11542371).
FT /FTId=VAR_058329.
FT CONFLICT 122 122 K -> N (in Ref. 1; BAA21881).
FT CONFLICT 190 190 N -> D (in Ref. 4; BAD96336).
FT CONFLICT 214 214 I -> M (in Ref. 1; BAA21881).
SQ SEQUENCE 226 AA; 26534 MW; 2735A2562D1143C3 CRC64;
MEADASVDMF SKVLEHQLLQ TTKLVEEHLD SEIQKLDQMD EDELERLKEK RLQALRKAQQ
QKQEWLSKGH GEYREIPSER DFFQEVKESE NVVCHFYRDS TFRCKILDRH LAILSKKHLE
TKFLKLNVEK APFLCERLHI KVIPTLALLK DGKTQDYVVG FTDLGNTDDF TTETLEWRLG
SSDILNYSGN LMEPPFQNQK KFGTNFTKLE KKTIRGKKYD SDSDDD
//
MIM
612564
*RECORD*
*FIELD* NO
612564
*FIELD* TI
*612564 THIOREDOXIN DOMAIN-CONTAINING PROTEIN 9; TXNDC9
;;PHOSDUCIN-LIKE PROTEIN 3; PHLP3
read more*FIELD* TX
CLONING
Stirling et al. (2006) stated that the human TXNDC9 gene, which they
called PHLP3, encodes a 226-amino acid protein with a helical N
terminus, a central thioredoxin (TXN; 187700) domain, and an acidic C
terminus.
GENE FUNCTION
Using coimmunoprecipitation analysis and pull-down assays, Stirling et
al. (2006) showed that human PHLP3 interacted with the chaperonin
containing TCP1 (CCT) complex (see 605139). Mutation analysis revealed
that both the N- and C-terminal domains of PHLP3 were required for the
interaction. PHLP3 formed a ternary complex with CCT and either
denatured actin (see 102560) or tubulin (see 602529) and inhibited their
folding. PHLP3 did not compete with the denatured substrates and had no
effect on the basal ATPase activity of CCT, but it slowed the ATPase
activity of CCT in the presence of substrates. In vivo, the yeast PHLP3
homolog appeared to coordinate the proper biogenesis of actin and
tubulin with prefoldin (see 604897), a chaperone that facilitates
CCT-mediated actin and tubulin folding.
MAPPING
Hartz (2009) mapped the TXNDC9 gene to chromosome 2q11.2 based on an
alignment of the TXNDC9 sequence (GenBank GENBANK BC022864) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 1/29/2009.
2. Stirling, P. C.; Cuellar, J.; Alfaro, G. A.; El Khadali, F.; Beh,
C. T.; Valpuesta, J. M.; Melki, R.; Leroux, M. R.: PhLP3 modulates
CCT-mediated actin and tubulin folding via ternary complexes with
substrates. J. Biol. Chem. 281: 7012-7021, 2006.
*FIELD* CD
Patricia A. Hartz: 1/29/2009
*FIELD* ED
mgross: 01/29/2009
*RECORD*
*FIELD* NO
612564
*FIELD* TI
*612564 THIOREDOXIN DOMAIN-CONTAINING PROTEIN 9; TXNDC9
;;PHOSDUCIN-LIKE PROTEIN 3; PHLP3
read more*FIELD* TX
CLONING
Stirling et al. (2006) stated that the human TXNDC9 gene, which they
called PHLP3, encodes a 226-amino acid protein with a helical N
terminus, a central thioredoxin (TXN; 187700) domain, and an acidic C
terminus.
GENE FUNCTION
Using coimmunoprecipitation analysis and pull-down assays, Stirling et
al. (2006) showed that human PHLP3 interacted with the chaperonin
containing TCP1 (CCT) complex (see 605139). Mutation analysis revealed
that both the N- and C-terminal domains of PHLP3 were required for the
interaction. PHLP3 formed a ternary complex with CCT and either
denatured actin (see 102560) or tubulin (see 602529) and inhibited their
folding. PHLP3 did not compete with the denatured substrates and had no
effect on the basal ATPase activity of CCT, but it slowed the ATPase
activity of CCT in the presence of substrates. In vivo, the yeast PHLP3
homolog appeared to coordinate the proper biogenesis of actin and
tubulin with prefoldin (see 604897), a chaperone that facilitates
CCT-mediated actin and tubulin folding.
MAPPING
Hartz (2009) mapped the TXNDC9 gene to chromosome 2q11.2 based on an
alignment of the TXNDC9 sequence (GenBank GENBANK BC022864) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 1/29/2009.
2. Stirling, P. C.; Cuellar, J.; Alfaro, G. A.; El Khadali, F.; Beh,
C. T.; Valpuesta, J. M.; Melki, R.; Leroux, M. R.: PhLP3 modulates
CCT-mediated actin and tubulin folding via ternary complexes with
substrates. J. Biol. Chem. 281: 7012-7021, 2006.
*FIELD* CD
Patricia A. Hartz: 1/29/2009
*FIELD* ED
mgross: 01/29/2009