Full text data of THUMPD1
THUMPD1
[Confidence: low (only semi-automatic identification from reviews)]
THUMP domain-containing protein 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
THUMP domain-containing protein 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NXG2
ID THUM1_HUMAN Reviewed; 353 AA.
AC Q9NXG2; Q9BWC3;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 2.
DT 22-JAN-2014, entry version 88.
DE RecName: Full=THUMP domain-containing protein 1;
GN Name=THUMPD1;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, 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 [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP STRUCTURE BY NMR OF 170-254.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the THUMP domain of THUMP domain-containing
RT protein 1.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- SIMILARITY: Belongs to the THUMPD1 family.
CC -!- SIMILARITY: Contains 1 THUMP domain.
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; AK000281; BAA91050.1; -; mRNA.
DR EMBL; BC000448; AAH00448.1; -; mRNA.
DR RefSeq; NP_060206.2; NM_017736.3.
DR UniGene; Hs.700004; -.
DR PDB; 2DIR; NMR; -; A=170-254.
DR PDBsum; 2DIR; -.
DR ProteinModelPortal; Q9NXG2; -.
DR SMR; Q9NXG2; 170-254.
DR IntAct; Q9NXG2; 1.
DR STRING; 9606.ENSP00000370741; -.
DR PhosphoSite; Q9NXG2; -.
DR DMDM; 61248576; -.
DR PaxDb; Q9NXG2; -.
DR PRIDE; Q9NXG2; -.
DR DNASU; 55623; -.
DR Ensembl; ENST00000381337; ENSP00000370741; ENSG00000066654.
DR Ensembl; ENST00000396083; ENSP00000379392; ENSG00000066654.
DR GeneID; 55623; -.
DR KEGG; hsa:55623; -.
DR UCSC; uc002dho.3; human.
DR CTD; 55623; -.
DR GeneCards; GC16M020744; -.
DR HGNC; HGNC:23807; THUMPD1.
DR HPA; HPA027851; -.
DR neXtProt; NX_Q9NXG2; -.
DR PharmGKB; PA134983093; -.
DR eggNOG; COG1818; -.
DR HOGENOM; HOG000139150; -.
DR HOVERGEN; HBG053030; -.
DR InParanoid; Q9NXG2; -.
DR KO; K06963; -.
DR OrthoDB; EOG7MKW6R; -.
DR PhylomeDB; Q9NXG2; -.
DR ChiTaRS; THUMPD1; human.
DR EvolutionaryTrace; Q9NXG2; -.
DR GenomeRNAi; 55623; -.
DR NextBio; 60236; -.
DR PRO; PR:Q9NXG2; -.
DR ArrayExpress; Q9NXG2; -.
DR Bgee; Q9NXG2; -.
DR CleanEx; HS_THUMPD1; -.
DR Genevestigator; Q9NXG2; -.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR InterPro; IPR004114; THUMP.
DR Pfam; PF02926; THUMP; 1.
DR SMART; SM00981; THUMP; 1.
DR PROSITE; PS51165; THUMP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 353 THUMP domain-containing protein 1.
FT /FTId=PRO_0000072530.
FT DOMAIN 147 254 THUMP.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 86 86 Phosphoserine.
FT MOD_RES 88 88 Phosphoserine.
FT VARIANT 311 311 E -> D (in dbSNP:rs11074471).
FT /FTId=VAR_037645.
FT CONFLICT 84 84 Q -> R (in Ref. 1; BAA91050).
FT CONFLICT 285 285 K -> E (in Ref. 1; BAA91050).
FT CONFLICT 352 352 F -> S (in Ref. 1; BAA91050).
FT HELIX 171 188
FT STRAND 195 201
FT HELIX 210 224
FT STRAND 232 234
FT STRAND 236 244
FT STRAND 247 254
SQ SEQUENCE 353 AA; 39315 MW; 7F0BBD91D204AA1B CRC64;
MAAPAQQTTQ PGGGKRKGKA QYVLAKRARR CDAGGPRQLE PGLQGILITC NMNERKCVEE
AYSLLNEYGD DMYGPEKFTD KDQQPSGSEG EDDDAEAALK KEVGDIKAST EMRLRRFQSV
ESGANNVVFI RTLGIEPEKL VHHILQDMYK TKKKKTRVIL RMLPISGTCK AFLEDMKKYA
ETFLEPWFKA PNKGTFQIVY KSRNNSHVNR EEVIRELAGI VCTLNSENKV DLTNPQYTVV
VEIIKAVCCL SVVKDYMLFR KYNLQEVVKS PKDPSQLNSK QGNGKEAKLE SADKSDQNNT
AEGKNNQQVP ENTEELGQTK PTSNPQVVNE GGAKPELASQ ATEGSKSNEN DFS
//
ID THUM1_HUMAN Reviewed; 353 AA.
AC Q9NXG2; Q9BWC3;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 2.
DT 22-JAN-2014, entry version 88.
DE RecName: Full=THUMP domain-containing protein 1;
GN Name=THUMPD1;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, 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 [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP STRUCTURE BY NMR OF 170-254.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the THUMP domain of THUMP domain-containing
RT protein 1.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- SIMILARITY: Belongs to the THUMPD1 family.
CC -!- SIMILARITY: Contains 1 THUMP domain.
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; AK000281; BAA91050.1; -; mRNA.
DR EMBL; BC000448; AAH00448.1; -; mRNA.
DR RefSeq; NP_060206.2; NM_017736.3.
DR UniGene; Hs.700004; -.
DR PDB; 2DIR; NMR; -; A=170-254.
DR PDBsum; 2DIR; -.
DR ProteinModelPortal; Q9NXG2; -.
DR SMR; Q9NXG2; 170-254.
DR IntAct; Q9NXG2; 1.
DR STRING; 9606.ENSP00000370741; -.
DR PhosphoSite; Q9NXG2; -.
DR DMDM; 61248576; -.
DR PaxDb; Q9NXG2; -.
DR PRIDE; Q9NXG2; -.
DR DNASU; 55623; -.
DR Ensembl; ENST00000381337; ENSP00000370741; ENSG00000066654.
DR Ensembl; ENST00000396083; ENSP00000379392; ENSG00000066654.
DR GeneID; 55623; -.
DR KEGG; hsa:55623; -.
DR UCSC; uc002dho.3; human.
DR CTD; 55623; -.
DR GeneCards; GC16M020744; -.
DR HGNC; HGNC:23807; THUMPD1.
DR HPA; HPA027851; -.
DR neXtProt; NX_Q9NXG2; -.
DR PharmGKB; PA134983093; -.
DR eggNOG; COG1818; -.
DR HOGENOM; HOG000139150; -.
DR HOVERGEN; HBG053030; -.
DR InParanoid; Q9NXG2; -.
DR KO; K06963; -.
DR OrthoDB; EOG7MKW6R; -.
DR PhylomeDB; Q9NXG2; -.
DR ChiTaRS; THUMPD1; human.
DR EvolutionaryTrace; Q9NXG2; -.
DR GenomeRNAi; 55623; -.
DR NextBio; 60236; -.
DR PRO; PR:Q9NXG2; -.
DR ArrayExpress; Q9NXG2; -.
DR Bgee; Q9NXG2; -.
DR CleanEx; HS_THUMPD1; -.
DR Genevestigator; Q9NXG2; -.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR InterPro; IPR004114; THUMP.
DR Pfam; PF02926; THUMP; 1.
DR SMART; SM00981; THUMP; 1.
DR PROSITE; PS51165; THUMP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 353 THUMP domain-containing protein 1.
FT /FTId=PRO_0000072530.
FT DOMAIN 147 254 THUMP.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 86 86 Phosphoserine.
FT MOD_RES 88 88 Phosphoserine.
FT VARIANT 311 311 E -> D (in dbSNP:rs11074471).
FT /FTId=VAR_037645.
FT CONFLICT 84 84 Q -> R (in Ref. 1; BAA91050).
FT CONFLICT 285 285 K -> E (in Ref. 1; BAA91050).
FT CONFLICT 352 352 F -> S (in Ref. 1; BAA91050).
FT HELIX 171 188
FT STRAND 195 201
FT HELIX 210 224
FT STRAND 232 234
FT STRAND 236 244
FT STRAND 247 254
SQ SEQUENCE 353 AA; 39315 MW; 7F0BBD91D204AA1B CRC64;
MAAPAQQTTQ PGGGKRKGKA QYVLAKRARR CDAGGPRQLE PGLQGILITC NMNERKCVEE
AYSLLNEYGD DMYGPEKFTD KDQQPSGSEG EDDDAEAALK KEVGDIKAST EMRLRRFQSV
ESGANNVVFI RTLGIEPEKL VHHILQDMYK TKKKKTRVIL RMLPISGTCK AFLEDMKKYA
ETFLEPWFKA PNKGTFQIVY KSRNNSHVNR EEVIRELAGI VCTLNSENKV DLTNPQYTVV
VEIIKAVCCL SVVKDYMLFR KYNLQEVVKS PKDPSQLNSK QGNGKEAKLE SADKSDQNNT
AEGKNNQQVP ENTEELGQTK PTSNPQVVNE GGAKPELASQ ATEGSKSNEN DFS
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