Full text data of NUDCD3
NUDCD3
(KIAA1068)
[Confidence: low (only semi-automatic identification from reviews)]
NudC domain-containing protein 3
Note: presumably soluble (membrane word is not in UniProt keywords or features)
NudC domain-containing protein 3
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8IVD9
ID NUDC3_HUMAN Reviewed; 361 AA.
AC Q8IVD9; Q9BTI3; Q9H7W9; Q9UPT4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-APR-2007, sequence version 3.
DT 22-JAN-2014, entry version 98.
DE RecName: Full=NudC domain-containing protein 3;
GN Name=NUDCD3; Synonyms=KIAA1068;
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=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PRO-3 AND
RP CYS-235.
RC TISSUE=Brain, Pancreas, and Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-361.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-361.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, 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 [8]
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 [9]
RP STRUCTURE BY NMR OF 176-286.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CS domain of human KIAA1068.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- SIMILARITY: Contains 1 CS domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH03691.1; Type=Erroneous initiation;
CC Sequence=AAQ96892.1; Type=Erroneous gene model prediction;
CC Sequence=BAB14855.1; 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; AC004453; AAQ96892.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC003691; AAH03691.1; ALT_INIT; mRNA.
DR EMBL; BC011673; AAH11673.2; -; mRNA.
DR EMBL; BC035014; AAH35014.1; -; mRNA.
DR EMBL; AB028991; BAA83020.1; -; mRNA.
DR EMBL; AK024226; BAB14855.1; ALT_INIT; mRNA.
DR RefSeq; NP_056147.2; NM_015332.3.
DR UniGene; Hs.488171; -.
DR PDB; 1WGV; NMR; -; A=176-286.
DR PDBsum; 1WGV; -.
DR ProteinModelPortal; Q8IVD9; -.
DR SMR; Q8IVD9; 176-286.
DR IntAct; Q8IVD9; 4.
DR STRING; 9606.ENSP00000347626; -.
DR PhosphoSite; Q8IVD9; -.
DR DMDM; 145559509; -.
DR PaxDb; Q8IVD9; -.
DR PRIDE; Q8IVD9; -.
DR DNASU; 23386; -.
DR Ensembl; ENST00000355451; ENSP00000347626; ENSG00000015676.
DR GeneID; 23386; -.
DR KEGG; hsa:23386; -.
DR UCSC; uc003tkz.3; human.
DR CTD; 23386; -.
DR GeneCards; GC07M044421; -.
DR HGNC; HGNC:22208; NUDCD3.
DR HPA; HPA019136; -.
DR HPA; HPA019528; -.
DR HPA; HPA019529; -.
DR MIM; 610296; gene.
DR neXtProt; NX_Q8IVD9; -.
DR PharmGKB; PA134989375; -.
DR eggNOG; NOG245384; -.
DR HOGENOM; HOG000036072; -.
DR HOVERGEN; HBG100537; -.
DR InParanoid; Q8IVD9; -.
DR OMA; WNAILEG; -.
DR OrthoDB; EOG7HQN8G; -.
DR ChiTaRS; NUDCD3; human.
DR EvolutionaryTrace; Q8IVD9; -.
DR GeneWiki; NUDCD3_(gene); -.
DR GenomeRNAi; 23386; -.
DR NextBio; 45504; -.
DR PRO; PR:Q8IVD9; -.
DR ArrayExpress; Q8IVD9; -.
DR Bgee; Q8IVD9; -.
DR CleanEx; HS_NUDCD3; -.
DR Genevestigator; Q8IVD9; -.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR025934; NudC_N_dom.
DR InterPro; IPR027761; NUDCD3.
DR PANTHER; PTHR12356:SF4; PTHR12356:SF4; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF14050; Nudc_N; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 361 NudC domain-containing protein 3.
FT /FTId=PRO_0000057985.
FT DOMAIN 185 277 CS.
FT MOD_RES 146 146 Phosphoserine.
FT MOD_RES 355 355 Phosphoserine.
FT VARIANT 3 3 T -> P (in dbSNP:rs307007).
FT /FTId=VAR_054036.
FT VARIANT 235 235 R -> C (in dbSNP:rs11550029).
FT /FTId=VAR_031709.
FT CONFLICT 205 205 V -> L (in Ref. 2; AAH35014).
FT STRAND 179 185
FT STRAND 191 195
FT STRAND 198 204
FT HELIX 212 214
FT STRAND 215 219
FT STRAND 221 229
FT STRAND 231 244
FT TURN 248 250
FT STRAND 252 255
FT STRAND 259 265
FT STRAND 267 270
SQ SEQUENCE 361 AA; 40822 MW; 06B54758C395818A CRC64;
METGAAELYD QALLGILQHV GNVQDFLRVL FGFLYRKTDF YRLLRHPSDR MGFPPGAAQA
LVLQVFKTFD HMARQDDEKR RQELEEKIRR KEEEEAKTVS AAAAEKEPVP VPVQEIEIDS
TTELDGHQEV EKVQPPGPVK EMAHGSQEAE APGAVAGAAE VPREPPILPR IQEQFQKNPD
SYNGAVRENY TWSQDYTDLE VRVPVPKHVV KGKQVSVALS SSSIRVAMLE ENGERVLMEG
KLTHKINTES SLWSLEPGKC VLVNLSKVGE YWWNAILEGE EPIDIDKINK ERSMATVDEE
EQAVLDRLTF DYHQKLQGKP QSHELKVHEM LKKGWDAEGS PFRGQRFDPA MFNISPGAVQ
F
//
ID NUDC3_HUMAN Reviewed; 361 AA.
AC Q8IVD9; Q9BTI3; Q9H7W9; Q9UPT4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-APR-2007, sequence version 3.
DT 22-JAN-2014, entry version 98.
DE RecName: Full=NudC domain-containing protein 3;
GN Name=NUDCD3; Synonyms=KIAA1068;
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=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PRO-3 AND
RP CYS-235.
RC TISSUE=Brain, Pancreas, and Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-361.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-361.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, 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 [8]
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 [9]
RP STRUCTURE BY NMR OF 176-286.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CS domain of human KIAA1068.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- SIMILARITY: Contains 1 CS domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH03691.1; Type=Erroneous initiation;
CC Sequence=AAQ96892.1; Type=Erroneous gene model prediction;
CC Sequence=BAB14855.1; 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; AC004453; AAQ96892.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC003691; AAH03691.1; ALT_INIT; mRNA.
DR EMBL; BC011673; AAH11673.2; -; mRNA.
DR EMBL; BC035014; AAH35014.1; -; mRNA.
DR EMBL; AB028991; BAA83020.1; -; mRNA.
DR EMBL; AK024226; BAB14855.1; ALT_INIT; mRNA.
DR RefSeq; NP_056147.2; NM_015332.3.
DR UniGene; Hs.488171; -.
DR PDB; 1WGV; NMR; -; A=176-286.
DR PDBsum; 1WGV; -.
DR ProteinModelPortal; Q8IVD9; -.
DR SMR; Q8IVD9; 176-286.
DR IntAct; Q8IVD9; 4.
DR STRING; 9606.ENSP00000347626; -.
DR PhosphoSite; Q8IVD9; -.
DR DMDM; 145559509; -.
DR PaxDb; Q8IVD9; -.
DR PRIDE; Q8IVD9; -.
DR DNASU; 23386; -.
DR Ensembl; ENST00000355451; ENSP00000347626; ENSG00000015676.
DR GeneID; 23386; -.
DR KEGG; hsa:23386; -.
DR UCSC; uc003tkz.3; human.
DR CTD; 23386; -.
DR GeneCards; GC07M044421; -.
DR HGNC; HGNC:22208; NUDCD3.
DR HPA; HPA019136; -.
DR HPA; HPA019528; -.
DR HPA; HPA019529; -.
DR MIM; 610296; gene.
DR neXtProt; NX_Q8IVD9; -.
DR PharmGKB; PA134989375; -.
DR eggNOG; NOG245384; -.
DR HOGENOM; HOG000036072; -.
DR HOVERGEN; HBG100537; -.
DR InParanoid; Q8IVD9; -.
DR OMA; WNAILEG; -.
DR OrthoDB; EOG7HQN8G; -.
DR ChiTaRS; NUDCD3; human.
DR EvolutionaryTrace; Q8IVD9; -.
DR GeneWiki; NUDCD3_(gene); -.
DR GenomeRNAi; 23386; -.
DR NextBio; 45504; -.
DR PRO; PR:Q8IVD9; -.
DR ArrayExpress; Q8IVD9; -.
DR Bgee; Q8IVD9; -.
DR CleanEx; HS_NUDCD3; -.
DR Genevestigator; Q8IVD9; -.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR025934; NudC_N_dom.
DR InterPro; IPR027761; NUDCD3.
DR PANTHER; PTHR12356:SF4; PTHR12356:SF4; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF14050; Nudc_N; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 361 NudC domain-containing protein 3.
FT /FTId=PRO_0000057985.
FT DOMAIN 185 277 CS.
FT MOD_RES 146 146 Phosphoserine.
FT MOD_RES 355 355 Phosphoserine.
FT VARIANT 3 3 T -> P (in dbSNP:rs307007).
FT /FTId=VAR_054036.
FT VARIANT 235 235 R -> C (in dbSNP:rs11550029).
FT /FTId=VAR_031709.
FT CONFLICT 205 205 V -> L (in Ref. 2; AAH35014).
FT STRAND 179 185
FT STRAND 191 195
FT STRAND 198 204
FT HELIX 212 214
FT STRAND 215 219
FT STRAND 221 229
FT STRAND 231 244
FT TURN 248 250
FT STRAND 252 255
FT STRAND 259 265
FT STRAND 267 270
SQ SEQUENCE 361 AA; 40822 MW; 06B54758C395818A CRC64;
METGAAELYD QALLGILQHV GNVQDFLRVL FGFLYRKTDF YRLLRHPSDR MGFPPGAAQA
LVLQVFKTFD HMARQDDEKR RQELEEKIRR KEEEEAKTVS AAAAEKEPVP VPVQEIEIDS
TTELDGHQEV EKVQPPGPVK EMAHGSQEAE APGAVAGAAE VPREPPILPR IQEQFQKNPD
SYNGAVRENY TWSQDYTDLE VRVPVPKHVV KGKQVSVALS SSSIRVAMLE ENGERVLMEG
KLTHKINTES SLWSLEPGKC VLVNLSKVGE YWWNAILEGE EPIDIDKINK ERSMATVDEE
EQAVLDRLTF DYHQKLQGKP QSHELKVHEM LKKGWDAEGS PFRGQRFDPA MFNISPGAVQ
F
//
MIM
610296
*RECORD*
*FIELD* NO
610296
*FIELD* TI
*610296 NUDC DOMAIN-CONTAINING PROTEIN 3; NUDCD3
;;KIAA1068;;
NUDC-LIKE PROTEIN; NUDCL
read more*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated adult brain cDNA
library, Kikuno et al. (1999) cloned NUDCD3, which they designated
KIAA1068. The deduced protein contains 354 amino acids. RT-PCR ELISA
detected low NUDCD3 expression in heart, brain, and ovary, and in most
specific brain regions examined; little to none was detected in fetal
brain and in other peripheral tissues examined.
By searching a database for sequences similar to NUDC (610325), followed
by RT-PCR of a HeLa cell cDNA library, Zhou et al. (2006) cloned NUDCD3,
which they called NUDCL. The deduced 361-amino acid protein has a
calculated molecular mass of 41 kD. The N-terminal half contains a
coiled-coil domain, and the C-terminal half contains a nuclear movement
domain and a p23 (PTGES3; 607061) domain. Western blot analysis detected
ubiquitous Nudcl expression in all mouse tissues tested. NUDCL
colocalized with Golgi marker proteins in HeLa cells during interphase
and mitosis.
GENE FUNCTION
Zhou et al. (2006) found the expression and phosphorylation of NUDCL
increased during mitosis in HeLa cells. Depletion of NUDCL by RNA
interference inhibited cell growth and induced mitotic arrest with
multiple mitotic defects, resulting in cell death. The majority of NUDCL
depletion-induced mitotic defects appeared to result from loss of dynein
(see DYNC1H1; 600112) function, as suggested by the failure of
gamma-tubulin (see TUBG1; 191135) to be recruited to spindle poles and
by the mislocalization of the dynein complex from kinetochores, spindle
microtubules, and spindle poles during mitosis. Depletion of NUDCL also
resulted in the aggregation of dynein intermediate chains (see DYNC1I1;
604366) throughout the cytoplasm during mitosis. NUDCL bound to the
dynein complex, and its depletion induced degradation of dynein
intermediate chain, which was suppressed by a proteasome inhibitor. Zhou
et al. (2006) concluded that NUDCL influences the stabilization of
dynein intermediate chain.
MAPPING
By radiation hybrid analysis, Kikuno et al. (1999) mapped the NUDCD3
gene to chromosome 7.
*FIELD* RF
1. 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.
2. Zhou, T.; Zimmerman, W.; Liu, X.; Erikson, R. L.: A mammalian
NudC-like protein essential for dynein stability and cell viability. Proc.
Nat. Acad. Sci. 103: 9039-9044, 2006.
*FIELD* CD
Patricia A. Hartz: 8/4/2006
*FIELD* ED
mgross: 08/16/2006
wwang: 8/10/2006
wwang: 8/4/2006
*RECORD*
*FIELD* NO
610296
*FIELD* TI
*610296 NUDC DOMAIN-CONTAINING PROTEIN 3; NUDCD3
;;KIAA1068;;
NUDC-LIKE PROTEIN; NUDCL
read more*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated adult brain cDNA
library, Kikuno et al. (1999) cloned NUDCD3, which they designated
KIAA1068. The deduced protein contains 354 amino acids. RT-PCR ELISA
detected low NUDCD3 expression in heart, brain, and ovary, and in most
specific brain regions examined; little to none was detected in fetal
brain and in other peripheral tissues examined.
By searching a database for sequences similar to NUDC (610325), followed
by RT-PCR of a HeLa cell cDNA library, Zhou et al. (2006) cloned NUDCD3,
which they called NUDCL. The deduced 361-amino acid protein has a
calculated molecular mass of 41 kD. The N-terminal half contains a
coiled-coil domain, and the C-terminal half contains a nuclear movement
domain and a p23 (PTGES3; 607061) domain. Western blot analysis detected
ubiquitous Nudcl expression in all mouse tissues tested. NUDCL
colocalized with Golgi marker proteins in HeLa cells during interphase
and mitosis.
GENE FUNCTION
Zhou et al. (2006) found the expression and phosphorylation of NUDCL
increased during mitosis in HeLa cells. Depletion of NUDCL by RNA
interference inhibited cell growth and induced mitotic arrest with
multiple mitotic defects, resulting in cell death. The majority of NUDCL
depletion-induced mitotic defects appeared to result from loss of dynein
(see DYNC1H1; 600112) function, as suggested by the failure of
gamma-tubulin (see TUBG1; 191135) to be recruited to spindle poles and
by the mislocalization of the dynein complex from kinetochores, spindle
microtubules, and spindle poles during mitosis. Depletion of NUDCL also
resulted in the aggregation of dynein intermediate chains (see DYNC1I1;
604366) throughout the cytoplasm during mitosis. NUDCL bound to the
dynein complex, and its depletion induced degradation of dynein
intermediate chain, which was suppressed by a proteasome inhibitor. Zhou
et al. (2006) concluded that NUDCL influences the stabilization of
dynein intermediate chain.
MAPPING
By radiation hybrid analysis, Kikuno et al. (1999) mapped the NUDCD3
gene to chromosome 7.
*FIELD* RF
1. 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.
2. Zhou, T.; Zimmerman, W.; Liu, X.; Erikson, R. L.: A mammalian
NudC-like protein essential for dynein stability and cell viability. Proc.
Nat. Acad. Sci. 103: 9039-9044, 2006.
*FIELD* CD
Patricia A. Hartz: 8/4/2006
*FIELD* ED
mgross: 08/16/2006
wwang: 8/10/2006
wwang: 8/4/2006