NUDC2_MOUSE
ID NUDC2_MOUSE Reviewed; 157 AA.
AC Q9CQ48; Q8CD03; Q9CY63; Q9D0V4;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=NudC domain-containing protein 2;
GN Name=Nudcd2; Synonyms=D11Ertd603e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Head, Liver, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 5-155.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of NUDC domain-containing protein 2 (13542905) from Mus
RT musculus at 1.95 A resolution.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: May regulate the LIS1/dynein pathway by stabilizing LIS1 with
CC Hsp90 chaperone. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with LIS1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250}. Note=Associates with centrosomes in interphase and to
CC spindle poles and kinetochores during mitosis. {ECO:0000250}.
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DR EMBL; AK004388; BAB23283.1; -; mRNA.
DR EMBL; AK005909; BAB24313.1; -; mRNA.
DR EMBL; AK010850; BAB27222.1; -; mRNA.
DR EMBL; AK012388; BAB28205.1; -; mRNA.
DR EMBL; AK031779; BAC27545.1; -; mRNA.
DR EMBL; AL646055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005646; AAH05646.1; -; mRNA.
DR CCDS; CCDS24549.1; -.
DR RefSeq; NP_001277626.1; NM_001290697.1.
DR RefSeq; NP_080299.4; NM_026023.5.
DR PDB; 2RH0; X-ray; 1.95 A; A/B/C/D=5-155.
DR PDBsum; 2RH0; -.
DR AlphaFoldDB; Q9CQ48; -.
DR SMR; Q9CQ48; -.
DR BioGRID; 206717; 4.
DR IntAct; Q9CQ48; 2.
DR MINT; Q9CQ48; -.
DR STRING; 10090.ENSMUSP00000020578; -.
DR iPTMnet; Q9CQ48; -.
DR PhosphoSitePlus; Q9CQ48; -.
DR EPD; Q9CQ48; -.
DR jPOST; Q9CQ48; -.
DR MaxQB; Q9CQ48; -.
DR PaxDb; Q9CQ48; -.
DR PeptideAtlas; Q9CQ48; -.
DR PRIDE; Q9CQ48; -.
DR ProteomicsDB; 291924; -.
DR Antibodypedia; 45873; 85 antibodies from 20 providers.
DR DNASU; 52653; -.
DR Ensembl; ENSMUST00000020578; ENSMUSP00000020578; ENSMUSG00000020328.
DR GeneID; 52653; -.
DR KEGG; mmu:52653; -.
DR UCSC; uc007ily.3; mouse.
DR CTD; 134492; -.
DR MGI; MGI:1277103; Nudcd2.
DR VEuPathDB; HostDB:ENSMUSG00000020328; -.
DR eggNOG; KOG2265; Eukaryota.
DR GeneTree; ENSGT00390000001644; -.
DR InParanoid; Q9CQ48; -.
DR OMA; DPRSFMG; -.
DR OrthoDB; 1310591at2759; -.
DR PhylomeDB; Q9CQ48; -.
DR TreeFam; TF332391; -.
DR BioGRID-ORCS; 52653; 5 hits in 73 CRISPR screens.
DR EvolutionaryTrace; Q9CQ48; -.
DR PRO; PR:Q9CQ48; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CQ48; protein.
DR Bgee; ENSMUSG00000020328; Expressed in pharyngeal arch 2 and 256 other tissues.
DR ExpressionAtlas; Q9CQ48; baseline and differential.
DR Genevisible; Q9CQ48; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR CDD; cd06494; p23_NUDCD2_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR037898; NudC_fam.
DR InterPro; IPR037902; p23_NUDCD2.
DR PANTHER; PTHR12356; PTHR12356; 1.
DR Pfam; PF04969; CS; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW Kinetochore; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8WVJ2"
FT CHAIN 2..157
FT /note="NudC domain-containing protein 2"
FT /id="PRO_0000057983"
FT DOMAIN 14..104
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REGION 134..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVJ2"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVJ2"
FT MOD_RES 145
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT CONFLICT 9
FT /note="S -> R (in Ref. 1; BAB23283/BAB27222)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="W -> R (in Ref. 1; BAC27545)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="P -> T (in Ref. 1; BAB23283)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:2RH0"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:2RH0"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:2RH0"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2RH0"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:2RH0"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:2RH0"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:2RH0"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:2RH0"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2RH0"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:2RH0"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:2RH0"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2RH0"
FT HELIX 112..130
FT /evidence="ECO:0007829|PDB:2RH0"
SQ SEQUENCE 157 AA; 17660 MW; C7F485C957893803 CRC64;
MSAPFEERSG VVPCGTPWGQ WYQTLEEVFI EVQVPPGTRA QDIQCGLQSR HVALAVGGRE
ILKGKLFDST IADEGTWTLE DRKMVRIVLT KTKRDAANCW TSLLESEYAA DPWVQDQMQR
KLTLERFQKE NPGFDFSGAE ISGNYTKGGP DFSNLEK
