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   24-JAN-2024, entry version 153.
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,
RC   Pancreas, 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; 6.
DR   IntAct; Q9CQ48; 2.
DR   MINT; Q9CQ48; -.
DR   STRING; 10090.ENSMUSP00000020578; -.
DR   GlyGen; Q9CQ48; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9CQ48; -.
DR   PhosphoSitePlus; Q9CQ48; -.
DR   SwissPalm; Q9CQ48; -.
DR   EPD; Q9CQ48; -.
DR   jPOST; Q9CQ48; -.
DR   MaxQB; Q9CQ48; -.
DR   PaxDb; 10090-ENSMUSP00000020578; -.
DR   PeptideAtlas; Q9CQ48; -.
DR   ProteomicsDB; 291924; -.
DR   Pumba; Q9CQ48; -.
DR   Antibodypedia; 45873; 99 antibodies from 21 providers.
DR   DNASU; 52653; -.
DR   Ensembl; ENSMUST00000020578.11; ENSMUSP00000020578.5; ENSMUSG00000020328.11.
DR   GeneID; 52653; -.
DR   KEGG; mmu:52653; -.
DR   UCSC; uc007ily.3; mouse.
DR   AGR; MGI:1277103; -.
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; 5387420at2759; -.
DR   PhylomeDB; Q9CQ48; -.
DR   TreeFam; TF332391; -.
DR   BioGRID-ORCS; 52653; 5 hits in 78 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 259 other cell types or tissues.
DR   ExpressionAtlas; Q9CQ48; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
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: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   Gene3D; 1.20.5.740; Single helix bin; 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; NUCLEAR MOVEMENT PROTEIN NUDC; 1.
DR   PANTHER; PTHR12356:SF18; NUDC DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF04969; CS; 1.
DR   SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR   PROSITE; PS51203; CS; 1.
DR   Genevisible; Q9CQ48; MM.
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
//