ID   NUDC2_HUMAN             Reviewed;         157 AA.
AC   Q8WVJ2; B2R4V0;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=NudC domain-containing protein 2;
GN   Name=NUDCD2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION
RP   WITH LIS1.
RX   PubMed=20133715; DOI=10.1073/pnas.0914307107;
RA   Yang Y., Yan X., Cai Y., Lu Y., Si J., Zhou T.;
RT   "NudC-like protein 2 regulates the LIS1/dynein pathway by stabilizing LIS1
RT   with Hsp90.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:3499-3504(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Trachea;
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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].
RC   TISSUE=Kidney;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [6]
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., Buerckstuemmer T.,
RA   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   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: May regulate the LIS1/dynein pathway by stabilizing LIS1 with
CC       Hsp90 chaperone. {ECO:0000269|PubMed:20133715}.
CC   -!- SUBUNIT: Interacts with LIS1. {ECO:0000269|PubMed:20133715}.
CC   -!- INTERACTION:
CC       Q8WVJ2; O75426: FBXO24; NbExp=2; IntAct=EBI-1052153, EBI-6425658;
CC       Q8WVJ2; P07900: HSP90AA1; NbExp=4; IntAct=EBI-1052153, EBI-296047;
CC       Q8WVJ2; Q86SG6: NEK8; NbExp=3; IntAct=EBI-1052153, EBI-1752987;
CC       Q8WVJ2; Q96CV9: OPTN; NbExp=3; IntAct=EBI-1052153, EBI-748974;
CC       Q8WVJ2; P43034: PAFAH1B1; NbExp=8; IntAct=EBI-1052153, EBI-720620;
CC       Q8WVJ2; O14744: PRMT5; NbExp=2; IntAct=EBI-1052153, EBI-351098;
CC   -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC       {ECO:0000269|PubMed:20133715}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000269|PubMed:20133715}. Cytoplasm,
CC       cytoskeleton, spindle pole {ECO:0000269|PubMed:20133715}.
CC       Note=Associates with centrosomes in interphase and to spindle poles and
CC       kinetochores during mitosis.
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DR   EMBL; FJ215684; ACJ05660.1; -; mRNA.
DR   EMBL; AK311957; BAG34897.1; -; mRNA.
DR   EMBL; BX538290; CAD98085.1; -; mRNA.
DR   EMBL; CH471062; EAW61527.1; -; Genomic_DNA.
DR   EMBL; BC017934; AAH17934.1; -; mRNA.
DR   CCDS; CCDS4361.1; -.
DR   RefSeq; NP_660309.1; NM_145266.5.
DR   AlphaFoldDB; Q8WVJ2; -.
DR   SMR; Q8WVJ2; -.
DR   BioGRID; 126402; 418.
DR   DIP; DIP-59509N; -.
DR   IntAct; Q8WVJ2; 46.
DR   MINT; Q8WVJ2; -.
DR   STRING; 9606.ENSP00000304854; -.
DR   GlyConnect; 1583; 1 N-Linked glycan (1 site).
DR   GlyGen; Q8WVJ2; 3 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q8WVJ2; -.
DR   PhosphoSitePlus; Q8WVJ2; -.
DR   BioMuta; NUDCD2; -.
DR   EPD; Q8WVJ2; -.
DR   jPOST; Q8WVJ2; -.
DR   MassIVE; Q8WVJ2; -.
DR   MaxQB; Q8WVJ2; -.
DR   PaxDb; 9606-ENSP00000304854; -.
DR   PeptideAtlas; Q8WVJ2; -.
DR   ProteomicsDB; 74798; -.
DR   Pumba; Q8WVJ2; -.
DR   TopDownProteomics; Q8WVJ2; -.
DR   Antibodypedia; 45873; 99 antibodies from 21 providers.
DR   DNASU; 134492; -.
DR   Ensembl; ENST00000302764.9; ENSP00000304854.3; ENSG00000170584.11.
DR   GeneID; 134492; -.
DR   KEGG; hsa:134492; -.
DR   MANE-Select; ENST00000302764.9; ENSP00000304854.3; NM_145266.6; NP_660309.1.
DR   UCSC; uc003lze.4; human.
DR   AGR; HGNC:30535; -.
DR   CTD; 134492; -.
DR   GeneCards; NUDCD2; -.
DR   HGNC; HGNC:30535; NUDCD2.
DR   HPA; ENSG00000170584; Low tissue specificity.
DR   MIM; 620136; gene.
DR   neXtProt; NX_Q8WVJ2; -.
DR   OpenTargets; ENSG00000170584; -.
DR   PharmGKB; PA134991349; -.
DR   VEuPathDB; HostDB:ENSG00000170584; -.
DR   eggNOG; KOG2265; Eukaryota.
DR   GeneTree; ENSGT00390000001644; -.
DR   InParanoid; Q8WVJ2; -.
DR   OMA; DPRSFMG; -.
DR   OrthoDB; 5387420at2759; -.
DR   PhylomeDB; Q8WVJ2; -.
DR   TreeFam; TF332391; -.
DR   PathwayCommons; Q8WVJ2; -.
DR   SignaLink; Q8WVJ2; -.
DR   SIGNOR; Q8WVJ2; -.
DR   BioGRID-ORCS; 134492; 42 hits in 1165 CRISPR screens.
DR   ChiTaRS; NUDCD2; human.
DR   GeneWiki; NUDCD2; -.
DR   GenomeRNAi; 134492; -.
DR   Pharos; Q8WVJ2; Tdark.
DR   PRO; PR:Q8WVJ2; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q8WVJ2; Protein.
DR   Bgee; ENSG00000170584; Expressed in oocyte and 188 other cell types or tissues.
DR   ExpressionAtlas; Q8WVJ2; 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; IDA:HPA.
DR   GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR   GO; GO:0072686; C:mitotic spindle; IDA:HPA.
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; Q8WVJ2; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Centromere; Chromosome; Cytoplasm; Cytoskeleton; Kinetochore;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..157
FT                   /note="NudC domain-containing protein 2"
FT                   /id="PRO_0000057982"
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:0007744|PubMed:22814378"
FT   MOD_RES         142
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         145
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQ48"
SQ   SEQUENCE   157 AA;  17676 MW;  8A425EA4F6F321FD CRC64;
     MSAPFEERSG VVPCGTPWGQ WYQTLEEVFI EVQVPPGTRA QDIQCGLQSR HVALSVGGRE
     ILKGKLFDST IADEGTWTLE DRKMVRIVLT KTKRDAANCW TSLLESEYAA DPWVQDQMQR
     KLTLERFQKE NPGFDFSGAE ISGNYTKGGP DFSNLEK
//