NEDD1_HUMAN
ID NEDD1_HUMAN Reviewed; 660 AA.
AC Q8NHV4; B0AZN0; B4E145; G3V3F1; Q8NA30;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Protein NEDD1;
DE AltName: Full=Neural precursor cell expressed developmentally down-regulated protein 1;
DE Short=NEDD-1;
GN Name=NEDD1;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis, Thymus, and Tongue;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [6]
RP INTERACTION WITH FAM29A, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19029337; DOI=10.1083/jcb.200807046;
RA Zhu H., Coppinger J.A., Jang C.-Y., Yates J.R. III, Fang G.;
RT "FAM29A promotes microtubule amplification via recruitment of the NEDD1-
RT gamma-tubulin complex to the mitotic spindle.";
RL J. Cell Biol. 183:835-848(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP FUNCTION, PHOSPHORYLATION AT THR-550 BY CDK1, AND PHOSPHORYLATION AT
RP THR-382; SER-397; SER-426 AND SER-637 BY PLK1.
RX PubMed=19509060; DOI=10.1242/jcs.042747;
RA Zhang X., Chen Q., Feng J., Hou J., Yang F., Liu J., Jiang Q., Zhang C.;
RT "Sequential phosphorylation of Nedd1 by Cdk1 and Plk1 is required for
RT targeting of the gammaTuRC to the centrosome.";
RL J. Cell Sci. 122:2240-2251(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; SER-397; SER-411;
RP SER-468 AND SER-516, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [14]
RP INTERACTION WITH HSPA1A; HSPA1B AND GAMMA-TUBULIN, AND SUBCELLULAR
RP LOCATION.
RX PubMed=27137183; DOI=10.1007/s00018-016-2236-8;
RA Fang C.T., Kuo H.H., Pan T.S., Yu F.C., Yih L.H.;
RT "HSP70 regulates the function of mitotic centrosomes.";
RL Cell. Mol. Life Sci. 73:3949-3960(2016).
CC -!- FUNCTION: Required for mitosis progression. Promotes the nucleation of
CC microtubules from the spindle. {ECO:0000269|PubMed:19029337,
CC ECO:0000269|PubMed:19509060}.
CC -!- SUBUNIT: Interacts with FAM29A (PubMed:19029337). Interacts with HSPA1A
CC and HSPA1B. Interacts with gamma-tubulin in a HSPA1A/B-dependent manner
CC (PubMed:27137183). {ECO:0000269|PubMed:19029337,
CC ECO:0000269|PubMed:27137183}.
CC -!- INTERACTION:
CC Q8NHV4; Q7Z4H7: HAUS6; NbExp=2; IntAct=EBI-2555055, EBI-2558196;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:19029337, ECO:0000269|PubMed:27137183}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NHV4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NHV4-2; Sequence=VSP_043411;
CC Name=3;
CC IsoId=Q8NHV4-3; Sequence=VSP_053794;
CC -!- PTM: During mitosis, prior phosphorylation on Thr-550 by CDK1 promotes
CC subsequent phosphorylation by PLK1 on Thr-382, Ser-397, Ser-426 and
CC Ser-637. Phosphorylated NEDD1 can interact with gamma-tubulin for
CC targeting the gamma-tubulin ring complex (gTuRC) to the centrosome, an
CC important step for spindle formation. {ECO:0000269|PubMed:19509060}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27605.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK093221; BAC04099.1; -; mRNA.
DR EMBL; AK303656; BAG64657.1; -; mRNA.
DR EMBL; AK315821; BAF98712.1; -; mRNA.
DR EMBL; AC007564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC013417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97577.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW97579.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW97580.1; -; Genomic_DNA.
DR EMBL; BC027605; AAH27605.1; ALT_INIT; mRNA.
DR CCDS; CCDS44955.1; -. [Q8NHV4-3]
DR CCDS; CCDS44956.1; -. [Q8NHV4-2]
DR CCDS; CCDS9063.1; -. [Q8NHV4-1]
DR RefSeq; NP_001128647.1; NM_001135175.1. [Q8NHV4-3]
DR RefSeq; NP_001128648.1; NM_001135176.1. [Q8NHV4-1]
DR RefSeq; NP_001128649.1; NM_001135177.1. [Q8NHV4-2]
DR RefSeq; NP_690869.1; NM_152905.3. [Q8NHV4-1]
DR RefSeq; XP_005268701.1; XM_005268644.2. [Q8NHV4-3]
DR RefSeq; XP_006719300.1; XM_006719237.3. [Q8NHV4-2]
DR RefSeq; XP_011536205.1; XM_011537903.2. [Q8NHV4-2]
DR AlphaFoldDB; Q8NHV4; -.
DR SMR; Q8NHV4; -.
DR BioGRID; 125728; 218.
DR DIP; DIP-48838N; -.
DR IntAct; Q8NHV4; 102.
DR STRING; 9606.ENSP00000451211; -.
DR GlyGen; Q8NHV4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NHV4; -.
DR PhosphoSitePlus; Q8NHV4; -.
DR BioMuta; NEDD1; -.
DR DMDM; 74762597; -.
DR EPD; Q8NHV4; -.
DR jPOST; Q8NHV4; -.
DR MassIVE; Q8NHV4; -.
DR MaxQB; Q8NHV4; -.
DR PaxDb; Q8NHV4; -.
DR PeptideAtlas; Q8NHV4; -.
DR PRIDE; Q8NHV4; -.
DR ProteomicsDB; 32921; -.
DR ProteomicsDB; 73763; -. [Q8NHV4-1]
DR ProteomicsDB; 73764; -. [Q8NHV4-2]
DR Antibodypedia; 30194; 227 antibodies from 33 providers.
DR DNASU; 121441; -.
DR Ensembl; ENST00000266742.9; ENSP00000266742.5; ENSG00000139350.12. [Q8NHV4-1]
DR Ensembl; ENST00000411739.6; ENSP00000411307.2; ENSG00000139350.12. [Q8NHV4-2]
DR Ensembl; ENST00000429527.6; ENSP00000404978.2; ENSG00000139350.12. [Q8NHV4-1]
DR Ensembl; ENST00000457368.2; ENSP00000407964.2; ENSG00000139350.12. [Q8NHV4-2]
DR Ensembl; ENST00000557644.5; ENSP00000451211.1; ENSG00000139350.12. [Q8NHV4-3]
DR GeneID; 121441; -.
DR KEGG; hsa:121441; -.
DR MANE-Select; ENST00000266742.9; ENSP00000266742.5; NM_152905.4; NP_690869.1.
DR UCSC; uc001teu.5; human. [Q8NHV4-1]
DR CTD; 121441; -.
DR DisGeNET; 121441; -.
DR GeneCards; NEDD1; -.
DR HGNC; HGNC:7723; NEDD1.
DR HPA; ENSG00000139350; Low tissue specificity.
DR MIM; 600372; gene.
DR neXtProt; NX_Q8NHV4; -.
DR OpenTargets; ENSG00000139350; -.
DR PharmGKB; PA31531; -.
DR VEuPathDB; HostDB:ENSG00000139350; -.
DR eggNOG; KOG4378; Eukaryota.
DR GeneTree; ENSGT00390000001561; -.
DR HOGENOM; CLU_415014_0_0_1; -.
DR InParanoid; Q8NHV4; -.
DR OMA; RHLKYSS; -.
DR PhylomeDB; Q8NHV4; -.
DR TreeFam; TF329816; -.
DR PathwayCommons; Q8NHV4; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; Q8NHV4; -.
DR SIGNOR; Q8NHV4; -.
DR BioGRID-ORCS; 121441; 766 hits in 1088 CRISPR screens.
DR ChiTaRS; NEDD1; human.
DR GeneWiki; NEDD1; -.
DR GenomeRNAi; 121441; -.
DR Pharos; Q8NHV4; Tbio.
DR PRO; PR:Q8NHV4; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8NHV4; protein.
DR Bgee; ENSG00000139350; Expressed in secondary oocyte and 179 other tissues.
DR ExpressionAtlas; Q8NHV4; baseline and differential.
DR Genevisible; Q8NHV4; HS.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005814; C:centriole; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000242; C:pericentriolar material; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0043015; F:gamma-tubulin binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Mitosis; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..660
FT /note="Protein NEDD1"
FT /id="PRO_0000051095"
FT REPEAT 1..31
FT /note="WD 1"
FT REPEAT 32..71
FT /note="WD 2"
FT REPEAT 75..114
FT /note="WD 3"
FT REPEAT 117..156
FT /note="WD 4"
FT REPEAT 160..200
FT /note="WD 5"
FT REPEAT 204..244
FT /note="WD 6"
FT REPEAT 246..285
FT /note="WD 7"
FT REPEAT 289..332
FT /note="WD 8"
FT REGION 369..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 382
FT /note="Phosphothreonine; by PLK1"
FT /evidence="ECO:0000269|PubMed:19509060"
FT MOD_RES 397
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:19509060,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 426
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:19509060"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 550
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:19509060"
FT MOD_RES 637
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:19509060"
FT VAR_SEQ 1..89
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043411"
FT VAR_SEQ 1
FT /note="M -> MHFTGAVM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053794"
FT CONFLICT 170
FT /note="Y -> C (in Ref. 1; BAC04099)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="M -> V (in Ref. 1; BAC04099)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="L -> P (in Ref. 1; BAC04099)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 71966 MW; 12817A567C13098B CRC64;
MQENLRFASS GDDIKIWDAS SMTLVDKFNP HTSPHGISSI CWSSNNNFLV TASSSGDKIV
VSSCKCKPVP LLELAEGQKQ TCVNLNSTSM YLVSGGLNNT VNIWDLKSKR VHRSLKDHKD
QVTCVTYNWN DCYIASGSLS GEIILHSVTT NLSSTPFGHG SNQSVRHLKY SLFKKSLLGS
VSDNGIVTLW DVNSQSPYHN FDSVHKAPAS GICFSPVNEL LFVTIGLDKR IILYDTSSKK
LVKTLVADTP LTAVDFMPDG ATLAIGSSRG KIYQYDLRML KSPVKTISAH KTSVQCIAFQ
YSTVLTKSSL NKGCSNKPTT VNKRSVNVNA ASGGVQNSGI VREAPATSIA TVLPQPMTSA
MGKGTVAVQE KAGLPRSINT DTLSKETDSG KNQDFSSFDD TGKSSLGDMF SPIRDDAVVN
KGSDESIGKG DGFDFLPQLN SVFPPRKNPV TSSTSVLHSS PLNVFMGSPG KEENENRDLT
AESKKIYMGK QESKDSFKQL AKLVTSGAES GNLNTSPSSN QTRNSEKFEK PENEIEAQLI
CEPPINGSST PNPKIASSVT AGVASSLSEK IADSIGNNRQ NAPLTSIQIR FIQNMIQETL
DDFREACHRD IVNLQVEMIK QFHMQLNEMH SLLERYSVNE GLVAEIERLR EENKRLRAHF
