NEDD1_MOUSE
ID NEDD1_MOUSE Reviewed; 660 AA.
AC P33215; Q6NXV3; Q8BN12; Q8BN86; Q8BQL9; Q9CWK2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Protein NEDD1;
DE AltName: Full=Neural precursor cell expressed developmentally down-regulated protein 1;
DE Short=NEDD-1;
GN Name=Nedd1; Synonyms=Nedd-1;
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 [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=1378265; DOI=10.1016/0006-291x(92)91747-e;
RA Kumar S., Tomooka Y., Noda M.;
RT "Identification of a set of genes with developmentally down-regulated
RT expression in the mouse brain.";
RL Biochem. Biophys. Res. Commun. 185:1155-1161(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Head, and Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Egg;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379 AND SER-411, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Spleen;
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).
CC -!- FUNCTION: Required for mitosis progression. Promotes the nucleation of
CC microtubules from the spindle (By similarity). May play an important
CC role during the embryonic development and differentiation of the
CC central nervous system (PubMed:1378265). {ECO:0000250|UniProtKB:Q8NHV4,
CC ECO:0000269|PubMed:1378265}.
CC -!- SUBUNIT: Interacts with FAM29A. Interacts with HSPA1A and HSPA1B.
CC Interacts with gamma-tubulin in a HSPA1A/B-dependent manner.
CC {ECO:0000250|UniProtKB:Q8NHV4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q8NHV4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P33215-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P33215-2; Sequence=VSP_016263, VSP_016264;
CC -!- DEVELOPMENTAL STAGE: Down-regulated during the development of brain.
CC -!- PTM: During mitosis, prior phosphorylation on Thr-550 by CDK1 promotes
CC subsequent phosphorylation by PLK1 on Ser-397, Ser-426 and Ser-637.
CC Phosphorylated NEDD1 can interact with gamma-tubulin for targeting the
CC gamma-tubulin ring complex (gTuRC) to the centrosome, an important step
CC for spindle formation. {ECO:0000250|UniProtKB:Q8NHV4}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
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DR EMBL; D10712; BAA01554.1; -; mRNA.
DR EMBL; AK048393; BAC33321.1; -; mRNA.
DR EMBL; AK085355; BAC39429.2; -; mRNA.
DR EMBL; AK090040; BAC41060.1; -; mRNA.
DR EMBL; AK010591; BAB27048.1; -; mRNA.
DR EMBL; AK153746; BAE32166.1; -; mRNA.
DR EMBL; BC052430; AAH52430.1; -; mRNA.
DR EMBL; BC066870; AAH66870.1; -; mRNA.
DR CCDS; CCDS24123.1; -. [P33215-1]
DR PIR; I60167; I60167.
DR RefSeq; NP_032708.2; NM_008682.2. [P33215-1]
DR AlphaFoldDB; P33215; -.
DR SMR; P33215; -.
DR BioGRID; 201721; 115.
DR IntAct; P33215; 105.
DR MINT; P33215; -.
DR STRING; 10090.ENSMUSP00000020163; -.
DR iPTMnet; P33215; -.
DR PhosphoSitePlus; P33215; -.
DR EPD; P33215; -.
DR jPOST; P33215; -.
DR MaxQB; P33215; -.
DR PaxDb; P33215; -.
DR PeptideAtlas; P33215; -.
DR PRIDE; P33215; -.
DR ProteomicsDB; 253060; -. [P33215-1]
DR ProteomicsDB; 253061; -. [P33215-2]
DR Antibodypedia; 30194; 227 antibodies from 33 providers.
DR Ensembl; ENSMUST00000020163; ENSMUSP00000020163; ENSMUSG00000019988. [P33215-1]
DR GeneID; 17997; -.
DR KEGG; mmu:17997; -.
DR UCSC; uc007gud.2; mouse. [P33215-1]
DR UCSC; uc007gue.2; mouse. [P33215-2]
DR CTD; 121441; -.
DR MGI; MGI:97293; Nedd1.
DR VEuPathDB; HostDB:ENSMUSG00000019988; -.
DR eggNOG; KOG4378; Eukaryota.
DR GeneTree; ENSGT00390000001561; -.
DR HOGENOM; CLU_415014_0_0_1; -.
DR InParanoid; P33215; -.
DR OMA; RHLKYSS; -.
DR OrthoDB; 234690at2759; -.
DR PhylomeDB; P33215; -.
DR TreeFam; TF329816; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 17997; 25 hits in 76 CRISPR screens.
DR ChiTaRS; Nedd1; mouse.
DR PRO; PR:P33215; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P33215; protein.
DR Bgee; ENSMUSG00000019988; Expressed in animal zygote and 228 other tissues.
DR ExpressionAtlas; P33215; baseline and differential.
DR Genevisible; P33215; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0000931; C:gamma-tubulin large complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000242; C:pericentriolar material; IDA:MGI.
DR GO; GO:0000922; C:spindle pole; IDA:MGI.
DR GO; GO:0043015; F:gamma-tubulin binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007019; P:microtubule depolymerization; ISO:MGI.
DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR GO; GO:0031109; P:microtubule polymerization or depolymerization; ISO:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0070201; P:regulation of establishment of protein localization; ISO:MGI.
DR Gene3D; 2.130.10.10; -; 2.
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; 3.
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_0000051096"
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 MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHV4"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 397
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q8NHV4"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 426
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q8NHV4"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHV4"
FT MOD_RES 550
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q8NHV4"
FT MOD_RES 637
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q8NHV4"
FT VAR_SEQ 500..508
FT /note="FTKLISSGA -> VSPRKEYPV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016263"
FT VAR_SEQ 509..660
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016264"
FT CONFLICT 13
FT /note="D -> G (in Ref. 3; AAH66870)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="V -> E (in Ref. 2; BAC41060)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="D -> G (in Ref. 2; BAC33321)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="P -> L (in Ref. 1; BAA01554 and 2; BAC41060)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 71292 MW; E26CACECE07344BF CRC64;
MQENLRFASS GDDVKIWDAS FLTLVDKFNP HTSPHGISSI CWSSNNNFLV TASSSGDKIV
VSSCKCKPVP LLELAEGQKQ TCVDLNSTSM YLASGGLNNT VNIWDLKSKR LHRSLKDHKC
EVTCVAYNWN DCYIASGSLS GEIILHSVTT NTSSTPFGHG SKQPIRHIKY SLFRKSLLGS
VSDNGVVTLW DVNSQSSYHT FDSTHKAPAS GICFSPVNEL LFVTIGLDKR IILYDTSSKK
LVKTLVADTP LTAVDFMPDG ATLAIGSSRG KIYQYDLRML KSPVKTISAH KTSVQCIAFQ
YSTSLTKASL SKGSSNKATA VNKRSVPVSS SSGAAQNSGI VREAPSPSIA TVLPQPVTTA
LGKGSGAAQD EAGLARSKST DIFSKETDAG KSQDFSSFDD TGKNSLGDMF SPIRDDAVVS
KGGDESIGKG DGLDFLPQLN SVFPLRKNAG ASSSLVLHSS PLNVLMGSSG KEENESHEPS
AESKRAYLGK QEPKDAMKQF TKLISSGAEP GILNTCPSSN QARNLEKFEK PEKDIEAQLI
HEPSVNGSST TVPKAASSVT AGVASSLSEK IVDTLGNSRP GAPLTSVQIR FIQNMIQETL
DDFREACHRD IVNLQVEMIK QFHIQLNEMH SLLERYSVNE GLVAEIERLR EENKRLRAHF
