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RecName: Full=Nuclear distribution protein nudE-like 1; Short=Protein Nudel

UniProtKB/Swiss-Prot: Q78PB6.1

Identical Proteins FASTA Graphics 

LOCUS       NDEL1_RAT                345 aa            linear   ROD 29-MAY-2024
DEFINITION  RecName: Full=Nuclear distribution protein nudE-like 1;
            Short=Protein Nudel.
ACCESSION   Q78PB6
VERSION     Q78PB6.1
DBSOURCE    UniProtKB: locus NDEL1_RAT, accession Q78PB6;
            class: standard.
            extra accessions:Q6IRI4
            created: Jun 13, 2006.
            sequence updated: Jul 5, 2004.
            annotation updated: May 29, 2024.
            xrefs: AY008298.1, AAG21830.1, BC070909.1, AAH70909.1, NP_579854.1,
            XP_006246640.1, 2V71_A, 2V71_B
            xrefs (non-sequence databases): PDBsum:2V71, AlphaFoldDB:Q78PB6,
            SMR:Q78PB6, IntAct:Q78PB6, MINT:Q78PB6,
            STRING:10116.ENSRNOP00000005574, iPTMnet:Q78PB6,
            PhosphoSitePlus:Q78PB6, jPOST:Q78PB6,
            PaxDb:10116-ENSRNOP00000005574, Ensembl:ENSRNOT00000005574.8,
            Ensembl:ENSRNOP00000005574.6, Ensembl:ENSRNOG00000004139.9,
            GeneID:170845, KEGG:rno:170845, UCSC:RGD:621235, AGR:RGD:621235,
            CTD:81565, RGD:621235, VEuPathDB:HostDB:ENSRNOG00000004139,
            eggNOG:KOG1853, GeneTree:ENSGT00390000000111,
            HOGENOM:CLU_057872_0_0_1, InParanoid:Q78PB6, OrthoDB:2910907at2759,
            PhylomeDB:Q78PB6, TreeFam:TF325693, Reactome:R-RNO-141444,
            Reactome:R-RNO-2467813, Reactome:R-RNO-2500257,
            Reactome:R-RNO-5663220, Reactome:R-RNO-68877,
            Reactome:R-RNO-9648025, EvolutionaryTrace:Q78PB6, PRO:PR:Q78PB6,
            Proteomes:UP000002494, Bgee:ENSRNOG00000004139, GO:0030424,
            GO:1904115, GO:0043203, GO:0044297, GO:0031252, GO:0090724,
            GO:0005813, GO:0005871, GO:0000776, GO:0005874, GO:0005875,
            GO:0005815, GO:0060053, GO:0005635, GO:0005819, GO:0008021,
            GO:0043014, GO:0048487, GO:0042802, GO:0008017, GO:0070012,
            GO:0044877, GO:0016477, GO:0021955, GO:0051642, GO:0021799,
            GO:0007059, GO:0051303, GO:0000132, GO:0001833, GO:0008286,
            GO:0032418, GO:0000226, GO:0007020, GO:0007100, GO:0060052,
            GO:0001764, GO:0031175, GO:1990138, GO:0051081, GO:0045773,
            GO:0048680, GO:1900029, GO:0140650, GO:0033157, GO:0010975,
            GO:0008090, GO:0047496, Gene3D:6.10.250.1080, InterPro:IPR033494,
            InterPro:IPR006964, PANTHER:PTHR10921, PANTHER:PTHR10921:SF0,
            Pfam:PF04880
KEYWORDS    3D-structure; Alternative splicing; Centromere; Chromosome; Coiled
            coil; Cytoplasm; Cytoskeleton; Developmental protein;
            Differentiation; Kinetochore; Lipoprotein; Microtubule;
            Neurogenesis; Palmitate; Phosphoprotein; Reference proteome;
            Transport.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Umezu,M., Kitagawa,M., Aoki,J. and Arai,H.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-SEP-2000) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).;
            STRAIN=Sprague-Dawley; TISSUE=Liver
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).;
            TISSUE=Heart
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Niethammer,M., Smith,D.S., Ayala,R., Peng,J., Ko,J., Lee,M.S.,
            Morabito,M. and Tsai,L.H.
  TITLE     NUDEL is a novel Cdk5 substrate that associates with LIS1 and
            cytoplasmic dynein
  JOURNAL   Neuron 28 (3), 697-711 (2000)
   PUBMED   11163260
  REMARK    INTERACTION WITH PAFAH1B1 AND DYNEIN, AND SUBCELLULAR LOCATION.;
            TISSUE=Brain
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Hayashi,M.A., Portaro,F.C., Bastos,M.F., Guerreiro,J.R.,
            Oliveira,V., Gorrao,S.S., Tambourgi,D.V., Sant'Anna,O.A.,
            Whiting,P.J., Camargo,L.M., Konno,K., Brandon,N.J. and Camargo,A.C.
  TITLE     Inhibition of NUDEL (nuclear distribution
            element-like)-oligopeptidase activity by disrupted-in-schizophrenia
            1
  JOURNAL   Proc Natl Acad Sci U S A 102 (10), 3828-3833 (2005)
   PUBMED   15728732
  REMARK    PUTATIVE FUNCTION AS AN OLIGOPEPTIDASE.
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Kamiya,A., Tomoda,T., Chang,J., Takaki,M., Zhan,C., Morita,M.,
            Cascio,M.B., Elashvili,S., Koizumi,H., Takanezawa,Y., Dickerson,F.,
            Yolken,R., Arai,H. and Sawa,A.
  TITLE     DISC1-NDEL1/NUDEL protein interaction, an essential component for
            neurite outgrowth, is modulated by genetic variations of DISC1
  JOURNAL   Hum Mol Genet 15 (22), 3313-3323 (2006)
   PUBMED   17035248
  REMARK    FUNCTION, INTERACTION WITH DISC1, INDUCTION, AND SUBCELLULAR
            LOCATION.
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Lundby,A., Secher,A., Lage,K., Nordsborg,N.B., Dmytriyev,A.,
            Lundby,C. and Olsen,J.V.
  TITLE     Quantitative maps of protein phosphorylation sites across 14
            different rat organs and tissues
  JOURNAL   Nat Commun 3, 876 (2012)
   PUBMED   22673903
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND
            IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
            Publication Status: Online-Only
COMMENT     On Jun 13, 2006 this sequence version replaced gi:81884834.
            [FUNCTION] Required for organization of the cellular microtubule
            array and microtubule anchoring at the centrosome. May regulate
            microtubule organization at least in part by targeting the
            microtubule severing protein KATNA1 to the centrosome. Also
            positively regulates the activity of the minus-end directed
            microtubule motor protein dynein. May enhance dynein-mediated
            microtubule sliding by targeting dynein to the microtubule plus
            ends. Required for several dynein- and microtubule-dependent
            processes such as the maintenance of Golgi integrity, the
            centripetal motion of secretory vesicles and the coupling of the
            nucleus and centrosome. Also required during brain development for
            the migration of newly formed neurons from the
            ventricular/subventricular zone toward the cortical plate. Required
            for mitosis in some cell types but appears to be dispensible for
            mitosis in cortical neuronal progenitors, which instead requires
            NDE1. Facilitates the polymerization of neurofilaments from the
            individual subunits NEFH and NEFL. Positively regulates lysosome
            peripheral distribution and ruffled border formation in osteoclasts
            (By similarity). Plays a role, together with DISC1, in the
            regulation of neurite outgrowth. {ECO:0000250,
            ECO:0000250|UniProtKB:Q9ERR1, ECO:0000269|PubMed:17035248}.
            [SUBUNIT] Self-associates. Interacts with dynactin, tubulin gamma,
            KATNA1, KATNB1, microtubules, PCM1, PCNT, and YWHAE. Interacts
            directly with NEFL and indirectly with NEFH. Interacts (via
            C-terminus) with CENPF. Interacts with DISC1, dynein and PAFAH1B1.
            Interacts with ZNF365. Interacts with PLEKHM1 (via N- and
            C-terminus). {ECO:0000250, ECO:0000250|UniProtKB:Q9ERR1}.
            [SUBCELLULAR LOCATION] Cytoplasm, cytoskeleton. Cytoplasm,
            cytoskeleton, microtubule organizing center, centrosome.
            Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton,
            spindle. Note=Localizes to the mitotic spindle and to the
            microtubules of the manchette in elongated spermatids (By
            similarity). Localizes to the interphase centrosome. Localizes to
            the cell body of the motor neurons and colocalizes with assembled
            neurofilaments within axonal processes. Colocalizes with DISC1 in
            the perinuclear region, including the centrosome. {ECO:0000250}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=2; Name=1; IsoId=Q78PB6-1; Sequence=Displayed; Name=2;
            IsoId=Q78PB6-2; Sequence=VSP_019312, VSP_019313.
            [INDUCTION] Up-regulated during neurite outgrowth upon
            differentiation with NGF. {ECO:0000269|PubMed:17035248}.
            [PTM] Phosphorylated in mitosis. Can be phosphorylated by CDK1,
            CDK5 and MAPK1. Phosphorylation by CDK5 promotes interaction with
            KATNA1 and YWHAE (By similarity). {ECO:0000250}.
            [PTM] Palmitoylation at Cys-273 reduces affinity for dynein.
            {ECO:0000250}.
            [SIMILARITY] Belongs to the nudE family. {ECO:0000305}.
            [CAUTION] Was originally thought to function as an oligopeptidase
            (NUDEL-oligopeptidase or endooligopeptidase A) which could regulate
            peptide levels relevant to brain function.
            {ECO:0000305|PubMed:15728732}.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
     gene            1..345
                     /gene="Ndel1"
                     /gene_synonym="Nude2"
                     /gene_synonym="Nudel"
     Protein         1..345
                     /product="Nuclear distribution protein nudE-like 1"
                     /note="Protein Nudel"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..345
                     /region_name="Mature chain"
                     /note="Nuclear distribution protein nudE-like 1.
                     /id=PRO_0000240215."
     Region          12..164
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:2V71."
     Region          <27..>195
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          28..190
                     /region_name="Coiled-coil region"
                     /note="/evidence=ECO:0000255."
     Region          42
                     /region_name="Conflict"
                     /note="E -> Q (in Ref. 2; AAH70909).
                     /evidence=ECO:0000305."
     Region          56..166
                     /region_name="Region of interest in the sequence"
                     /note="Self-association. /evidence=ECO:0000250."
     Region          64..189
                     /region_name="Region of interest in the sequence"
                     /note="Interaction with KATNB1. /evidence=ECO:0000250."
     Region          114..133
                     /region_name="Region of interest in the sequence"
                     /note="Required for interaction with PAFAH1B1.
                     /evidence=ECO:0000250."
     Region          135..309
                     /region_name="NUDE_C"
                     /note="NUDE protein, C-terminal conserved region;
                     pfam04880"
                     /db_xref="CDD:461464"
     Region          175..345
                     /region_name="Region of interest in the sequence"
                     /note="Interaction with CENPF. /evidence=ECO:0000250."
     Region          189..256
                     /region_name="Region of interest in the sequence"
                     /note="Interaction with YWHAE. /evidence=ECO:0000250."
     Region          191..345
                     /region_name="Region of interest in the sequence"
                     /note="Interaction with NEFL. /evidence=ECO:0000250."
     Region          195..256
                     /region_name="Region of interest in the sequence"
                     /note="Interaction with KATNA1. /evidence=ECO:0000250."
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9GZM8."
     Region          217..240
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphothreonine; by CDK1 and MAPK1.
                     /evidence=ECO:0000250|UniProtKB:Q9GZM8."
     Region          227..278
                     /region_name="Region of interest in the sequence"
                     /note="Interaction with DISC1. /evidence=ECO:0000250."
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9GZM8."
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine; by CDK1.
                     /evidence=ECO:0000250|UniProtKB:Q9GZM8."
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphothreonine; by CDK1 and MAPK1.
                     /evidence=ECO:0000250|UniProtKB:Q9GZM8."
     Region          256..291
                     /region_name="Region of interest in the sequence"
                     /note="Required for localization to the centrosome and
                     interaction with dynein, dynactin, tubulin gamma, PCM1 and
                     PCNT. /evidence=ECO:0000250."
     Site            273
                     /site_type="lipid-binding"
                     /note="S-palmitoyl cysteine; by ZDHHC2, ZDHHC3 and ZDHHC7.
                     /evidence=ECO:0000250."
     Region          314..345
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          316..328
                     /region_name="Splicing variant"
                     /note="AVNGFDPAPPPPG -> QEKVIFPTLFMGQ (in isoform 2).
                     /evidence=ECO:0000303|PubMed:15489334. /id=VSP_019312."
     Region          329..345
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 2).
                     /evidence=ECO:0000303|PubMed:15489334. /id=VSP_019313."
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903."
ORIGIN      
        1 mdgedipdfs slkeetaywk elslkykqsf qeardelvef qegsreleae leaqlvqaeq
       61 rnrdlqadnq rlkyevealk eklehqyaqs ykqvsvledd lsqtraikeq lhkyvreleq
      121 anddlerakr ativsledfe qrlnqaiern afleseldek esllvsvqrl kdeardlrqe
      181 lavrerqqev trksapsspt ldcekmdsav qaslslpatp vgkgtensfp spkaipngfg
      241 tspltpsari salnivgdll rkvgaleskl aacrnfakdq asrksyvpgs vncgvmnsng
      301 pecprsgrat ffhkgavngf dpappppglg ssrpssapgm lplsv
//
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