NUMB_MOUSE
ID NUMB_MOUSE Reviewed; 653 AA.
AC Q9QZS3; P70422; Q8CIB1; Q9DC57; Q9QZR1; Q9QZS4;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Protein numb homolog;
DE Short=m-Nb;
DE Short=m-Numb;
GN Name=Numb;
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 4).
RX PubMed=8755477; DOI=10.1016/s0896-6273(00)80279-2;
RA Zhong W., Feder J.N., Jiang M.-M., Jan L.Y., Jan Y.N.;
RT "Asymmetric localization of a mammalian numb homolog during mouse cortical
RT neurogenesis.";
RL Neuron 17:43-53(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RX PubMed=10551880; DOI=10.1074/jbc.274.46.33097;
RA Dho S.E., French M.B., Woods S.A., McGlade C.J.;
RT "Characterization of four mammalian Numb protein isoforms: Identification
RT of cytoplasmic and membrane-associated variants of the phosphotyrosine
RT binding domain.";
RL J. Biol. Chem. 274:33097-33104(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=Czech II; TISSUE=Lung;
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 INTERACTION WITH LNX.
RX PubMed=9535908; DOI=10.1074/jbc.273.15.9179;
RA Dho S.E., Jacob S., Wolting C.D., French M.B., Rohrschneider L.R.,
RA McGlade C.J.;
RT "The mammalian numb phosphotyrosine-binding domain. Characterization of
RT binding specificity and identification of a novel PDZ domain-containing
RT numb binding protein, LNX.";
RL J. Biol. Chem. 273:9179-9187(1998).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=10841580; DOI=10.1073/pnas.97.12.6844;
RA Zhong W., Jiang M.M., Schonemann M.D., Meneses J.J., Pedersen R.A.,
RA Jan L.Y., Jan Y.N.;
RT "Mouse numb is an essential gene involved in cortical neurogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:6844-6849(2000).
RN [7]
RP UBIQUITINATION BY LNX.
RX PubMed=11782429; DOI=10.1093/emboj/21.1.93;
RA Nie J., McGill M.A., Dermer M., Dho S.E., Wolting C.D., McGlade C.J.;
RT "LNX functions as a RING type E3 ubiquitin ligase that targets the cell
RT fate determinant Numb for ubiquitin-dependent degradation.";
RL EMBO J. 21:93-102(2002).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=12410312; DOI=10.1038/nature01124;
RA Petersen P.H., Zou K., Hwang J.K., Jan Y.N., Zhong W.;
RT "Progenitor cell maintenance requires numb and numblike during mouse
RT neurogenesis.";
RL Nature 419:929-934(2002).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=15273690; DOI=10.1038/nn1289;
RA Petersen P.H., Zou K., Krauss S., Zhong W.;
RT "Continuing role for mouse Numb and Numbl in maintaining progenitor cells
RT during cortical neurogenesis.";
RL Nat. Neurosci. 7:803-811(2004).
RN [10]
RP FUNCTION, INTERACTION WITH CDH1, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=17174898; DOI=10.1016/j.cell.2006.10.041;
RA Kuo C.T., Mirzadeh Z., Soriano-Navarro M., Rasin M., Wang D., Shen J.,
RA Sestan N., Garcia-Verdugo J., Alvarez-Buylla A., Jan L.Y., Jan Y.N.;
RT "Postnatal deletion of Numb/Numblike reveals repair and remodeling capacity
RT in the subventricular neurogenic niche.";
RL Cell 127:1253-1264(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-243 AND SER-244, AND
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, 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 [14]
RP STRUCTURE BY NMR OF 19-172.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of phosphotyrosine interaction domain of mouse NUMB
RT protein.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Regulates clathrin-mediated receptor endocytosis (By
CC similarity). Plays a role in the process of neurogenesis
CC (PubMed:10841580, PubMed:12410312, PubMed:15273690, PubMed:17174898).
CC Required throughout embryonic neurogenesis to maintain neural
CC progenitor cells, also called radial glial cells (RGCs), by allowing
CC their daughter cells to choose progenitor over neuronal cell fate
CC (PubMed:15273690, PubMed:12410312). Not required for the proliferation
CC of neural progenitor cells before the onset of neurogenesis
CC (PubMed:15273690, PubMed:12410312). Also involved postnatally in the
CC subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts
CC survival and ependymal wall integrity (PubMed:17174898). May also
CC mediate local repair of brain ventricular wall damage
CC (PubMed:17174898). {ECO:0000250|UniProtKB:P49757,
CC ECO:0000269|PubMed:10841580, ECO:0000269|PubMed:12410312,
CC ECO:0000269|PubMed:15273690, ECO:0000269|PubMed:17174898}.
CC -!- SUBUNIT: Interacts with SIAH1 (By similarity). Interacts with LNX
CC (PubMed:9535908). Interacts with CDH1 (PubMed:17174898). Interacts with
CC TFAP2A and TFAP2B (By similarity). Interacts with RALBP1 in a complex
CC also containing EPN1 and TFAP2A during interphase and mitosis (By
CC similarity). Interacts with AAK1 (By similarity). May interact with
CC DUOXA1 (By similarity). {ECO:0000250|UniProtKB:P49757,
CC ECO:0000269|PubMed:17174898, ECO:0000269|PubMed:9535908}.
CC -!- INTERACTION:
CC Q9QZS3-1; P42566: EPS15; Xeno; NbExp=3; IntAct=EBI-9547433, EBI-396684;
CC Q9QZS3-1; Q96D71: REPS1; Xeno; NbExp=3; IntAct=EBI-9547433, EBI-1171195;
CC Q9QZS3-2; P42566: EPS15; Xeno; NbExp=3; IntAct=EBI-3896014, EBI-396684;
CC Q9QZS3-2; P08151: GLI1; Xeno; NbExp=4; IntAct=EBI-3896014, EBI-308084;
CC Q9QZS3-2; Q96J02: ITCH; Xeno; NbExp=2; IntAct=EBI-3896014, EBI-1564678;
CC Q9QZS3-2; Q96D71: REPS1; Xeno; NbExp=2; IntAct=EBI-3896014, EBI-1171195;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P49757};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P49757}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P49757}. Endosome membrane
CC {ECO:0000250|UniProtKB:P49757}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P49757}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P49757}. Note=Localizes to perinuclear endosomes
CC in an AAK1-dependent manner. {ECO:0000250|UniProtKB:P49757}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=p72, 72 kDa;
CC IsoId=Q9QZS3-1; Sequence=Displayed;
CC Name=2; Synonyms=p66, 66 kDa;
CC IsoId=Q9QZS3-2; Sequence=VSP_004351;
CC Name=3; Synonyms=p71, 71 kDa;
CC IsoId=Q9QZS3-3; Sequence=VSP_004350;
CC Name=4; Synonyms=p65, 65 kDa;
CC IsoId=Q9QZS3-4; Sequence=VSP_004350, VSP_004351;
CC -!- TISSUE SPECIFICITY: Expressed in subventricular zone (SVZ)
CC neuroprogenitors and ependymal cells. {ECO:0000269|PubMed:17174898}.
CC -!- DEVELOPMENTAL STAGE: Expressed in neural progenitors and neuron cells
CC throughout the developing nervous system. Expressed in somites and
CC throughout the neural tube from 8.5 dpc, onward.
CC {ECO:0000269|PubMed:10841580, ECO:0000269|PubMed:12410312,
CC ECO:0000269|PubMed:15273690}.
CC -!- PTM: Phosphorylated on Ser-276 and Ser-295 by CaMK1. {ECO:0000250}.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent
CC proteasomal degradation (By similarity) Isoform 1 and isoform 2 are
CC ubiquitinated by LNX leading to their subsequent proteasomal
CC degradation. {ECO:0000250, ECO:0000269|PubMed:11782429}.
CC -!- DISRUPTION PHENOTYPE: Mutant animals exhibit severe defects in cranial
CC neuronal tube closure and die around 11.5 dpc, but neurogenesis
CC abnormalities are limited. Mice lacking both Numb and Numbl genes die
CC around 9.5 dpc, with severe defects in somite and vasculature
CC formation, neuronal tube closure and axial turning. Conditional
CC mutants, with expression abrogated in neural progenitor cells from 8.5
CC dpc are viable, fertile and exhibit no obvious phenotypes. Conditional
CC double-knockout (cdKO) mutants (Numb and Numbl genes), with expression
CC abrogated in neural progenitor cells from 8.5 dpc (just before the
CC onset of neurogenesis), display a loss of neuronal progenitor cells
CC formation and an overexpression of neurons as neurogenesis progresses;
CC cdKO mutants become necrotic at 12.5 dpc and die around this stage.
CC Conditional double-knockout (cdKO) mutants (Numb and Numbl genes), with
CC expression abrogated in neural progenitor cells from 10.5 dpc (just
CC after the onset of neurogenesis), display a premature depletion of
CC neural progenitor cells in the dorsal forebrain ventrical zone of the
CC neocortex and in the hippocampal CA fields as neurogenesis progresses;
CC cdKO mutants are viable and fertile, but showed a reduction in the
CC thickness of the neocortex and the hippocampus and a enlargement of the
CC lateral ventricles. Tamoxifen-inducible double-knockout (cdKO) mutants
CC (Numb and Numbl genes), with expression abrogated postnatally in the
CC subventricular zone (SVZ) neuroprogenitors and in ependymal cells,
CC display a loss of SVZ neuroblasts and show a disorganized ependyma
CC lacking both interdigitation junction between neighboring cells and
CC increasing number of separated cells. {ECO:0000269|PubMed:10841580,
CC ECO:0000269|PubMed:12410312, ECO:0000269|PubMed:15273690,
CC ECO:0000269|PubMed:17174898}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF169191; AAD47834.1; -; mRNA.
DR EMBL; AF169192; AAD47835.1; -; mRNA.
DR EMBL; AF170709; AAD47836.1; -; mRNA.
DR EMBL; AK004553; BAB23367.1; -; mRNA.
DR EMBL; BC033459; AAH33459.1; -; mRNA.
DR EMBL; U70674; AAB09586.1; -; mRNA.
DR CCDS; CCDS26032.1; -. [Q9QZS3-2]
DR CCDS; CCDS49108.1; -. [Q9QZS3-1]
DR CCDS; CCDS70400.1; -. [Q9QZS3-4]
DR CCDS; CCDS70401.1; -. [Q9QZS3-3]
DR RefSeq; NP_001129547.1; NM_001136075.2. [Q9QZS3-1]
DR RefSeq; NP_001258984.1; NM_001272055.1. [Q9QZS3-3]
DR RefSeq; NP_001258985.1; NM_001272056.1. [Q9QZS3-4]
DR RefSeq; NP_035079.1; NM_010949.2. [Q9QZS3-2]
DR RefSeq; XP_006515639.1; XM_006515576.1. [Q9QZS3-1]
DR RefSeq; XP_006515640.1; XM_006515577.2. [Q9QZS3-1]
DR RefSeq; XP_006515641.1; XM_006515578.1. [Q9QZS3-3]
DR RefSeq; XP_011242314.1; XM_011244012.2. [Q9QZS3-1]
DR PDB; 1WJ1; NMR; -; A=19-172.
DR PDB; 5YQG; X-ray; 2.10 A; E/F=271-301.
DR PDBsum; 1WJ1; -.
DR PDBsum; 5YQG; -.
DR AlphaFoldDB; Q9QZS3; -.
DR SMR; Q9QZS3; -.
DR BioGRID; 201877; 40.
DR CORUM; Q9QZS3; -.
DR IntAct; Q9QZS3; 21.
DR MINT; Q9QZS3; -.
DR STRING; 10090.ENSMUSP00000119303; -.
DR iPTMnet; Q9QZS3; -.
DR PhosphoSitePlus; Q9QZS3; -.
DR EPD; Q9QZS3; -.
DR jPOST; Q9QZS3; -.
DR MaxQB; Q9QZS3; -.
DR PaxDb; Q9QZS3; -.
DR PeptideAtlas; Q9QZS3; -.
DR PRIDE; Q9QZS3; -.
DR ProteomicsDB; 295466; -. [Q9QZS3-1]
DR ProteomicsDB; 295467; -. [Q9QZS3-2]
DR ProteomicsDB; 295468; -. [Q9QZS3-3]
DR ProteomicsDB; 295469; -. [Q9QZS3-4]
DR Antibodypedia; 131; 900 antibodies from 43 providers.
DR DNASU; 18222; -.
DR Ensembl; ENSMUST00000021647; ENSMUSP00000021647; ENSMUSG00000021224. [Q9QZS3-2]
DR Ensembl; ENSMUST00000117217; ENSMUSP00000113591; ENSMUSG00000021224. [Q9QZS3-4]
DR Ensembl; ENSMUST00000129335; ENSMUSP00000119303; ENSMUSG00000021224. [Q9QZS3-1]
DR Ensembl; ENSMUST00000154043; ENSMUSP00000117899; ENSMUSG00000021224. [Q9QZS3-3]
DR GeneID; 18222; -.
DR KEGG; mmu:18222; -.
DR UCSC; uc007odu.2; mouse. [Q9QZS3-2]
DR UCSC; uc007odv.2; mouse. [Q9QZS3-1]
DR UCSC; uc007odw.2; mouse. [Q9QZS3-3]
DR UCSC; uc007ody.2; mouse. [Q9QZS3-4]
DR CTD; 8650; -.
DR MGI; MGI:107423; Numb.
DR VEuPathDB; HostDB:ENSMUSG00000021224; -.
DR eggNOG; KOG3537; Eukaryota.
DR GeneTree; ENSGT00940000156005; -.
DR HOGENOM; CLU_031797_1_1_1; -.
DR InParanoid; Q9QZS3; -.
DR OMA; CSFPVKX; -.
DR OrthoDB; 1110016at2759; -.
DR PhylomeDB; Q9QZS3; -.
DR TreeFam; TF314159; -.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR BioGRID-ORCS; 18222; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Numb; mouse.
DR EvolutionaryTrace; Q9QZS3; -.
DR PRO; PR:Q9QZS3; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9QZS3; protein.
DR Bgee; ENSMUSG00000021224; Expressed in metanephric ureteric bud and 266 other tissues.
DR ExpressionAtlas; Q9QZS3; baseline and differential.
DR Genevisible; Q9QZS3; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0045294; F:alpha-catenin binding; IPI:MGI.
DR GO; GO:0008013; F:beta-catenin binding; IPI:MGI.
DR GO; GO:0045296; F:cadherin binding; IPI:MGI.
DR GO; GO:0034332; P:adherens junction organization; IGI:MGI.
DR GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0021670; P:lateral ventricle development; IMP:UniProtKB.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; IMP:MGI.
DR GO; GO:0021849; P:neuroblast division in subventricular zone; IMP:UniProtKB.
DR GO; GO:0007405; P:neuroblast proliferation; IGI:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IMP:UniProtKB.
DR GO; GO:0045664; P:regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR GO; GO:0099150; P:regulation of postsynaptic specialization assembly; ISO:MGI.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR016698; Numb/numb-like.
DR InterPro; IPR010449; Numb_domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR PANTHER; PTHR47368; PTHR47368; 1.
DR Pfam; PF06311; NumbF; 1.
DR Pfam; PF00640; PID; 1.
DR PIRSF; PIRSF017607; Numb/numb-like; 1.
DR SMART; SM00462; PTB; 1.
DR PROSITE; PS01179; PID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Developmental protein;
KW Endosome; Membrane; Neurogenesis; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..653
FT /note="Protein numb homolog"
FT /id="PRO_0000058002"
FT DOMAIN 33..193
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 213..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 102
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49757"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49757"
FT MOD_RES 243
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 276
FT /note="Phosphoserine; by CaMK1"
FT /evidence="ECO:0000250|UniProtKB:Q2LC84"
FT MOD_RES 295
FT /note="Phosphoserine; by CaMK1"
FT /evidence="ECO:0000250|UniProtKB:Q2LC84"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49757"
FT MOD_RES 438
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49757"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49757"
FT VAR_SEQ 68..78
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10551880,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:8755477"
FT /id="VSP_004350"
FT VAR_SEQ 367..415
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10551880,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:8755477"
FT /id="VSP_004351"
FT CONFLICT 225
FT /note="V -> A (in Ref. 4; AAH33459)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="S -> C (in Ref. 3; BAB23367)"
FT /evidence="ECO:0000305"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:1WJ1"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:1WJ1"
FT STRAND 38..48
FT /evidence="ECO:0007829|PDB:1WJ1"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1WJ1"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:1WJ1"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:1WJ1"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:1WJ1"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:1WJ1"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1WJ1"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1WJ1"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1WJ1"
FT STRAND 121..132
FT /evidence="ECO:0007829|PDB:1WJ1"
FT STRAND 134..149
FT /evidence="ECO:0007829|PDB:1WJ1"
FT HELIX 151..169
FT /evidence="ECO:0007829|PDB:1WJ1"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:5YQG"
SQ SEQUENCE 653 AA; 70813 MW; 6A2B69AA54B9A928 CRC64;
MNKLRQSFRR KKDVYVPEAS RPHQWQTDEE GVRTGKCSFP VKYLGHVEVD ESRGMHICED
AVKRLKAERK FFKGFFGKTG KKAVKAVLWV SADGLRVVDE KTKDLIVDQT IEKVSFCAPD
RNFDRAFSYI CRDGTTRRWI CHCFMAVKDT GERLSHAVGC AFAACLERKQ KREKECGVTA
TFDASRTTFT REGSFRVTTA TEQAEREEIM KQLQDAKKAE TDKTVVGPSV APGNTAPSPS
SPTSPTPDGT ASSEMNNPHA IPRRHAPIEQ LARQGSFRGF PALSQKMSPF KRQLSLRINE
LPSTMQRKTD FPIKNTVPEV EGEAESISSL CSQITSAFST PSEDPFSSAP MTKPVTLVAP
QSPVLQANGT DSASHVLTAK PANTALAHVA MPVRETNPWA HVPDAANKEI AAIHPGTEWG
QSSGAASPGL FQAGHRRTPS EADRWLEEVS KSVRAQQPQV SAAPLQPVLQ PPPPAAIAPP
APPFQGHAFL TSQPVPVGVV PPLQPAFVPT QSYPVANGMP YPASNVPVVG ITPSQMVANV
FGTAGHPQTT HPHQSPSLAK QQTFPQYETS SATTSPFFKP PAQHLNGSAA FNGVDNGGLA
SGNRHAEVPP GTCPVDPFEA QWAALESKSK QRTNPSPTNP FSSDLQKTFE IEL
