Q9QZS3 (NUMB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein numb homolog
Short name=m-Nb
Short name=m-Numb

Gene names

Name:

Numb

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	653 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in the process of neurogenesis. Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate. Not required for the proliferation of neural progenitor cells before the onset of neurogenesis. Also involved postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity. May also mediate local repair of brain ventricular wall damage. Ref.6 Ref.8 Ref.9 Ref.10
Subunit structure	May interact with DUOXA1 By similarity. Interacts with TFAP2B By similarity. Interacts with CDH1, EPS15, LNX and NOTCH1. Interacts with RALBP1 in a complex also containing EPN1 and TFAP2A during interphase and mitosis. Ref.5 Ref.10
Subcellular location	Membrane; Peripheral membrane protein.
Tissue specificity	Expressed in subventricular zone (SVZ) neuroprogenitors and ependymal cells. Ref.10
Developmental stage	Expressed in neural progenitors and neuron cells throughout the developing nervous system. Expressed in somites and throughout the neural tube from 8.5 dpc, onward. Ref.6 Ref.8 Ref.9
Post-translational modification	Phosphorylated on Ser-276 and Ser-295 by CaMK1 By similarity. Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation By similarity Isoform 1 and isoform 2 are ubiquitinated by LNX leading to their subsequent proteasomal degradation. Ref.7
Disruption phenotype	Exhibit severe defects in cranial neuronal tube closure and die around 11.5 dpc, but neurogenesis abnormalities are limited. Mice lacking both Numb and Numbl genes die around 9.5 dpc, with severe defects in somite and vasculature formation, neuronal tube closure and axial turning. Conditional mutants, with expression abrogated in neural progenitor cells from 8.5 dpc are viable, fertile and exhibit no obvious phenotypes. Conditional double-knockout (cdKO) mutants (Numb and Numbl genes), with expression abrogated in neural progenitor cells from 8.5 dpc (just before the onset of neurogenesis), display a loss of neuronal progenitor cells formation and an overexpression of neurons as neurogenesis progresses; cdKO mutants become necrotic at 12.5 dpc and die around this stage. Conditional double-knockout (cdKO) mutants (Numb and Numbl genes), with expression abrogated in neural progenitor cells from 10.5 dpc (just after the onset of neurogenesis), display a premature depletion of neural progenitor cells in the dorsal forebrain ventrical zone of the neocortex and in the hippocampal CA fields as neurogenesis progresses; cdKO mutants are viable and fertile, but showed a reduction in the thickness of the neocortex and the hippocampus and a enlargement of the lateral ventricles. Tamoxifene-inducible double-knockout (cdKO) mutants (Numb and Numbl genes), with expression abrogated postnatally in the subventricular zone (SVZ) neuroprogenitors and in ependymal cells, display a loss of SVZ neuroblasts and show a disorganized ependyma lacking both interdigitation junction between neighboring cells and increasing number of separated cells. Ref.6 Ref.8 Ref.9 Ref.10
Sequence similarities	Contains 1 PID domain.

Ontologies

Keywords
Biological process	Neurogenesis
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Molecular function	Developmental protein
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adherens junction organization Inferred from genetic interaction PubMed 17589506. Source: MGI axonogenesis Inferred from direct assay PubMed 15598981. Source: MGI lateral ventricle development Inferred from mutant phenotype Ref.10. Source: UniProtKB lung epithelial cell differentiation Inferred from mutant phenotype PubMed 21385765. Source: MGI negative regulation of Notch signaling pathway Inferred from mutant phenotype PubMed 21385765. Source: MGI neuroblast division in subventricular zone Inferred from mutant phenotype Ref.10. Source: UniProtKB positive regulation of neurogenesis Inferred from mutant phenotype Ref.8. Source: UniProtKB positive regulation of polarized epithelial cell differentiation Inferred from mutant phenotype PubMed 21385765. Source: MGI
Cellular_component	apical part of cell Inferred from direct assay PubMed 12361975PubMed 21385765. Source: MGI basolateral plasma membrane Inferred from direct assay PubMed 17589506. Source: MGI early endosome Inferred from direct assay Ref.7. Source: MGI extrinsic to plasma membrane Inferred from direct assay PubMed 10551807. Source: MGI nucleus Inferred from direct assay PubMed 10551807. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GLI1	P08151	4	EBI-3896014,EBI-308084	From a different organism.
ITCH	Q96J02	2	EBI-3896014,EBI-1564678	From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9QZS3-1)

Also known as: p72; 72 kDa;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9QZS3-2)

Also known as: p66; 66 kDa;

The sequence of this isoform differs from the canonical sequence as follows:
     367-415: Missing.

Isoform 3 (identifier: Q9QZS3-3)

Also known as: p71; 71 kDa;

The sequence of this isoform differs from the canonical sequence as follows:
     68-78: Missing.

Isoform 4 (identifier: Q9QZS3-4)

Also known as: p65; 65 kDa;

The sequence of this isoform differs from the canonical sequence as follows:
     68-78: Missing.
     367-415: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 653

653

Protein numb homolog

PRO_0000058002

Regions

Domain

33 – 193

161

PID

Amino acid modifications

Modified residue

244

1

Phosphoserine By similarity

Modified residue

276

1

Phosphoserine; by CaMK1 By similarity

Modified residue

295

1

Phosphoserine; by CaMK1 By similarity

Modified residue

633

1

Phosphothreonine Ref.11

Modified residue

636

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

68 – 78

11

Missing in isoform 3 and isoform 4.

VSP_004350

Alternative sequence

367 – 415

49

Missing in isoform 2 and isoform 4.

VSP_004351

Experimental info

Sequence conflict

225

1

V → A in AAH33459. Ref.4

Sequence conflict

362

1

S → C in BAB23367. Ref.3

Secondary structure

1

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653

Helix Strand Turn

Details...

Helix

26 – 31

6

Turn

32 – 35

4

Beta strand

38 – 48

11

Beta strand

50 – 52

3

Helix

55 – 67

13

Beta strand

84 – 91

8

Beta strand

94 – 98

5

Turn

100 – 102

3

Beta strand

105 – 107

3

Turn

111 – 113

3

Beta strand

116 – 118

3

Beta strand

121 – 132

12

Beta strand

134 – 149

16

Helix

151 – 169

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (p72) (72 kDa) [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 6A2B69AA54B9A928	FASTA	653	70,813
	10 20 30 40 50 60 MNKLRQSFRR KKDVYVPEAS RPHQWQTDEE GVRTGKCSFP VKYLGHVEVD ESRGMHICED 70 80 90 100 110 120 AVKRLKAERK FFKGFFGKTG KKAVKAVLWV SADGLRVVDE KTKDLIVDQT IEKVSFCAPD 130 140 150 160 170 180 RNFDRAFSYI CRDGTTRRWI CHCFMAVKDT GERLSHAVGC AFAACLERKQ KREKECGVTA 190 200 210 220 230 240 TFDASRTTFT REGSFRVTTA TEQAEREEIM KQLQDAKKAE TDKTVVGPSV APGNTAPSPS 250 260 270 280 290 300 SPTSPTPDGT ASSEMNNPHA IPRRHAPIEQ LARQGSFRGF PALSQKMSPF KRQLSLRINE 310 320 330 340 350 360 LPSTMQRKTD FPIKNTVPEV EGEAESISSL CSQITSAFST PSEDPFSSAP MTKPVTLVAP 370 380 390 400 410 420 QSPVLQANGT DSASHVLTAK PANTALAHVA MPVRETNPWA HVPDAANKEI AAIHPGTEWG 430 440 450 460 470 480 QSSGAASPGL FQAGHRRTPS EADRWLEEVS KSVRAQQPQV SAAPLQPVLQ PPPPAAIAPP 490 500 510 520 530 540 APPFQGHAFL TSQPVPVGVV PPLQPAFVPT QSYPVANGMP YPASNVPVVG ITPSQMVANV 550 560 570 580 590 600 FGTAGHPQTT HPHQSPSLAK QQTFPQYETS SATTSPFFKP PAQHLNGSAA FNGVDNGGLA 610 620 630 640 650 SGNRHAEVPP GTCPVDPFEA QWAALESKSK QRTNPSPTNP FSSDLQKTFE IEL
	Isoform 2 (p66) (66 kDa) [UniParc]. Checksum: 709C36BE4DEF6AE0	FASTA	604	65,766
	10 20 30 40 50 60 MNKLRQSFRR KKDVYVPEAS RPHQWQTDEE GVRTGKCSFP VKYLGHVEVD ESRGMHICED 70 80 90 100 110 120 AVKRLKAERK FFKGFFGKTG KKAVKAVLWV SADGLRVVDE KTKDLIVDQT IEKVSFCAPD 130 140 150 160 170 180 RNFDRAFSYI CRDGTTRRWI CHCFMAVKDT GERLSHAVGC AFAACLERKQ KREKECGVTA 190 200 210 220 230 240 TFDASRTTFT REGSFRVTTA TEQAEREEIM KQLQDAKKAE TDKTVVGPSV APGNTAPSPS 250 260 270 280 290 300 SPTSPTPDGT ASSEMNNPHA IPRRHAPIEQ LARQGSFRGF PALSQKMSPF KRQLSLRINE 310 320 330 340 350 360 LPSTMQRKTD FPIKNTVPEV EGEAESISSL CSQITSAFST PSEDPFSSAP MTKPVTLVAP 370 380 390 400 410 420 QSPVLQGTEW GQSSGAASPG LFQAGHRRTP SEADRWLEEV SKSVRAQQPQ VSAAPLQPVL 430 440 450 460 470 480 QPPPPAAIAP PAPPFQGHAF LTSQPVPVGV VPPLQPAFVP TQSYPVANGM PYPASNVPVV 490 500 510 520 530 540 GITPSQMVAN VFGTAGHPQT THPHQSPSLA KQQTFPQYET SSATTSPFFK PPAQHLNGSA 550 560 570 580 590 600 AFNGVDNGGL ASGNRHAEVP PGTCPVDPFE AQWAALESKS KQRTNPSPTN PFSSDLQKTF EIEL
	Isoform 3 (p71) (71 kDa) [UniParc]. Checksum: 2419437F0400E691	FASTA	642	69,440
	10 20 30 40 50 60 MNKLRQSFRR KKDVYVPEAS RPHQWQTDEE GVRTGKCSFP VKYLGHVEVD ESRGMHICED 70 80 90 100 110 120 AVKRLKATGK KAVKAVLWVS ADGLRVVDEK TKDLIVDQTI EKVSFCAPDR NFDRAFSYIC 130 140 150 160 170 180 RDGTTRRWIC HCFMAVKDTG ERLSHAVGCA FAACLERKQK REKECGVTAT FDASRTTFTR 190 200 210 220 230 240 EGSFRVTTAT EQAEREEIMK QLQDAKKAET DKTVVGPSVA PGNTAPSPSS PTSPTPDGTA 250 260 270 280 290 300 SSEMNNPHAI PRRHAPIEQL ARQGSFRGFP ALSQKMSPFK RQLSLRINEL PSTMQRKTDF 310 320 330 340 350 360 PIKNTVPEVE GEAESISSLC SQITSAFSTP SEDPFSSAPM TKPVTLVAPQ SPVLQANGTD 370 380 390 400 410 420 SASHVLTAKP ANTALAHVAM PVRETNPWAH VPDAANKEIA AIHPGTEWGQ SSGAASPGLF 430 440 450 460 470 480 QAGHRRTPSE ADRWLEEVSK SVRAQQPQVS AAPLQPVLQP PPPAAIAPPA PPFQGHAFLT 490 500 510 520 530 540 SQPVPVGVVP PLQPAFVPTQ SYPVANGMPY PASNVPVVGI TPSQMVANVF GTAGHPQTTH 550 560 570 580 590 600 PHQSPSLAKQ QTFPQYETSS ATTSPFFKPP AQHLNGSAAF NGVDNGGLAS GNRHAEVPPG 610 620 630 640 TCPVDPFEAQ WAALESKSKQ RTNPSPTNPF SSDLQKTFEI EL
	Isoform 4 (p65) (65 kDa) [UniParc]. Checksum: 6DFF734800C4D49C	FASTA	593	64,394
	10 20 30 40 50 60 MNKLRQSFRR KKDVYVPEAS RPHQWQTDEE GVRTGKCSFP VKYLGHVEVD ESRGMHICED 70 80 90 100 110 120 AVKRLKATGK KAVKAVLWVS ADGLRVVDEK TKDLIVDQTI EKVSFCAPDR NFDRAFSYIC 130 140 150 160 170 180 RDGTTRRWIC HCFMAVKDTG ERLSHAVGCA FAACLERKQK REKECGVTAT FDASRTTFTR 190 200 210 220 230 240 EGSFRVTTAT EQAEREEIMK QLQDAKKAET DKTVVGPSVA PGNTAPSPSS PTSPTPDGTA 250 260 270 280 290 300 SSEMNNPHAI PRRHAPIEQL ARQGSFRGFP ALSQKMSPFK RQLSLRINEL PSTMQRKTDF 310 320 330 340 350 360 PIKNTVPEVE GEAESISSLC SQITSAFSTP SEDPFSSAPM TKPVTLVAPQ SPVLQGTEWG 370 380 390 400 410 420 QSSGAASPGL FQAGHRRTPS EADRWLEEVS KSVRAQQPQV SAAPLQPVLQ PPPPAAIAPP 430 440 450 460 470 480 APPFQGHAFL TSQPVPVGVV PPLQPAFVPT QSYPVANGMP YPASNVPVVG ITPSQMVANV 490 500 510 520 530 540 FGTAGHPQTT HPHQSPSLAK QQTFPQYETS SATTSPFFKP PAQHLNGSAA FNGVDNGGLA 550 560 570 580 590 SGNRHAEVPP GTCPVDPFEA QWAALESKSK QRTNPSPTNP FSSDLQKTFE IEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Asymmetric localization of a mammalian numb homolog during mouse cortical neurogenesis." Zhong W., Feder J.N., Jiang M.-M., Jan L.Y., Jan Y.N. Neuron 17:43-53(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[2]	"Characterization of four mammalian Numb protein isoforms: Identification of cytoplasmic and membrane-associated variants of the phosphotyrosine binding domain." Dho S.E., French M.B., Woods S.A., McGlade C.J. J. Biol. Chem. 274:33097-33104(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Strain: C57BL/6J. Tissue: Lung.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Strain: Czech II. Tissue: Lung.
[5]	"The mammalian numb phosphotyrosine-binding domain. Characterization of binding specificity and identification of a novel PDZ domain-containing numb binding protein, LNX." Dho S.E., Jacob S., Wolting C.D., French M.B., Rohrschneider L.R., McGlade C.J. J. Biol. Chem. 273:9179-9187(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LNX.
[6]	"Mouse numb is an essential gene involved in cortical neurogenesis." Zhong W., Jiang M.M., Schonemann M.D., Meneses J.J., Pedersen R.A., Jan L.Y., Jan Y.N. Proc. Natl. Acad. Sci. U.S.A. 97:6844-6849(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
[7]	"LNX functions as a RING type E3 ubiquitin ligase that targets the cell fate determinant Numb for ubiquitin-dependent degradation." Nie J., McGill M.A., Dermer M., Dho S.E., Wolting C.D., McGlade C.J. EMBO J. 21:93-102(2002) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION BY LNX.
[8]	"Progenitor cell maintenance requires numb and numblike during mouse neurogenesis." Petersen P.H., Zou K., Hwang J.K., Jan Y.N., Zhong W. Nature 419:929-934(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
[9]	"Continuing role for mouse Numb and Numbl in maintaining progenitor cells during cortical neurogenesis." Petersen P.H., Zou K., Krauss S., Zhong W. Nat. Neurosci. 7:803-811(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
[10]	"Postnatal deletion of Numb/Numblike reveals repair and remodeling capacity in the subventricular neurogenic niche." Kuo C.T., Mirzadeh Z., Soriano-Navarro M., Rasin M., Wang D., Shen J., Sestan N., Garcia-Verdugo J., Alvarez-Buylla A., Jan L.Y., Jan Y.N. Cell 127:1253-1264(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CDH1, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[11]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-633 AND SER-636, MASS SPECTROMETRY. Tissue: Liver.
[12]	"Solution structure of phosphotyrosine interaction domain of mouse NUMB protein." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 19-172.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF169191 mRNA. Translation: AAD47834.1.
AF169192 mRNA. Translation: AAD47835.1.
AF170709 mRNA. Translation: AAD47836.1.
AK004553 mRNA. Translation: BAB23367.1.
BC033459 mRNA. Translation: AAH33459.1.
U70674 mRNA. Translation: AAB09586.1.

IPI

IPI00137943.
IPI00221542.
IPI00221544.
IPI00221545.

RefSeq

NP_001129547.1. NM_001136075.2.
NP_001258984.1. NM_001272055.1.
NP_001258985.1. NM_001272056.1.
NP_035079.1. NM_010949.2.

UniGene

Mm.4390.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WJ1	NMR	-	A	19-172	[»]

ProteinModelPortal

Q9QZS3.

SMR

Q9QZS3. Positions 21-172.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9QZS3. 2 interactions.

MINT

MINT-237633.

PTM databases

PhosphoSite

Q9QZS3.

Proteomic databases

PaxDb

Q9QZS3.

PRIDE

Q9QZS3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000021647; ENSMUSP00000021647; ENSMUSG00000021224.
ENSMUST00000117217; ENSMUSP00000113591; ENSMUSG00000021224.
ENSMUST00000129335; ENSMUSP00000119303; ENSMUSG00000021224.
ENSMUST00000154043; ENSMUSP00000117899; ENSMUSG00000021224.

GeneID

18222.

KEGG

mmu:18222.

UCSC

uc007odu.1. mouse.
uc007odv.1. mouse.
uc007odw.1. mouse.
uc007ody.1. mouse.

Organism-specific databases

CTD

8650.

MGI

MGI:107423. Numb.

Phylogenomic databases

eggNOG

NOG331167.

GeneTree

ENSGT00530000062937.

HOGENOM

HOG000220819.

HOVERGEN

HBG006672.

InParanoid

Q9QZS3.

KO

K06057.

OMA

FPIKNAV.

Enzyme and pathway databases

Reactome

REACT_115202. Signal Transduction.

Gene expression databases

ArrayExpress

Q9QZS3.

Bgee

Q9QZS3.

CleanEx

MM_NUMB.

Genevestigator

Q9QZS3.

GermOnline

ENSMUSG00000021224. Mus musculus.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR016698. Numb/numb-like.
IPR010449. Numb_domain.
IPR011993. PH_like_dom.
IPR006020. PTyr_interaction_dom.
[Graphical view]

Pfam

PF06311. NumbF. 1 hit.
PF00640. PID. 1 hit.
[Graphical view]

PIRSF

PIRSF017607. Numb/numb-like. 1 hit.

SMART

SM00462. PTB. 1 hit.
[Graphical view]

PROSITE

PS01179. PID. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9QZS3.

NextBio

293644.

SOURCE

Search...

Entry information

Entry name

NUMB_MOUSE

Accession

Primary (citable) accession number: Q9QZS3
Secondary accession number(s): P70422 , Q8CIB1, Q9DC57, Q9QZR1, Q9QZS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	May 1, 2000
Last modified:	April 3, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program