Numb-like protein - Homo sapiens (Human)

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Q9Y6R0 (NUMBL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Numb-like protein

Alternative name(s):
Numb-related protein
Short name=Numb-R

Gene names

Name:

NUMBL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	609 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 embryonic neurogenesis. Also required postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity. Negative regulator of NF-kappa-B signaling pathway. The inhibition of NF-kappa-B activation is mediated at least in part, by preventing MAP3K7IP2 to interact with polyubiquitin chains of TRAF6 and RIPK1 and by stimulating the 'Lys-48'-linked polyubiquitination and degradation of TRAF6 in cortical neurons. Ref.5 Ref.7
Subunit structure	Interacts (via PTB domain) with MAP3K7IP2 (via C-terminal). Interacts (via C-terminal) with TRAF6 (via TRAF domains). Associates with EPS15 and NOTCH1. Ref.5 Ref.7
Subcellular location	Cytoplasm By similarity. Note: Symmetrically distributed throughout the cytoplasm in non dividing neuroblasts of the CNS By similarity. Ref.5
Domain	The PTB domain is necessary for the inhibition of MAP3K7IP2-mediated activation of NF-kappa-B.
Sequence similarities	Contains 1 PID domain.

Ontologies

Keywords
Biological process	Neurogenesis Ubl conjugation pathway
Cellular component	Cytoplasm
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytokine-mediated signaling pathway Inferred from direct assay Ref.5. Source: UniProtKB lateral ventricle development Inferred from sequence or structural similarity. Source: UniProtKB neuroblast division in subventricular zone Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of neurogenesis Inferred from sequence or structural similarity. Source: UniProtKB protein metabolic process Inferred from direct assay Ref.7. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RBFOX1	Q9NWB1	2	EBI-945925,EBI-945906

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 609

609

Numb-like protein

PRO_0000057999

Regions

Domain

74 – 223

150

PID

Compositional bias

427 – 446

Poly-Gln

Amino acid modifications

Modified residue

263

Phosphoserine By similarity

Modified residue

279

Phosphothreonine Ref.6

Secondary structure

609

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9Y6R0 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 69458D161B60F4B4
Show »

FASTA

609

64,891

        10         20         30         40         50         60 
MSRSAAASGG PRRPERHLPP APCGAPGPPE TCRTEPDGAG TMNKLRQSLR RRKPAYVPEA 

        70         80         90        100        110        120 
SRPHQWQADE DAVRKGTCSF PVRYLGHVEV EESRGMHVCE DAVKKLKAMG RKSVKSVLWV 

       130        140        150        160        170        180 
SADGLRVVDD KTKDLLVDQT IEKVSFCAPD RNLDKAFSYI CRDGTTRRWI CHCFLALKDS 

       190        200        210        220        230        240 
GERLSHAVGC AFAACLERKQ RREKECGVTA AFDASRTSFA REGSFRLSGG GRPAEREAPD 

       250        260        270        280        290        300 
KKKAEAAAAP TVAPGPAQPG HVSPTPATTS PGEKGEAGTP VAAGTTAAAI PRRHAPLEQL 

       310        320        330        340        350        360 
VRQGSFRGFP ALSQKNSPFK RQLSLRLNEL PSTLQRRTDF QVKGTVPEME PPGAGDSDSI 

       370        380        390        400        410        420 
NALCTQISSS FASAGAPAPG PPPATTGTSA WGEPSVPPAA AFQPGHKRTP SEAERWLEEV 

       430        440        450        460        470        480 
SQVAKAQQQQ QQQQQQQQQQ QQQQQQAASV APVPTMPPAL QPFPAPVGPF DAAPAQVAVF 

       490        500        510        520        530        540 
LPPPHMQPPF VPAYPGLGYP PMPRVPVVGI TPSQMVANAF CSAAQLQPQP ATLLGKAGAF 

       550        560        570        580        590        600 
PPPAIPSAPG SQARPRPNGA PWPPEPAPAP APELDPFEAQ WAALEGKATV EKPSNPFSGD 


LQKTFEIEL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Binding specificity and in vivo targets of the EH domain, a novel protein-protein interaction module." Salcini A.E., Confalonieri S., Doria M., Santolini E., Tassi E., Minenkova O., Cesareni G., Pelicci P.G., Di Fiore P.P. Genes Dev. 11:2239-2249(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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] OF 9-609. Tissue: Eye.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 42-609.
[4]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[5]	"NUMBL interacts with TAB2 and inhibits TNFalpha and IL-1beta-induced NF-kappaB activation." Ma Q., Zhou L., Shi H., Huo K. Cell. Signal. 20:1044-1051(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MAP3K7IP2, SUBCELLULAR LOCATION.
[6]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-279, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"NUMBL interacts with TRAF6 and promotes the degradation of TRAF6." Zhou L., Ma Q., Shi H., Huo K. Biochem. Biophys. Res. Commun. 392:409-414(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TRAF6.
[8]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[9]	"Human numb-like protein, phosphotyrosine interaction domain." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 60-204.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF015041 mRNA. Translation: AAD01549.1.
BC001794 mRNA. No translation available.
BT009807 mRNA. Translation: AAP88809.1.

IPI

IPI00002560.

RefSeq

NP_004747.1. NM_004756.3.

UniGene

Hs.326953.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3F0W	X-ray	2.70	A	60-204	[»]

ProteinModelPortal

Q9Y6R0.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y6R0. 17 interactions.

MINT

MINT-1497553.

STRING

9606.ENSP00000252891.

PTM databases

PhosphoSite

Q9Y6R0.

Polymorphism databases

DMDM

14194976.

Proteomic databases

PaxDb

Q9Y6R0.

PRIDE

Q9Y6R0.

Protocols and materials databases

DNASU

9253.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000252891; ENSP00000252891; ENSG00000105245.
ENST00000540131; ENSP00000442759; ENSG00000105245.
ENST00000598779; ENSP00000472400; ENSG00000105245.

GeneID

9253.

KEGG

hsa:9253.

UCSC

uc002oon.3. human.

Organism-specific databases

CTD

9253.

GeneCards

GC19M041171.

HGNC

HGNC:8061. NUMBL.

MIM

604018. gene.

neXtProt

NX_Q9Y6R0.

PharmGKB

PA31846.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG331167.

HOGENOM

HOG000220819.

HOVERGEN

HBG006672.

InParanoid

Q9Y6R0.

K06057.

OMA

PAPCGAP.

OrthoDB

EOG4DR9D8.

PhylomeDB

Q9Y6R0.

Gene expression databases

ArrayExpress

Q9Y6R0.

Bgee

Q9Y6R0.

CleanEx

HS_NUMBL.

Genevestigator

Q9Y6R0.

GermOnline

ENSG00000105245. Homo sapiens.

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

ChiTaRS

NUMBL. human.

EvolutionaryTrace

Q9Y6R0.

GenomeRNAi

9253.

NextBio

34685.

SOURCE

Search...

Entry information

Entry name

NUMBL_HUMAN

Accession

Primary (citable) accession number: Q9Y6R0
Secondary accession number(s): Q7Z4J9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents