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Protein

Protein numb homolog

Gene

NUMB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Neurogenesis

Enzyme and pathway databases

ReactomeiR-HSA-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-HSA-437239. Recycling pathway of L1.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
SignaLinkiP49757.
SIGNORiP49757.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein numb homolog
Short name:
h-Numb
Alternative name(s):
Protein S171
Gene namesi
Name:NUMB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:8060. NUMB.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: Ensembl
  • basolateral plasma membrane Source: Ensembl
  • clathrin-coated vesicle Source: UniProtKB
  • early endosome Source: Ensembl
  • extrinsic component of plasma membrane Source: Ensembl
  • focal adhesion Source: UniProtKB
  • nucleus Source: Ensembl
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31845.

Polymorphism and mutation databases

BioMutaiNUMB.
DMDMi14195675.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 651651Protein numb homologPRO_0000058001Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei243 – 2431PhosphothreonineBy similarity
Modified residuei244 – 2441PhosphoserineCombined sources
Modified residuei276 – 2761Phosphoserine; by CaMK1By similarity
Modified residuei295 – 2951Phosphoserine; by CaMK1By similarity
Modified residuei438 – 4381PhosphoserineCombined sources
Modified residuei634 – 6341PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on Ser-276 and Ser-295 by CaMK1.By similarity
Isoform 1 and isoform 2 are ubiquitinated by LNX leading to their subsequent proteasomal degradation (By similarity). Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP49757.
MaxQBiP49757.
PaxDbiP49757.
PRIDEiP49757.

PTM databases

iPTMnetiP49757.
PhosphoSiteiP49757.

Expressioni

Gene expression databases

BgeeiP49757.
ExpressionAtlasiP49757. baseline and differential.
GenevisibleiP49757. HS.

Organism-specific databases

HPAiCAB011478.

Interactioni

Subunit structurei

Interacts with CDH1 and TFAP2B (By similarity). Interacts with EPS15, LNX and NOTCH1. May interact with DUOXA1. Interacts with RALBP1 in a complex also containing EPN1 and TFAP2A during interphase and mitosis.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PRKCZQ055134EBI-7199607,EBI-295351
REPS1Q96D713EBI-915016,EBI-1171195

Protein-protein interaction databases

BioGridi114202. 53 interactions.
DIPiDIP-37981N.
IntActiP49757. 38 interactions.
MINTiMINT-1492704.
STRINGi9606.ENSP00000347169.

Structurei

3D structure databases

ProteinModelPortaliP49757.
SMRiP49757. Positions 21-172.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 193161PIDPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PID domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3537. Eukaryota.
ENOG410XT15. LUCA.
GeneTreeiENSGT00530000062937.
HOGENOMiHOG000220819.
HOVERGENiHBG006672.
InParanoidiP49757.
KOiK06057.
OMAiRKTDFPM.
OrthoDBiEOG7MKW5J.
PhylomeDBiP49757.
TreeFamiTF314159.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR016698. Numb/numb-like.
IPR010449. Numb_domain.
IPR011993. PH_dom-like.
IPR006020. PTB/PI_dom.
[Graphical view]
PfamiPF06311. NumbF. 1 hit.
PF00640. PID. 1 hit.
[Graphical view]
PIRSFiPIRSF017607. Numb/numb-like. 1 hit.
SMARTiSM00462. PTB. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS01179. PID. 1 hit.
[Graphical view]

Sequences (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P49757-1) [UniParc]FASTAAdd to basket

Also known as: p72

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.

« Hide

        10         20         30         40         50
MNKLRQSFRR KKDVYVPEAS RPHQWQTDEE GVRTGKCSFP VKYLGHVEVD
60 70 80 90 100
ESRGMHICED AVKRLKAERK FFKGFFGKTG KKAVKAVLWV SADGLRVVDE
110 120 130 140 150
KTKDLIVDQT IEKVSFCAPD RNFDRAFSYI CRDGTTRRWI CHCFMAVKDT
160 170 180 190 200
GERLSHAVGC AFAACLERKQ KREKECGVTA TFDASRTTFT REGSFRVTTA
210 220 230 240 250
TEQAEREEIM KQMQDAKKAE TDKIVVGSSV APGNTAPSPS SPTSPTSDAT
260 270 280 290 300
TSLEMNNPHA IPRRHAPIEQ LARQGSFRGF PALSQKMSPF KRQLSLRINE
310 320 330 340 350
LPSTMQRKTD FPIKNAVPEV EGEAESISSL CSQITNAFST PEDPFSSAPM
360 370 380 390 400
TKPVTVVAPQ SPTFQANGTD SAFHVLAKPA HTALAPVAMP VRETNPWAHA
410 420 430 440 450
PDAANKEIAA TCSGTEWGQS SGAASPGLFQ AGHRRTPSEA DRWLEEVSKS
460 470 480 490 500
VRAQQPQASA APLQPVLQPP PPTAISQPAS PFQGNAFLTS QPVPVGVVPA
510 520 530 540 550
LQPAFVPAQS YPVANGMPYP APNVPVVGIT PSQMVANVFG TAGHPQAAHP
560 570 580 590 600
HQSPSLVRQQ TFPHYEASSA TTSPFFKPPA QHLNGSAAFN GVDDGRLASA
610 620 630 640 650
DRHTEVPTGT CPVDPFEAQW AALENKSKQR TNPSPTNPFS SDLQKTFEIE

L
Length:651
Mass (Da):70,804
Last modified:June 1, 2001 - v2
Checksum:i5B590BE49A74FCF2
GO
Isoform 2 (identifier: P49757-2) [UniParc]FASTAAdd to basket

Also known as: p66

The sequence of this isoform differs from the canonical sequence as follows:
     366-413: Missing.

Show »
Length:603
Mass (Da):65,899
Checksum:iC7106FBD389F5E39
GO
Isoform 3 (identifier: P49757-3) [UniParc]FASTAAdd to basket

Also known as: p71

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

Show »
Length:640
Mass (Da):69,431
Checksum:i918C5B5DD5CD87B8
GO
Isoform 4 (identifier: P49757-4) [UniParc]FASTAAdd to basket

Also known as: p65

The sequence of this isoform differs from the canonical sequence as follows:
     68-78: Missing.
     366-413: Missing.

Show »
Length:592
Mass (Da):64,527
Checksum:i645599F01321222D
GO
Isoform 5 (identifier: P49757-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     219-316: Missing.
     366-413: Missing.

Show »
Length:505
Mass (Da):55,319
Checksum:i086027BD202D2782
GO
Isoform 6 (identifier: P49757-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     68-78: Missing.
     219-316: Missing.
     366-413: Missing.

Show »
Length:494
Mass (Da):53,947
Checksum:i7B90A93A1C41BEF7
GO
Isoform 7 (identifier: P49757-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     219-316: Missing.
     317-365: Missing.
     366-413: Missing.

Show »
Length:456
Mass (Da):50,198
Checksum:i6E557041549FBFB6
GO
Isoform 8 (identifier: P49757-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     68-78: Missing.
     219-316: Missing.
     317-365: Missing.
     366-413: Missing.

Show »
Length:445
Mass (Da):48,825
Checksum:iCF5A95DB5A1A91AE
GO
Isoform 9 (identifier: P49757-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-254: Missing.
     366-413: Missing.

Show »
Length:349
Mass (Da):37,396
Checksum:iC2238BAC87304A30
GO

Sequence cautioni

The sequence AAH20788.1 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311G → S in AAD27959 (Ref. 4) Curated
Sequence conflicti68 – 681E → Q in AAD27959 (Ref. 4) Curated
Sequence conflicti193 – 1931G → R in AAD27959 (Ref. 4) Curated
Sequence conflicti450 – 4501S → N in AAD27959 (Ref. 4) Curated
Sequence conflicti533 – 5331Q → K in AAH68476 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti387 – 3871V → I.
Corresponds to variant rs17182272 [ dbSNP | Ensembl ].
VAR_051249
Natural varianti595 – 5951G → D.
Corresponds to variant rs17781919 [ dbSNP | Ensembl ].
VAR_051250

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 254254Missing in isoform 9. 2 PublicationsVSP_053745Add
BLAST
Alternative sequencei68 – 7811Missing in isoform 3, isoform 4, isoform 6 and isoform 8. 3 PublicationsVSP_004348Add
BLAST
Alternative sequencei219 – 31698Missing in isoform 5, isoform 6, isoform 7 and isoform 8. 1 PublicationVSP_047756Add
BLAST
Alternative sequencei317 – 36549Missing in isoform 7 and isoform 8. 1 PublicationVSP_053763Add
BLAST
Alternative sequencei366 – 41348Missing in isoform 2, isoform 4, isoform 5, isoform 6, isoform 7, isoform 8 and isoform 9. 6 PublicationsVSP_004349Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF015040 mRNA. Translation: AAD01548.1.
AF171938 mRNA. Translation: AAD54279.1.
AF171939 mRNA. Translation: AAD54280.1.
AF171940 mRNA. Translation: AAD54281.1.
AF171941 mRNA. Translation: AAD54282.1.
EU265734 mRNA. Translation: ABY89090.1.
EU265735 mRNA. Translation: ABY89091.1.
EU265736 mRNA. Translation: ABY89092.1.
EU265737 mRNA. Translation: ABY89093.1.
EU265738 mRNA. Translation: ABY89094.1.
AF108092 mRNA. Translation: AAD27959.1.
AK294591 mRNA. Translation: BAG57779.1.
AK304193 mRNA. Translation: BAG65073.1.
AC004846 Genomic DNA. No translation available.
AC005280 Genomic DNA. No translation available.
AL391733 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81106.1.
BC020788 mRNA. Translation: AAH20788.1. Sequence problems.
BC068476 mRNA. Translation: AAH68476.1.
BX248073 mRNA. Translation: CAD62362.1.
AF109907 Genomic DNA. Translation: AAC97962.1.
L40393 mRNA. Translation: AAC42000.1.
CCDSiCCDS32115.1. [P49757-2]
CCDS32116.1. [P49757-1]
CCDS55927.1. [P49757-4]
CCDS9814.1. [P49757-3]
RefSeqiNP_001005743.1. NM_001005743.1. [P49757-1]
NP_001005744.1. NM_001005744.1. [P49757-2]
NP_001005745.1. NM_001005745.1. [P49757-4]
NP_001307043.1. NM_001320114.1. [P49757-2]
NP_003735.3. NM_003744.5. [P49757-3]
XP_005268199.1. XM_005268142.3. [P49757-1]
XP_005268201.1. XM_005268144.3. [P49757-3]
XP_005268203.1. XM_005268146.3. [P49757-2]
XP_011535555.1. XM_011537253.1. [P49757-1]
XP_011535556.1. XM_011537254.1. [P49757-1]
XP_011535557.1. XM_011537255.1. [P49757-1]
XP_011535559.1. XM_011537257.1. [P49757-3]
XP_011535560.1. XM_011537258.1. [P49757-3]
XP_011535562.1. XM_011537260.1. [P49757-2]
XP_011535565.1. XM_011537263.1. [P49757-5]
XP_011535566.1. XM_011537264.1. [P49757-6]
UniGeneiHs.525443.
Hs.654609.
Hs.714879.

Genome annotation databases

EnsembliENST00000355058; ENSP00000347169; ENSG00000133961. [P49757-1]
ENST00000356296; ENSP00000348644; ENSG00000133961. [P49757-2]
ENST00000359560; ENSP00000352563; ENSG00000133961. [P49757-3]
ENST00000535282; ENSP00000441258; ENSG00000133961. [P49757-2]
ENST00000544991; ENSP00000446001; ENSG00000133961. [P49757-7]
ENST00000554521; ENSP00000450817; ENSG00000133961. [P49757-8]
ENST00000554546; ENSP00000452416; ENSG00000133961. [P49757-4]
ENST00000555238; ENSP00000451300; ENSG00000133961. [P49757-1]
ENST00000555394; ENSP00000451625; ENSG00000133961. [P49757-2]
ENST00000555738; ENSP00000452069; ENSG00000133961. [P49757-6]
ENST00000557597; ENSP00000451117; ENSG00000133961. [P49757-3]
ENST00000559312; ENSP00000452888; ENSG00000133961. [P49757-7]
ENST00000560335; ENSP00000453209; ENSG00000133961. [P49757-5]
GeneIDi8650.
KEGGihsa:8650.
UCSCiuc001xny.2. human. [P49757-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF015040 mRNA. Translation: AAD01548.1.
AF171938 mRNA. Translation: AAD54279.1.
AF171939 mRNA. Translation: AAD54280.1.
AF171940 mRNA. Translation: AAD54281.1.
AF171941 mRNA. Translation: AAD54282.1.
EU265734 mRNA. Translation: ABY89090.1.
EU265735 mRNA. Translation: ABY89091.1.
EU265736 mRNA. Translation: ABY89092.1.
EU265737 mRNA. Translation: ABY89093.1.
EU265738 mRNA. Translation: ABY89094.1.
AF108092 mRNA. Translation: AAD27959.1.
AK294591 mRNA. Translation: BAG57779.1.
AK304193 mRNA. Translation: BAG65073.1.
AC004846 Genomic DNA. No translation available.
AC005280 Genomic DNA. No translation available.
AL391733 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81106.1.
BC020788 mRNA. Translation: AAH20788.1. Sequence problems.
BC068476 mRNA. Translation: AAH68476.1.
BX248073 mRNA. Translation: CAD62362.1.
AF109907 Genomic DNA. Translation: AAC97962.1.
L40393 mRNA. Translation: AAC42000.1.
CCDSiCCDS32115.1. [P49757-2]
CCDS32116.1. [P49757-1]
CCDS55927.1. [P49757-4]
CCDS9814.1. [P49757-3]
RefSeqiNP_001005743.1. NM_001005743.1. [P49757-1]
NP_001005744.1. NM_001005744.1. [P49757-2]
NP_001005745.1. NM_001005745.1. [P49757-4]
NP_001307043.1. NM_001320114.1. [P49757-2]
NP_003735.3. NM_003744.5. [P49757-3]
XP_005268199.1. XM_005268142.3. [P49757-1]
XP_005268201.1. XM_005268144.3. [P49757-3]
XP_005268203.1. XM_005268146.3. [P49757-2]
XP_011535555.1. XM_011537253.1. [P49757-1]
XP_011535556.1. XM_011537254.1. [P49757-1]
XP_011535557.1. XM_011537255.1. [P49757-1]
XP_011535559.1. XM_011537257.1. [P49757-3]
XP_011535560.1. XM_011537258.1. [P49757-3]
XP_011535562.1. XM_011537260.1. [P49757-2]
XP_011535565.1. XM_011537263.1. [P49757-5]
XP_011535566.1. XM_011537264.1. [P49757-6]
UniGeneiHs.525443.
Hs.654609.
Hs.714879.

3D structure databases

ProteinModelPortaliP49757.
SMRiP49757. Positions 21-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114202. 53 interactions.
DIPiDIP-37981N.
IntActiP49757. 38 interactions.
MINTiMINT-1492704.
STRINGi9606.ENSP00000347169.

PTM databases

iPTMnetiP49757.
PhosphoSiteiP49757.

Polymorphism and mutation databases

BioMutaiNUMB.
DMDMi14195675.

Proteomic databases

EPDiP49757.
MaxQBiP49757.
PaxDbiP49757.
PRIDEiP49757.

Protocols and materials databases

DNASUi8650.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355058; ENSP00000347169; ENSG00000133961. [P49757-1]
ENST00000356296; ENSP00000348644; ENSG00000133961. [P49757-2]
ENST00000359560; ENSP00000352563; ENSG00000133961. [P49757-3]
ENST00000535282; ENSP00000441258; ENSG00000133961. [P49757-2]
ENST00000544991; ENSP00000446001; ENSG00000133961. [P49757-7]
ENST00000554521; ENSP00000450817; ENSG00000133961. [P49757-8]
ENST00000554546; ENSP00000452416; ENSG00000133961. [P49757-4]
ENST00000555238; ENSP00000451300; ENSG00000133961. [P49757-1]
ENST00000555394; ENSP00000451625; ENSG00000133961. [P49757-2]
ENST00000555738; ENSP00000452069; ENSG00000133961. [P49757-6]
ENST00000557597; ENSP00000451117; ENSG00000133961. [P49757-3]
ENST00000559312; ENSP00000452888; ENSG00000133961. [P49757-7]
ENST00000560335; ENSP00000453209; ENSG00000133961. [P49757-5]
GeneIDi8650.
KEGGihsa:8650.
UCSCiuc001xny.2. human. [P49757-1]

Organism-specific databases

CTDi8650.
GeneCardsiNUMB.
HGNCiHGNC:8060. NUMB.
HPAiCAB011478.
MIMi603728. gene.
neXtProtiNX_P49757.
PharmGKBiPA31845.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3537. Eukaryota.
ENOG410XT15. LUCA.
GeneTreeiENSGT00530000062937.
HOGENOMiHOG000220819.
HOVERGENiHBG006672.
InParanoidiP49757.
KOiK06057.
OMAiRKTDFPM.
OrthoDBiEOG7MKW5J.
PhylomeDBiP49757.
TreeFamiTF314159.

Enzyme and pathway databases

ReactomeiR-HSA-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-HSA-437239. Recycling pathway of L1.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
SignaLinkiP49757.
SIGNORiP49757.

Miscellaneous databases

ChiTaRSiNUMB. human.
GeneWikiiNUMB_(gene).
GenomeRNAii8650.
NextBioi32435.
PROiP49757.
SOURCEiSearch...

Gene expression databases

BgeeiP49757.
ExpressionAtlasiP49757. baseline and differential.
GenevisibleiP49757. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR016698. Numb/numb-like.
IPR010449. Numb_domain.
IPR011993. PH_dom-like.
IPR006020. PTB/PI_dom.
[Graphical view]
PfamiPF06311. NumbF. 1 hit.
PF00640. PID. 1 hit.
[Graphical view]
PIRSFiPIRSF017607. Numb/numb-like. 1 hit.
SMARTiSM00462. PTB. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS01179. PID. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 2).
  2. "Distinct human NUMB isoforms regulate differentiation vs. proliferation in the neuronal lineage."
    Verdi J.M., Bashirullah A., Goldhawk D.E., Kubu C.J., Jamali M., Meakin S.O., Lipshitz H.D.
    Proc. Natl. Acad. Sci. U.S.A. 96:10472-10476(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
    Tissue: Neuron.
  3. "Characterization and role of NUMB in the human extravillous trophopblast."
    Haider M., Qiu Q., Bani-Yaghoub M., Tsang B.K., Gruslin A.
    Placenta 32:441-449(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 6; 7; 8 AND 9), ALTERNATIVE SPLICING.
    Tissue: Placenta.
  4. Ye Q., Jiang K., Han W., Moore M.A.S.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 9).
    Tissue: Brain and Trachea.
  6. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-256 (ISOFORMS 3/4).
    Tissue: Liver and Testis.
  9. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-529 (ISOFORM 1).
    Tissue: Cervix carcinoma.
  10. "Complete sequence of the gene for presenilin 1."
    Rowen L., Madan A., Qin S., Abbasi N., Dors M., Ratcliffe A., Madan A., Dickhoff R., Shaffer T., James R., Lasky S., Hood L.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 79-651 (ISOFORMS 2/4).
    Tissue: Fetal brain.
  11. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 517-651.
    Tissue: Brain.
  12. Cited for: INTERACTION WITH SIAH1, DEGRADATION.
  13. "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis."
    Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.
    J. Biol. Chem. 278:30597-30604(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RALBP1.
  14. "A novel transmembrane protein recruits numb to the plasma membrane during asymmetric cell division."
    Qin H., Percival-Smith A., Li C., Jia C.Y.H., Gloor G., Li S.S.-C.
    J. Biol. Chem. 279:11304-11312(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DUOXA1.
  15. "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.
  16. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "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.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNUMB_HUMAN
AccessioniPrimary (citable) accession number: P49757
Secondary accession number(s): B1P2N5
, B1P2N6, B1P2N7, B1P2N8, B1P2N9, B4E2B1, Q6NUQ7, Q86SY1, Q8WW73, Q9UBG1, Q9UEQ4, Q9UKE8, Q9UKE9, Q9UKF0, Q9UQJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.