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Protein

Nestin

Gene

Nes

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for brain and eye development. Promotes the disassembly of phosphorylated vimentin intermediate filaments (IF) during mitosis and may play a role in the trafficking and distribution of IF proteins and other cellular factors to daughter cells during progenitor cell division (By similarity). Required for survival, renewal and mitogen-stimulated proliferation of neural progenitor cells.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Nestin
Gene namesi
Name:Nes
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:101784. Nes.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • intermediate filament Source: MGI
  • intracellular Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality with the neuroepithelium of developing neural tube exhibiting low numbers of neural stem cells and high levels of apoptosis. No effect on cytoskeletal integrity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18641864NestinPRO_0000285856Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei312 – 3121PhosphoserineBy similarity
Modified residuei316 – 3161PhosphothreonineBy similarity
Modified residuei356 – 3561PhosphoserineBy similarity
Modified residuei359 – 3591PhosphoserineBy similarity
Modified residuei389 – 3891PhosphothreonineBy similarity
Modified residuei565 – 5651PhosphoserineBy similarity
Modified residuei575 – 5751PhosphoserineBy similarity
Modified residuei688 – 6881PhosphoserineBy similarity
Modified residuei841 – 8411PhosphoserineBy similarity
Modified residuei1106 – 11061PhosphoserineBy similarity
Modified residuei1177 – 11771PhosphoserineBy similarity
Modified residuei1188 – 11881PhosphoserineBy similarity
Modified residuei1195 – 11951PhosphoserineBy similarity
Modified residuei1216 – 12161PhosphoserineBy similarity
Modified residuei1290 – 12901PhosphoserineBy similarity
Modified residuei1541 – 15411Phosphoserine1 Publication
Modified residuei1656 – 16561PhosphoserineBy similarity
Modified residuei1665 – 16651PhosphoserineBy similarity
Modified residuei1745 – 17451PhosphoserineBy similarity
Modified residuei1747 – 17471PhosphoserineBy similarity
Modified residuei1837 – 18371Phosphoserine1 Publication
Modified residuei1860 – 18601PhosphoserineBy similarity
Modified residuei1861 – 18611PhosphoserineBy similarity

Post-translational modificationi

Constitutively phosphorylated. This increases during mitosis when the cytoplasmic intermediate filament network is reorganized (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ6P5H2.
PaxDbiQ6P5H2.
PRIDEiQ6P5H2.

PTM databases

PhosphoSiteiQ6P5H2.

Expressioni

Gene expression databases

BgeeiQ6P5H2.
CleanExiMM_NES.
GenevisibleiQ6P5H2. MM.

Interactioni

Subunit structurei

Forms homodimers and homotetramers in vitro. In mixtures with other intermediate filament proteins such as vimentin and alpha-internexin, this protein preferentially forms heterodimers which can assemble to form intermediate filaments if nestin does not exceed 25%. Interacts with FHOD3 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ6P5H2. 5 interactions.
STRINGi10090.ENSMUSP00000088493.

Structurei

3D structure databases

ProteinModelPortaliQ6P5H2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 77Head
Regioni8 – 314307RodAdd
BLAST
Regioni8 – 4336Coil 1AAdd
BLAST
Regioni44 – 5512Linker 1Add
BLAST
Regioni56 – 15196Coil 1BAdd
BLAST
Regioni152 – 17423Linker 12Add
BLAST
Regioni175 – 19319Coil 2AAdd
BLAST
Regioni194 – 1963Linker 2
Regioni197 – 314118Coil 2BAdd
BLAST
Regioni315 – 18641550TailAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00730000110953.
HOGENOMiHOG000113766.
HOVERGENiHBG006463.
InParanoidiQ6P5H2.
KOiK07609.
OMAiQSPEDHA.
OrthoDBiEOG773XKP.
PhylomeDBiQ6P5H2.
TreeFamiTF336633.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR031211. Nestin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF131. PTHR23239:SF131. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6P5H2-1) [UniParc]FASTAAdd to basket

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
MEGCVGEESF QMWELNRRLE AYLTRVKTLE EQNQLLSAEL GGLRAQSGDA
60 70 80 90 100
SWRARADDEL AALRVLVDQR WREKHEAEVQ RDNLAEELES VAGRCQQVRL
110 120 130 140 150
ARERTIEEAA CSRRALEAEK NARGWLSTQA AELERELEAL RASHEEERAH
160 170 180 190 200
LNAQAACTPR RPPAPAHASP IRAPEVEELA RRLGEVWRGA VRDYQERVAH
210 220 230 240 250
MESSLGQARE RLGQAVRGAR ESRLEVQQLQ ADRDSLQERR EALEQRLEGR
260 270 280 290 300
WQDRLQATEK FQLAVEALEQ EKQGLQSQIA QILEGGQQLA HLKMSLSLEV
310 320 330 340 350
ATYRTLLEAE NSRLQTPGRS SQASLGFPDP KLKLHFLGIP EDQHLGSVLP
360 370 380 390 400
VLSPTSFSSP LPNTLETPVT AFLKTQEFLK ARTPTLASTP IPPMSEAPYP
410 420 430 440 450
KNAEVRAQDV PHSLLQGGRQ QAPEPLWAEA TVPSSTGVLP ELEEPGGEQP
460 470 480 490 500
DHFPDDPTSL APPLNPHHSI LEAKDRESSE SRVSSIFQEE EGQIWELVKK
510 520 530 540 550
EAATEVKVEN SLAQEIQESG LDTEEIQDSQ GPLQMETLEA LGDEPLMSLK
560 570 580 590 600
TQNHETPGKE NCNSSIEENS GTVKSPEKEK QTPLKSLEEK NVEAEKTLEN
610 620 630 640 650
GVLELSKPLG EEEPRMEDQE LMSPEHTLET VSFLGKENQE VVRSSEEQNL
660 670 680 690 700
ESLITFKEES QYPLGGPEAE DQMLERLVEK EDQRFPRSPE EDQQAFRPLE
710 720 730 740 750
KENQEPLRFE EAEDQVLERL IEKERQESLK SPEEEDQQAF RLLEKENQEP
760 770 780 790 800
LRFEDAEDQV LERLIEKERQ ESLKSPEEED QQAFRLLEKE NQEPLRFEEA
810 820 830 840 850
EDQVLERLVE KESQESLKSP EEEDQRTGKP LEKENQESLR SLDENQETIV
860 870 880 890 900
LLESKNQRPL RSLEVEEEEQ RIVKPLEKVS QVSLESLEKE NVQSPRYLEE
910 920 930 940 950
DDHMIKSLLE DKTHEILGSL EDRNGENFIP PENETQGSLR PPEEEDQRIV
960 970 980 990 1000
NHLEKESQEF LRSPEAEEEE EQVMVRSLEG ENHDPLSSVV KEEQMAESKL
1010 1020 1030 1040 1050
ENESQDSRKS LEDESQETFG SLEKENLESL RSLAGQDQEE QKLEQETQQP
1060 1070 1080 1090 1100
LRAVEDEQMT VNPPEKVDPE LPKPLRNDQE VVRSLDKENQ ESLVSLNEGG
1110 1120 1130 1140 1150
METVKSSETE NIESLETVGE CLGRRKSVDT QEPLWSTEVT SETIEPLEDE
1160 1170 1180 1190 1200
TQEPLGCVDE NQEVLTPLER ESQELRSLGK WNPETVESPG GVEDSQQCLE
1210 1220 1230 1240 1250
VEEGPEREQH QESLRSLGEV EWELPGSGSQ QRWEDVVEDG EGQEASLGAT
1260 1270 1280 1290 1300
GVETEDKAEL HLRGQGGEEK AVEEGELLQD AVGEAWSLGS SEPKEQRVPA
1310 1320 1330 1340 1350
EPLDDLEGQP EQTGTLEVPV AQGMPEATEQ DEDRAQAGEQ DSVEVTLGLE
1360 1370 1380 1390 1400
AARAGLELEQ EVVGLEDPRH FAREEAIHPS LGEESVKAKI DQGLEEPGKE
1410 1420 1430 1440 1450
PKEAGALDSG IPELPKTSSE TLECKGWEES GEGWGEEEAS LETSDHEGSH
1460 1470 1480 1490 1500
APQPRPPKTE EDEGLQAALT VPGPKLLEPC SPIPILTDAH ELQPQAEGIQ
1510 1520 1530 1540 1550
EAGWQPEAGT EALGRVEDEP EFGRGEIPEG LQDWEEGRED SEADELGETL
1560 1570 1580 1590 1600
PDSTPLGLYL KSPASPKWEQ AGEQRLFPQG EARKEGWSPA ALAAQGLSDP
1610 1620 1630 1640 1650
PEEEQQGHDS DLSSEEFEDL GTEASLLPGV PKEVSDHLGQ EPPVLQPACW
1660 1670 1680 1690 1700
DQGGESDGFA DEEESGEEGE EEDADEEEGA ESGTQWWGPG PSGGGVKVQD
1710 1720 1730 1740 1750
VTQRGDLEHE SVGDSGLWDD GLSGAAANVL VTALETVSQD SAEPSGSEGS
1760 1770 1780 1790 1800
ESASLEGEEG QAIDHLDAPQ EVTSVVPGAG DTFDISGQGP NLESEQVNGR
1810 1820 1830 1840 1850
MENGLEQAEG QVVLHGDEDQ GIPLQEQGTL KAPLVGSPVH LGPSQPLKFT
1860
LSGVDGDSWS SGED
Length:1,864
Mass (Da):207,124
Last modified:July 5, 2004 - v1
Checksum:iB9DF21005D977983
GO
Isoform 2 (identifier: Q6P5H2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     750-793: Missing.

Show »
Length:1,820
Mass (Da):201,770
Checksum:i270C501DACA10100
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841G → C in AAF04456 (PubMed:10842089).Curated
Sequence conflicti257 – 2571A → P in AAF04456 (PubMed:10842089).Curated
Sequence conflicti265 – 2651V → L in AAF04456 (PubMed:10842089).Curated
Sequence conflicti319 – 3191R → G in AAF04456 (PubMed:10842089).Curated
Sequence conflicti458 – 4581T → S in AAF04456 (PubMed:10842089).Curated
Sequence conflicti535 – 5351M → K in AAF04456 (PubMed:10842089).Curated
Sequence conflicti544 – 5441E → K in AAF04456 (PubMed:10842089).Curated
Sequence conflicti558 – 5581G → R in AAF04456 (PubMed:10842089).Curated
Sequence conflicti570 – 5701S → L in AAF04456 (PubMed:10842089).Curated
Sequence conflicti587 – 5871L → S in AAF04456 (PubMed:10842089).Curated
Sequence conflicti673 – 6731M → I in AAF04456 (PubMed:10842089).Curated
Sequence conflicti704 – 7041Q → L in AAF04456 (PubMed:10842089).Curated
Sequence conflicti734 – 7341E → D in AAF04456 (PubMed:10842089).Curated
Sequence conflicti851 – 8511L → P in AAF04456 (PubMed:10842089).Curated
Sequence conflicti855 – 8551K → R in AAF04456 (PubMed:10842089).Curated
Sequence conflicti900 – 9001E → D in AAF04456 (PubMed:10842089).Curated
Sequence conflicti1008 – 10114RKSL → GKFF in AAF04456 (PubMed:10842089).Curated
Sequence conflicti1021 – 10211S → F in AAF04456 (PubMed:10842089).Curated
Sequence conflicti1157 – 11571C → S in AAF04456 (PubMed:10842089).Curated
Sequence conflicti1241 – 12411E → EV in AAF04456 (PubMed:10842089).Curated
Sequence conflicti1382 – 13821G → A in ABK96808 (Ref. 5) Curated
Sequence conflicti1404 – 14041A → T in AAF04456 (PubMed:10842089).Curated
Sequence conflicti1410 – 14101G → S in AAF04456 (PubMed:10842089).Curated
Sequence conflicti1577 – 15771F → S in AAF04456 (PubMed:10842089).Curated
Sequence conflicti1586 – 15916GWSPAA → DWGPAV in AAF04456 (PubMed:10842089).Curated
Sequence conflicti1684 – 16841T → A in AAF04456 (PubMed:10842089).Curated
Sequence conflicti1821 – 18211G → D in AAF04456 (PubMed:10842089).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei750 – 79344Missing in isoform 2. 1 PublicationVSP_024923Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076623 mRNA. Translation: AAF04456.2.
BC060693 mRNA. Translation: AAH60693.1.
BC062893 mRNA. Translation: AAH62893.1.
AK009706 mRNA. Translation: BAB26451.1.
AK075690 mRNA. Translation: BAC35892.1.
S78708 mRNA. Translation: AAP32014.1.
EF101559 mRNA. Translation: ABK96808.1.
CCDSiCCDS17461.1. [Q6P5H2-1]
RefSeqiNP_057910.3. NM_016701.3. [Q6P5H2-1]
UniGeneiMm.331129.

Genome annotation databases

EnsembliENSMUST00000090973; ENSMUSP00000088493; ENSMUSG00000004891. [Q6P5H2-1]
ENSMUST00000160694; ENSMUSP00000125571; ENSMUSG00000004891. [Q6P5H2-2]
GeneIDi18008.
KEGGimmu:18008.
UCSCiuc008ptm.1. mouse. [Q6P5H2-2]
uc008ptn.1. mouse. [Q6P5H2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076623 mRNA. Translation: AAF04456.2.
BC060693 mRNA. Translation: AAH60693.1.
BC062893 mRNA. Translation: AAH62893.1.
AK009706 mRNA. Translation: BAB26451.1.
AK075690 mRNA. Translation: BAC35892.1.
S78708 mRNA. Translation: AAP32014.1.
EF101559 mRNA. Translation: ABK96808.1.
CCDSiCCDS17461.1. [Q6P5H2-1]
RefSeqiNP_057910.3. NM_016701.3. [Q6P5H2-1]
UniGeneiMm.331129.

3D structure databases

ProteinModelPortaliQ6P5H2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6P5H2. 5 interactions.
STRINGi10090.ENSMUSP00000088493.

PTM databases

PhosphoSiteiQ6P5H2.

Proteomic databases

MaxQBiQ6P5H2.
PaxDbiQ6P5H2.
PRIDEiQ6P5H2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000090973; ENSMUSP00000088493; ENSMUSG00000004891. [Q6P5H2-1]
ENSMUST00000160694; ENSMUSP00000125571; ENSMUSG00000004891. [Q6P5H2-2]
GeneIDi18008.
KEGGimmu:18008.
UCSCiuc008ptm.1. mouse. [Q6P5H2-2]
uc008ptn.1. mouse. [Q6P5H2-1]

Organism-specific databases

CTDi10763.
MGIiMGI:101784. Nes.

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00730000110953.
HOGENOMiHOG000113766.
HOVERGENiHBG006463.
InParanoidiQ6P5H2.
KOiK07609.
OMAiQSPEDHA.
OrthoDBiEOG773XKP.
PhylomeDBiQ6P5H2.
TreeFamiTF336633.

Miscellaneous databases

ChiTaRSiNes. mouse.
NextBioi293025.
PROiQ6P5H2.
SOURCEiSearch...

Gene expression databases

BgeeiQ6P5H2.
CleanExiMM_NES.
GenevisibleiQ6P5H2. MM.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR031211. Nestin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF131. PTHR23239:SF131. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nestin expression during mouse eye and lens development."
    Yang J., Bian W., Gao X., Chen L., Jing N.
    Mech. Dev. 94:287-291(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: BALB/c.
  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] (ISOFORM 1).
    Strain: C57BL/6.
    Tissue: Brain.
  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] OF 1-764 AND 1510-1864.
    Strain: C57BL/6J.
    Tissue: Tongue.
  4. "Intermediate filaments in cardiac myogenesis: nestin in the developing mouse heart."
    Kachinsky A.M., Dominov J.A., Miller J.B.
    J. Histochem. Cytochem. 43:843-847(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-57.
    Tissue: Heart.
  5. "Novel metastatic mouse tumor cells express multiple properties of macrophages."
    Huysentruyt L.C., Banerjee D., Seyfried T.N.
    Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1358-1514.
    Strain: VM.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1837, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Nestin is required for the proper self-renewal of neural stem cells."
    Park D., Xiang A.P., Mao F.F., Zhang L., Di C.G., Liu X.M., Shao Y., Ma B.F., Lee J.H., Ha K.S., Walton N., Lahn B.T.
    Stem Cells 28:2162-2171(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiNEST_MOUSE
AccessioniPrimary (citable) accession number: Q6P5H2
Secondary accession number(s): A1E2I2
, Q80X00, Q8BPH7, Q9CV43, Q9R0C4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: July 5, 2004
Last modified: July 22, 2015
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.