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P21263

- NEST_RAT

UniProt

P21263 - NEST_RAT

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Protein

Nestin

Gene

Nes

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Required for brain and eye development By similarity. 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. Required for survival, renewal and mitogen-stimulated proliferation of neural progenitor cells.By similarity2 Publications

GO - Molecular functioni

  1. CCR5 chemokine receptor binding Source: RGD
  2. intermediate filament binding Source: UniProtKB
  3. structural molecule activity Source: InterPro

GO - Biological processi

  1. brain development Source: UniProtKB
  2. embryonic camera-type eye development Source: UniProtKB
  3. neuron differentiation Source: RGD
  4. positive regulation of intermediate filament depolymerization Source: UniProtKB
  5. positive regulation of neural precursor cell proliferation Source: UniProtKB
  6. response to drug Source: RGD
  7. response to ionizing radiation Source: RGD
  8. response to nutrient levels Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Nestin
Gene namesi
Name:Nes
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3162. Nes.

Subcellular locationi

GO - Cellular componenti

  1. intermediate filament Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18931893NestinPRO_0000063854Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei312 – 3121PhosphoserineBy similarity
Modified residuei316 – 3161Phosphothreonine1 Publication
Modified residuei356 – 3561PhosphoserineBy similarity
Modified residuei359 – 3591PhosphoserineBy similarity
Modified residuei389 – 3891PhosphothreonineBy similarity
Modified residuei562 – 5621PhosphoserineBy similarity
Modified residuei685 – 6851PhosphoserineBy similarity
Modified residuei1145 – 11451PhosphoserineBy similarity
Modified residuei1216 – 12161PhosphoserineBy similarity
Modified residuei1229 – 12291PhosphoserineBy similarity
Modified residuei1570 – 15701PhosphoserineBy similarity
Modified residuei1686 – 16861PhosphoserineBy similarity
Modified residuei1695 – 16951PhosphoserineBy similarity
Modified residuei1772 – 17721PhosphoserineBy similarity
Modified residuei1774 – 17741PhosphoserineBy similarity
Modified residuei1866 – 18661PhosphoserineBy similarity
Modified residuei1889 – 18891PhosphoserineBy similarity
Modified residuei1890 – 18901PhosphoserineBy similarity

Post-translational modificationi

Constitutively phosphorylated. This increases during mitosis when the cytoplasmic intermediate filament network is reorganized.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP21263.
PRIDEiP21263.

PTM databases

PhosphoSiteiP21263.

Expressioni

Tissue specificityi

CNS stem cells.

Developmental stagei

Upon terminal neural differentiation, nestin is down-regulated and replaced by neurofilaments.

Gene expression databases

GenevestigatoriP21263.

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% By similarity. Interacts with FHOD3.By similarity1 Publication

Protein-protein interaction databases

IntActiP21263. 3 interactions.
MINTiMINT-3376397.
STRINGi10116.ENSRNOP00000025314.

Structurei

3D structure databases

ProteinModelPortaliP21263.
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 – 18931579TailAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000113766.
HOVERGENiHBG006463.
InParanoidiP21263.
KOiK07609.
PhylomeDBiP21263.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 2 hits.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P21263-1) [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 GGLRAQSGDT
60 70 80 90 100
SWRARADDEL ASLRILVDQR WREKLEAEVQ RDNLAEELES VAGRCQQVRL
110 120 130 140 150
ARERTVQEAA CSRRALEAEK NARGWLSTQA AELERELEAL RAAHEEERAH
160 170 180 190 200
LNAQAACAPR RPPAPPHGSP VRAPEVEDLA RRLGEVWRGA VRDYQERVAH
210 220 230 240 250
MESSLGQARE RLSQAVRGAR ECRLEVQQLQ ADRDSLQERR EALEQRLEGR
260 270 280 290 300
WQDRLQATDK FQLAVEALEQ EKQGLQSQIA QILEGGQQLA HLKMSLSLEV
310 320 330 340 350
ATYRTLLEAE NSRLQTPGRG SQASLGFLDP KLKPNFLGIP EDQYLGSVLP
360 370 380 390 400
ALSPTSFPSP LPNTLETPVT AFLKTQEFLQ ARTPTLASTP IPPISEAPCP
410 420 430 440 450
PNAEVRAQEV PLSLLQTQAP EPLWAEATVP SSSAILPELE EPGGKQQGHF
460 470 480 490 500
PDDLTSLATT LNPHHPTLEA KDGESSGSRV SSIFQEDEGQ IWELVEKEAD
510 520 530 540 550
IEVKVENSSA QKTQESGLDT EETQDSQGPL QKETLKALGE EPLMSLKIQN
560 570 580 590 600
YETAGKENCN SSTEGHLGTL EGPEKEKQIP LKSLEEKNVE SEKTLENGVP
610 620 630 640 650
VLSELLGKED TRTEDQELMS PKGTLKRFSS LGKESQEVVR PSKEGNLESW
660 670 680 690 700
TAFKEESQHP LGFPGAEDQM LERLVEKEDQ SFPRSPEEED QEACRPLQKE
710 720 730 740 750
NQEPLGYEEA EGQILERLIE KESQESLRSP EEEDQEAGRS LQKGNQEPLG
760 770 780 790 800
YEEAEGQILE RLIEKESQES LRSAEEEDQE ACRSLQKENQ EPLGYEEAED
810 820 830 840 850
QILERLIEKE SQESLRSPEE EDQEAGRSLQ KENQEPLGYE EAEDQMLERL
860 870 880 890 900
IEKESQESLK SPEENQRIGK PLERENQKSL RYLEENQETF VPLESRNQRP
910 920 930 940 950
LRSLEVEEEE QRIVKPLEKV SQDSLGSLAE ENVQPLRYLE EDNCINKSLL
960 970 980 990 1000
EDKTHKSLGS LEDRNGDSII IPQESETQVS LRPPEEEDQR IVNHLEKESQ
1010 1020 1030 1040 1050
EFSRSSEEEE RVMERSLEGE NHESLSSVEK EDQMVESQLE KESQDSGKSL
1060 1070 1080 1090 1100
EDESQETFGP LEKENAESLR SLAGQDQEEQ KLEQETQQTL RAVGNEQMAV
1110 1120 1130 1140 1150
SPPEKVDPEL PKPLGNDQEI ARSLGKENQE SLVSLKEKGI ETVKSLETEI
1160 1170 1180 1190 1200
IEPLETAEED LERRKSIDTQ EPLWSTEVAR ETVEPPEDEP PGSLGSVDEN
1210 1220 1230 1240 1250
RETLTSLEKE SQELSSLGKW NVETRVEDSQ QCLQVEEGLQ EEQHQESLRE
1260 1270 1280 1290 1300
VKQELPSSGN QQRWEDVVEG KAVGQEAPLA TTGVGTEDKA ELHLRGQGGE
1310 1320 1330 1340 1350
EEAAAEGELL QDIVGEAWSL GSSEPKEQRV PAEALDNLEG GALEVPVAQS
1360 1370 1380 1390 1400
MPEVTERDED RAQAGEQDSI EVTLGLEAAR TGLELEQEVV GLEDPRHFAR
1410 1420 1430 1440 1450
EEAIPPSLGE ESVKAKIAQG LEGPGKEPKE AGALDSGILE LPKTSSEALE
1460 1470 1480 1490 1500
CQGHEESESM EGWEEEEASL ETSDHEGSDA PQPRPPETEE DEGAQAALTA
1510 1520 1530 1540 1550
PGPKLLEPCS PIPILTDAHE LQPQAEGIQE AGWQPEAGSE ALERVENEPE
1560 1570 1580 1590 1600
FGLGEIPEGL QDWEEGREES EADDLGETLP DSTPLGLYLR SPASPKWDLA
1610 1620 1630 1640 1650
GEQRLSPQGD AGKEDWGPAV PAAQGLSGPP EEEEEQGHGS DLSSEEFEDL
1660 1670 1680 1690 1700
GTEASLLPGV PKEVADHVGQ VPPVLQPACW DQGGESDGFA DEEESGEEGE
1710 1720 1730 1740 1750
EEDADEEGAE SGAQWWGSGA SGGGCKVQDI AQRGDPVQES VGVSGLWDDG
1760 1770 1780 1790 1800
LRGAAANVPA LEMVSQDSAE PSGSEESESA SLEGEEGQVT DHLDAPQEVT
1810 1820 1830 1840 1850
SMVPGVGDAF DIGGQSPNLD SEQVNGKMEN GLEQAEGQVV LDGDEDQELL
1860 1870 1880 1890
LQGQEVGALK VPLVASPVHL GPSQPLKFTL SGVDGDSWSS GED
Length:1,893
Mass (Da):208,797
Last modified:May 1, 2007 - v2
Checksum:i03AE6B616A1A7623
GO
Isoform 2 (identifier: P21263-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     736-823: Missing.

Show »
Length:1,805
Mass (Da):198,623
Checksum:iDC2A89784654D647
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti168 – 1725GSPVR → RIPGP in AAA41685. (PubMed:1689217)Curated
Sequence conflicti425 – 4262AE → LK in AAA41685. (PubMed:1689217)Curated
Sequence conflicti460 – 4601T → N in AAA41685. (PubMed:1689217)Curated
Sequence conflicti477 – 4771G → E in AAA41685. (PubMed:1689217)Curated
Sequence conflicti943 – 9431N → D in AAA41685. (PubMed:1689217)Curated
Sequence conflicti1011 – 10111R → Q in AAA41685. (PubMed:1689217)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei736 – 82388Missing in isoform 2. 1 PublicationVSP_024924Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34384 mRNA. Translation: AAA41685.1.
AF538924 mRNA. Translation: AAN33053.1.
PIRiA34736.
RefSeqiNP_037119.1. NM_012987.1.
UniGeneiRn.9701.

Genome annotation databases

GeneIDi25491.
KEGGirno:25491.
UCSCiRGD:3162. rat. [P21263-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34384 mRNA. Translation: AAA41685.1 .
AF538924 mRNA. Translation: AAN33053.1 .
PIRi A34736.
RefSeqi NP_037119.1. NM_012987.1.
UniGenei Rn.9701.

3D structure databases

ProteinModelPortali P21263.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P21263. 3 interactions.
MINTi MINT-3376397.
STRINGi 10116.ENSRNOP00000025314.

PTM databases

PhosphoSitei P21263.

Proteomic databases

PaxDbi P21263.
PRIDEi P21263.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 25491.
KEGGi rno:25491.
UCSCi RGD:3162. rat. [P21263-1 ]

Organism-specific databases

CTDi 10763.
RGDi 3162. Nes.

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000113766.
HOVERGENi HBG006463.
InParanoidi P21263.
KOi K07609.
PhylomeDBi P21263.

Miscellaneous databases

NextBioi 606861.
PROi P21263.

Gene expression databases

Genevestigatori P21263.

Family and domain databases

InterProi IPR001664. IF.
IPR018039. Intermediate_filament_CS.
[Graphical view ]
PANTHERi PTHR23239. PTHR23239. 1 hit.
Pfami PF00038. Filament. 2 hits.
[Graphical view ]
PROSITEi PS00226. IF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "CNS stem cells express a new class of intermediate filament protein."
    Lendahl U., Zimmerman L.B., McKay R.D.G.
    Cell 60:585-595(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Nestin promotes the phosphorylation-dependent disassembly of vimentin intermediate filaments during mitosis."
    Chou Y.-H., Khuon S., Herrmann H., Goldman R.D.
    Mol. Biol. Cell 14:1468-1478(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    Tissue: Glial tumor.
  3. "Mitotic reorganization of the intermediate filament protein nestin involves phosphorylation by cdc2 kinase."
    Sahlgren C.M., Mikhailov A., Hellman J., Chou Y.H., Lendahl U., Goldman R.D., Eriksson J.E.
    J. Biol. Chem. 276:16456-16463(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 314-319, PHOSPHORYLATION AT THR-316.
  4. "Fhos2, a novel formin-related actin-organizing protein, probably associates with the nestin intermediate filament."
    Kanaya H., Takeya R., Takeuchi K., Watanabe N., Jing N., Sumimoto H.
    Genes Cells 10:665-678(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FHOD3.
  5. "Nestin is essential for mitogen-stimulated proliferation of neural progenitor cells."
    Xue X.J., Yuan X.B.
    Mol. Cell. Neurosci. 45:26-36(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: Sprague-Dawley.

Entry informationi

Entry nameiNEST_RAT
AccessioniPrimary (citable) accession number: P21263
Secondary accession number(s): Q8CJ14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 2007
Last modified: October 1, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3