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Protein

Nestin

Gene

Nes

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • brain development Source: UniProtKB
  • embryonic camera-type eye development Source: UniProtKB
  • neuron differentiation Source: RGD
  • positive regulation of intermediate filament depolymerization Source: UniProtKB
  • positive regulation of neural precursor cell proliferation Source: UniProtKB
  • response to drug Source: RGD
  • response to ionizing radiation Source: RGD
  • 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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3162. Nes.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000638541 – 1893NestinAdd BLAST1893

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei312PhosphoserineBy similarity1
Modified residuei316Phosphothreonine1 Publication1
Modified residuei356PhosphoserineBy similarity1
Modified residuei359PhosphoserineBy similarity1
Modified residuei389PhosphothreonineBy similarity1
Modified residuei562PhosphoserineBy similarity1
Modified residuei620PhosphoserineBy similarity1
Modified residuei685PhosphoserineBy similarity1
Modified residuei729PhosphoserineBy similarity1
Modified residuei817PhosphoserineBy similarity1
Modified residuei903PhosphoserineBy similarity1
Modified residuei1005PhosphoserineBy similarity1
Cross-linki1136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei1145PhosphoserineBy similarity1
Modified residuei1216PhosphoserineBy similarity1
Modified residuei1229PhosphoserineBy similarity1
Modified residuei1322PhosphoserineBy similarity1
Modified residuei1570PhosphoserineBy similarity1
Modified residuei1594PhosphoserineBy similarity1
Modified residuei1686PhosphoserineBy similarity1
Modified residuei1695PhosphoserineBy similarity1
Modified residuei1772PhosphoserineBy similarity1
Modified residuei1774PhosphoserineBy similarity1
Modified residuei1866PhosphoserineCombined sources1
Modified residuei1889PhosphoserineCombined sources1
Modified residuei1890PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP21263.
PRIDEiP21263.

PTM databases

iPTMnetiP21263.
PhosphoSitePlusiP21263.

Expressioni

Tissue specificityi

CNS stem cells.

Developmental stagei

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

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

GO - Molecular functioni

  • CCR5 chemokine receptor binding Source: RGD
  • intermediate filament binding Source: UniProtKB

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP21263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 7Head7
Regioni8 – 314RodAdd BLAST307
Regioni8 – 43Coil 1AAdd BLAST36
Regioni44 – 55Linker 1Add BLAST12
Regioni56 – 151Coil 1BAdd BLAST96
Regioni152 – 174Linker 12Add BLAST23
Regioni175 – 193Coil 2AAdd BLAST19
Regioni194 – 196Linker 23
Regioni197 – 314Coil 2BAdd BLAST118
Regioni315 – 1893TailAdd BLAST1579

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IRNV. Eukaryota.
ENOG410XZH4. LUCA.
HOGENOMiHOG000113766.
HOVERGENiHBG006463.
InParanoidiP21263.
PhylomeDBiP21263.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR031211. Nestin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 2 hits.
PTHR23239:SF131. PTHR23239:SF131. 2 hits.
PfamiPF00038. Filament. 2 hits.
[Graphical view]
SMARTiSM01391. 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: 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)DescriptionActionsGraphical viewLength
Sequence conflicti168 – 172GSPVR → RIPGP in AAA41685 (PubMed:1689217).Curated5
Sequence conflicti425 – 426AE → LK in AAA41685 (PubMed:1689217).Curated2
Sequence conflicti460T → N in AAA41685 (PubMed:1689217).Curated1
Sequence conflicti477G → E in AAA41685 (PubMed:1689217).Curated1
Sequence conflicti943N → D in AAA41685 (PubMed:1689217).Curated1
Sequence conflicti1011R → Q in AAA41685 (PubMed:1689217).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_024924736 – 823Missing in isoform 2. 1 PublicationAdd BLAST88

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34384 mRNA. Translation: AAA41685.1.
AF538924 mRNA. Translation: AAN33053.1.
PIRiA34736.
UniGeneiRn.9701.

Genome annotation databases

UCSCiRGD:3162. rat. [P21263-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34384 mRNA. Translation: AAA41685.1.
AF538924 mRNA. Translation: AAN33053.1.
PIRiA34736.
UniGeneiRn.9701.

3D structure databases

ProteinModelPortaliP21263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP21263.
PhosphoSitePlusiP21263.

Proteomic databases

PaxDbiP21263.
PRIDEiP21263.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3162. rat. [P21263-1]

Organism-specific databases

RGDi3162. Nes.

Phylogenomic databases

eggNOGiENOG410IRNV. Eukaryota.
ENOG410XZH4. LUCA.
HOGENOMiHOG000113766.
HOVERGENiHBG006463.
InParanoidiP21263.
PhylomeDBiP21263.

Miscellaneous databases

PROiP21263.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR031211. Nestin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 2 hits.
PTHR23239:SF131. PTHR23239:SF131. 2 hits.
PfamiPF00038. Filament. 2 hits.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 106 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

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.