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P48681

- NEST_HUMAN

UniProt

P48681 - NEST_HUMAN

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Protein
Nestin
Gene
NES, Nbla00170
Organism
Homo sapiens (Human)
Status
Reviewed - 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. Required for survival, renewal and mitogen-stimulated proliferation of neural progenitor cells By similarity.

GO - Molecular functioni

  1. intermediate filament binding Source: UniProtKB
  2. structural molecule activity Source: InterPro

GO - Biological processi

  1. G2/M transition of mitotic cell cycle Source: DFLAT
  2. brain development Source: UniProtKB
  3. cell projection morphogenesis Source: Ensembl
  4. central nervous system development Source: UniProtKB
  5. embryonic camera-type eye development Source: UniProtKB
  6. negative regulation of catalytic activity Source: UniProtKB
  7. negative regulation of neuron apoptotic process Source: Ensembl
  8. negative regulation of protein binding Source: UniProtKB
  9. positive regulation of intermediate filament depolymerization Source: UniProtKB
  10. positive regulation of neural precursor cell proliferation Source: UniProtKB
  11. stem cell proliferation Source: DFLAT
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Nestin
Gene namesi
Name:NES
ORF Names:Nbla00170
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:7756. NES.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: DFLAT
  2. intermediate filament Source: UniProtKB
  3. intermediate filament cytoskeleton Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31556.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16211621Nestin
PRO_0000063853Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei311 – 3111Phosphoserine1 Publication
Modified residuei315 – 3151Phosphothreonine1 Publication
Modified residuei325 – 3251Phosphoserine2 Publications
Modified residuei355 – 3551Phosphoserine1 Publication
Modified residuei358 – 3581Phosphoserine2 Publications
Modified residuei388 – 3881Phosphothreonine1 Publication
Modified residuei398 – 3981Phosphoserine2 Publications
Modified residuei471 – 4711Phosphoserine3 Publications
Modified residuei548 – 5481Phosphoserine3 Publications
Modified residuei564 – 5641Phosphoserine1 Publication
Modified residuei578 – 5781Phosphoserine2 Publications
Modified residuei588 – 5881Phosphoserine1 Publication
Modified residuei680 – 6801Phosphoserine3 Publications
Modified residuei746 – 7461Phosphoserine2 Publications
Modified residuei768 – 7681Phosphoserine2 Publications
Modified residuei790 – 7901Phosphoserine1 Publication
Modified residuei820 – 8201Phosphoserine1 Publication
Modified residuei831 – 8311Phosphoserine1 Publication
Modified residuei851 – 8511Phosphothreonine1 Publication
Modified residuei894 – 8941Phosphoserine1 Publication
Modified residuei905 – 9051Phosphoserine2 Publications
Modified residuei913 – 9131Phosphoserine1 Publication
Modified residuei934 – 9341Phosphoserine1 Publication
Modified residuei1261 – 12611Phosphoserine1 Publication
Modified residuei1282 – 12821Phosphoserine1 Publication
Modified residuei1286 – 12861Phosphoserine1 Publication
Modified residuei1347 – 13471Phosphoserine1 Publication
Modified residuei1409 – 14091Phosphoserine1 Publication
Modified residuei1418 – 14181Phosphoserine4 Publications
Modified residuei1452 – 14521Phosphoserine1 Publication
Modified residuei1496 – 14961Phosphoserine1 Publication
Modified residuei1498 – 14981Phosphoserine1 Publication
Modified residuei1577 – 15771Phosphoserine1 Publication
Modified residuei1617 – 16171Phosphoserine1 Publication
Modified residuei1618 – 16181Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP48681.
PaxDbiP48681.
PRIDEiP48681.

PTM databases

PhosphoSiteiP48681.

Expressioni

Tissue specificityi

CNS stem cells.

Developmental stagei

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

Gene expression databases

ArrayExpressiP48681.
BgeeiP48681.
CleanExiHS_NES.
GenevestigatoriP48681.

Organism-specific databases

HPAiCAB005889.
CAB058692.
HPA007007.
HPA026111.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi115983. 5 interactions.
STRINGi9606.ENSP00000357206.

Structurei

3D structure databases

ProteinModelPortaliP48681.
SMRiP48681. Positions 7-155, 220-311.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 77Head
Regioni8 – 313306Rod
Add
BLAST
Regioni8 – 4336Coil 1A
Add
BLAST
Regioni44 – 5512Linker 1
Add
BLAST
Regioni56 – 15196Coil 1B
Add
BLAST
Regioni152 – 17322Linker 12
Add
BLAST
Regioni174 – 19219Coil 2A
Add
BLAST
Regioni193 – 1953Linker 2
Regioni196 – 313118Coil 2B
Add
BLAST
Regioni314 – 16211308Tail
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000113766.
HOVERGENiHBG006463.
InParanoidiP48681.
KOiK07609.
OMAiDHASLAP.
OrthoDBiEOG773XKP.
PhylomeDBiP48681.
TreeFamiTF336633.

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]

Sequencei

Sequence statusi: Complete.

P48681-1 [UniParc]FASTAAdd to Basket

« Hide

MEGCMGEESF QMWELNRRLE AYLARVKALE EQNELLSAEL GGLRAQSADT     50
SWRAHADDEL AALRALVDQR WREKHAAEVA RDNLAEELEG VAGRCQQLRL 100
ARERTTEEVA RNRRAVEAEK CARAWLSSQV AELERELEAL RVAHEEERVG 150
LNAQAACAPR CPAPPRGPPA PAPEVEELAR RLGEAWRGAV RGYQERVAHM 200
ETSLGQARER LGRAVQGARE GRLELQQLQA ERGGLLERRA ALEQRLEGRW 250
QERLRATEKF QLAVEALEQE KQGLQSQIAQ VLEGRQQLAH LKMSLSLEVA 300
TYRTLLEAEN SRLQTPGGGS KTSLSFQDPK LELQFPRTPE GRRLGSLLPV 350
LSPTSLPSPL PATLETPVPA FLKNQEFLQA RTPTLASTPI PPTPQAPSPA 400
VDAEIRAQDA PLSLLQTQGG RKQAPEPLRA EARVAIPASV LPGPEEPGGQ 450
RQEASTGQSP EDHASLAPPL SPDHSSLEAK DGESGGSRVF SICRGEGEGQ 500
IWGLVEKETA IEGKVVSSLQ QEIWEEEDLN RKEIQDSQVP LEKETLKSLG 550
EEIQESLKTL ENQSHETLER ENQECPRSLE EDLETLKSLE KENKELLKDV 600
EVVRPLEKEA VGQLKPTGKE DTQTLQSLQK ENQELMKSLE GNLETFLFPG 650
TENQELVSSL QENLESLTAL EKENQEPLRS PEVGDEEALR PLTKENQEPL 700
RSLEDENKEA FRSLEKENQE PLKTLEEEDQ SIVRPLETEN HKSLRSLEEQ 750
DQETLRTLEK ETQQRRRSLG EQDQMTLRPP EKVDLEPLKS LDQEIARPLE 800
NENQEFLKSL KEESVEAVKS LETEILESLK SAGQENLETL KSPETQAPLW 850
TPEEINQGAM NPLEKEIQEP LESVEVNQET FRLLEEENQE SLRSLGAWNL 900
ENLRSPEEVD KESQRNLEEE ENLGKGEYQE SLRSLEEEGQ ELPQSADVQR 950
WEDTVEKDQE LAQESPPGMA GVENEDEAEL NLREQDGFTG KEEVVEQGEL 1000
NATEEVWIPG EGHPESPEPK EQRGLVEGAS VKGGAEGLQD PEGQSQQVGA 1050
PGLQAPQGLP EAIEPLVEDD VAPGGDQASP EVMLGSEPAM GESAAGAEPG 1100
PGQGVGGLGD PGHLTREEVM EPPLEEESLE AKRVQGLEGP RKDLEEAGGL 1150
GTEFSELPGK SRDPWEPPRE GREESEAEAP RGAEEAFPAE TLGHTGSDAP 1200
SPWPLGSEEA EEDVPPVLVS PSPTYTPILE DAPGPQPQAE GSQEASWGVQ 1250
GRAEALGKVE SEQEELGSGE IPEGPQEEGE ESREESEEDE LGETLPDSTP 1300
LGFYLRSPTS PRWDPTGEQR PPPQGETGKE GWDPAVLASE GLEAPPSEKE 1350
EGEEGEEECG RDSDLSEEFE DLGTEAPFLP GVPGEVAEPL GQVPQLLLDP 1400
AAWDRDGESD GFADEEESGE EGEEDQEEGR EPGAGRWGPG SSVGSLQALS 1450
SSQRGEFLES DSVSVSVPWD DSLRGAVAGA PKTALETESQ DSAEPSGSEE 1500
ESDPVSLERE DKVPGPLEIP SGMEDAGPGA DIIGVNGQGP NLEGKSQHVN 1550
GGVMNGLEQS EEVGQGMPLV SEGDRGSPFQ EEEGSALKTS WAGAPVHLGQ 1600
GQFLKFTQRE GDRESWSSGE D 1621
Length:1,621
Mass (Da):177,439
Last modified:May 1, 2007 - v2
Checksum:i0E4F967C11F44C13
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti130 – 1301V → A.
Corresponds to variant rs4278369 [ dbSNP | Ensembl ].
VAR_061301
Natural varianti815 – 8151V → I.1 Publication
Corresponds to variant rs951781 [ dbSNP | Ensembl ].
VAR_049814
Natural varianti1016 – 10161S → N.1 Publication
Corresponds to variant rs2365718 [ dbSNP | Ensembl ].
VAR_049815
Natural varianti1101 – 11011P → L.1 Publication
Corresponds to variant rs2886443 [ dbSNP | Ensembl ].
VAR_049816
Natural varianti1133 – 11331R → S.
Corresponds to variant rs17393797 [ dbSNP | Ensembl ].
VAR_049817
Natural varianti1275 – 12751P → L.3 Publications
Corresponds to variant rs3748570 [ dbSNP | Ensembl ].
VAR_049818

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241A → G in CAA46780. 1 Publication
Sequence conflicti39 – 391E → G in CAA46780. 1 Publication
Sequence conflicti45 – 451A → R in CAA46780. 1 Publication
Sequence conflicti96 – 961Q → E in CAA46780. 1 Publication
Sequence conflicti130 – 1301V → G in CAA46780. 1 Publication
Sequence conflicti161 – 1611C → L in CAA46780. 1 Publication
Sequence conflicti167 – 1671Missing in CAA46780. 1 Publication
Sequence conflicti205 – 2073GQA → DQT in CAA46780. 1 Publication
Sequence conflicti212 – 2121G → A in CAA46780. 1 Publication
Sequence conflicti221 – 2211G → V in CAA46780. 1 Publication
Sequence conflicti595 – 61218ELLKD…KEAVG → RAIKGCGGSETSRKRGCR in CAA46780. 1 Publication
Add
BLAST
Sequence conflicti857 – 90852QGAMN…RSPEE → KSGGNESSRKGNSRTTGVCG SEPRDIQTPGRGESGIIEIS GSMEPGEFEISRG in CAA46780. 1 Publication
Add
BLAST
Sequence conflicti975 – 9751E → K in CAA46780. 1 Publication
Sequence conflicti1008 – 10081I → F in CAA46780. 1 Publication
Sequence conflicti1050 – 10501A → T in CAA46780. 1 Publication
Sequence conflicti1235 – 12351P → L in CAA46780. 1 Publication
Sequence conflicti1256 – 12561Missing in CAA46780. 1 Publication
Sequence conflicti1314 – 132512DPTGE…PPPQG → TPLESRGHPLK in CAA46780. 1 Publication
Add
BLAST
Sequence conflicti1344 – 13452AP → E in CAA46780. 1 Publication
Sequence conflicti1472 – 14721S → N in BAE45713. 1 Publication
Sequence conflicti1542 – 15421L → M in BAE45713. 1 Publication
Sequence conflicti1563 – 15686VGQGMP → SGARNA in CAA46780. 1 Publication
Sequence conflicti1589 – 15913TSW → RSS in CAA46780. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL590666 Genomic DNA. Translation: CAI16338.1.
X65964 Genomic DNA. Translation: CAA46780.1.
AF004335 Genomic DNA. Translation: AAB64426.1.
AB073350 mRNA. Translation: BAE45713.1.
CCDSiCCDS1151.1.
PIRiS21424.
RefSeqiNP_006608.1. NM_006617.1.
UniGeneiHs.527971.

Genome annotation databases

EnsembliENST00000368223; ENSP00000357206; ENSG00000132688.
GeneIDi10763.
KEGGihsa:10763.
UCSCiuc001fpq.3. human.

Polymorphism databases

DMDMi146345464.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL590666 Genomic DNA. Translation: CAI16338.1 .
X65964 Genomic DNA. Translation: CAA46780.1 .
AF004335 Genomic DNA. Translation: AAB64426.1 .
AB073350 mRNA. Translation: BAE45713.1 .
CCDSi CCDS1151.1.
PIRi S21424.
RefSeqi NP_006608.1. NM_006617.1.
UniGenei Hs.527971.

3D structure databases

ProteinModelPortali P48681.
SMRi P48681. Positions 7-155, 220-311.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115983. 5 interactions.
STRINGi 9606.ENSP00000357206.

PTM databases

PhosphoSitei P48681.

Polymorphism databases

DMDMi 146345464.

Proteomic databases

MaxQBi P48681.
PaxDbi P48681.
PRIDEi P48681.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368223 ; ENSP00000357206 ; ENSG00000132688 .
GeneIDi 10763.
KEGGi hsa:10763.
UCSCi uc001fpq.3. human.

Organism-specific databases

CTDi 10763.
GeneCardsi GC01M156639.
H-InvDB HIX0001169.
HGNCi HGNC:7756. NES.
HPAi CAB005889.
CAB058692.
HPA007007.
HPA026111.
MIMi 600915. gene.
neXtProti NX_P48681.
PharmGKBi PA31556.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000113766.
HOVERGENi HBG006463.
InParanoidi P48681.
KOi K07609.
OMAi DHASLAP.
OrthoDBi EOG773XKP.
PhylomeDBi P48681.
TreeFami TF336633.

Miscellaneous databases

GeneWikii Nestin_(protein).
GenomeRNAii 10763.
NextBioi 40873.
PROi P48681.
SOURCEi Search...

Gene expression databases

ArrayExpressi P48681.
Bgeei P48681.
CleanExi HS_NES.
Genevestigatori P48681.

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

« Hide 'large scale' publications
  1. "Characterization of the human nestin gene reveals a close evolutionary relationship to neurofilaments."
    Dahlstrand J., McKay R.D.G., Zimmerman L.B., Lendahl U.
    J. Cell Sci. 103:589-597(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-1016; LEU-1101 AND LEU-1275.
    Tissue: Placenta.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Heterogeneity of neural progenitor cells revealed by enhancers in the nestin gene."
    Yaworsky P.J., Kappen C.
    Dev. Biol. 205:309-321(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 297-310.
  4. "Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma."
    Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S., Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S., Hirato J., Nakagawara A.
    Cancer Lett. 197:63-68(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 604-1621, VARIANT ILE-815.
    Tissue: Neuroblastoma.
  5. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680; SER-1409 AND SER-1418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311; THR-315; SER-325; THR-388; SER-398; SER-471; SER-548; SER-564; SER-578; SER-588; SER-746; SER-768; THR-851; SER-905 AND SER-1418, VARIANT [LARGE SCALE ANALYSIS] LEU-1275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-398; SER-471; SER-548 AND SER-680, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; SER-355; SER-358; SER-471; SER-548; SER-578; SER-680; SER-746; SER-768; SER-790; SER-820; SER-831; SER-894; SER-905; SER-913; SER-934; SER-1261; SER-1282; SER-1286; SER-1347; SER-1418; SER-1452; SER-1496; SER-1498; SER-1577; SER-1617 AND SER-1618, VARIANT [LARGE SCALE ANALYSIS] LEU-1275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNEST_HUMAN
AccessioniPrimary (citable) accession number: P48681
Secondary accession number(s): O00552, Q3LIF5, Q5SYZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 1, 2007
Last modified: July 9, 2014
This is version 115 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 1
    Human chromosome 1: 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

External Data

Dasty 3

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