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P62258

- 1433E_HUMAN

UniProt

P62258 - 1433E_HUMAN

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Protein

14-3-3 protein epsilon

Gene

YWHAE

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

Functioni

Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei57 – 571Interaction with phosphoserine on interacting protein
Sitei130 – 1301Interaction with phosphoserine on interacting protein

GO - Molecular functioni

  1. enzyme binding Source: UniProtKB
  2. histone deacetylase binding Source: BHF-UCL
  3. ion channel binding Source: BHF-UCL
  4. MHC class II protein complex binding Source: UniProt
  5. phosphoprotein binding Source: BHF-UCL
  6. phosphoserine binding Source: BHF-UCL
  7. poly(A) RNA binding Source: UniProtKB
  8. potassium channel regulator activity Source: BHF-UCL
  9. protein heterodimerization activity Source: BHF-UCL

GO - Biological processi

  1. apoptotic process Source: Reactome
  2. apoptotic signaling pathway Source: Reactome
  3. cerebral cortex development Source: Ensembl
  4. G2/M transition of mitotic cell cycle Source: Reactome
  5. hippocampus development Source: Ensembl
  6. hippo signaling Source: Reactome
  7. intracellular signal transduction Source: ProtInc
  8. intrinsic apoptotic signaling pathway Source: Reactome
  9. membrane organization Source: Reactome
  10. membrane repolarization during cardiac muscle cell action potential Source: BHF-UCL
  11. mitotic cell cycle Source: Reactome
  12. negative regulation of peptidyl-serine dephosphorylation Source: BHF-UCL
  13. neuron migration Source: Ensembl
  14. neurotrophin TRK receptor signaling pathway Source: Reactome
  15. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
  16. protein targeting Source: Ensembl
  17. regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
  18. regulation of heart rate by cardiac conduction Source: BHF-UCL
  19. regulation of heart rate by hormone Source: BHF-UCL
  20. regulation of membrane repolarization Source: BHF-UCL
  21. regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
  22. substantia nigra development Source: UniProt
  23. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_118607. Signaling by Hippo.
REACT_13526. NADE modulates death signalling.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_200744. HSF1 activation.
REACT_200780. Regulation of HSF1-mediated heat shock response.
SignaLinkiP62258.

Names & Taxonomyi

Protein namesi
Recommended name:
14-3-3 protein epsilon
Short name:
14-3-3E
Gene namesi
Name:YWHAE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:12851. YWHAE.

Subcellular locationi

Cytoplasm By similarity. Melanosome 2 Publications
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

GO - Cellular componenti

  1. cytoplasmic vesicle membrane Source: Reactome
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. focal adhesion Source: UniProtKB
  5. kinesin complex Source: Ensembl
  6. membrane Source: UniProtKB
  7. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

Orphaneti217385. 17p13.3 microduplication syndrome.
261257. Distal 17p13.3 microdeletion syndrome.
531. Miller-Dieker syndrome.
PharmGKBiPA37440.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25525514-3-3 protein epsilonPRO_0000058618Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei50 – 501N6-acetyllysine1 Publication
Modified residuei69 – 691N6-acetyllysine1 Publication
Modified residuei118 – 1181N6-acetyllysine1 Publication
Modified residuei123 – 1231N6-acetyllysine1 Publication
Modified residuei210 – 2101Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP62258.
PaxDbiP62258.
PeptideAtlasiP62258.
PRIDEiP62258.

2D gel databases

OGPiP42655.
UCD-2DPAGEP62258.

PTM databases

PhosphoSiteiP62258.

Miscellaneous databases

PMAP-CutDBP62258.

Expressioni

Gene expression databases

BgeeiP62258.
CleanExiHS_YWHAE.
ExpressionAtlasiP62258. baseline and differential.
GenevestigatoriP62258.

Organism-specific databases

HPAiCAB016200.
CAB021109.
CAB047350.
HPA008445.

Interactioni

Subunit structurei

Homodimer. Heterodimerizes with YWHAZ. Interacts with NDEL1, ARHGEF28 and TIAM2 (By similarity). Interacts with HCV core protein. Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm. Weakly interacts with CDKN1B. Interacts with GAB2. Interacts with phosphorylated GRB10. Interacts with PKA-phosphorylated AANAT. Interacts with the phosphorylated (by AKT1) form of SRPK2.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
O929725EBI-356498,EBI-9213553From a different organism.
APAF1O147272EBI-356498,EBI-446492
CBX4O00257-32EBI-356498,EBI-4392727
CDK14O949213EBI-356498,EBI-1043945
FBXO4Q9UKT55EBI-356498,EBI-960409
HDAC4P565244EBI-356498,EBI-308629
KANK1Q14678-23EBI-356498,EBI-6173812
LRRK2Q5S0076EBI-356498,EBI-5323863
MAP3K3Q997593EBI-356498,EBI-307281
MDM4O151513EBI-356498,EBI-398437
MLF1P583403EBI-356498,EBI-721328
Prdx6O352442EBI-356498,EBI-915490From a different organism.
Rnd3P615882EBI-356498,EBI-6930266From a different organism.
STACQ994692EBI-356498,EBI-2652799
WWTR1Q9GZV53EBI-356498,EBI-747743
YWHABP319463EBI-356498,EBI-359815
YWHAGP619814EBI-356498,EBI-359832
YWHAZP631045EBI-356498,EBI-347088

Protein-protein interaction databases

BioGridi113363. 314 interactions.
DIPiDIP-36676N.
IntActiP62258. 151 interactions.
MINTiMINT-4998623.
STRINGi9606.ENSP00000264335.

Structurei

Secondary structure

1
255
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1714Combined sources
Helixi20 – 3112Combined sources
Helixi39 – 7335Combined sources
Helixi76 – 10631Combined sources
Helixi108 – 1114Combined sources
Helixi115 – 13521Combined sources
Helixi138 – 16225Combined sources
Helixi168 – 18316Combined sources
Helixi188 – 20417Combined sources
Helixi205 – 2084Combined sources
Turni211 – 2133Combined sources
Helixi214 – 23118Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BR9X-ray1.75A1-233[»]
3UALX-ray1.80A1-232[»]
3UBWX-ray1.90A1-234[»]
ProteinModelPortaliP62258.
SMRiP62258. Positions 3-232.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62258.

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.Curated

Phylogenomic databases

eggNOGiCOG5040.
GeneTreeiENSGT00760000119116.
HOVERGENiHBG050423.
InParanoidiP62258.
KOiK06630.
OMAiMQESDKP.
OrthoDBiEOG7HHWT3.
PhylomeDBiP62258.
TreeFamiTF102003.

Family and domain databases

Gene3Di1.20.190.20. 1 hit.
InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P62258-1) [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
MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK
60 70 80 90 100
NVIGARRASW RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI
110 120 130 140 150
LDVLDKHLIP AANTGESKVF YYKMKGDYHR YLAEFATGND RKEAAENSLV
160 170 180 190 200
AYKAASDIAM TELPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD
210 220 230 240 250
DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE EQNKEALQDV

EDENQ
Length:255
Mass (Da):29,174
Last modified:July 5, 2004 - v1
Checksum:i07817CCBD1F75B26
GO
Isoform SV (identifier: P62258-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: Missing.

Note: Unable to dimerize with YWHAZ.

Show »
Length:233
Mass (Da):26,504
Checksum:i20302F1E0AB73C8A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1072KH → NY AA sequence (PubMed:2026444)Curated
Sequence conflicti143 – 1431E → F AA sequence (PubMed:2026444)Curated
Sequence conflicti148 – 1481S → T AA sequence (PubMed:2026444)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2222Missing in isoform SV. 2 PublicationsVSP_040621Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20972 mRNA. Translation: AAC50175.1.
U54778 mRNA. Translation: AAC50710.1.
U43399 mRNA. Translation: AAC50625.1.
U43430 mRNA. Translation: AAD00026.1.
U28936 mRNA. Translation: AAA75301.1.
AB017103 Genomic DNA. Translation: BAA32538.1.
AY883089 mRNA. Translation: AAX68683.1.
AK128785 mRNA. Translation: BAG54733.1.
AK295260 mRNA. Translation: BAG58249.1.
AK316185 mRNA. Translation: BAH14556.1.
BT007161 mRNA. Translation: AAP35825.1.
CH471108 Genomic DNA. Translation: EAW90628.1.
CH471108 Genomic DNA. Translation: EAW90629.1.
BC000179 mRNA. Translation: AAH00179.1.
BC001440 mRNA. Translation: AAH01440.1.
CCDSiCCDS11001.1. [P62258-1]
PIRiA61235.
I38947.
RefSeqiNP_006752.1. NM_006761.4. [P62258-1]
UniGeneiHs.513851.

Genome annotation databases

EnsembliENST00000264335; ENSP00000264335; ENSG00000108953. [P62258-1]
ENST00000571732; ENSP00000461762; ENSG00000108953. [P62258-2]
ENST00000616643; ENSP00000481059; ENSG00000274474. [P62258-1]
GeneIDi7531.
KEGGihsa:7531.
UCSCiuc002fsj.3. human. [P62258-1]

Polymorphism databases

DMDMi51702210.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20972 mRNA. Translation: AAC50175.1 .
U54778 mRNA. Translation: AAC50710.1 .
U43399 mRNA. Translation: AAC50625.1 .
U43430 mRNA. Translation: AAD00026.1 .
U28936 mRNA. Translation: AAA75301.1 .
AB017103 Genomic DNA. Translation: BAA32538.1 .
AY883089 mRNA. Translation: AAX68683.1 .
AK128785 mRNA. Translation: BAG54733.1 .
AK295260 mRNA. Translation: BAG58249.1 .
AK316185 mRNA. Translation: BAH14556.1 .
BT007161 mRNA. Translation: AAP35825.1 .
CH471108 Genomic DNA. Translation: EAW90628.1 .
CH471108 Genomic DNA. Translation: EAW90629.1 .
BC000179 mRNA. Translation: AAH00179.1 .
BC001440 mRNA. Translation: AAH01440.1 .
CCDSi CCDS11001.1. [P62258-1 ]
PIRi A61235.
I38947.
RefSeqi NP_006752.1. NM_006761.4. [P62258-1 ]
UniGenei Hs.513851.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BR9 X-ray 1.75 A 1-233 [» ]
3UAL X-ray 1.80 A 1-232 [» ]
3UBW X-ray 1.90 A 1-234 [» ]
ProteinModelPortali P62258.
SMRi P62258. Positions 3-232.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113363. 314 interactions.
DIPi DIP-36676N.
IntActi P62258. 151 interactions.
MINTi MINT-4998623.
STRINGi 9606.ENSP00000264335.

PTM databases

PhosphoSitei P62258.

Polymorphism databases

DMDMi 51702210.

2D gel databases

OGPi P42655.
UCD-2DPAGE P62258.

Proteomic databases

MaxQBi P62258.
PaxDbi P62258.
PeptideAtlasi P62258.
PRIDEi P62258.

Protocols and materials databases

DNASUi 7531.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264335 ; ENSP00000264335 ; ENSG00000108953 . [P62258-1 ]
ENST00000571732 ; ENSP00000461762 ; ENSG00000108953 . [P62258-2 ]
ENST00000616643 ; ENSP00000481059 ; ENSG00000274474 . [P62258-1 ]
GeneIDi 7531.
KEGGi hsa:7531.
UCSCi uc002fsj.3. human. [P62258-1 ]

Organism-specific databases

CTDi 7531.
GeneCardsi GC17M001247.
H-InvDB HIX0013751.
HIX0030006.
HGNCi HGNC:12851. YWHAE.
HPAi CAB016200.
CAB021109.
CAB047350.
HPA008445.
MIMi 605066. gene.
neXtProti NX_P62258.
Orphaneti 217385. 17p13.3 microduplication syndrome.
261257. Distal 17p13.3 microdeletion syndrome.
531. Miller-Dieker syndrome.
PharmGKBi PA37440.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5040.
GeneTreei ENSGT00760000119116.
HOVERGENi HBG050423.
InParanoidi P62258.
KOi K06630.
OMAi MQESDKP.
OrthoDBi EOG7HHWT3.
PhylomeDBi P62258.
TreeFami TF102003.

Enzyme and pathway databases

Reactomei REACT_118607. Signaling by Hippo.
REACT_13526. NADE modulates death signalling.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_200744. HSF1 activation.
REACT_200780. Regulation of HSF1-mediated heat shock response.
SignaLinki P62258.

Miscellaneous databases

ChiTaRSi YWHAE. human.
EvolutionaryTracei P62258.
GeneWikii YWHAE.
GenomeRNAii 7531.
NextBioi 29461.
PMAP-CutDB P62258.
PROi P62258.
SOURCEi Search...

Gene expression databases

Bgeei P62258.
CleanExi HS_YWHAE.
ExpressionAtlasi P62258. baseline and differential.
Genevestigatori P62258.

Family and domain databases

Gene3Di 1.20.190.20. 1 hit.
InterProi IPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view ]
PANTHERi PTHR18860. PTHR18860. 1 hit.
Pfami PF00244. 14-3-3. 1 hit.
[Graphical view ]
PIRSFi PIRSF000868. 14-3-3. 1 hit.
PRINTSi PR00305. 1433ZETA.
SMARTi SM00101. 14_3_3. 1 hit.
[Graphical view ]
SUPFAMi SSF48445. SSF48445. 1 hit.
PROSITEi PS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "14-3-3 epsilon has no homology to LIS1 and lies telomeric to it on chromosome 17p13.3 outside the Miller-Dieker syndrome chromosome region."
    Chong S.S., Tanigami A., Roschke A.V., Ledbetter D.H.
    Genome Res. 6:735-741(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Functional identification of a novel 14-3-3 epsilon splicing variant suggests dimerization is not necessary for 14-3-3 epsilon to inhibit UV-induced apoptosis."
    Han D., Ye G., Liu T., Chen C., Yang X., Wan B., Pan Y., Yu L.
    Biochem. Biophys. Res. Commun. 396:401-406(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SV), ALTERNATIVE SPLICING.
    Tissue: Brain.
  5. "Sequence determination of human epsilon 14-3-3 protein."
    Luk S.C.W., Lee C.Y., Waye M.M.Y.
    Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Heart.
  6. "14-3-3 epsilon genomic sequence."
    Tanigami A., Chong S.S., Ledbetter D.H.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "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 1 AND SV).
    Tissue: Caudate nucleus, Heart and Subthalamic nucleus.
  8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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).
    Tissue: Placenta.
  11. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-19.
    Tissue: Platelet.
  12. Bienvenut W.V.
    Submitted (MAY-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-19; 30-50 AND 131-170, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  13. "Isolation and partial characterization of the structures of fibroblast activating factor-related proteins from U937 cells."
    Demeter J., Medzihradszky D., Kha H., Goetzl E.J., Turck C.W.
    Immunology 72:350-354(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 103-108; 120-123; 131-141 AND 143-153.
    Tissue: Histiocytic lymphoma.
  14. Lubec G., Afjehi-Sadat L.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 131-141 AND 154-190, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  15. "Hepatitis C virus core protein interacts with 14-3-3 protein and activates the kinase Raf-1."
    Aoki H., Hayashi J., Moriyama M., Arakawa Y., Hino O.
    J. Virol. 74:1736-1741(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCV CORE PROTEIN.
  16. "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-binding switch in melatonin synthesis."
    Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H., Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T., Beauverger P., Ferry G., Boutin J.A., Klein D.C.
    Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AANAT.
  17. "Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization."
    Fujita N., Sato S., Katayama K., Tsuruo T.
    J. Biol. Chem. 277:28706-28713(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDKN1B, SUBCELLULAR LOCATION.
  18. "Phosphorylation of grb10 regulates its interaction with 14-3-3."
    Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J.
    J. Biol. Chem. 280:16987-16993(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRB10.
  19. "JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage."
    Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.
    Nat. Cell Biol. 7:278-285(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ABL1, IDENTIFICATION BY MASS SPECTROMETRY.
  20. "Protein kinase A phosphorylates and regulates dimerization of 14-3-3 epsilon."
    Gu Y.-M., Jin Y.-H., Choi J.-K., Baek K.-H., Yeo C.-Y., Lee K.-Y.
    FEBS Lett. 580:305-310(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YWHAZ.
  21. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  22. "Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein."
    Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M., James D.E., Daly R.J.
    EMBO J. 27:2305-2316(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAB2.
  23. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  24. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle and cell death in neurons."
    Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.
    J. Biol. Chem. 284:24512-24525(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRPK2.
  26. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50; LYS-69; LYS-118 AND LYS-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "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-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "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-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-233, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.

Entry informationi

Entry namei1433E_HUMAN
AccessioniPrimary (citable) accession number: P62258
Secondary accession number(s): B3KY71
, D3DTH5, P29360, P42655, Q4VJB6, Q53XZ5, Q63631, Q7M4R4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: November 26, 2014
This is version 128 of the entry and version 1 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3