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P31947

- 1433S_HUMAN

UniProt

P31947 - 1433S_HUMAN

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Protein
14-3-3 protein sigma
Gene
SFN, HME1
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. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway. May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53.1 Publication
p53-regulated inhibitor of G2/M progression.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei56 – 561Interaction with phosphoserine on interacting protein
Sitei129 – 1291Interaction with phosphoserine on interacting protein

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. protein kinase C inhibitor activity Source: ProtInc

GO - Biological processi

  1. apoptotic process Source: Reactome
  2. establishment of skin barrier Source: UniProtKB
  3. intrinsic apoptotic signaling pathway Source: Reactome
  4. intrinsic apoptotic signaling pathway in response to DNA damage Source: HGNC
  5. keratinocyte differentiation Source: Ensembl
  6. keratinocyte proliferation Source: Ensembl
  7. membrane organization Source: Reactome
  8. negative regulation of cell proliferation Source: Ensembl
  9. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: HGNC
  10. negative regulation of protein kinase activity Source: ProtInc
  11. negative regulation of protein serine/threonine kinase activity Source: GOC
  12. positive regulation of cell growth Source: Ensembl
  13. positive regulation of epidermal cell differentiation Source: UniProtKB
  14. positive regulation of protein export from nucleus Source: Ensembl
  15. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
  16. regulation of cyclin-dependent protein serine/threonine kinase activity Source: Ensembl
  17. regulation of epidermal cell division Source: UniProtKB
  18. release of cytochrome c from mitochondria Source: HGNC
  19. signal transduction Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
SignaLinkiP31947.

Names & Taxonomyi

Protein namesi
Recommended name:
14-3-3 protein sigma
Alternative name(s):
Epithelial cell marker protein 1
Stratifin
Gene namesi
Name:SFN
Synonyms:HME1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10773. SFN.

Subcellular locationi

Cytoplasm. Nucleus By similarity. Secreted
Note: May be secreted by a non-classical secretory pathway.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytoplasmic vesicle membrane Source: Reactome
  3. cytosol Source: Reactome
  4. extracellular space Source: ProtInc
  5. extracellular vesicular exosome Source: UniProt
  6. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA177.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24824814-3-3 protein sigma
PRO_0000058643Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Phosphoserine1 Publication
Modified residuei248 – 2481Phosphoserine4 Publications

Post-translational modificationi

Ubiquitinated. Ubiquitination by RFFL induces proteasomal degradation and indirectly regulates p53/TP53 activation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP31947.
PaxDbiP31947.
PeptideAtlasiP31947.
PRIDEiP31947.

2D gel databases

OGPiP31947.
SWISS-2DPAGEP31947.

PTM databases

PhosphoSiteiP31947.

Expressioni

Tissue specificityi

Present mainly in tissues enriched in stratified squamous keratinizing epithelium.

Gene expression databases

BgeeiP31947.
CleanExiHS_SFN.
GenevestigatoriP31947.

Organism-specific databases

HPAiCAB006268.
CAB040552.
HPA011105.

Interactioni

Subunit structurei

Homodimer. Interacts with KRT17 and SAMSN1 By similarity. Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. Interacts with GAB2. Interacts with SRPK2. Interacts with COPS6. Interacts with RFWD2; this interaction leads to proteasomal degradation.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005192EBI-476295,EBI-375543
AJUBAQ96IF12EBI-476295,EBI-949782
BADQ929344EBI-476295,EBI-700771
COPS6Q7L5N17EBI-476295,EBI-486838
ERRFI1Q9UJM33EBI-476295,EBI-2941912
GPRIN2O602692EBI-476295,EBI-740397
HDAC4P565244EBI-476295,EBI-308629
HDAC5Q9UQL63EBI-476295,EBI-715576
HDAC7Q8WUI43EBI-476295,EBI-1048378
HNRNPDQ14103-47EBI-476295,EBI-432545
MARK3P274482EBI-476295,EBI-707595
PLK4O004442EBI-476295,EBI-746202
RAF1P040492EBI-476295,EBI-365996
REPS2Q8NFH8-22EBI-476295,EBI-8029141
RFWD2Q8NHY26EBI-476295,EBI-1176214
TP53P046374EBI-476295,EBI-366083
YWHAZP631042EBI-476295,EBI-347088

Protein-protein interaction databases

BioGridi109072. 138 interactions.
DIPiDIP-29861N.
IntActiP31947. 149 interactions.
MINTiMINT-108060.
STRINGi9606.ENSP00000340989.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1513
Helixi19 – 3113
Helixi38 – 6932
Helixi80 – 10425
Helixi107 – 1104
Helixi114 – 13421
Beta strandi137 – 1393
Helixi140 – 16122
Helixi167 – 18216
Helixi187 – 20418
Helixi205 – 2073
Helixi210 – 23021

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YWTX-ray2.40A/B1-248[»]
1YZ5X-ray2.80A/B1-248[»]
3IQJX-ray1.15A1-231[»]
3IQUX-ray1.05A1-231[»]
3IQVX-ray1.20A1-231[»]
3LW1X-ray1.28A1-248[»]
3MHRX-ray1.15A1-231[»]
3O8IX-ray2.00A1-231[»]
3P1NX-ray1.40A1-231[»]
3P1OX-ray1.90A1-231[»]
3P1PX-ray1.95A1-231[»]
3P1QX-ray1.70A1-231[»]
3P1RX-ray1.70A1-231[»]
3P1SX-ray1.65A1-231[»]
3SMKX-ray2.10A1-231[»]
3SMLX-ray1.90A1-231[»]
3SMMX-ray2.00A1-231[»]
3SMNX-ray2.00A1-231[»]
3SMOX-ray1.80A1-231[»]
3SPRX-ray1.99A1-231[»]
3T0LX-ray1.60A1-231[»]
3T0MX-ray1.62A1-231[»]
3U9XX-ray1.80A1-231[»]
3UX0X-ray1.75A1-231[»]
4DATX-ray1.40A1-231[»]
4DAUX-ray2.00A1-231[»]
4DHMX-ray1.70A1-231[»]
4DHNX-ray1.80A1-231[»]
4DHOX-ray1.70A1-231[»]
4DHPX-ray1.75A1-231[»]
4DHQX-ray1.75A1-231[»]
4DHRX-ray1.40A1-231[»]
4DHSX-ray1.74A1-231[»]
4DHTX-ray1.80A1-231[»]
4DHUX-ray1.67A1-231[»]
4FL5X-ray1.90A/B1-231[»]
4FR3X-ray1.90A1-231[»]
4HQWX-ray2.35A1-231[»]
4HRUX-ray3.15A1-231[»]
4IEAX-ray1.70A1-231[»]
4JC3X-ray2.05A1-231[»]
4JDDX-ray2.10A1-231[»]
ProteinModelPortaliP31947.
SMRiP31947. Positions 1-231.

Miscellaneous databases

EvolutionaryTraceiP31947.

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.

Phylogenomic databases

eggNOGiCOG5040.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP31947.
KOiK06644.
OMAiEQKGNEE.
OrthoDBiEOG7HHWT3.
PhylomeDBiP31947.
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: P31947-1) [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

MERASLIQKA KLAEQAERYE DMAAFMKGAV EKGEELSCEE RNLLSVAYKN    50
VVGGQRAAWR VLSSIEQKSN EEGSEEKGPE VREYREKVET ELQGVCDTVL 100
GLLDSHLIKE AGDAESRVFY LKMKGDYYRY LAEVATGDDK KRIIDSARSA 150
YQEAMDISKK EMPPTNPIRL GLALNFSVFH YEIANSPEEA ISLAKTTFDE 200
AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG EAPQEPQS 248
Length:248
Mass (Da):27,774
Last modified:July 1, 1993 - v1
Checksum:i7F4B44E3AA59ECE6
GO
Isoform 2 (identifier: P31947-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     85-116: Missing.

Note: No experimental confirmation available.

Show »
Length:216
Mass (Da):24,336
Checksum:i14CBC2F26014D926
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti155 – 1551M → I.
Corresponds to variant rs11542705 [ dbSNP | Ensembl ].
VAR_048095

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei85 – 11632Missing in isoform 2.
VSP_021768Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 771K → M in CAG46703. 1 Publication
Sequence conflicti120 – 1201Y → H in AAA59546. 1 Publication
Sequence conflicti242 – 2421A → V in AAA59546. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M93010 mRNA. Translation: AAA59546.1.
X57348 mRNA. Translation: CAA40623.1.
AF029081 Genomic DNA. Translation: AAC52029.1.
AF029082 mRNA. Translation: AAC52030.1.
CR541905 mRNA. Translation: CAG46703.1.
CR541926 mRNA. Translation: CAG46724.1.
AL034380 Genomic DNA. Translation: CAB92118.1.
BC000329 mRNA. Translation: AAH00329.1.
BC000995 mRNA. Translation: AAH00995.1.
BC001550 mRNA. Translation: AAH01550.1.
BC002995 mRNA. Translation: AAH02995.1.
BC023552 mRNA. Translation: AAH23552.1.
CCDSiCCDS288.1. [P31947-1]
PIRiS34753.
S38956.
RefSeqiNP_006133.1. NM_006142.3. [P31947-1]
UniGeneiHs.523718.

Genome annotation databases

EnsembliENST00000339276; ENSP00000340989; ENSG00000175793. [P31947-1]
GeneIDi2810.
KEGGihsa:2810.
UCSCiuc001bnc.1. human. [P31947-1]

Polymorphism databases

DMDMi398953.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M93010 mRNA. Translation: AAA59546.1 .
X57348 mRNA. Translation: CAA40623.1 .
AF029081 Genomic DNA. Translation: AAC52029.1 .
AF029082 mRNA. Translation: AAC52030.1 .
CR541905 mRNA. Translation: CAG46703.1 .
CR541926 mRNA. Translation: CAG46724.1 .
AL034380 Genomic DNA. Translation: CAB92118.1 .
BC000329 mRNA. Translation: AAH00329.1 .
BC000995 mRNA. Translation: AAH00995.1 .
BC001550 mRNA. Translation: AAH01550.1 .
BC002995 mRNA. Translation: AAH02995.1 .
BC023552 mRNA. Translation: AAH23552.1 .
CCDSi CCDS288.1. [P31947-1 ]
PIRi S34753.
S38956.
RefSeqi NP_006133.1. NM_006142.3. [P31947-1 ]
UniGenei Hs.523718.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YWT X-ray 2.40 A/B 1-248 [» ]
1YZ5 X-ray 2.80 A/B 1-248 [» ]
3IQJ X-ray 1.15 A 1-231 [» ]
3IQU X-ray 1.05 A 1-231 [» ]
3IQV X-ray 1.20 A 1-231 [» ]
3LW1 X-ray 1.28 A 1-248 [» ]
3MHR X-ray 1.15 A 1-231 [» ]
3O8I X-ray 2.00 A 1-231 [» ]
3P1N X-ray 1.40 A 1-231 [» ]
3P1O X-ray 1.90 A 1-231 [» ]
3P1P X-ray 1.95 A 1-231 [» ]
3P1Q X-ray 1.70 A 1-231 [» ]
3P1R X-ray 1.70 A 1-231 [» ]
3P1S X-ray 1.65 A 1-231 [» ]
3SMK X-ray 2.10 A 1-231 [» ]
3SML X-ray 1.90 A 1-231 [» ]
3SMM X-ray 2.00 A 1-231 [» ]
3SMN X-ray 2.00 A 1-231 [» ]
3SMO X-ray 1.80 A 1-231 [» ]
3SPR X-ray 1.99 A 1-231 [» ]
3T0L X-ray 1.60 A 1-231 [» ]
3T0M X-ray 1.62 A 1-231 [» ]
3U9X X-ray 1.80 A 1-231 [» ]
3UX0 X-ray 1.75 A 1-231 [» ]
4DAT X-ray 1.40 A 1-231 [» ]
4DAU X-ray 2.00 A 1-231 [» ]
4DHM X-ray 1.70 A 1-231 [» ]
4DHN X-ray 1.80 A 1-231 [» ]
4DHO X-ray 1.70 A 1-231 [» ]
4DHP X-ray 1.75 A 1-231 [» ]
4DHQ X-ray 1.75 A 1-231 [» ]
4DHR X-ray 1.40 A 1-231 [» ]
4DHS X-ray 1.74 A 1-231 [» ]
4DHT X-ray 1.80 A 1-231 [» ]
4DHU X-ray 1.67 A 1-231 [» ]
4FL5 X-ray 1.90 A/B 1-231 [» ]
4FR3 X-ray 1.90 A 1-231 [» ]
4HQW X-ray 2.35 A 1-231 [» ]
4HRU X-ray 3.15 A 1-231 [» ]
4IEA X-ray 1.70 A 1-231 [» ]
4JC3 X-ray 2.05 A 1-231 [» ]
4JDD X-ray 2.10 A 1-231 [» ]
ProteinModelPortali P31947.
SMRi P31947. Positions 1-231.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109072. 138 interactions.
DIPi DIP-29861N.
IntActi P31947. 149 interactions.
MINTi MINT-108060.
STRINGi 9606.ENSP00000340989.

Chemistry

BindingDBi P31947.
ChEMBLi CHEMBL1909482.

PTM databases

PhosphoSitei P31947.

Polymorphism databases

DMDMi 398953.

2D gel databases

OGPi P31947.
SWISS-2DPAGE P31947.

Proteomic databases

MaxQBi P31947.
PaxDbi P31947.
PeptideAtlasi P31947.
PRIDEi P31947.

Protocols and materials databases

DNASUi 2810.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000339276 ; ENSP00000340989 ; ENSG00000175793 . [P31947-1 ]
GeneIDi 2810.
KEGGi hsa:2810.
UCSCi uc001bnc.1. human. [P31947-1 ]

Organism-specific databases

CTDi 2810.
GeneCardsi GC01P027189.
HGNCi HGNC:10773. SFN.
HPAi CAB006268.
CAB040552.
HPA011105.
MIMi 601290. gene.
neXtProti NX_P31947.
PharmGKBi PA177.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5040.
HOGENOMi HOG000240379.
HOVERGENi HBG050423.
InParanoidi P31947.
KOi K06644.
OMAi EQKGNEE.
OrthoDBi EOG7HHWT3.
PhylomeDBi P31947.
TreeFami TF102003.

Enzyme and pathway databases

Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
SignaLinki P31947.

Miscellaneous databases

EvolutionaryTracei P31947.
GeneWikii Stratifin.
GenomeRNAii 2810.
NextBioi 11071.
PROi P31947.
SOURCEi Search...

Gene expression databases

Bgeei P31947.
CleanExi HS_SFN.
Genevestigatori P31947.

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. "Complementary DNA cloning of a novel epithelial cell marker protein, HME1, that may be down-regulated in neoplastic mammary cells."
    Prasad G.L., Valverius E.M., McDuffie E., Cooper H.L.
    Cell Growth Differ. 3:507-513(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Epithelium.
  2. "Molecular cloning and expression of the transformation sensitive epithelial marker stratifin. A member of a protein family that has been involved in the protein kinase C signalling pathway."
    Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., Walbum E., Vandekerckhove J., Celis J.E.
    J. Mol. Biol. 231:982-998(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 19-25; 42-49; 118-122; 130-139; 149-159; 161-181; 196-199; 225-229 AND 231-239.
    Tissue: Keratinocyte.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "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].
  6. "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] (ISOFORMS 1 AND 2).
    Tissue: Cervix, Lung and Placenta.
  7. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
    Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
    Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 42-49 AND 118-122.
    Tissue: Keratinocyte.
  8. "Exportin 7 defines a novel general nuclear export pathway."
    Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.
    EMBO J. 23:3227-3236(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH XPO7; ARHGAP1; EIF4A1; VPS26A; VPS29 AND VPS35.
  9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing MDM2."
    Yang W., Dicker D.T., Chen J., El-Deiry W.S.
    Cell Cycle 7:670-682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MDM2 UBIQUITINATION, UBIQUITINATION BY RFFL.
  11. "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.
  12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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.
  15. "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-5 AND SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "COP9 signalosome subunit 6 stabilizes COP1, which functions as an E3 ubiquitin ligase for 14-3-3sigma."
    Choi H.H., Gully C., Su C.H., Velazquez-Torres G., Chou P.C., Tseng C., Zhao R., Phan L., Shaiken T., Chen J., Yeung S.C., Lee M.H.
    Oncogene 30:4791-4801(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COPS6 AND RFWD2.
  18. "A structural basis for 14-3-3sigma functional specificity."
    Wilker E.W., Grant R.A., Artim S.C., Yaffe M.B.
    J. Biol. Chem. 280:18891-18898(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH PHOSPHOSERINE PEPTIDE.
  19. "Identification and structural characterization of two 14-3-3 binding sites in the human peptidylarginine deiminase type VI."
    Rose R., Rose M., Ottmann C.
    J. Struct. Biol. 180:65-72(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-231 IN COMPLEX WITH PADI6 PHOSPHOPEPTIDES.

Entry informationi

Entry namei1433S_HUMAN
AccessioniPrimary (citable) accession number: P31947
Secondary accession number(s): Q6FH30, Q6FH51, Q96DH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: September 3, 2014
This is version 154 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 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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