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P31946

- 1433B_HUMAN

UniProt

P31946 - 1433B_HUMAN

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Protein

14-3-3 protein beta/alpha

Gene
YWHAB
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. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei58 – 581Interaction with phosphoserine on interacting protein By similarity
Sitei129 – 1291Interaction with phosphoserine on interacting protein By similarity

GO - Molecular functioni

  1. enzyme binding Source: BHF-UCL
  2. histone deacetylase binding Source: BHF-UCL
  3. phosphoprotein binding Source: BHF-UCL
  4. phosphoserine binding Source: BHF-UCL
  5. protein binding Source: UniProtKB
  6. protein domain specific binding Source: UniProtKB
  7. transcription corepressor activity Source: Ensembl

GO - Biological processi

  1. activation of MAPKK activity Source: Reactome
  2. apoptotic process Source: Reactome
  3. axon guidance Source: Reactome
  4. cytoplasmic sequestering of protein Source: BHF-UCL
  5. epidermal growth factor receptor signaling pathway Source: Reactome
  6. Fc-epsilon receptor signaling pathway Source: Reactome
  7. fibroblast growth factor receptor signaling pathway Source: Reactome
  8. gene expression Source: Reactome
  9. hippo signaling Source: Reactome
  10. innate immune response Source: Reactome
  11. insulin receptor signaling pathway Source: Reactome
  12. intrinsic apoptotic signaling pathway Source: Reactome
  13. MAPK cascade Source: Reactome
  14. membrane organization Source: Reactome
  15. mRNA metabolic process Source: Reactome
  16. negative regulation of protein dephosphorylation Source: BHF-UCL
  17. negative regulation of transcription, DNA-templated Source: Ensembl
  18. neurotrophin TRK receptor signaling pathway Source: Reactome
  19. positive regulation of catalytic activity Source: BHF-UCL
  20. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
  21. protein heterooligomerization Source: Ensembl
  22. protein targeting Source: Ensembl
  23. Ras protein signal transduction Source: Reactome
  24. RNA metabolic process Source: Reactome
  25. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_118607. Signaling by Hippo.
REACT_12002. ARMS-mediated activation.
REACT_12076. Frs2-mediated activation.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_2077. RAF activation.
REACT_23898. Rap1 signalling.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.
REACT_614. RAF phosphorylates MEK.
REACT_962. MEK activation.
SignaLinkiP31946.

Names & Taxonomyi

Protein namesi
Recommended name:
14-3-3 protein beta/alpha
Alternative name(s):
Protein 1054
Protein kinase C inhibitor protein 1
Short name:
KCIP-1
Cleaved into the following chain:
Gene namesi
Name:YWHAB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:12849. YWHAB.

Subcellular locationi

Cytoplasm. Melanosome
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic vesicle membrane Source: Reactome
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProtKB
  5. melanosome Source: UniProtKB-SubCell
  6. nucleus Source: Ensembl
  7. perinuclear region of cytoplasm Source: UniProtKB
  8. transcriptional repressor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37438.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24624614-3-3 protein beta/alphaPRO_0000367900Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 24624514-3-3 protein beta/alpha, N-terminally processedPRO_0000000003Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine; in 14-3-3 protein beta/alpha; alternate2 Publications
Modified residuei2 – 21N-acetylthreonine; in 14-3-3 protein beta/alpha, N-terminally processed2 Publications
Modified residuei60 – 601Phosphoserine By similarity
Modified residuei70 – 701N6-acetyllysine1 Publication
Modified residuei84 – 841Nitrated tyrosine By similarity
Modified residuei106 – 1061Nitrated tyrosine By similarity
Modified residuei117 – 1171N6-acetyllysine1 Publication
Modified residuei186 – 1861Phosphoserine By similarity

Post-translational modificationi

The alpha, brain-specific form differs from the beta form in being phosphorylated By similarity. Phosphorylated on Ser-60 by protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion By similarity.1 Publication
Isoform Short contains a N-acetylmethionine at position 1 By similarity.

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

MaxQBiP31946.
PaxDbiP31946.
PRIDEiP31946.

2D gel databases

OGPiP31946.
REPRODUCTION-2DPAGEIPI00216318.

PTM databases

PhosphoSiteiP31946.

Expressioni

Gene expression databases

ArrayExpressiP31946.
BgeeiP31946.
CleanExiHS_YWHAB.
GenevestigatoriP31946.

Organism-specific databases

HPAiCAB003759.
HPA007925.
HPA011212.

Interactioni

Subunit structurei

Homodimer. Interacts with SAMSN1 and PRKCE By similarity. Interacts with SSH1 and TORC2/CRTC2. Interacts with ABL1; the interaction results in cytoplasmic location of ABL1 and inhibition of cABL-mediated apoptosis. Interacts with ROR2 (dimer); the interaction results in phosphorylation of YWHAB on tyrosine residues. Interacts with GAB2 and YAP1 (phosphorylated form). Interacts with the phosphorylated (by AKT1) form of SRPK2. Interacts with PKA-phosphorylated AANAT. Interacts with MYO1C and SIRT2.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q763533EBI-359815,EBI-6248077From a different organism.
ADAM22Q9P0K1-32EBI-359815,EBI-1567267
BRAFP150563EBI-359815,EBI-365980
CBLP226813EBI-359815,EBI-518228
CBX4O002572EBI-359815,EBI-722425
CDC25AP303048EBI-359815,EBI-747671
CDC25BP303054EBI-359815,EBI-1051746
CDK14O949215EBI-359815,EBI-1043945
CSNK1A1P678283EBI-359815,EBI-7540603From a different organism.
DACT1Q9NYF04EBI-359815,EBI-3951744
DYRK1AQ13627-23EBI-359815,EBI-1053621
GAB2Q9UQC24EBI-359815,EBI-975200
GEMP550403EBI-359815,EBI-744104
GemP550413EBI-359815,EBI-7082069From a different organism.
HDAC4P565243EBI-359815,EBI-308629
let-756Q111842EBI-359815,EBI-3843983From a different organism.
LRRK2Q5S0073EBI-359815,EBI-5323863
MAP3K3Q997592EBI-359815,EBI-307281
MAP3K5Q996833EBI-359815,EBI-476263
MARK2Q7KZI73EBI-359815,EBI-516560
MARK3P274484EBI-359815,EBI-707595
RAF1P0404917EBI-359815,EBI-365996
RMDN3Q96TC75EBI-359815,EBI-1056589
RND3P615872EBI-359815,EBI-1111534
Rnd3P615885EBI-359815,EBI-6930266From a different organism.
SRPK2P783622EBI-359815,EBI-593303
SSH1Q8WYL53EBI-359815,EBI-1222387
Synpo2Q91YE83EBI-359815,EBI-7623057From a different organism.
TSC2P498154EBI-359815,EBI-396587
YAP1P469375EBI-359815,EBI-1044059
YWHAEP622583EBI-359815,EBI-356498
Zfp36P228935EBI-359815,EBI-647803From a different organism.

Protein-protein interaction databases

BioGridi113361. 298 interactions.
DIPiDIP-743N.
IntActiP31946. 240 interactions.
MINTiMINT-99570.
STRINGi9606.ENSP00000300161.

Structurei

Secondary structure

1
246
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1713
Helixi21 – 3313
Helixi40 – 6930
Helixi75 – 10531
Helixi107 – 1104
Helixi114 – 13320
Helixi139 – 16123
Helixi167 – 18216
Helixi187 – 20216
Helixi203 – 2075
Turni210 – 2123
Helixi213 – 23220

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BQ0X-ray2.50A/B2-239[»]
2C23X-ray2.65A2-239[»]
4DNKX-ray2.20A/B1-246[»]
ProteinModelPortaliP31946.
SMRiP31946. Positions 1-234.

Miscellaneous databases

EvolutionaryTraceiP31946.

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.

Phylogenomic databases

eggNOGiCOG5040.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP31946.
KOiK16197.
OMAiMGREYRE.
OrthoDBiEOG7HHWT3.
PhylomeDBiP31946.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform Long (identifier: P31946-1) [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

MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY    50
KNVVGARRSS WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL 100
ELLDKYLIPN ATQPESKVFY LKMKGDYFRY LSEVASGDNK QTTVSNSQQA 150
YQEAFEISKK EMQPTHPIRL GLALNFSVFY YEILNSPEKA CSLAKTAFDE 200
AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD AGEGEN 246
Length:246
Mass (Da):28,082
Last modified:January 23, 2007 - v3
Checksum:i6BE1A9BF97468017
GO
Isoform Short (identifier: P31946-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: Missing.

Note: Contains a N-acetylmethionine at position 1 (By similarity).

Show »
Length:244
Mass (Da):27,850
Checksum:iCE0A59BF8C33FE2F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti99 – 991V → I Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
VAR_064762

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 22Missing in isoform Short. VSP_018632

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X57346 mRNA. Translation: CAA40621.1.
AK292717 mRNA. Translation: BAF85406.1.
AL008725 Genomic DNA. Translation: CAA15497.1.
CH471077 Genomic DNA. Translation: EAW75893.1.
CH471077 Genomic DNA. Translation: EAW75894.1.
CH471077 Genomic DNA. Translation: EAW75896.1.
BC001359 mRNA. Translation: AAH01359.1.
CCDSiCCDS13339.1. [P31946-1]
PIRiS34755.
RefSeqiNP_003395.1. NM_003404.4. [P31946-1]
NP_647539.1. NM_139323.3. [P31946-1]
UniGeneiHs.643544.

Genome annotation databases

EnsembliENST00000353703; ENSP00000300161; ENSG00000166913. [P31946-1]
ENST00000372839; ENSP00000361930; ENSG00000166913. [P31946-1]
GeneIDi7529.
KEGGihsa:7529.
UCSCiuc002xmt.3. human. [P31946-1]

Polymorphism databases

DMDMi1345590.

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X57346 mRNA. Translation: CAA40621.1 .
AK292717 mRNA. Translation: BAF85406.1 .
AL008725 Genomic DNA. Translation: CAA15497.1 .
CH471077 Genomic DNA. Translation: EAW75893.1 .
CH471077 Genomic DNA. Translation: EAW75894.1 .
CH471077 Genomic DNA. Translation: EAW75896.1 .
BC001359 mRNA. Translation: AAH01359.1 .
CCDSi CCDS13339.1. [P31946-1 ]
PIRi S34755.
RefSeqi NP_003395.1. NM_003404.4. [P31946-1 ]
NP_647539.1. NM_139323.3. [P31946-1 ]
UniGenei Hs.643544.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BQ0 X-ray 2.50 A/B 2-239 [» ]
2C23 X-ray 2.65 A 2-239 [» ]
4DNK X-ray 2.20 A/B 1-246 [» ]
ProteinModelPortali P31946.
SMRi P31946. Positions 1-234.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113361. 298 interactions.
DIPi DIP-743N.
IntActi P31946. 240 interactions.
MINTi MINT-99570.
STRINGi 9606.ENSP00000300161.

PTM databases

PhosphoSitei P31946.

Polymorphism databases

DMDMi 1345590.

2D gel databases

OGPi P31946.
REPRODUCTION-2DPAGE IPI00216318.

Proteomic databases

MaxQBi P31946.
PaxDbi P31946.
PRIDEi P31946.

Protocols and materials databases

DNASUi 7529.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000353703 ; ENSP00000300161 ; ENSG00000166913 . [P31946-1 ]
ENST00000372839 ; ENSP00000361930 ; ENSG00000166913 . [P31946-1 ]
GeneIDi 7529.
KEGGi hsa:7529.
UCSCi uc002xmt.3. human. [P31946-1 ]

Organism-specific databases

CTDi 7529.
GeneCardsi GC20P043515.
HGNCi HGNC:12849. YWHAB.
HPAi CAB003759.
HPA007925.
HPA011212.
MIMi 601289. gene.
neXtProti NX_P31946.
PharmGKBi PA37438.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5040.
HOGENOMi HOG000240379.
HOVERGENi HBG050423.
InParanoidi P31946.
KOi K16197.
OMAi MGREYRE.
OrthoDBi EOG7HHWT3.
PhylomeDBi P31946.
TreeFami TF102003.

Enzyme and pathway databases

Reactomei REACT_118607. Signaling by Hippo.
REACT_12002. ARMS-mediated activation.
REACT_12076. Frs2-mediated activation.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_2077. RAF activation.
REACT_23898. Rap1 signalling.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.
REACT_614. RAF phosphorylates MEK.
REACT_962. MEK activation.
SignaLinki P31946.

Miscellaneous databases

ChiTaRSi YWHAB. human.
EvolutionaryTracei P31946.
GeneWikii YWHAB.
GenomeRNAii 7529.
NextBioi 29453.
PROi P31946.
SOURCEi Search...

Gene expression databases

ArrayExpressi P31946.
Bgeei P31946.
CleanExi HS_YWHAB.
Genevestigatori P31946.

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. "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].
    Tissue: Keratinocyte.
  2. "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] (ISOFORM LONG).
    Tissue: Thymus.
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Skin.
  6. Bienvenut W.V., Zebisch A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-11; 14-57; 63-70; 106-117; 130-169 AND 215-246, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  7. "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 3-20.
    Tissue: Platelet.
  8. "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.
  9. "The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector."
    Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G., Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H., Okamoto M., Montminy M.
    Cell 119:61-74(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRTC2.
  10. "A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia."
    Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.
    J. Cell Biol. 165:465-471(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SSH1.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  12. "Inactivation of YAP oncoprotein by the Hippo pathway is involved in cell contact inhibition and tissue growth control."
    Zhao B., Wei X., Li W., Udan R.S., Yang Q., Kim J., Xie J., Ikenoue T., Yu J., Li L., Zheng P., Ye K., Chinnaiyan A., Halder G., Lai Z.C., Guan K.L.
    Genes Dev. 21:2747-2761(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YAP1.
  13. "Homodimerization of Ror2 tyrosine kinase receptor induces 14-3-3(beta) phosphorylation and promotes osteoblast differentiation and bone formation."
    Liu Y., Ross J.F., Bodine P.V.N., Billiard J.
    Mol. Endocrinol. 21:3050-3061(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ROR2, FUNCTION, PHOSPHORYLATION, DIMERIZATION, IDENTIFICATION BY MASS SPECTROMETRY.
  14. "Sirt2 interacts with 14-3-3 beta/gamma and down-regulates the activity of p53."
    Jin Y.H., Kim Y.J., Kim D.W., Baek K.H., Kang B.Y., Yeo C.Y., Lee K.Y.
    Biochem. Biophys. Res. Commun. 368:690-695(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIRT2.
  15. "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.
  16. "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: FUNCTION, INTERACTION WITH SRPK2.
  17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "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-70 AND LYS-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Crystal structure of human myosin 1c - the motor in GLUT4 exocytosis: implications for Ca(2+)-regulation and 14-3-3 binding."
    Stefan Munnich M.H., Manstein D.J.
    J. Mol. Biol. 426:2070-2081(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYO1C.
  22. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-239, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.
  23. Cited for: VARIANT ILE-99.

Entry informationi

Entry namei1433B_HUMAN
AccessioniPrimary (citable) accession number: P31946
Secondary accession number(s): A8K9K2, E1P616
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 167 of the entry and version 3 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 20
    Human chromosome 20: 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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