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P63104 (1433Z_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
14-3-3 protein zeta/delta
Alternative name(s):
Protein kinase C inhibitor protein 1
Short name=KCIP-1
Gene names
Name:YWHAZ
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.14 Ref.15 Ref.21 Ref.23

Subunit structure

Interacts with CDK16 and BSPRY By similarity. Interacts with WEE1 (C-terminal). Interacts with SAMSN1 By similarity. Interacts with MLF1 (phosphorylated form); the interaction retains it in the cytoplasm By similarity. Interacts with Thr-phosphorylated ITGB2 By similarity. Interacts with BCL2L11 By similarity. Homodimer. Heterodimerizes with YWHAE. Homo- and hetero-dimerization is inhibited by phosphorylation on Ser-58. Interacts with FOXO4, NOXA1, SSH1 and ARHGEF2. Interacts with Pseudomonas aeruginosa exoS (unphosphorylated form). Interacts with BAX; the interaction occurs in the cytoplasm. Under stress conditions, MAPK8-mediated phosphorylation releases BAX to mitochondria. Interacts with phosphorylated RAF1; the interaction is inhibited when YWHAZ is phosphorylated on Thr-232. Interacts with TP53; the interaction enhances p53 transcriptional activity. The Ser-58 phosphorylated form inhibits this interaction and p53 transcriptional activity. Interacts with ABL1 (phosphorylated form); the interaction retains ABL1 in the cytoplasm. Interacts with PKA-phosphorylated AANAT; the interaction modulates AANAT enzymatic activity by increasing affinity for arylalkylamines and acetyl-CoA and protecting the enzyme from dephosphorylation and proteasomal degradation. It may also prevent thiol-dependent inactivation. Interacts with AKT1; the interaction phosphorylates YWHAZ and modulates dimerization. Interacts with GAB2 and TLK2. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.23 Ref.25 Ref.26 Ref.27

Subcellular location

Cytoplasm. Melanosome. Note: Located to stage I to stage IV melanosomes. Ref.24

Post-translational modification

The delta, brain-specific form differs from the zeta form in being phosphorylated By similarity. Phosphorylation on Ser-184 by MAPK8; promotes dissociation of BAX and translocation of BAX to mitochondria. Phosphorylation on Thr-232; inhibits binding of RAF1. Phosphorylated on Ser-58 by PKA and protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion. Phosphorylation on Ser-58 by PKA; disrupts homodimerization and heterodimerization with YHAE and TP53. Ref.9 Ref.12 Ref.13 Ref.15 Ref.19 Ref.20 Ref.23

Sequence similarities

Belongs to the 14-3-3 family.

Caution

Was originally (Ref.1) thought to have phospholipase A2 activity.

Sequence caution

The sequence AAH51814.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAH73141.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

histamine secretion by mast cell

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

membrane organization

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Traceable author statement PubMed 16130169. Source: ProtInc

platelet activation

Traceable author statement. Source: Reactome

positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway

Traceable author statement. Source: Reactome

protein targeting to mitochondrion

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement PubMed 16130169. Source: ProtInc

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cell leading edge

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Traceable author statement PubMed 16130169. Source: ProtInc

cytoplasmic vesicle membrane

Traceable author statement. Source: Reactome

cytosol

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 23580065. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProtKB

mast cell granule

Inferred from electronic annotation. Source: GOC

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionidentical protein binding

Inferred from physical interaction Ref.23PubMed 20618440. Source: IntAct

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 10102273. Source: UniProtKB

transcription factor binding

Inferred from physical interaction Ref.17. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-347088,EBI-347088
AANATQ294953EBI-347088,EBI-446413From a different organism.
ABL1P005192EBI-347088,EBI-375543
ACTBP607093EBI-347088,EBI-353944
ADAM22Q9P0K13EBI-347088,EBI-1567236
ADAM22Q9P0K1-33EBI-347088,EBI-1567267
ARAFP103983EBI-347088,EBI-365961
ARHGEF2Q929742EBI-347088,EBI-302405
ATP5A1P257053EBI-347088,EBI-351437
ATP5BP065762EBI-347088,EBI-356231
BADQ929345EBI-347088,EBI-700771
BadQ613373EBI-347088,EBI-400328From a different organism.
BRAFP150563EBI-347088,EBI-365980
CALM3P621582EBI-347088,EBI-397435
CBX4O00257-32EBI-347088,EBI-4392727
CDC25AP303042EBI-347088,EBI-747671
CDC25BP303054EBI-347088,EBI-1051746
CDK17Q005372EBI-347088,EBI-624648
CDK18Q070022EBI-347088,EBI-746238
CFL1P235283EBI-347088,EBI-352733
CPS1P313272EBI-347088,EBI-536811
CSNK1A1P678284EBI-347088,EBI-7540603From a different organism.
EEF1A1P681042EBI-347088,EBI-352162
EGFRP005334EBI-347088,EBI-297353
ENO1P067332EBI-347088,EBI-353877
FSCN1Q166583EBI-347088,EBI-351076
GCH1P307934EBI-347088,EBI-958183
GSK3BP498414EBI-347088,EBI-373586
HDAC4P565245EBI-347088,EBI-308629
HDAC5Q9UQL62EBI-347088,EBI-715576
HDAC7Q8WUI43EBI-347088,EBI-1048378
HIST1H2AMP0C0S82EBI-347088,EBI-1390628
HIST1H3DP684313EBI-347088,EBI-79722
HIST2H4BP628053EBI-347088,EBI-302023
HNRNPCP079102EBI-347088,EBI-357966
HSPB1P047922EBI-347088,EBI-352682
KIF23Q022415EBI-347088,EBI-306852
LMNAP025452EBI-347088,EBI-351935
LRRK2Q5S0074EBI-347088,EBI-5323863
MAP3K5Q996833EBI-347088,EBI-476263
MAPTP106368EBI-347088,EBI-366182
MAPTP10636-39EBI-347088,EBI-7145070
MAPTP291722EBI-347088,EBI-7291149From a different organism.
MARK2Q7KZI76EBI-347088,EBI-516560
MARK3P274489EBI-347088,EBI-707595
MLTKQ9NYL24EBI-347088,EBI-602273
NCLP193382EBI-347088,EBI-346967
NPM1P067482EBI-347088,EBI-78579
PARD3Q8TEW04EBI-347088,EBI-81968
PRKCEQ021565EBI-347088,EBI-706254
PRMT5O147442EBI-347088,EBI-351098
RAF1P0404912EBI-347088,EBI-365996
REPS2Q8NFH8-22EBI-347088,EBI-8029141
RND3P6158711EBI-347088,EBI-1111534
Rnd3P615883EBI-347088,EBI-6930266From a different organism.
RPS3P233962EBI-347088,EBI-351193
SFNP319472EBI-347088,EBI-476295
SIK1P570594EBI-347088,EBI-1181640
SIK3Q9Y2K25EBI-347088,EBI-1181460
SORBS2O948752EBI-347088,EBI-311323
STK11Q158316EBI-347088,EBI-306838
STK25O005062EBI-347088,EBI-618295
TGFBR1P368974EBI-347088,EBI-1027557
TP53P046372EBI-347088,EBI-366083
TSC2P498157EBI-347088,EBI-396587
VCPP550722EBI-347088,EBI-355164
VIMP086702EBI-347088,EBI-353844
WEE1P302913EBI-347088,EBI-914695
YAP1P469373EBI-347088,EBI-1044059
YWHAEP622585EBI-347088,EBI-356498

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P63104-1)

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.
Isoform 2 (identifier: P63104-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-98: MDKNELVQKA...ELRDICNDVL → MSQPCRKLWRHNYETSSCIEFLK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24524514-3-3 protein zeta/delta
PRO_0000058627

Sites

Site561Interaction with phosphoserine on interacting protein By similarity
Site1271Interaction with phosphoserine on interacting protein By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7 Ref.31 Ref.35 Ref.36
Modified residue31N6-acetyllysine Ref.31
Modified residue581Phosphoserine; by PKA and PKB/AKT1 Ref.12 Ref.13 Ref.19 Ref.23
Modified residue681N6-acetyllysine Ref.31
Modified residue1841Phosphoserine; by MAPK8 Ref.15 Ref.20
Modified residue2071Phosphoserine Ref.30 Ref.32
Modified residue2321Phosphothreonine; by CK1 Ref.9 Ref.32

Natural variations

Alternative sequence1 – 9898MDKNE…CNDVL → MSQPCRKLWRHNYETSSCIE FLK in isoform 2.
VSP_047505

Experimental info

Mutagenesis491K → E: Loss of interaction with NOXA1. Ref.25
Mutagenesis581S → A: Loss of sphingosine-activated PKA phosphorylation. Promotes homodimerization and heterodimerization with YWHAE. Enhanced transcriptional activity of P53. Ref.19 Ref.23
Mutagenesis581S → E: Loss of homodimerization. Reduced dimerization with YWHAE. Significantly reduced interaction with P53. No enhancement of P53 transcriptional activity. Ref.19 Ref.23
Mutagenesis1841S → A: On DNA damage, loss of MAPK8-mediated phosphorylation. Loss of binding ABL1. Attenuates ABL1-mediated apoptosis. No loss of interaction with BAX under stress conditions. Inhibits translocation of BAX to mitochondria. Ref.15 Ref.20
Sequence conflict221M → V in AAH68456. Ref.5
Sequence conflict1361D → G in BAH12451. Ref.3

Secondary structure

......................... 245
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: D464DF2286BBFE60

FASTA24527,745
        10         20         30         40         50         60 
MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR 

        70         80         90        100        110        120 
VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QAESKVFYLK 

       130        140        150        160        170        180 
MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE 

       190        200        210        220        230        240 
ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG 


EGGEN 

« Hide

Isoform 2 [UniParc].

Checksum: BE97CE3F0A74C75C
Show »

FASTA17019,333

References

« Hide 'large scale' references
[1]"Cloning and expression of a human 14-3-3 protein mediating phospholipolysis. Identification of an arachidonoyl-enzyme intermediate during catalysis."
Zupan L.A., Steffens D.L., Berry C.A., Landt M.L., Gross R.W.
J. Biol. Chem. 267:8707-8710(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]"Two unique 5' untranslated regions in mRNAs encoding human 14-3-3 zeta: differential expression in hemopoietic cells."
Seluja G.A., Pietromonaco S.F., Elias L.
Biochim. Biophys. Acta 1395:281-287(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Bone marrow.
[3]"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. expand/collapse author list , 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 2).
Tissue: Hippocampus and Tongue.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORM 1).
Tissue: Brain, Colon, Eye, Melanoma, PNS, Skin, Testis and Uterus.
[6]"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 1-18.
Tissue: Platelet.
[7]Bienvenut W.V., Potts A., Barblan J., Claeys D., Quadroni M.
Submitted (NOV-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-9; 12-18; 28-49; 61-68; 86-91; 128-158 AND 213-222, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma and Platelet.
[8]Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 92-103; 140-157; 194-212 AND 223-245, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[9]"14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction."
Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y., Morrice N., Moelling K., Aitken A.
J. Biol. Chem. 272:28882-28888(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-232, INTERACTION WITH RAF1, FUNCTION.
[10]"Nuclear localization of protein kinase U-alpha is regulated by 14-3-3."
Zhang S., Xing H., Muslin A.J.
J. Biol. Chem. 274:24865-24872(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TLK2.
[11]"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.
[12]"Identification of 14-3-3zeta as a protein kinase B/Akt substrate."
Powell D.W., Rane M.J., Chen Q., Singh S., McLeish K.R.
J. Biol. Chem. 277:21639-21642(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-58, INTERACTION WITH AKT1.
[13]"The dimeric versus monomeric status of 14-3-3zeta is controlled by phosphorylation of Ser58 at the dimer interface."
Woodcock J.M., Murphy J., Stomski F.C., Berndt M.C., Lopez A.F.
J. Biol. Chem. 278:36323-36327(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-58, DIMERIZATION.
[14]"Cellular stabilization of the melatonin rhythm enzyme induced by nonhydrolyzable phosphonate incorporation."
Zheng W., Zhang Z., Ganguly S., Weller J.L., Klein D.C., Cole P.A.
Nat. Struct. Biol. 10:1054-1057(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AANAT, FUNCTION.
[15]"JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins."
Tsuruta F., Sunayama J., Mori Y., Hattori S., Shimizu S., Tsujimoto Y., Yoshioka K., Masuyama N., Gotoh Y.
EMBO J. 23:1889-1899(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-184, INTERACTION WITH BAX, FUNCTION, MUTAGENESIS OF SER-184.
[16]"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.
[17]"14-3-3 protein interacts with nuclear localization sequence of forkhead transcription factor FoxO4."
Obsilova V., Vecer J., Herman P., Pabianova A., Sulc M., Teisinger J., Boura E., Obsil T.
Biochemistry 44:11608-11617(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MLLT7.
[18]"Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin."
Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B., Sampath R., Bamburg J.R., Bernard O.
EMBO J. 24:473-486(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SSH1.
[19]"Sphingosine activates protein kinase A type II by a novel cAMP-independent mechanism."
Ma Y., Pitson S., Hercus T., Murphy J., Lopez A., Woodcock J.
J. Biol. Chem. 280:26011-26017(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-58, MUTAGENESIS OF SER-58.
[20]"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, PHOSPHORYLATION AT SER-184, MUTAGENESIS OF SER-184.
[21]"Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N-acetyltransferase mediated by phosphoserine-205."
Ganguly S., Weller J.L., Ho A., Chemineau P., Malpaux B., Klein D.C.
Proc. Natl. Acad. Sci. U.S.A. 102:1222-1227(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AANAT, FUNCTION.
[22]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"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: PHOSPHORYLATION AT SER-58, DIMERIZATION, INTERACTION WITH TP53 AND YWHAE, FUNCTION, MUTAGENESIS OF SER-58.
[24]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[25]"Regulation of Nox1 activity via PKA-mediated phosphorylation of NoxA1 and 14-3-3 binding."
Kim J.-S., Diebold B.A., Babior B.M., Knaus U.G., Bokoch G.M.
J. Biol. Chem. 282:34787-34800(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NOXA1, MUTAGENESIS OF LYS-49.
[26]"p21-activated kinase 1 phosphorylates and regulates 14-3-3 binding to GEF-H1, a microtubule-localized Rho exchange factor."
Zenke F.T., Krendel M., DerMardirossian C., King C.C., Bohl B.P., Bokoch G.M.
J. Biol. Chem. 279:18392-18400(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGEF2.
[27]"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.
[28]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"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].
[30]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[31]"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 MET-1; LYS-3 AND LYS-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"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-207 AND THR-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[33]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"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].
[36]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding."
Rittinger K., Budman J., Xu J., Volinia S., Cantley L.C., Smerdon S.J., Gamblin S.J., Yaffe M.B.
Mol. Cell 4:153-166(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[38]"Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation."
Obsil T., Ghirlando R., Klein D.C., Ganguly S., Dyda F.
Cell 105:257-267(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH AANAT.
[39]"Molecular basis for the recognition of phosphorylated and phosphoacetylated histone h3 by 14-3-3."
Macdonald N., Welburn J.P.I., Noble M.E.M., Nguyen A., Yaffe M.B., Clynes D., Moggs J.G., Orphanides G., Thomson S., Edmunds J.W., Clayton A.L., Endicott J.A., Mahadevan L.C.
Mol. Cell 20:199-211(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH HISTONE H3 PHOSPHOPEPTIDE.
[40]"Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis."
Ottmann C., Yasmin L., Weyand M., Veesenmeyer J.L., Diaz M.H., Palmer R.H., Francis M.S., Hauser A.R., Wittinghofer A., Hallberg B.
EMBO J. 26:902-913(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-230 IN COMPLEX WITH PSEUDOMONAS AERUGINOSA EXOS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86400 mRNA. Translation: AAA36446.1.
U28964 mRNA. Translation: AAC52052.1.
AK289945 mRNA. Translation: BAF82634.1.
AK296902 mRNA. Translation: BAH12451.1.
CH471060 Genomic DNA. Translation: EAW91823.1.
BC003623 mRNA. Translation: AAH03623.3.
BC051814 mRNA. Translation: AAH51814.1. Different initiation.
BC063824 mRNA. Translation: AAH63824.2.
BC068456 mRNA. Translation: AAH68456.2.
BC072426 mRNA. Translation: AAH72426.2.
BC073141 mRNA. Translation: AAH73141.1. Different initiation.
BC083508 mRNA. Translation: AAH83508.2.
BC099904 mRNA. Translation: AAH99904.1.
BC101483 mRNA. Translation: AAI01484.1.
BC108281 mRNA. Translation: AAI08282.1.
BC111951 mRNA. Translation: AAI11952.1.
PIRPSHUAM. A38246.
RefSeqNP_001129171.1. NM_001135699.1.
NP_001129172.1. NM_001135700.1.
NP_001129173.1. NM_001135701.1.
NP_001129174.1. NM_001135702.1.
NP_003397.1. NM_003406.3.
NP_663723.1. NM_145690.2.
XP_005251118.1. XM_005251061.1.
XP_005251119.1. XM_005251062.1.
XP_005251120.1. XM_005251063.1.
UniGeneHs.492407.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IB1X-ray2.70A/B/C/D1-245[»]
1QJAX-ray2.00A/B1-245[»]
1QJBX-ray2.00A/B1-245[»]
2C1JX-ray2.60A/B1-245[»]
2C1NX-ray2.00A/B1-245[»]
2O02X-ray1.50A/B1-230[»]
2WH0X-ray2.25A/B/C/D1-245[»]
3CU8X-ray2.40A/B1-245[»]
3NKXX-ray2.40A/B1-245[»]
3RDHX-ray2.39A/B/C/D1-245[»]
4BG6X-ray2.30A/B1-245[»]
4FJ3X-ray1.95A/B1-230[»]
4HKCX-ray2.20A1-245[»]
4IHLX-ray2.20A/B1-230[»]
4N7GX-ray2.25A1-230[»]
4N7YX-ray2.16A/B1-230[»]
4N84X-ray2.50A/B1-230[»]
ProteinModelPortalP63104.
SMRP63104. Positions 1-230.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113366. 371 interactions.
DIPDIP-563N.
IntActP63104. 513 interactions.
MINTMINT-89071.

Chemistry

DrugBankDB01381. Ginkgo biloba.

PTM databases

PhosphoSiteP63104.

Polymorphism databases

DMDM52000887.

2D gel databases

DOSAC-COBS-2DPAGEP63104.
OGPP63104.
UCD-2DPAGEP63104.

Proteomic databases

PaxDbP63104.
PRIDEP63104.

Protocols and materials databases

DNASU7534.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000353245; ENSP00000309503; ENSG00000164924. [P63104-1]
ENST00000395951; ENSP00000379281; ENSG00000164924. [P63104-1]
ENST00000395953; ENSP00000379283; ENSG00000164924. [P63104-1]
ENST00000395956; ENSP00000379286; ENSG00000164924. [P63104-1]
ENST00000395957; ENSP00000379287; ENSG00000164924. [P63104-1]
ENST00000395958; ENSP00000379288; ENSG00000164924. [P63104-1]
ENST00000419477; ENSP00000395114; ENSG00000164924. [P63104-1]
ENST00000457309; ENSP00000398599; ENSG00000164924. [P63104-1]
ENST00000522542; ENSP00000430072; ENSG00000164924. [P63104-2]
GeneID7534.
KEGGhsa:7534.
UCSCuc003yjv.2. human. [P63104-1]

Organism-specific databases

CTD7534.
GeneCardsGC08M101930.
HGNCHGNC:12855. YWHAZ.
HPACAB005065.
MIM601288. gene.
neXtProtNX_P63104.
PharmGKBPA37444.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5040.
HOVERGENHBG050423.
InParanoidP63104.
KOK16197.
OrthoDBEOG7HHWT3.
PhylomeDBP63104.
TreeFamTF102003.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_21257. Metabolism of RNA.
REACT_578. Apoptosis.
REACT_604. Hemostasis.
REACT_6900. Immune System.
REACT_71. Gene Expression.
SignaLinkP63104.

Gene expression databases

ArrayExpressP63104.
BgeeP63104.
GenevestigatorP63104.

Family and domain databases

Gene3D1.20.190.20. 1 hit.
InterProIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERPTHR18860. PTHR18860. 1 hit.
PfamPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFPIRSF000868. 14-3-3. 1 hit.
PRINTSPR00305. 1433ZETA.
SMARTSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMSSF48445. SSF48445. 1 hit.
PROSITEPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSYWHAZ. human.
EvolutionaryTraceP63104.
GeneWikiYWHAZ.
GenomeRNAi7534.
NextBio29475.
PROP63104.
SOURCESearch...

Entry information

Entry name1433Z_HUMAN
AccessionPrimary (citable) accession number: P63104
Secondary accession number(s): A8K1N0 expand/collapse secondary AC list , B7Z465, P29213, P29312, Q32P43, Q5XJ08, Q6GPI2, Q6IN74, Q6NUR9, Q6P3U9, Q86V33
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM