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

Names and origin

Protein names

Recommended name:
14-3-3 protein zeta/delta

Alternative name(s):
Protein kinase C inhibitor protein 1
Short name=KCIP-1

Gene names

Name:

YWHAZ

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	245 AA.
Sequence status	Complete.
Protein existence	Evidence 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. The sequence AAH73141.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	gene expression Traceable author statement. Source: Reactome histamine secretion by mast cell Inferred from electronic annotation. Source: Compara mRNA metabolic process Traceable author statement. Source: Reactome negative regulation of apoptotic process Traceable author statement PubMed 16130169. Source: ProtInc platelet activation Traceable author statement. Source: Reactome protein targeting to mitochondrion Inferred from electronic annotation. Source: Compara signal transduction Traceable author statement PubMed 16130169. Source: ProtInc
Cellular_component	cell leading edge Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: Compara nucleoplasm Traceable author statement. Source: Reactome perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara postsynaptic density Inferred from electronic annotation. Source: Compara protein complex Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AANAT	Q29495	3	EBI-347088,EBI-446413	From a different organism.
ABL1	P00519	2	EBI-347088,EBI-375543
ADAM22	Q9P0K1-3	3	EBI-347088,EBI-1567267
CBX4	O00257-3	2	EBI-347088,EBI-4392727
CFL1	P23528	2	EBI-347088,EBI-352733
EGFR	P00533	4	EBI-347088,EBI-297353
GCH1	P30793	4	EBI-347088,EBI-958183
GSK3B	P49841	4	EBI-347088,EBI-373586
LRRK2	Q5S007	3	EBI-347088,EBI-5323863
MAP3K5	Q99683	2	EBI-347088,EBI-476263
MAPT	P10636	5	EBI-347088,EBI-366182
MARK2	Q7KZI7	3	EBI-347088,EBI-516560
MARK3	P27448	6	EBI-347088,EBI-707595
MLTK	Q9NYL2	4	EBI-347088,EBI-602273
PARD3	Q8TEW0	3	EBI-347088,EBI-81968
RAF1	P04049	3	EBI-347088,EBI-365996
SIK1	P57059	4	EBI-347088,EBI-1181640
SIK3	Q9Y2K2	5	EBI-347088,EBI-1181460
STK25	O00506	2	EBI-347088,EBI-618295
TGFBR1	P36897	4	EBI-347088,EBI-1027557
VIM	P84198	5	EBI-347088,EBI-457639	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 245

245

14-3-3 protein zeta/delta

PRO_0000058627

Sites

Site

56

1

Interaction with phosphoserine on interacting protein By similarity

Site

127

1

Interaction with phosphoserine on interacting protein By similarity

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.7 Ref.30

Modified residue

3

1

N6-acetyllysine Ref.30

Modified residue

58

1

Phosphoserine; by PKA and PKB/AKT1 Ref.12 Ref.13 Ref.19 Ref.23

Modified residue

68

1

N6-acetyllysine Ref.30

Modified residue

184

1

Phosphoserine; by MAPK8 Ref.15 Ref.20

Modified residue

207

1

Phosphoserine Ref.29 Ref.31

Modified residue

232

1

Phosphothreonine; by CK1 Ref.9 Ref.31

Experimental info

Mutagenesis

49

1

K → E: Loss of interaction with NOXA1. Ref.25

Mutagenesis

58

1

S → A: Loss of sphingosine-activated PKA phosphorylation. Promotes homodimerization and heterodimerization with YWHAE. Enhanced transcriptional activity of P53. Ref.19 Ref.23

Mutagenesis

58

1

S → E: Loss of homodimerization. Reduced dimerization with YWHAE. Significantly reduced interaction with P53. No enhancement of P53 transcriptional activity. Ref.19 Ref.23

Mutagenesis

184

1

S → 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 conflict

22

1

M → V in AAH68456. Ref.5

Secondary structure

1

.

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.

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.

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.

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.

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.

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245

Helix Strand Turn

Details...

Helix

3 – 15

13

Helix

19 – 31

13

Helix

38 – 67

30

Turn

69 – 71

3

Helix

76 – 103

28

Helix

105 – 108

4

Helix

112 – 131

20

Helix

135 – 159

25

Helix

165 – 180

16

Helix

185 – 200

16

Helix

201 – 205

5

Turn

208 – 210

3

Helix

211 – 228

18

Sequences

	Sequence		Length	Mass (Da)
	P63104 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: D464DF2286BBFE60	FASTA	245	27,745
	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

References

	« Hide 'large scale' referencesShow '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]. 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]. 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. , 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]. Tissue: Hippocampus.
[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. , 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]. 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, 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, 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, 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], MASS SPECTROMETRY. 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]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[30]	"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, MASS SPECTROMETRY.
[31]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[32]	"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].
[33]	"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].
[34]	"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).
[35]	"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.
[36]	"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.
[37]	"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.
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.

IPI

IPI00021263.

PIR

PSHUAM. A38246.

RefSeq

NP_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.

UniGene

Hs.492407.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IB1	X-ray	2.70	A/B/C/D	1-245	[»]
1QJA	X-ray	2.00	A/B	1-245	[»]
1QJB	X-ray	2.00	A/B	1-245	[»]
2C1J	X-ray	2.60	A/B	1-245	[»]
2C1N	X-ray	2.00	A/B	1-245	[»]
2O02	X-ray	1.50	A/B	1-230	[»]
2WH0	X-ray	2.25	A/B/C/D	1-245	[»]
3CU8	X-ray	2.40	A/B	1-245	[»]
3NKX	X-ray	2.40	A/B	1-245	[»]
3RDH	X-ray	2.39	A/B/C/D	1-245	[»]
4FJ3	X-ray	1.95	A/B	1-230	[»]

ProteinModelPortal

P63104.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-563N.

IntAct

P63104. 159 interactions.

MINT

MINT-89071.

PTM databases

PhosphoSite

P63104.

Polymorphism databases

DMDM

52000887.

2D gel databases

DOSAC-COBS-2DPAGE

P63104.

OGP

P63104.

UCD-2DPAGE

P63104.

Proteomic databases

PaxDb

P63104.

PRIDE

P63104.

Protocols and materials databases

DNASU

7534.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000353245; ENSP00000309503; ENSG00000164924.
ENST00000395951; ENSP00000379281; ENSG00000164924.
ENST00000395953; ENSP00000379283; ENSG00000164924.
ENST00000395956; ENSP00000379286; ENSG00000164924.
ENST00000395957; ENSP00000379287; ENSG00000164924.
ENST00000395958; ENSP00000379288; ENSG00000164924.
ENST00000419477; ENSP00000395114; ENSG00000164924.
ENST00000457309; ENSP00000398599; ENSG00000164924.

GeneID

7534.

KEGG

hsa:7534.

UCSC

uc003yjv.2. human.

Organism-specific databases

CTD

7534.

GeneCards

GC08M101930.

HGNC

HGNC:12855. YWHAZ.

HPA

CAB005065.

MIM

601288. gene.

neXtProt

NX_P63104.

PharmGKB

PA37444.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5040.

HOVERGEN

HBG050423.

InParanoid

P63104.

KO

K16197.

OrthoDB

EOG4N30PR.

PhylomeDB

P63104.

Enzyme and pathway databases

Pathway_Interaction_DB

a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
pi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
foxopathway. FoxO family signaling.
igf1_pathway. IGF1 pathway.
insulin_glucose_pathway. Insulin-mediated glucose transport.
p38_mk2pathway. p38 signaling mediated by MAPKAP kinases.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
pi3kplctrkpathway. Trk receptor signaling mediated by PI3K and PLC-gamma.

Reactome

REACT_11123. Membrane Trafficking.
REACT_21257. Metabolism of RNA.
REACT_604. Hemostasis.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P63104.

Bgee

P63104.

Genevestigator

P63104.

GermOnline

ENSG00000164924. Homo sapiens.

Family and domain databases

Gene3D

1.20.190.20. 1 hit.

InterPro

IPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]

PANTHER

PTHR18860. PTHR18860. 1 hit.

Pfam

PF00244. 14-3-3. 1 hit.
[Graphical view]

PIRSF

PIRSF000868. 14-3-3. 1 hit.

PRINTS

PR00305. 1433ZETA.

SMART

SM00101. 14_3_3. 1 hit.
[Graphical view]

SUPFAM

SSF48445. 14-3-3. 1 hit.

PROSITE

PS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

YWHAZ. human.

DrugBank

DB01381. Ginkgo biloba.

EvolutionaryTrace

P63104.

GenomeRNAi

7534.

NextBio

29475.

SOURCE

Search...

Entry information

Entry name

1433Z_HUMAN

Accession

Primary (citable) accession number: P63104
Secondary accession number(s): A8K1N0 , 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:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.