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

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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	245 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 pathway. 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.
Subunit structure	Homodimer. Heterodimerizes with YWHAE. Homo- and hetero-dimerization is inhibited by phosphorylation on Ser-58. Interacts with FOXO4, NOXA1, SSH1 and ARHGEF2. Interacts with PCTK1 and BSPRY By similarity. Interacts with WEE1 (C-terminal) 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 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 acivity. 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 AANAT ('Thr-31' phosphorylated form); the interaction modulates AANAT enzymatic activity through preventing dephosphorylation and/or proteolysis and stabilizing substrate binding. Subsequently, a second molecule of AANAT ('Ser-205' phosphorylated form), can bind the other YWHAZ monomer with similar effect. Interacts with AKT1; the interaction phosphorylates YWHAZ and modulates dimerization.
Subcellular location	Cytoplasm. Melanosome. Note: Located to stage I to stage IV melanosomes.
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 Ser-58 by PKA; disrupts homodimerization and heterodimerization with YHAE and TP53. This phosphorylation appears to be activated by sphingosine. Phosphorylation on Thr-232; inhibits binding of RAF1.
Sequence similarities	Belongs to the 14-3-3 family.
Caution	Was originally (Ref.1) thought to have phospholipase A2 activity.

Ontologies

Keywords
Cellular component	Cytoplasm
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	anti-apoptosis Traceable author statement. Source: ProtInc signal transduction Traceable author statement. Source: ProtInc
Cellular component	melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	transcription factor binding Ref.13 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABL1	P00519	1	EBI-347088,EBI-375543
ADAM22	Q9P0K1-1	2	EBI-347088,EBI-1567258
ADAM22	Q9P0K1-3	2	EBI-347088,EBI-1567267
BRAF	P15056	1	EBI-347088,EBI-365980
C22orf9	Q6ICG6	1	EBI-347088,EBI-1053969
CFL1	P23528	1	EBI-347088,EBI-352733
DFFA	O00273	1	EBI-347088,EBI-727171
DISC1	Q9NRI5	2	EBI-347088,EBI-529989
EDC3	Q96F86	1	EBI-347088,EBI-997311
EGFR	P00533	1	EBI-347088,EBI-297353
EPB41L3	Q9Y2J2	1	EBI-347088,EBI-310986
HNRNPL	P14866	1	EBI-347088,EBI-719024
KIF5B	P33176	1	EBI-347088,EBI-355878
KLC1	Q07866	1	EBI-347088,EBI-721019
KLC4	Q9NSK0	1	EBI-347088,EBI-949319
LARP1	Q6PKG0	1	EBI-347088,EBI-1052114
LIMK1	P53667	1	EBI-347088,EBI-444403
MAP3K5	Q99683	1	EBI-347088,EBI-476263
MARK2	Q7KZI7	1	EBI-347088,EBI-516560
MET	P08581	1	EBI-347088,EBI-1039152
NADK	O95544	1	EBI-347088,EBI-743949
NCKAP1	Q9Y2A7	1	EBI-347088,EBI-389845
NOLC1	Q14978	1	EBI-347088,EBI-396155
PABPC4	Q13310	1	EBI-347088,EBI-372844
PAK4	O96013	1	EBI-347088,EBI-713738
QSK	Q9Y2K2	2	EBI-347088,EBI-1181460
RAF1	P04049	2	EBI-347088,EBI-365996
RAI14	Q9P0K7	1	EBI-347088,EBI-1023749
RALGPS2	Q86X27	1	EBI-347088,EBI-1050841
RPL31	P62899	1	EBI-347088,EBI-1053664
SAMD4B	Q5PRF9	1	EBI-347088,EBI-1047489
SF3B1	O75533	1	EBI-347088,EBI-876542
SFRS10	P62995	1	EBI-347088,EBI-725485
SIK1	P57059	1	EBI-347088,EBI-1181640
TJP2	Q9UDY2	1	EBI-347088,EBI-1042602
USP8	P40818	1	EBI-347088,EBI-1050865
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.5

Modified residue

58

1

Phosphoserine; by PKA and PKB/AKT1

Modified residue

184

1

Phosphoserine; by MAPK8

Modified residue

232

1

Phosphothreonine; by CK1

Experimental info

Mutagenesis

49

1

K → E: Loss of interaction with NOXA1. Ref.21

Mutagenesis

58

1

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

Mutagenesis

58

1

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

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.

Sequence conflict

22

1

M → V in AAH68456. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

245

Helix Strand Turn

Details...

Helix

3 – 15

13

Helix

19 – 31

13

Helix

38 – 65

28

Helix

78 – 103

26

Helix

105 – 108

4

Helix

112 – 131

20

Helix

138 – 159

22

Helix

165 – 180

16

Helix

185 – 201

17

Helix

203 – 205

3

Turn

208 – 210

3

Helix

211 – 229

19

Sequences

	Sequence		Length	Mass (Da)
	P63104-1 [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: 1577711] [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: 9512661] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Bone marrow.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Colon, Eye, Melanoma, PNS, Skin, Testis and Uterus.
[4]	"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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-18. Tissue: Platelet.
[5]	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.
[6]	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.
[7]	"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: 9360956] [Abstract] Cited for: PHOSPHORYLATION AT THR-232, INTERACTION WITH RAF1, FUNCTION.
[8]	"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: 11956222] [Abstract] Cited for: PHOSPHORYLATION AT SER-58, INTERACTION WITH AKT1.
[9]	"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: 12865427] [Abstract] Cited for: PHOSPHORYLATION AT SER-58, DIMERIZATION.
[10]	"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: 14578935] [Abstract] Cited for: INTERACTION WITH AANAT, FUNCTION.
[11]	"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: 15071501] [Abstract] Cited for: PHOSPHORYLATION AT SER-184, INTERACTION WITH BAX, FUNCTION, MUTAGENESIS OF SER-184.
[12]	"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: 15159416] [Abstract] Cited for: INTERACTION WITH SSH1.
[13]	"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: 16114898] [Abstract] Cited for: INTERACTION WITH MLLT7.
[14]	"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: 15660133] [Abstract] Cited for: INTERACTION WITH SSH1.
[15]	"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: 15883165] [Abstract] Cited for: PHOSPHORYLATION AT SER-58, MUTAGENESIS OF SER-58.
[16]	"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: 15696159] [Abstract] Cited for: INTERACTION WITH ABL1, MASS SPECTROMETRY, PHOSPHORYLATION AT SER-184, MUTAGENESIS OF SER-184.
[17]	"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: 15644438] [Abstract] Cited for: INTERACTION WITH AANAT, FUNCTION.
[18]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, MASS SPECTROMETRY. Tissue: Epithelium.
[19]	"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: 16376338] [Abstract] Cited for: PHOSPHORYLATION AT SER-58, DIMERIZATION, INTERACTION WITH TP53 AND YWHAE, FUNCTION, MUTAGENESIS OF SER-58.
[20]	"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: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[21]	"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: 17913709] [Abstract] Cited for: INTERACTION WITH NOXA1, MUTAGENESIS OF LYS-49.
[22]	"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: 14970201] [Abstract] Cited for: INTERACTION WITH ARHGEF2.
[23]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, MASS SPECTROMETRY.
[24]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[25]	"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: 10488331] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[26]	"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: 11336675] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH AANAT.
[27]	"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: 16246723] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH HISTONE H3 PHOSPHOPEPTIDE.
[28]	"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: 17235285] [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

EMBLGenBankDDBJ

M86400 mRNA. Translation: AAA36446.1.
U28964 mRNA. Translation: AAC52052.1.
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.
NP_001129172.1.
NP_001129173.1.
NP_001129174.1.
NP_003397.1.
NP_663723.1.

UniGene

Hs.492407
Hs.594673

3D structure databases

PDBPDBe

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	[»]
3CU8	X-ray	2.40	A/B	1-245	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P63104. 69 interactions.

PTM databases

PhosphoSite

P63104.

2-D gel databases

Cornea-2DPAGE

P29312.

DOSAC-COBS-2DPAGE

P63104.

OGP

P63104.

Proteomic databases

PRIDE

P63104.

Genome annotation databases

Ensembl

ENSG00000164924. Homo sapiens. [Contig view]

GeneID

7534.

KEGG

hsa:7534.

Organism-specific databases

GeneCards

GC08M102000.

H-InvDB

HIX0034328.

HGNC

HGNC:12855. YWHAZ.

HPA

CAB005065.

MIM

601288. gene.

PharmGKB

PA37444.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P63104.

OMA

P63104. VMDKNEL.

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.

Gene expression databases

ArrayExpress

P63104.

Bgee

P63104.

GermOnline

ENSG00000164924. Homo sapiens.

Family and domain databases

InterPro

IPR000308. 14-3-3.
[Graphical view]

Gene3D

G3DSA:1.20.190.20. 14-3-3. 1 hit.

PANTHER

PTHR18860. 14-3-3. 1 hit.

Pfam

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

PIRSF

PIRSF000868. 14-3-3. 1 hit.

PRINTS

PR00305. 1433ZETA.

ProDom

PD000600. 14-3-3. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

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

PROSITE

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

ProtoNet

Search...

Other Resources

DrugBank

DB01381. Ginkgo biloba.

NextBio

29475.

SOURCE

Search...

Entry information

Entry name

1433Z_HUMAN

Accession

Primary (citable) accession number: P63104
Secondary accession number(s): 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:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)