14-3-3 protein zeta/delta - Homo sapiens (Human)

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

Last modified November 25, 2008. Version 61. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

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Protein attributes

Sequence length	245 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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. Interacts with PCTK1. Binds to the C-terminal part of WEE1. Interacts with BSPRY. Binds to phosphorylated MLF1 and retains it in the cytoplasm By similarity. Interacts with MLLT7/FOXO4, NOXA1, SSH1 and ARHGEF2.
Subcellular location	Cytoplasm. Melanosome. Note= Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Post-translational modification	Isoform delta differs from isoform zeta in being phosphorylated By similarity.
Sequence similarities	Belongs to the 14-3-3 family.
Caution	Was originally (Ref.1) thought to have phospholipase A2 activity.

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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	protein domain specific binding Inferred from electronic annotation. Source: InterPro transcription factor binding Ref.8 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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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
SNF1LK	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.

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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

Amino acid modifications

Modified residue

N-acetylmethionine

Modified residue

184

Phosphoserine By similarity

Modified residue

232

Phosphothreonine

Experimental info

Mutagenesis

K → E: Loss of interaction with NOXA1

Sequence conflict

M → V in AAH68456. Ref.3

Secondary structure

245

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P63104-1 [UniParc].

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

« Hide

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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. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 140-157 AND 194-212, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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).
[15]	"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.
[16]	"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.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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.

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

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P63104.

PTM databases

PhosphoSite

P63104.

2-D gel databases

Cornea-2DPAGE

P29312.

DOSAC-COBS-2DPAGE

P63104.

OGP

P63104.

Genome annotation databases

Ensembl

ENSG00000164924. Homo sapiens. [Contig view]

GeneID

7534.

KEGG

hsa:7534.

Organism-specific databases

H-InvDB

HIX0034328.

HGNC

HGNC:12855. YWHAZ.

HPA

CAB005065.

MIM

601288. gene.

PharmGKB

PA37444.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOVERGEN

P63104.

Gene expression databases

ArrayExpress

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.

LinkHub

P63104.

NextBio

29475.

SOURCE

Search...

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Entry information

Entry name

1433Z_HUMAN

Accession

Primary (citable) accession number: P63104
Secondary accession number(s): P29213

Q86V33

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	September 13, 2004
Last modified:	November 25, 2008
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 8

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents