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UniProtKB/Swiss-Prot entry P63104

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name 1433Z_HUMAN
Primary accession number P63104
Secondary accession numbers P29213 P29312 Q32P43 Q5XJ08 Q6GPI2 Q6IN74 Q6NUR9 Q6P3U9 Q86V33
Integrated into Swiss-Prot on September 13, 2004
Sequence was last modified on September 13, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 59)
Name and origin of the protein
Protein name 14-3-3 protein zeta/delta
Synonyms Protein kinase C inhibitor protein 1
KCIP-1
Gene name
Name: YWHAZ
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=1577711 [NCBI, ExPASy, EBI, Israel, Japan]
Zupan L.A., Steffens D.L., Berry C.A., Landt M.L., Gross R.W.;
"Cloning and expression of a human 14-3-3 protein mediating phospholipolysis. Identification of an arachidonoyl-enzyme intermediate during catalysis.";
J. Biol. Chem. 267:8707-8710(1992).
[2]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Bone marrow;
DOI=10.1016/S0167-4781(97)00171-1; PubMed=9512661 [NCBI, ExPASy, EBI, Israel, Japan]
Seluja G.A., Pietromonaco S.F., Elias L.;
"Two unique 5' untranslated regions in mRNAs encoding human 14-3-3 zeta: differential expression in hemopoietic cells.";
Biochim. Biophys. Acta 1395:281-287(1998).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Colon, Eye, Melanoma, PNS, Skin, Testis, and Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
 PROTEIN SEQUENCE OF 1-18.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[5]
 PROTEIN SEQUENCE OF 1-9; 12-18; 28-49; 61-68; 86-91; 128-158 AND 213-222, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma, and Platelet;
Bienvenut W.V., Potts A., Barblan J., Claeys D., Quadroni M.;
Submitted (NOV-2005) to UniProtKB.
[6]
 PROTEIN SEQUENCE OF 140-157 AND 194-212, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
[7]
 INTERACTION WITH SSH1.
DOI=10.1083/jcb.200401136; PubMed=15159416 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia.";
J. Cell Biol. 165:465-471(2004).
[8]
 INTERACTION WITH MLLT7.
DOI=10.1021/bi050618r; PubMed=16114898 [NCBI, ExPASy, EBI, Israel, Japan]
Obsilova V., Vecer J., Herman P., Pabianova A., Sulc M., Teisinger J., Boura E., Obsil T.;
"14-3-3 protein interacts with nuclear localization sequence of forkhead transcription factor FoxO4.";
Biochemistry 44:11608-11617(2005).
[9]
 INTERACTION WITH SSH1.
DOI=10.1038/sj.emboj.7600543; PubMed=15660133 [NCBI, ExPASy, EBI, Israel, Japan]
Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B., Sampath R., Bamburg J.R., Bernard O.;
"Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin.";
EMBO J. 24:473-486(2005).
[10]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[11]
 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/pr060363j; PubMed=17081065 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[12]
 INTERACTION WITH NOXA1, AND MUTAGENESIS OF LYS-49.
DOI=10.1074/jbc.M704754200; PubMed=17913709 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.-S., Diebold B.A., Babior B.M., Knaus U.G., Bokoch G.M.;
"Regulation of Nox1 activity via PKA-mediated phosphorylation of NoxA1 and 14-3-3 binding.";
J. Biol. Chem. 282:34787-34800(2007).
[13]
 INTERACTION WITH ARHGEF2.
DOI=10.1074/jbc.M400084200; PubMed=14970201 [NCBI, ExPASy, EBI, Israel, Japan]
Zenke F.T., Krendel M., DerMardirossian C., King C.C., Bohl B.P., Bokoch G.M.;
"p21-activated kinase 1 phosphorylates and regulates 14-3-3 binding to GEF-H1, a microtubule-localized Rho exchange factor.";
J. Biol. Chem. 279:18392-18400(2004).
[14]
 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1016/S1097-2765(00)80363-9; PubMed=10488331 [NCBI, ExPASy, EBI, Israel, Japan]
Rittinger K., Budman J., Xu J., Volinia S., Cantley L.C., Smerdon S.J., Gamblin S.J., Yaffe M.B.;
"Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding.";
Mol. Cell 4:153-166(1999).
[15]
 X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH AANAT.
DOI=10.1016/S0092-8674(01)00316-6; PubMed=11336675 [NCBI, ExPASy, EBI, Israel, Japan]
Obsil T., Ghirlando R., Klein D.C., Ganguly S., Dyda F.;
"Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation.";
Cell 105:257-267(2001).
[16]
 X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH HISTONE H3 PHOSPHOPEPTIDE.
DOI=10.1016/j.molcel.2005.08.032; PubMed=16246723 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Molecular basis for the recognition of phosphorylated and phosphoacetylated histone h3 by 14-3-3.";
Mol. Cell 20:199-211(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M86400; AAA36446.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U28964; AAC52052.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003623; AAH03623.3; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC051814; AAH51814.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC063824; AAH63824.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC068456; AAH68456.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC072426; AAH72426.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC073141; AAH73141.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC083508; AAH83508.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC099904; AAH99904.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC101483; AAI01484.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC108281; AAI08282.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC111951; AAI11952.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A38246; PSHUAM.
RefSeq NP_003397.1; -.
NP_663723.1; -.
UniGene Hs.492407
3D structure databases
PDB
1IB1; X-ray; 2.70 A; A/B/C/D=1-245.[ExPASy / RCSB / EBI]
1QJA; X-ray; 2.00 A; A/B=1-245.[ExPASy / RCSB / EBI]
1QJB; X-ray; 2.00 A; A/B=1-245.[ExPASy / RCSB / EBI]
2C1J; X-ray; 2.60 A; A/B=1-245.[ExPASy / RCSB / EBI]
2C1N; X-ray; 2.00 A; A/B=1-245.[ExPASy / RCSB / EBI]
2O02; X-ray; 1.50 A; A/B=1-230.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1IB1; -.
1QJA; -.
1QJB; -.
2C1J; -.
2C1N; -.
2O02; -.
ModBase P63104.
Protein-protein interaction databases
IntAct P63104; -.
PTM databases
PhosphoSite P63104; -.
2D gel databases
Cornea-2DPAGE P29312; -.
DOSAC-COBS-2DPAGE P63104; -.
OGP P63104; -.
Organism-specific databases
H-InvDB HIX0034328; -.
HGNC HGNC:12855; YWHAZ.
GenAtlas YWHAZ.
HPA CAB005065; -.
MIM 601288; gene. [NCBI / EBI]
PharmGKB PA37444; -.
GeneCards P63104.
Gene expression databases
ArrayExpress P63104; -.
GermOnline ENSG00000164924; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from ProtInc).
GO:0008134; Molecular function: transcription factor binding (inferred from physical interaction from UniProtKB).
GO:0006916; Biological process: anti-apoptosis (traceable author statement from ProtInc).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000308; 14-3-3.
Graphical view of domain structure.
Gene3D G3DSA:1.20.190.20; 14-3-3; 1.
PANTHER PTHR18860; 14-3-3; 1.
Pfam PF00244; 14-3-3; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000868; 14-3-3; 1.
PRINTS PR00305; 1433ZETA.
ProDom PD000600; 14-3-3; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00101; 14_3_3; 1.
SMART graphical view of domain structure.
PROSITE PS00796; 1433_1; 1.
PS00797; 1433_2; 1.
BLOCKS P63104.
Genome annotation databases
Ensembl ENSG00000164924; Homo sapiens. [Contig view]
GeneID 7534; -.
KEGG hsa:7534; -.
Phylogenomic databases
HOVERGEN P63104; -.
Other
DrugBank DB01381; Ginkgo biloba.
LinkHub P63104; -.
SOURCE YWHAZ; Homo sapiens.
ProtoNet P63104.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   245  245     14-3-3 protein zeta/delta. PRO_0000058627
MOD_RES   1     1        N-acetylmethionine. 
MOD_RES   184   184        Phosphoserine (By similarity). 
MOD_RES   232   232        Phosphothreonine. 
MUTAGEN   49    49        K->E: Loss of interaction with NOXA1. 
CONFLICT   22    22        M -> V (in Ref. 3; AAH68456). 
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      
Sequence information
Length: 245 AA [This is the length of the unprocessed precursor] Molecular weight: 27745 Da [This is the MW of the unprocessed precursor] CRC64: D464DF2286BBFE60 [This is a checksum on the sequence] 
        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
P63104 in FASTA format

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View entry in raw text format (no links)
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