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

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

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 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.

Ontologies

Keywords

   Cellular componentCytoplasm
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Biological processanti-apoptosis

Traceable author statement. Source: ProtInc

signal transduction

Traceable author statement. Source: ProtInc

   Cellular componentmelanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein domain specific binding

Inferred from electronic annotation. Source: InterPro

transcription factor binding Ref.8

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Amino acid modifications

Modified residue11N-acetylmethionine
Modified residue1841Phosphoserine By similarity
Modified residue2321Phosphothreonine

Experimental info

Mutagenesis491K → E: Loss of interaction with NOXA1
Sequence conflict221M → V in AAH68456. Ref.3

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P63104-1 [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

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: 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.

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.
PIRPSHUAM. A38246.
RefSeqNP_001129171.1.
NP_001129172.1.
NP_001129173.1.
NP_001129174.1.
NP_003397.1.
NP_663723.1.
UniGeneHs.492407
Hs.594673

3D structure databases

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[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP63104.

PTM databases

PhosphoSiteP63104.

2-D gel databases

Cornea-2DPAGEP29312.
DOSAC-COBS-2DPAGEP63104.
OGPP63104.

Genome annotation databases

EnsemblENSG00000164924. Homo sapiens. [Contig view]
GeneID7534.
KEGGhsa:7534.

Organism-specific databases

H-InvDBHIX0034328.
HGNCHGNC:12855. YWHAZ.
HPACAB005065.
MIM601288. gene.
PharmGKBPA37444.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENP63104.

Gene expression databases

ArrayExpressP63104.
GermOnlineENSG00000164924. Homo sapiens.

Family and domain databases

InterProIPR000308. 14-3-3.
[Graphical view]
Gene3DG3DSA:1.20.190.20. 14-3-3. 1 hit.
PANTHERPTHR18860. 14-3-3. 1 hit.
PfamPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFPIRSF000868. 14-3-3. 1 hit.
PRINTSPR00305. 1433ZETA.
ProDomPD000600. 14-3-3. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00101. 14_3_3. 1 hit.
[Graphical view]
PROSITEPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB01381. Ginkgo biloba.
LinkHubP63104.
NextBio29475.
SOURCESearch...

Entry information

Entry name1433Z_HUMAN
AccessionPrimary (citable) accession number: P63104
Secondary accession number(s): P29213 expand/collapse secondary AC list , 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: November 25, 2008
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents