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UniProtKB/Swiss-Prot entry P61981

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

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Entry information
Entry name 1433G_HUMAN
Primary accession number P61981
Secondary accession numbers O70457 P35214 Q6FH52 Q9UDP2 Q9UN99
Integrated into Swiss-Prot on June 7, 2004
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 56)
Name and origin of the protein
Protein name 14-3-3 protein gamma
Synonyms Protein kinase C inhibitor protein 1
KCIP-1
Gene name
Name: YWHAG
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], PHOSPHORYLATION, AND INTERACTION WITH RAF1.
TISSUE=Vascular smooth muscle;
DOI=10.1089/104454999315105; PubMed=10433554 [NCBI, ExPASy, EBI, Israel, Japan]
Autieri M.V., Carbone C.J.;
"14-3-3gamma interacts with and is phosphorylated by multiple protein kinase C isoforms in PDGF-stimulated human vascular smooth muscle cells.";
DNA Cell Biol. 18:555-564(1999).
[2]
 NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Fetal brain;
DOI=10.1006/geno.1999.5887; PubMed=10486217 [NCBI, ExPASy, EBI, Israel, Japan]
Horie M., Suzuki M., Takahashi E., Tanigami A.;
"Cloning, expression, and chromosomal mapping of the human 14-3-3gamma gene (YWHAG) to 7q11.23.";
Genomics 60:241-243(1999).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01782; PubMed=12853948 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Endometrial tumor;
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).
[6]
 PROTEIN SEQUENCE OF 2-12.
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).
[7]
 PROTEIN SEQUENCE OF 2-10; 13-19; 29-42; 62-69; 133-143 AND 218-227, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, AND MASS SPECTROMETRY.
TISSUE=Platelet;
Bienvenut W.V., Claeys D.;
Submitted (NOV-2005) to UniProtKB.
[8]
 PROTEIN SEQUENCE OF 2-10; 13-50; 62-69; 133-172 AND 199-227, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, PHOSPHORYLATION AT THR-145, AND MASS SPECTROMETRY.
TISSUE=Hepatoma;
Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
Submitted (JUL-2007) to UniProtKB.
[9]
 PROTEIN SEQUENCE OF 92-110 AND 199-217, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[10]
 INTERACTION WITH CRTC2.
DOI=10.1016/j.cell.2004.09.015; PubMed=15454081 [NCBI, ExPASy, EBI, Israel, Japan]
Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G., Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H., Okamoto M., Montminy M.;
"The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector.";
Cell 119:61-74(2004).
[11]
 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).
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
AF142498; AAD48408.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB024334; BAA85184.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR541904; CAG46702.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR541925; CAG46723.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC006388; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC020963; AAH20963.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_036611.2; -.
UniGene Hs.520974
3D structure databases
PDB
2B05; X-ray; 2.55 A; A/B/C/D/E/F=1-247.[ExPASy / RCSB / EBI]
PDBsum 2B05; -.
ModBase P61981.
Protein-protein interaction databases
IntAct P61981; -.
PTM databases
PhosphoSite P61981; -.
2D gel databases
Cornea-2DPAGE P61981; -.
REPRODUCTION-2DPAGE IPI00220642; -.
Organism-specific databases
H-InvDB HIX0006789; -.
HGNC HGNC:12852; YWHAG.
GenAtlas YWHAG.
HPA CAB013274; -.
MIM 605356; gene. [NCBI / EBI]
PharmGKB PA37441; -.
GeneCards P61981.
Gene expression databases
ArrayExpress P61981; -.
CleanEx HS_YWHAG; -.
GermOnline ENSG00000170027; Homo sapiens.
Ontologies
GO
GO:0005159; Molecular function: insulin-like growth factor receptor binding (inferred from physical interaction from UniProtKB).
GO:0005080; Molecular function: protein kinase C binding (inferred from physical interaction from UniProtKB).
GO:0008426; Molecular function: protein kinase C inhibitor activity (non-traceable author statement from UniProtKB).
GO:0006469; Biological process: negative regulation of protein kinase activity (non-traceable author statement from UniProtKB).
GO:0045664; Biological process: regulation of neuron differentiation (inferred from mutant phenotype from UniProtKB).
GO:0009966; Biological process: regulation of signal transduction (non-traceable author statement from UniProtKB).
GO:0048167; Biological process: regulation of synaptic plasticity (inferred from mutant phenotype from UniProtKB).
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 P61981.
Proteomic databases
PeptideAtlas P61981; -.
Genome annotation databases
Ensembl ENSG00000170027; Homo sapiens. [Contig view]
GeneID 7532; -.
KEGG hsa:7532; -.
Phylogenomic databases
HOGENOM P61981; -.
HOVERGEN P61981; -.
Other
SOURCE YWHAG; Homo sapiens.
ProtoNet P61981.
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
INIT_MET   1     1        Removed. 
CHAIN   2   247  246     14-3-3 protein gamma. PRO_0000058606
MOD_RES   2     2        N-acetylvaline; partial. 
MOD_RES   117   117        Phosphotyrosine (By similarity). 
MOD_RES   145   145        Phosphothreonine. 
CONFLICT   4     4        R -> P (in Ref. 1; AAD48408). 
CONFLICT   19    19        R -> G (in Ref. 1; AAD48408). 
CONFLICT   78    78        Missing (in Ref. 1; AAD48408). 
CONFLICT   89    89        I -> V (in Ref. 1; AAD48408). 
CONFLICT   104   104        L -> V (in Ref. 1; AAD48408). 
CONFLICT   109   109        I -> Y (in Ref. 1; AAD48408). 
CONFLICT   119   122        SKVF -> RKDL (in Ref. 1; AAD48408). 
CONFLICT   144   145        AT -> GD (in Ref. 1; AAD48408). 
CONFLICT   157   158        AH -> R (in Ref. 1; AAD48408). 
CONFLICT   200   202        AFD -> EFE (in Ref. 1; AAD48408). 
CONFLICT   214   214        D -> E (in Ref. 1; AAD48408). 
CONFLICT   240   240        D -> DH (in Ref. 1; AAD48408). 
HELIX   4    16  13      
HELIX   20    31  12      
HELIX   39    73  35      
HELIX   76   106  31      
TURN   107   111  5      
HELIX   117   137  21      
HELIX   140   164  25      
HELIX   170   185  16      
HELIX   190   206  17      
HELIX   208   210  3      
TURN   213   215  3      
HELIX   216   233  18      
Sequence information
Length: 247 AA [This is the length of the unprocessed precursor] Molecular weight: 28303 Da [This is the MW of the unprocessed precursor] CRC64: B0D16C6DE1F4455D [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW 

        70         80         90        100        110        120 
RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK 

       130        140        150        160        170        180 
VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS 

       190        200        210        220        230        240 
VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD 


DGGEGNN
P61981 in FASTA format

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