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P61981 (1433G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
14-3-3 protein gamma
Alternative name(s):
Protein kinase C inhibitor protein 1
Short name=KCIP-1

Cleaved into the following chain:

  1. 14-3-3 protein gamma, N-terminally processed
Gene names
Name:YWHAG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length247 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 pathways. 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. Ref.15

Subunit structure

Homodimer. Interacts with SAMSN1 By similarity. Interacts with RAF1, SSH1 and CRTC2/TORC2. Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm. Interacts with GAB2. Interacts with MDM4 (phosphorylated); negatively regulates MDM4 activity toward TP53. Interacts with PKA-phosphorylated AANAT. Ref.1 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.21

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Highly expressed in brain, skeletal muscle, and heart. Ref.2

Post-translational modification

Phosphorylated by various PKC isozymes. Ref.1 Ref.6

Sequence similarities

Belongs to the 14-3-3 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

cellular response to insulin stimulus

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

membrane organization

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of protein kinase activity

Non-traceable author statement Ref.1. Source: UniProtKB

negative regulation of protein serine/threonine kinase activity

Non-traceable author statement Ref.1. Source: GOC

positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway

Traceable author statement. Source: Reactome

protein targeting

Inferred from electronic annotation. Source: Ensembl

regulation of neuron differentiation

Inferred from mutant phenotype PubMed 11824616. Source: UniProtKB

regulation of signal transduction

Non-traceable author statement Ref.1Ref.2. Source: UniProtKB

regulation of synaptic plasticity

Inferred from mutant phenotype PubMed 11824616. Source: UniProtKB

   Cellular_componentcytoplasmic vesicle membrane

Traceable author statement. Source: Reactome

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProtKB

   Molecular_functioninsulin-like growth factor receptor binding

Inferred from physical interaction PubMed 12482592. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein kinase C binding

Inferred from physical interaction Ref.1. Source: UniProtKB

protein kinase C inhibitor activity

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24724714-3-3 protein gamma
PRO_0000367907
Initiator methionine11Removed; alternate Ref.6 Ref.7 Ref.8 Ref.11
Chain2 – 24724614-3-3 protein gamma, N-terminally processed
PRO_0000058606

Sites

Site571Interaction with phosphoserine on interacting protein
Site1321Interaction with phosphoserine on interacting protein

Amino acid modifications

Modified residue11N-acetylmethionine; in 14-3-3 protein gamma; alternate; partial Ref.6
Modified residue21N-acetylvaline; in 14-3-3 protein gamma, N-terminally processed; partial Ref.6 Ref.8 Ref.11 Ref.17
Modified residue21N-acetylvaline; partial Ref.6 Ref.8 Ref.11 Ref.17
Modified residue1451Phosphothreonine Ref.6

Experimental info

Sequence conflict41R → P in AAD48408. Ref.1
Sequence conflict191R → G in AAD48408. Ref.1
Sequence conflict781Missing in AAD48408. Ref.1
Sequence conflict891I → V in AAD48408. Ref.1
Sequence conflict1041L → V in AAD48408. Ref.1
Sequence conflict1091I → Y in AAD48408. Ref.1
Sequence conflict119 – 1224SKVF → RKDL in AAD48408. Ref.1
Sequence conflict144 – 1452AT → GD in AAD48408. Ref.1
Sequence conflict157 – 1582AH → R in AAD48408. Ref.1
Sequence conflict200 – 2023AFD → EFE in AAD48408. Ref.1
Sequence conflict2141D → E in AAD48408. Ref.1
Sequence conflict2401D → DH in AAD48408. Ref.1

Secondary structure

....................... 247
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61981 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B0D16C6DE1F4455D

FASTA24728,303
        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 

« Hide

References

« Hide 'large scale' references
[1]"14-3-3gamma interacts with and is phosphorylated by multiple protein kinase C isoforms in PDGF-stimulated human vascular smooth muscle cells."
Autieri M.V., Carbone C.J.
DNA Cell Biol. 18:555-564(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, INTERACTION WITH RAF1.
Tissue: Vascular smooth muscle.
[2]"Cloning, expression, and chromosomal mapping of the human 14-3-3gamma gene (YWHAG) to 7q11.23."
Horie M., Suzuki M., Takahashi E., Tanigami A.
Genomics 60:241-243(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Fetal brain.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The DNA sequence of human chromosome 7."
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. expand/collapse author list , 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.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Endometrial tumor.
[6]Bienvenut W.V., Boldt K., von Kriegsheim A.F., Zebisch A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-10; 13-56; 62-69; 133-172 AND 199-227, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND VAL-2, PHOSPHORYLATION AT THR-145, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma and Hepatoma.
[7]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-12.
Tissue: Platelet.
[8]Bienvenut W.V., Claeys D.
Submitted (NOV-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-10; 13-19; 29-42; 62-69; 133-143 AND 218-227, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Platelet.
[9]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 92-110; 199-217 AND 228-247, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[10]"Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-binding switch in melatonin synthesis."
Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H., Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T., Beauverger P., Ferry G., Boutin J.A., Klein D.C.
Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AANAT.
[11]"Proteomics-based target identification: bengamides as a new class of methionine aminopeptidase inhibitors."
Towbin H., Bair K.W., DeCaprio J.A., Eck M.J., Kim S., Kinder F.R., Morollo A., Mueller D.R., Schindler P., Song H.K., van Oostrum J., Versace R.W., Voshol H., Wood J., Zabludoff S., Phillips P.E.
J. Biol. Chem. 278:52964-52971(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector."
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.
Cell 119:61-74(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRTC2.
[13]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SSH1.
[14]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ABL1, IDENTIFICATION BY MASS SPECTROMETRY.
[15]"14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, resulting in p53 activation."
Jin Y., Dai M.S., Lu S.Z., Xu Y., Luo Z., Zhao Y., Lu H.
EMBO J. 25:1207-1218(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TP53 ACTIVATION, INTERACTION WITH MDM4.
[16]"Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein."
Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M., James D.E., Daly R.J.
EMBO J. 27:2305-2316(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GAB2.
[17]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Structural basis for protein-protein interactions in the 14-3-3 protein family."
Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V., Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.
Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS), IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF142498 mRNA. Translation: AAD48408.1.
AB024334 mRNA. Translation: BAA85184.1.
CR541904 mRNA. Translation: CAG46702.1.
CR541925 mRNA. Translation: CAG46723.1.
AC006388 Genomic DNA. No translation available.
BC020963 mRNA. Translation: AAH20963.1.
RefSeqNP_036611.2. NM_012479.3.
UniGeneHs.744840.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B05X-ray2.55A/B/C/D/E/F2-246[»]
3UZDX-ray1.86A1-247[»]
4E2EX-ray2.25A1-247[»]
4J6SX-ray3.08A/B/C/D2-247[»]
ProteinModelPortalP61981.
SMRP61981. Positions 1-235.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113364. 255 interactions.
IntActP61981. 101 interactions.
MINTMINT-248956.
STRING9606.ENSP00000306330.

Chemistry

BindingDBP61981.
ChEMBLCHEMBL1293296.

PTM databases

PhosphoSiteP61981.

Polymorphism databases

DMDM48428721.

2D gel databases

REPRODUCTION-2DPAGEIPI00220642.

Proteomic databases

PaxDbP61981.
PeptideAtlasP61981.
PRIDEP61981.

Protocols and materials databases

DNASU7532.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307630; ENSP00000306330; ENSG00000170027.
GeneID7532.
KEGGhsa:7532.
UCSCuc011kgj.1. human.

Organism-specific databases

CTD7532.
GeneCardsGC07M075956.
HGNCHGNC:12852. YWHAG.
HPACAB013274.
CAB018389.
HPA026918.
MIM605356. gene.
neXtProtNX_P61981.
PharmGKBPA37441.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5040.
HOGENOMHOG000240379.
HOVERGENHBG050423.
InParanoidP61981.
KOK16198.
OMACSETQHE.
OrthoDBEOG7HHWT3.
PhylomeDBP61981.
TreeFamTF102003.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_115566. Cell Cycle.
REACT_578. Apoptosis.
SignaLinkP61981.

Gene expression databases

ArrayExpressP61981.
BgeeP61981.
CleanExHS_YWHAG.
GenevestigatorP61981.

Family and domain databases

Gene3D1.20.190.20. 1 hit.
InterProIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERPTHR18860. PTHR18860. 1 hit.
PfamPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFPIRSF000868. 14-3-3. 1 hit.
PRINTSPR00305. 1433ZETA.
SMARTSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMSSF48445. SSF48445. 1 hit.
PROSITEPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSYWHAG. human.
EvolutionaryTraceP61981.
GeneWikiYWHAG.
GenomeRNAi7532.
NextBio29467.
PROP61981.
SOURCESearch...

Entry information

Entry name1433G_HUMAN
AccessionPrimary (citable) accession number: P61981
Secondary accession number(s): O70457 expand/collapse secondary AC list , P35214, Q6FH52, Q9UDP2, Q9UN99
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM