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

Last modified November 25, 2008. Version 58. 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 gamma
Alternative name(s):
    Protein kinase C inhibitor protein 1
      Short name=KCIP-1
Gene names
Name: YWHAG
OrganismHomo sapiens (Human)
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 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 RAF1, SSH1 and CRTC2/TORC2.

Subcellular location

CytoplasmBy similarity.

Tissue specificity

Highly expressed in brain, skeletal muscle, and heart.

Post-translational modification

Phosphorylated by various PKC isozymes.

Sequence similarities

Belongs to the 14-3-3 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ANKS1AQ926251EBI-359832,EBI-1048612
ARAFP103981EBI-359832,EBI-365961
ASCC3L1O756431EBI-359832,EBI-1045395
BAIAP2Q9UQB81EBI-359832,EBI-525456
BRAFP150561EBI-359832,EBI-365980
C22orf9Q6ICG61EBI-359832,EBI-1053969
CDKN1BP465271EBI-359832,EBI-519280
CGNQ9P2M71EBI-359832,EBI-79537
CLASP1Q7Z4601EBI-359832,EBI-913476
DENND4AQ7Z4011EBI-359832,EBI-1046479
EDC3Q96F861EBI-359832,EBI-997311
EPB41L3Q9Y2J21EBI-359832,EBI-310986
ERC1Q8IUD21EBI-359832,EBI-1044755
FAM82A2Q96TC71EBI-359832,EBI-1056589
GBF1Q925381EBI-359832,EBI-359050
IGF1RP080691EBI-359832,EBI-475981
IRS2Q9Y4H21EBI-359832,EBI-1049582
KIF23Q022411EBI-359832,EBI-306852
KIF5BP331761EBI-359832,EBI-355878
KIF5CO602821EBI-359832,EBI-717170
KLC1Q078661EBI-359832,EBI-721019
KLC2Q9H0B61EBI-359832,EBI-726994
KLC4Q9NSK01EBI-359832,EBI-949319
KRT31Q153231EBI-359832,EBI-948001
KRT33BQ145251EBI-359832,EBI-1049638
KRT85P783861EBI-359832,EBI-1049371
LARP1Q6PKG01EBI-359832,EBI-1052114
LBRQ147391EBI-359832,EBI-1055147
LUC7L2Q9Y3831EBI-359832,EBI-352851
MARK3P274481EBI-359832,EBI-707595
MLLT4P551961EBI-359832,EBI-365875
MPRIPQ6WCQ11EBI-359832,EBI-1022605
OSBPL3Q9H4L51EBI-359832,EBI-1051317
PAK4O960131EBI-359832,EBI-713738
PARD3Q8TEW01EBI-359832,EBI-81968
PI4KBQ9UBF81EBI-359832,EBI-1053214
PPFIBP1Q86W921EBI-359832,EBI-1045582
RABEP1Q152761EBI-359832,EBI-447043
RABGEF1Q9UJ411EBI-359832,EBI-913954
RACGAP1Q9H0H51EBI-359832,EBI-717233
RAF1P040491EBI-359832,EBI-365996
RAI14Q9P0K71EBI-359832,EBI-1023749
SAMD4BQ5PRF91EBI-359832,EBI-1047489
SHCBP1Q8NEM21EBI-359832,EBI-744700
SONP185831EBI-359832,EBI-1053513
SRRM2Q9UQ351EBI-359832,EBI-1050142
TJP2Q9UDY21EBI-359832,EBI-1042602

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; alternate
Chain2 – 24724614-3-3 protein gamma
PRO_0000058606

Amino acid modifications

Modified residue11N-acetylmethionine; alternate
Modified residue21N-acetylvaline; partial
Modified residue1171Phosphotyrosine By similarity
Modified residue1451Phosphothreonine

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
P61981-1 [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: 10433554] [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: 10486217] [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: 12853948] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Endometrial tumor.
[6]"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 2-12.
Tissue: Platelet.
[7]Bienvenut W.V., Boldt K., von Kriegsheim A.F., Zebisch A., Kolch W.
Submitted (OCT-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, MASS SPECTROMETRY.
Tissue: Colon carcinoma and Hepatoma.
[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, MASS SPECTROMETRY.
Tissue: Platelet.
[9]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 92-110 AND 199-217, MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[10]"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: 15454081] [Abstract]
Cited for: INTERACTION WITH CRTC2.
[11]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
UniGeneHs.520974

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2B05X-ray2.55A/B/C/D/E/F1-247[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP61981.

PTM databases

PhosphoSiteP61981.

2-D gel databases

Cornea-2DPAGEP61981.
REPRODUCTION-2DPAGEIPI00220642.

Proteomic databases

PeptideAtlasP61981.

Genome annotation databases

EnsemblENSG00000170027. Homo sapiens. [Contig view]
GeneID7532.
KEGGhsa:7532.

Organism-specific databases

H-InvDBHIX0006789.
HGNCHGNC:12852. YWHAG.
HPACAB013274.
CAB018389.
MIM605356. gene.
PharmGKBPA37441.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMP61981.
HOVERGENP61981.

Gene expression databases

ArrayExpressP61981.
CleanExHS_YWHAG.
GermOnlineENSG00000170027. 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

NextBio29467.
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: November 25, 2008
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 7

Human chromosome 7: 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) &midd