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Protein

14-3-3 protein gamma

Gene

YWHAG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • insulin-like growth factor receptor binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein kinase C binding Source: UniProtKB
  • protein kinase C inhibitor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-111447. Activation of BAD and translocation to mitochondria.
R-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-5625740. RHO GTPases activate PKNs.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
SignaLinkiP61981.

Names & Taxonomyi

Protein namesi
Recommended name:
14-3-3 protein gamma
Alternative name(s):
Protein kinase C inhibitor protein 1
Short name:
KCIP-1
Cleaved into the following chain:
Gene namesi
Name:YWHAG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:12852. YWHAG.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic vesicle membrane Source: Reactome
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • mitochondrion Source: GOC
  • myelin sheath Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37441.

Chemistry

ChEMBLiCHEMBL1293296.

Polymorphism and mutation databases

BioMutaiYWHAG.
DMDMi48428721.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24724714-3-3 protein gammaPRO_0000367907Add
BLAST
Initiator methionineiRemoved; alternateCombined sources4 Publications
Chaini2 – 24724614-3-3 protein gamma, N-terminally processedPRO_0000058606Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine; in 14-3-3 protein gamma; alternate; partial1 Publication
Modified residuei2 – 21N-acetylvaline; in 14-3-3 protein gamma, N-terminally processed; partialCombined sources3 Publications
Modified residuei2 – 21N-acetylvaline; partial3 Publications
Modified residuei71 – 711PhosphoserineBy similarity
Modified residuei133 – 1331PhosphotyrosineBy similarity
Modified residuei145 – 1451Phosphothreonine1 Publication
Modified residuei215 – 2151PhosphoserineBy similarity
Modified residuei234 – 2341PhosphothreonineCombined sources
Modified residuei235 – 2351PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by various PKC isozymes.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP61981.
MaxQBiP61981.
PaxDbiP61981.
PeptideAtlasiP61981.
PRIDEiP61981.
TopDownProteomicsiP61981.

2D gel databases

REPRODUCTION-2DPAGEIPI00220642.

PTM databases

iPTMnetiP61981.
PhosphoSiteiP61981.
SwissPalmiP61981.

Expressioni

Tissue specificityi

Highly expressed in brain, skeletal muscle, and heart.1 Publication

Gene expression databases

BgeeiP61981.
CleanExiHS_YWHAG.
GenevisibleiP61981. HS.

Organism-specific databases

HPAiCAB013274.
CAB018389.
HPA026918.

Interactioni

Subunit structurei

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 and SIRT2.Interacts with the 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703).By similarity10 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei57 – 571Interaction with phosphoserine on interacting protein
Sitei132 – 1321Interaction with phosphoserine on interacting protein

Binary interactionsi

WithEntry#Exp.IntActNotes
Q6ZR292EBI-359832,EBI-7302296
ACIN1Q9UKV32EBI-359832,EBI-396258
AKAP13Q128022EBI-359832,EBI-1373806
ANKS1AQ926252EBI-359832,EBI-1048612
ARAFP103984EBI-359832,EBI-365961
ARHGEF2Q929742EBI-359832,EBI-302405
ARHGEF7Q141552EBI-359832,EBI-717515
BAIAP2Q9UQB82EBI-359832,EBI-525456
BCLAF1Q9NYF82EBI-359832,EBI-437804
BRAFP150563EBI-359832,EBI-365980
CCNYQ8ND763EBI-359832,EBI-1049189
CDC5LQ994592EBI-359832,EBI-374880
CDK17Q005372EBI-359832,EBI-624648
CENPJQ9HC773EBI-359832,EBI-946194
CFAP20Q9Y6A42EBI-359832,EBI-1046872
CFL1P235282EBI-359832,EBI-352733
CGNQ9P2M72EBI-359832,EBI-79537
CHEK1O147577EBI-359832,EBI-974488
CLASP1Q7Z4602EBI-359832,EBI-913476
CLK2P497602EBI-359832,EBI-750020
CLK3P497612EBI-359832,EBI-745579
CSNK1A1P678283EBI-359832,EBI-7540603From a different organism.
DDX39BQ138382EBI-359832,EBI-348622
DENND4AQ7Z4012EBI-359832,EBI-1046479
DFFAO002732EBI-359832,EBI-727171
DYRK1AQ136272EBI-359832,EBI-1053596
EDC3Q96F862EBI-359832,EBI-997311
EML3Q32P442EBI-359832,EBI-1046713
EPB41L2O434912EBI-359832,EBI-1052044
EPB41L3Q9Y2J24EBI-359832,EBI-310986
ERC1Q8IUD22EBI-359832,EBI-1044755
FAM53CQ9NYF34EBI-359832,EBI-1644252
FRMD6Q96NE93EBI-359832,EBI-741729
GBF1Q925382EBI-359832,EBI-359050
GSK3AP498402EBI-359832,EBI-1044067
HDAC4P565248EBI-359832,EBI-308629
HDAC7Q8WUI43EBI-359832,EBI-1048378
IGF1RP080692EBI-359832,EBI-475981
IRS2Q9Y4H22EBI-359832,EBI-1049582
KANK1Q14678-23EBI-359832,EBI-6173812
KIAA0930Q6ICG63EBI-359832,EBI-1053969
KIF1BO603332EBI-359832,EBI-465633
KIF23Q022414EBI-359832,EBI-306852
KIF5BP331762EBI-359832,EBI-355878
KLC2Q9H0B62EBI-359832,EBI-726994
LARP1Q6PKG02EBI-359832,EBI-1052114
LBRQ147392EBI-359832,EBI-1055147
LRRK2Q5S0074EBI-359832,EBI-5323863
LSRQ86X292EBI-359832,EBI-1056946
LUC7L2Q9Y3832EBI-359832,EBI-352851
LUC7L3O952322EBI-359832,EBI-395671
MAP3K2Q9Y2U52EBI-359832,EBI-357393
MARK2Q7KZI72EBI-359832,EBI-516560
MARK3P274484EBI-359832,EBI-707595
MDM4O151517EBI-359832,EBI-398437
MFAP1P550812EBI-359832,EBI-1048159
MICALL1Q8N3F82EBI-359832,EBI-1056885
MLLT4P551962EBI-359832,EBI-365875
MPRIPQ6WCQ13EBI-359832,EBI-1022605
MYCBP2O755922EBI-359832,EBI-1043774
NADKO955443EBI-359832,EBI-743949
NOLC1Q149783EBI-359832,EBI-396155
OSBPL3Q9H4L52EBI-359832,EBI-1051317
PABPC1P119402EBI-359832,EBI-81531
PAK4O960132EBI-359832,EBI-713738
PI4KBQ9UBF82EBI-359832,EBI-1053214
PIK3C3Q8NEB93EBI-359832,EBI-1056470
PIK3R1P279862EBI-359832,EBI-79464
PNNQ9H3072EBI-359832,EBI-681904
PPFIBP1Q86W922EBI-359832,EBI-1045582
PPIGQ134272EBI-359832,EBI-396072
PRKDCP785272EBI-359832,EBI-352053
PRPF19Q9UMS42EBI-359832,EBI-395746
PRPF38BQ5VTL82EBI-359832,EBI-1045334
PRPF4BQ135232EBI-359832,EBI-395940
PTPN3P260452EBI-359832,EBI-1047946
PUF60Q9UHX12EBI-359832,EBI-1053259
RAB11FIP2Q7L8042EBI-359832,EBI-1049676
RABEP1Q152762EBI-359832,EBI-447043
RABGEF1Q9UJ412EBI-359832,EBI-913954
RACGAP1Q9H0H53EBI-359832,EBI-717233
RAF1P040493EBI-359832,EBI-365996
RAI14Q9P0K72EBI-359832,EBI-1023749
RALGPS2Q86X272EBI-359832,EBI-1050841
RASAL2Q9UJF22EBI-359832,EBI-359444
RASSF8Q8NHQ82EBI-359832,EBI-306805
RMDN3Q96TC74EBI-359832,EBI-1056589
Rnd3P615882EBI-359832,EBI-6930266From a different organism.
RNPS1Q152872EBI-359832,EBI-395959
SAMD4AQ9UPU92EBI-359832,EBI-1047497
SAMD4BQ5PRF92EBI-359832,EBI-1047489
SF3B3Q153932EBI-359832,EBI-346977
SH3BP4Q9P0V34EBI-359832,EBI-1049513
SH3BP5LQ7L8J42EBI-359832,EBI-747389
SHCBP1Q8NEM22EBI-359832,EBI-744700
SNRNP200O756432EBI-359832,EBI-1045395
SONP185832EBI-359832,EBI-1053513
SRGAP2O750442EBI-359832,EBI-1051034
SRPK1Q96SB42EBI-359832,EBI-539478
SRRM1Q8IYB32EBI-359832,EBI-1055880
SRRM2Q9UQ352EBI-359832,EBI-1050142
SRSF10O754942EBI-359832,EBI-353655
THRAP3Q9Y2W12EBI-359832,EBI-352039
TIAM1Q130092EBI-359832,EBI-1050007
TINF2Q9BSI42EBI-359832,EBI-717399
TJP2Q9UDY22EBI-359832,EBI-1042602
TMEM102Q8N9M52EBI-359832,EBI-1050459
TP53P046375EBI-359832,EBI-366083
TRA2BP629952EBI-359832,EBI-725485
TSC1Q925742EBI-359832,EBI-1047085
TSC2P498154EBI-359832,EBI-396587
TUBBP074372EBI-359832,EBI-350864
USP8P408182EBI-359832,EBI-1050865
YAP1P469374EBI-359832,EBI-1044059
YWHAEP622584EBI-359832,EBI-356498
ZBTB21Q9ULJ32EBI-359832,EBI-1051048

GO - Molecular functioni

  • insulin-like growth factor receptor binding Source: UniProtKB
  • protein kinase C binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113364. 294 interactions.
DIPiDIP-33406N.
IntActiP61981. 295 interactions.
MINTiMINT-248956.
STRINGi9606.ENSP00000306330.

Chemistry

BindingDBiP61981.

Structurei

Secondary structure

1
247
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1613Combined sources
Helixi20 – 3112Combined sources
Helixi39 – 7032Combined sources
Helixi79 – 10628Combined sources
Helixi108 – 1114Combined sources
Helixi117 – 13721Combined sources
Helixi140 – 16425Combined sources
Helixi170 – 18516Combined sources
Helixi190 – 20617Combined sources
Helixi207 – 2104Combined sources
Turni213 – 2153Combined sources
Helixi216 – 23318Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B05X-ray2.55A/B/C/D/E/F2-247[»]
3UZDX-ray1.86A1-247[»]
4E2EX-ray2.25A1-247[»]
4J6SX-ray3.08A/B/C/D1-247[»]
4O46X-ray2.90A/B/C/D/E/F1-247[»]
ProteinModelPortaliP61981.
SMRiP61981. Positions 1-235.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61981.

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.Curated

Phylogenomic databases

eggNOGiKOG0841. Eukaryota.
COG5040. LUCA.
GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP61981.
KOiK16198.
OMAiIKNCGET.
OrthoDBiEOG7HHWT3.
PhylomeDBiP61981.
TreeFamiTF102003.

Family and domain databases

InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61981-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK
60 70 80 90 100
NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV
110 120 130 140 150
LSLLDNYLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS
160 170 180 190 200
EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA
210 220 230 240
FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN
Length:247
Mass (Da):28,303
Last modified:January 23, 2007 - v2
Checksum:iB0D16C6DE1F4455D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41R → P in AAD48408 (PubMed:10433554).Curated
Sequence conflicti19 – 191R → G in AAD48408 (PubMed:10433554).Curated
Sequence conflicti78 – 781Missing in AAD48408 (PubMed:10433554).Curated
Sequence conflicti89 – 891I → V in AAD48408 (PubMed:10433554).Curated
Sequence conflicti104 – 1041L → V in AAD48408 (PubMed:10433554).Curated
Sequence conflicti109 – 1091I → Y in AAD48408 (PubMed:10433554).Curated
Sequence conflicti119 – 1224SKVF → RKDL in AAD48408 (PubMed:10433554).Curated
Sequence conflicti144 – 1452AT → GD in AAD48408 (PubMed:10433554).Curated
Sequence conflicti157 – 1582AH → R in AAD48408 (PubMed:10433554).Curated
Sequence conflicti200 – 2023AFD → EFE in AAD48408 (PubMed:10433554).Curated
Sequence conflicti214 – 2141D → E in AAD48408 (PubMed:10433554).Curated
Sequence conflicti240 – 2401D → DH in AAD48408 (PubMed:10433554).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5584.1.
RefSeqiNP_036611.2. NM_012479.3.
UniGeneiHs.744840.

Genome annotation databases

EnsembliENST00000307630; ENSP00000306330; ENSG00000170027.
GeneIDi7532.
KEGGihsa:7532.
UCSCiuc011kgj.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5584.1.
RefSeqiNP_036611.2. NM_012479.3.
UniGeneiHs.744840.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B05X-ray2.55A/B/C/D/E/F2-247[»]
3UZDX-ray1.86A1-247[»]
4E2EX-ray2.25A1-247[»]
4J6SX-ray3.08A/B/C/D1-247[»]
4O46X-ray2.90A/B/C/D/E/F1-247[»]
ProteinModelPortaliP61981.
SMRiP61981. Positions 1-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113364. 294 interactions.
DIPiDIP-33406N.
IntActiP61981. 295 interactions.
MINTiMINT-248956.
STRINGi9606.ENSP00000306330.

Chemistry

BindingDBiP61981.
ChEMBLiCHEMBL1293296.

PTM databases

iPTMnetiP61981.
PhosphoSiteiP61981.
SwissPalmiP61981.

Polymorphism and mutation databases

BioMutaiYWHAG.
DMDMi48428721.

2D gel databases

REPRODUCTION-2DPAGEIPI00220642.

Proteomic databases

EPDiP61981.
MaxQBiP61981.
PaxDbiP61981.
PeptideAtlasiP61981.
PRIDEiP61981.
TopDownProteomicsiP61981.

Protocols and materials databases

DNASUi7532.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307630; ENSP00000306330; ENSG00000170027.
GeneIDi7532.
KEGGihsa:7532.
UCSCiuc011kgj.2. human.

Organism-specific databases

CTDi7532.
GeneCardsiYWHAG.
HGNCiHGNC:12852. YWHAG.
HPAiCAB013274.
CAB018389.
HPA026918.
MIMi605356. gene.
neXtProtiNX_P61981.
PharmGKBiPA37441.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0841. Eukaryota.
COG5040. LUCA.
GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP61981.
KOiK16198.
OMAiIKNCGET.
OrthoDBiEOG7HHWT3.
PhylomeDBiP61981.
TreeFamiTF102003.

Enzyme and pathway databases

ReactomeiR-HSA-111447. Activation of BAD and translocation to mitochondria.
R-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-5625740. RHO GTPases activate PKNs.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
SignaLinkiP61981.

Miscellaneous databases

ChiTaRSiYWHAG. human.
EvolutionaryTraceiP61981.
GeneWikiiYWHAG.
GenomeRNAii7532.
NextBioi29467.
PROiP61981.
SOURCEiSearch...

Gene expression databases

BgeeiP61981.
CleanExiHS_YWHAG.
GenevisibleiP61981. HS.

Family and domain databases

InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. "Sirt2 interacts with 14-3-3 beta/gamma and down-regulates the activity of p53."
    Jin Y.H., Kim Y.J., Kim D.W., Baek K.H., Kang B.Y., Yeo C.Y., Lee K.Y.
    Biochem. Biophys. Res. Commun. 368:690-695(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIRT2.
  17. "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.
  18. "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, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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.
  20. "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.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234 AND SER-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  23. "Suppression of death-associated protein kinase 2 by interaction with 14-3-3 proteins."
    Yuasa K., Ota R., Matsuda S., Isshiki K., Inoue M., Tsuji A.
    Biochem. Biophys. Res. Commun. 464:70-75(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAPK2.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS), IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.

Entry informationi

Entry namei1433G_HUMAN
AccessioniPrimary (citable) accession number: P61981
Secondary accession number(s): O70457
, P35214, Q6FH52, Q9UDP2, Q9UN99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: January 23, 2007
Last modified: April 13, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.