Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  14-3-3 protein sigma  

UniProtKB / Swiss-Prot ID :  1433S_HUMAN

Gene Name (Synonyms) : 
SFN, HME1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus (By similarity). Secreted. Note=May be secreted by a non-classical secretory pathway. 

Protein 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. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity). p53-regulated inhibitor of G2/M progression. 

Protein Sequence MERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSN...
Predicted Secondary Structure CCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
155M -> I (in dbSNP:rs11542705). VAR_048095
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
5PhosphoserineMERASLIQK
CCHHHHHHH
32.02HPRD
Link
5PhosphoserineMERASLIQK
CCHHHHHHH
32.02Phosphositeplus
Link
11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IQKAKLAEQ
HHHHHHHHH
56.09Phosphositeplus
Link
45PhosphoserineRNLLSVAYK
HHHHHHHHH
14.10Phosphositeplus
Link
49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SVAYKNVVG
HHHHHHHHH
33.26Phosphositeplus
Link
68Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SIEQKSNEE
HHHHHHHHC
42.32Phosphositeplus
Link
77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GSEEKGPEV
CCCHHHHHH
75.59Phosphositeplus
Link-
122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VFYLKMKGD
EEEEEECCH
27.47Phosphositeplus
Link
122N6-acetyllysineVFYLKMKGD
EEEEEECCH
27.47HPRD
Link
122N6-acetyllysineVFYLKMKGD
EEEEEECCH
27.47Phosphositeplus
Link
124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YLKMKGDYY
EEEECCHHH
47.22Phosphositeplus
Link
128PhosphotyrosineKGDYYRYLA
CCHHHHHHH
9.49Phosphositeplus
Link
146PhosphoserineRIIDSARSA
HHHHHHHHH
18.38HPRD
Link
186PhosphoserineEIANSPEEA
HHHCCHHHH
25.35Phosphositeplus
Link
186Phosphoserine (MAPK8)EIANSPEEA
HHHCCHHHH
25.35PhosphoELM
Link
213PhosphotyrosineSEDSYKDST
CCCCCHHHH
31.01HPRD
Link
216PhosphoserineSYKDSTLIM
CCHHHHHHH
22.44HPRD
Link
216PhosphoserineSYKDSTLIM
CCHHHHHHH
22.44SysPTM
Link
248PhosphoserineQEPQS
CCCCC
53.56HPRD
Link
248PhosphoserineQEPQS
CCCCC
53.56PhosphoELM
Link
248PhosphoserineQEPQS
CCCCC
53.56Phosphositeplus
Link
248PhosphoserineQEPQS
CCCCC
53.56SysPTM
Link
248Phosphoserine.QEPQS
CCCCC
53.56UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
P3C2B_HUMANphysical interactionMINT-3975518MINT15778465
ABLM1_HUMANphysical interactionMINT-3974750MINT15778465
MDM4_HUMANphysical interactionMINT-1957929MINT16511572
CHST1_HUMANphysical interactionMINT-67184MINT16189514
GRIN2_HUMANphysical interactionMINT-68344MINT16189514
PACS2_HUMANphysical interactionMINT-3976506MINT15778465
FUSIP_HUMANphysical interactionMINT-3976116MINT15778465
SASH1_HUMANphysical interactionMINT-3975603MINT15778465
RAF1_HUMANphysical interactionMINT-3975386MINT15778465
GCR_HUMANphysical interactionMINT-14115MINT12730237
CDC2_HUMANphysical interactionMINT-15830MINT10524633
ARAF_HUMANphysical interactionMINT-3975364MINT15778465
BRAF1_HUMANphysical interactionMINT-3975375MINT15778465
PTN2_HUMANphysical interactionMINT-3975592MINT15778465
APC_HUMANphysical interactionMINT-3975353MINT15778465
MARK3_HUMANphysical interactionMINT-66900MINT16189514
MARK3_HUMANphysical interactionMINT-3975719MINT15778465
1433S_HUMANphysical interactionMINT-3974708MINT15778465
KINH_HUMANphysical interactionMINT-3975897MINT15778465
IRS1_HUMANphysical interactionMINT-3975430MINT15778465
HDAC4_HUMANphysical interactionMINT-3975818MINT15778465
BCAR1_HUMANphysical interactionMINT-3974941MINT15778465
WDR68_HUMANphysical interactionMINT-3976171MINT15778465
RAE1L_HUMANphysical interactionMINT-3976050MINT15778465
SPIR1_HUMANphysical interactionMINT-3975331MINT15778465
TBL3_HUMANphysical interactionMINT-67430MINT16189514
DYR1A_HUMANphysical interactionMINT-3975419MINT15778465
GRB7_HUMANphysical interactionMINT-3974985MINT15778465
CA106_HUMANphysical interactionMINT-3976368MINT15778465
Q5VUW2_HUMANphysical interactionMINT-3976484MINT15778465
MRCKG_HUMANphysical interactionMINT-3976305MINT15778465
REEP3_HUMANphysical interactionMINT-3976629MINT15778465
RICTR_HUMANphysical interactionMINT-3976590MINT15778465
RICTR_HUMANphysical interactionMINT-3976660MINT15778465
UBP43_HUMANphysical interactionMINT-3976446MINT15778465
MARK2_HUMANphysical interactionMINT-3975077MINT15778465
KLC1_HUMANphysical interactionMINT-3976028MINT15778465
DTX2_HUMANphysical interactionMINT-3975408MINT15778465
TENS4_HUMANphysical interactionMINT-3974963MINT15778465
LIPB2_HUMANphysical interactionMINT-3975178MINT15778465
SHCBP_HUMANphysical interactionMINT-3975636MINT15778465
PARD3_HUMANphysical interactionMINT-3975121MINT15778465
PAR3L_HUMANphysical interactionMINT-3975110MINT15778465
ANKS1_HUMANphysical interactionMINT-3976160MINT15778465
SGF29_HUMANphysical interactionMINT-3976264MINT15778465
EDC3_HUMANphysical interactionMINT-3976338MINT15778465
JUB_HUMANphysical interactionMINT-3975697MINT15778465
MAGI1_HUMANphysical interactionMINT-3974930MINT15778465
PKP2_HUMANphysical interactionMINT-3975132MINT15778465
KLC2_HUMANphysical interactionMINT-3975908MINT15778465
ISCU_HUMANphysical interactionMINT-3976149MINT15778465
REEP4_HUMANphysical interactionMINT-3976408MINT15778465
PKHF2_HUMANphysical interactionMINT-66436MINT16189514
MLTK_HUMANphysical interactionMINT-3975752MINT15778465
PI4KB_HUMANphysical interactionMINT-3975529MINT15778465
SAM4A_HUMANphysical interactionMINT-3976569MINT15778465
WDR37_HUMANphysical interactionMINT-3976543MINT15778465
M3K2_HUMANphysical interactionMINT-3975452MINT15778465
KLDC2_HUMANphysical interactionMINT-3976182MINT15778465
PKP3_HUMANphysical interactionMINT-3975156MINT15778465
PKHF2_HUMANphysical interactionEBI-753775
intact16189514
CH032_HUMANphysical interactionEBI-755893
intact16189514
CHST1_HUMANphysical interactionEBI-756232
intact16189514
PLK4_HUMANphysical interaction
physical interaction
EBI-754948
EBI-760497
intact16189514
16189514
MARK3_HUMANphysical interactionEBI-755284
intact16189514
Q96A78_HUMANphysical interactionEBI-757024
intact16189514
K0408_HUMANphysical interactionEBI-759649
intact16189514
Q8WU02_HUMANphysical interactionEBI-759502
intact16189514
GRIN2_HUMANphysical interactionEBI-760015
intact16189514
CDC2_HUMANin vivoHPRD:03185HPRD10524633
GCR_HUMANyeast 2-hybridHPRD:03185HPRD12730237
MARK3_HUMANyeast 2-hybridHPRD:03185HPRD16189514
BAD_HUMANyeast 2-hybridHPRD:03185HPRD16189514
CHST1_HUMANyeast 2-hybridHPRD:03185HPRD16189514
CH032_HUMANyeast 2-hybridHPRD:03185HPRD16189514
TBL3_HUMANyeast 2-hybridHPRD:03185HPRD16189514
PLK4_HUMANyeast 2-hybridHPRD:03185HPRD16189514
GRIN2_HUMANyeast 2-hybridHPRD:03185HPRD16189514
PKHF2_HUMANyeast 2-hybridHPRD:03185HPRD16189514
CI061_HUMANyeast 2-hybridHPRD:03185HPRD16189514
K0408_HUMANyeast 2-hybridHPRD:03185HPRD16189514
TTP_HUMANin vivoHPRD:03185HPRD11886850
TSC2_HUMANin vitroHPRD:03185HPRD12438239
BAX_HUMANin vivoHPRD:03185HPRD11574543
TRI25_HUMANin vivoHPRD:03185HPRD12075357
M3K5_HUMANyeast 2-hybridHPRD:03185HPRD15023544
MMP1_HUMANENSP00000340989STRING
TRI25_HUMANENSP00000340989STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures