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Protein Page:
14-3-3 sigma (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
14-3-3 sigma 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. Homodimer. Interacts with KRT17 and SAMSN1. Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. Interacts with GAB2. Interacts with SRPK2. Present mainly in tissues enriched in stratified squamous keratinizing epithelium. Belongs to the 14-3-3 family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Adaptor/scaffold
Chromosomal Location of Human Ortholog: 1p36.11
Cellular Component: cytoplasm; cytoplasmic vesicle membrane; cytosol; extracellular space
Molecular Function: protein binding; protein kinase C inhibitor activity
Biological Process: DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; DNA damage response, signal transduction resulting in induction of apoptosis; negative regulation of caspase activity; negative regulation of protein kinase activity; positive regulation of epidermal cell differentiation; regulation of epidermal cell division; release of cytochrome c from mitochondria; signal transduction
Reference #:  P31947 (UniProtKB)
Alt. Names/Synonyms: 14-3-3 protein sigma; 14-3-3 sigma; 1433S; Epithelial cell marker protein 1; HME1; SFN; stratifin; YWHAS
Gene Symbols: SFN
Molecular weight: 27,774 Da
Basal Isoelectric point: 4.68  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis Regulation  |  G2/M DNA Damage Checkpoint  |  Growth And Differentiation Control by MAPKs  |  Hippo Signaling  |  Mitochondrial Control of Apoptosis  |  PI3K/Akt Signaling  |  SAPK/JNK Signaling Cascades
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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14-3-3 sigma

Protein Structure Not Found.
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Sites Implicated In
apoptosis, induced: S186‑p
carcinogenesis, induced: S69‑p, S74‑p
transcription, induced: S69‑p, S74‑p
molecular association, regulation: S186‑p
phosphorylation: S186‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 S5‑p ___MERAsLIQKAkL
0 33 K11‑ub AsLIQKAkLAEQAER
1 2 Y19‑p LAEQAERyEDMAAFM
1 1 G28 DMAAFMKGAVEkGEE
0 1 K32‑ac FMKGAVEkGEELSCE
0 23 S45‑p CEERNLLsVAykNVV
0 7 Y48‑p RNLLsVAykNVVGGQ
0 8 K49‑ub NLLsVAykNVVGGQR
0 1 K49‑ac NLLsVAykNVVGGQR
0 3 S63‑p RAAWRVLssIEQksN
0 4 S64‑p AAWRVLssIEQksNE
0 1 K68‑ub VLssIEQksNEEGsE
2 1 S69‑p LssIEQksNEEGsEE
2 5 S74‑p QksNEEGsEEkGPEV
0 1 K77‑ub NEEGsEEkGPEVREY
1 1 T90 EYREKVETELQGVCD
1 1 T98 ELQGVCDTVLGLLDS
0 2 K109‑ub LLDSHLIkEAGDAEs
1 2 S116‑p kEAGDAEsRVFYLkM
0 5 K122‑ac EsRVFYLkMkGDYyR
0 68 K122‑ub EsRVFYLkMkGDYyR
0 5 K124‑ub RVFYLkMkGDYyRYL
0 34 Y128‑p LkMkGDYyRYLAEVA
0 2 T136‑p RYLAEVAtGDDKkRI
0 1 K141‑ac VAtGDDKkRIIDsAR
0 1 S146‑p DKkRIIDsARsAyQE
0 1 S149‑p RIIDsARsAyQEAMD
0 2 Y151‑p IDsARsAyQEAMDIS
0 2 K159‑ac QEAMDISkKEMPPTN
5 0 S186‑p FHYEIANsPEEAISL
0 1 S209‑p MADLHTLsEDSYKDs
0 2 S216‑p sEDSYKDsTLIMQLL
0 7 S248‑p EAPQEPQs_______
  14-3-3 sigma iso2  
S5 ___MERASLIQKAKL
K11 ASLIQKAKLAEQAER
Y19 LAEQAERYEDMAAFM
G28 DMAAFMKGAVEKGEE
K32 FMKGAVEKGEELSCE
S45 CEERNLLSVAYKNVV
Y48 RNLLSVAYKNVVGGQ
K49 NLLSVAYKNVVGGQR
K49 NLLSVAYKNVVGGQR
S63 RAAWRVLSSIEQKSN
S64 AAWRVLSSIEQKSNE
K68 VLSSIEQKSNEEGSE
S69 LSSIEQKSNEEGSEE
S74 QKSNEEGSEEKGPEV
K77 NEEGSEEKGPEVREY
- gap
- gap
- gap
- gap
K90 EYRVFYLKMKGDYYR
K90 EYRVFYLKMKGDYYR
K92 RVFYLKMKGDYYRYL
Y96 LKMKGDYYRYLAEVA
T104 RYLAEVATGDDKKRI
K109 VATGDDKKRIIDSAR
S114 DKKRIIDSARSAYQE
S117 RIIDSARSAYQEAMD
Y119 IDSARSAYQEAMDIS
K127 QEAMDISKKEMPPTN
S154 FHYEIANSPEEAISL
S177 MADLHTLSEDSYKDS
S184 SEDSYKDSTLIMQLL
S216 EAPQEPQS_______
  mouse

 
S5 ___MERASLIQKAkL
K11‑ub ASLIQKAkLAEQAER
Y19‑p LAEQAERyEDMAAFM
S28‑p DMAAFMKsAVEKGEE
K32 FMKsAVEKGEELSCE
S45‑p CEERNLLsVAyKNVV
Y48‑p RNLLsVAyKNVVGGQ
K49 NLLsVAyKNVVGGQR
K49 NLLsVAyKNVVGGQR
S63‑p RAAWRVLssIEQKsN
S64‑p AAWRVLssIEQKsNE
K68 VLssIEQKsNEEGsE
S69‑p LssIEQKsNEEGsEE
S74‑p QKsNEEGsEEKGPEV
K77 NEEGsEEKGPEVKEY
T90‑p EYREKVEtELRGVCD
T98‑p ELRGVCDtVLGLLDS
K109‑ub LLDSHLIkGAGDAEs
S116‑p kGAGDAEsRVFYLkM
K122‑ac EsRVFYLkMkGDYyR
K122‑ub EsRVFYLkMkGDYyR
K124‑ub RVFYLkMkGDYyRYL
Y128‑p LkMkGDYyRYLAEVA
T136‑p RYLAEVAtGDDKKRI
K141 VAtGDDKKRIIDSAR
S146 DKKRIIDSARSAYQE
S149 RIIDSARSAYQEAMD
Y151 IDSARSAYQEAMDIS
K159 QEAMDISKKEMPPTN
S186‑p FHYEIANsPEEAISL
S209 MADLHTLSEDSYKDs
S216‑p SEDSYKDsTLIMQLL
S248 EAPEEPQS_______
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