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Protein Page:
FIP1L1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
FIP1L1 a component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre- mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. FIP1L1 contributes to poly(A) site recognition and stimulates poly(A) addition. Binds to U-rich RNA sequence elements surrounding the poly(A) site. May act to tether poly(A) polymerase to the CPSF complex. A fusion of FIP1L1 and PDGFRA (FIP1L1-PDGFRA) is the cause of some cases of hypereosinophilic syndrome (HES), a disorder characterized by overproduction of eosinophils in the bone marrow, eosinophilia, tissue infiltration and organ damage. Four alternatively spliced isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: RNA processing
Cellular Component: nucleolus; mRNA cleavage and polyadenylation specificity factor complex; nucleus
Molecular Function: RNA binding
Biological Process: mRNA processing
Reference #:  Q6UN15 (UniProtKB)
Alt. Names/Synonyms: DKFZp586K0717; Factor interacting with PAP; FIP1; FIP1 like 1; FIP1 like 1 (S. cerevisiae); FIP1-like 1 protein; FIP1L1; FLJ33619; hFip1; Pre-mRNA 3'-end-processing factor FIP1; Rearranged in hypereosinophilia; RHE
Gene Symbols: FIP1L1
Molecular weight: 66,526 Da
Basal Isoelectric point: 5.42  Predict pI for various phosphorylation states
Select Structure to View Below

FIP1L1

Protein Structure Not Found.


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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


 SS 

SS: 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.


 MS 

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


       human

 
0 12 Y27-p DEEEEWLyGGPWDVH
0 1 S37-p PWDVHVHsDLAKDLD
0 1 S57 RPEEENASANPPSGI
0 1 S62 NASANPPSGIEDETA
0 12 S85-p VTETEDDsDsDsDDD
0 12 S87-p ETEDDsDsDsDDDED
0 10 S89-p EDDsDsDsDDDEDDV
1 6 Y110-p IKTGAPQyGsyGTAP
0 1 S112-p TGAPQyGsyGTAPVN
0 35 Y113-p GAPQyGsyGTAPVNL
0 2 K123-u APVNLNIkTGGRVyG
0 8 Y129-p IkTGGRVyGTTGTKV
0 1 D158-ca PLLEVDLdSFEDKPW
0 4 Y175-p PGADLSDyFNYGFNE
0 1 K186-a GFNEDTWkAYCEKQK
0 4 T221-p EDCTMEVtPGAEIQD
0 1 T253-g KETALPStKAEFtsP
0 1 T258-p PStKAEFtsPPSLFK
0 36 S259-p StKAEFtsPPSLFKT
0 2 S274-p GLPPSRNstssQsQt
0 1 T275-g LPPSRNstssQsQtS
0 1 S276-g PPSRNstssQsQtSt
0 3 S277-p PSRNstssQsQtStA
0 5 S279-p RNstssQsQtStASR
0 2 T281-p stssQsQtStASRKA
0 1 T283-p ssQsQtStASRKANS
0 1 S285 QsQtStASRKANSSV
0 1 S285 QsQtStASRKANSSV
0 2 K294-a KANSSVGkWQDRYGR
0 15 S304-p DRYGRAEsPDLRRLP
0 46 Y426-p RSARAFPyGNVAFPH
0 4 S440-p HLPGSAPsWPsLVDT
0 1 S443-p GSAPsWPsLVDTSKQ
0 3 Y453-p DTSKQWDyyARREKD
0 12 Y454-p TSKQWDyyARREKDR
0 3 T482-p RDRERERtRERERER
0 75 S492-p RERERDHsPtPsVFN
0 44 T494-p RERDHsPtPsVFNsD
0 26 S496-p RDHsPtPsVFNsDEE
0 43 S500-p PtPsVFNsDEERyRY
0 4 Y505-p FNsDEERyRYREyAE
0 4 Y510-p ERyRYREyAERGyER
0 3 Y515-p REyAERGyERHRASR
0 5 S548-p HKSSRSNsRRRHEsE
0 75 S554-p NsRRRHEsEEGDsHR
0 3 S559-p HEsEEGDsHRRHKHK
0 17 T591-p EQESTEAtPAE____
  mouse

 
Y26 DEEEEWLYGGPWDVH
S36 PWDVHVHSDLAKDLD
S56-p RPEEENAsANPPsGI
S61-p NAsANPPsGIEEEAA
S84-p VTETEDDsDsDsDDD
S86-p ETEDDsDsDsDDDED
S88-p EDDsDsDsDDDEDDV
Y109 IKTGAPQYGSYGTAP
S111 TGAPQYGSYGTAPVN
Y112 GAPQYGSYGTAPVNL
K122-u APVNLNIkAGGRVYG
Y128 IkAGGRVYGNTGTKV
D157 PLLEVDLDSFEDKPW
Y174 PGADLSDYFNYGFNE
K185 GFNEDTWKAYCEKQK
- gap
T229 KEAALPSTKAEFtsP
T234-p PSTKAEFtsPPSLFK
S235-p STKAEFtsPPSLFKT
S250 GLPPSRNSTSsQSQT
T251 LPPSRNSTSsQSQTS
S252 PPSRNSTSsQSQTST
S253-p PSRNSTSsQSQTSTA
S255 RNSTSsQSQTSTAsR
T257 STSsQSQTSTAsRKA
T259 SsQSQTSTAsRKASS
S261-p QSQTSTAsRKASSSV
S261-g QSQTSTAsRKASSSV
K270 KASSSVGKWQDRYGR
S280-p DRYGRAEsPDLRRLP
Y411 RSARAFPYGNVAFPH
S425 HLTSSAPSWPSLVDT
S428 SSAPSWPSLVDTTKQ
Y438 DTTKQWDYYARREKD
Y439 TTKQWDYYARREKDR
T469-p RDRERERtRERERER
S479-p RERERDHsPtPsVFN
T481-p RERDHsPtPsVFNsD
S483-p RDHsPtPsVFNsDEE
S487-p PtPsVFNsDEERyRY
Y492-p FNsDEERyRYREYAE
Y497 ERyRYREYAERGYER
Y502 REYAERGYERHRASR
S535-p HKSSRSNsRRRHEsE
S541-p NsRRRHEsEEGDsHR
S546-p HEsEEGDsHRRHKHK
A578 EQESTEAAPAE____
  rat

 
Y26 DEEEEWLYGGPWDVH
S36 PWDVHVHSDLAKDLD
S56 RPEEENASANPPSGI
S61 NASANPPSGIEEEAA
S84 VTETEDDSDSDSDDD
S86 ETEDDSDSDSDDDED
S88 EDDSDSDSDDDEDDV
Y109 IKTGAPQYGSYGTAP
S111 TGAPQYGSYGTAPVN
Y112 GAPQYGSYGTAPVNL
K122 APVNLNIKAGGRVYG
Y128 IKAGGRVYGNTGTKV
D157 PLLEVDLDSFEDKPW
Y174 PGADLSDYFNYGFNE
K185 GFNEDTWKAYCEKQK
- gap
T229 KEAALPSTKAEFTSP
T234 PSTKAEFTSPPSLFK
S235 STKAEFTSPPSLFKT
- gap
- gap
- gap
- gap
- gap
- gap
- under review  
- gap
- under review  
- gap
- gap
Y366 RSARAFPYGNVAFPH
S380 HLTSSAPSWPSLVDT
S383 SSAPSWPSLVDTTKQ
Y393 DTTKQWDYYARREKD
Y394 TTKQWDYYARREKDR
T424 RDRERERTRERERER
S434-p RERERDHsPtPSVFN
T436-p RERDHsPtPSVFNsD
S438 RDHsPtPSVFNsDEE
S442-p PtPSVFNsDEERYRY
Y447 FNsDEERYRYREYAE
Y452 ERYRYREYAERGYER
Y457 REYAERGYERHRASR
S490 HKSSRSNSRRRHEsE
S496-p NSRRRHEsEEGDSHR
S501 HEsEEGDSHRRHKHK
A533 EQESTEAAPAE____
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