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

Overview
RKIP a phosphatidylethanolamine-binding protein. Has lower affinity for phosphatidylinositol and phosphatidylcholine. May be involved in the function of the presynaptic cholinergic neurons of the central nervous system. Increases the production of choline acetyltransferase but not acetylcholinesterase. Expressed in brain. Increased expression in aged senescence-accelerated mice. Note: This description may include information from UniProtKB.
Protein type: Inhibitor protein
Cellular Component: cytoplasm
Molecular Function: serine-type endopeptidase inhibitor activity; protein binding; enzyme binding; phosphatidylethanolamine binding; protein kinase binding; ATP binding
Reference #:  P30086 (UniProtKB)
Alt. Names/Synonyms: HCNP; HCNPpp; Hippocampal cholinergic neurostimulating peptide; Neuropolypeptide h3; PBP; PEBP; PEBP-1; PEBP1; phosphatidylethanolamine binding protein 1; Phosphatidylethanolamine-binding protein 1; prostatic binding protein; Prostatic-binding protein; Raf kinase inhibitor protein; Raf kinase inhibitory protein; RKIP
Gene Symbols: PEBP1
Molecular weight: 21,057 Da
Basal Isoelectric point: 7.01  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RKIP

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
molecular association, regulation: S153‑p
phosphorylation: S153‑p
receptor desensitization, altered: S153‑p
receptor internalization, altered: S153‑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


 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 6 K7-u _MPVDLSkWSGPLsL
0 2 S13-p SkWSGPLsLQEVDEQ
0 6 T28-p PQHPLHVtYAGAAVD
0 4 T42-p DELGKVLtPTQVkNR
0 1 T44 LGKVLtPTQVkNRPt
0 6 K47-u VLtPTQVkNRPtsIs
0 16 T51-p TQVkNRPtsIsWDGL
0 30 S52-p QVkNRPtsIsWDGLD
0 10 S54-p kNRPtsIsWDGLDsG
0 1 S60-p IsWDGLDsGkLYTLV
0 8 K62-a WDGLDsGkLYTLVLT
0 1 S75-p LTDPDAPsRKDPkyR
0 1 K77 DPDAPsRKDPkyREW
0 2 K80-a APsRKDPkyREWHHF
0 5 Y81-p PsRKDPkyREWHHFL
0 1 S98-p NMKGNDIssGTVLsD
0 1 S99-p MKGNDIssGTVLsDy
0 2 S104-p IssGTVLsDyVGSGP
0 5 Y106-p sGTVLsDyVGSGPPk
0 9 K113-u yVGSGPPkGTGLHRy
0 1 T115 GSGPPkGTGLHRyVW
0 1 Y120-p kGTGLHRyVWLVyEQ
0 7 Y125-p HRyVWLVyEQDRPLk
0 10 K132 yEQDRPLKCDEPILS
0 2 K132-a yEQDRPLkCDEPILS
0 27 K132-u yEQDRPLkCDEPILS
5 7 S153-p RGKFKVAsFRKKYEL
0 2 Y169-p APVAGTCyQAEWDDy
0 4 Y176-p yQAEWDDyVPkLyEQ
0 6 K179-u EWDDyVPkLyEQLsG
0 122 Y181-p DDyVPkLyEQLsGk_
0 4 S185-p PkLyEQLsGk_____
0 5 K187 LyEQLsGK_______
0 10 K187-u LyEQLsGk_______
  mouse

 
Q7 _MAADISQWAGPLCL
C13 SQWAGPLCLQEVDEP
D28 PQHALRVDYAGVTVD
T42-p DELGKVLtPtQVMNR
T44-p LGKVLtPtQVMNRPs
M47 VLtPtQVMNRPssIs
S51-p tQVMNRPssIsWDGL
S52-p QVMNRPssIsWDGLD
S54-p MNRPssIsWDGLDPG
P60 IsWDGLDPGKLYTLV
K62 WDGLDPGKLYTLVLT
S75 LTDPDAPSRkDPKFR
K77-u DPDAPSRkDPKFREW
K80 APSRkDPKFREWHHF
F81 PSRkDPKFREWHHFL
S98 NMKGNDISSGTVLSD
S99 MKGNDISSGTVLSDY
S104 ISSGTVLSDYVGSGP
Y106 SGTVLSDYVGSGPPS
S113 YVGSGPPSGtGLHRY
T115-p GSGPPSGtGLHRYVW
Y120 SGtGLHRYVWLVYEQ
Y125 HRYVWLVYEQEQPLs
S132-p YEQEQPLsCDEPILS
S132 YEQEQPLSCDEPILS
S132 YEQEQPLSCDEPILS
T153-p RGKFKVEtFRKKYNL
Y169 APVAGTCYQAEWDDY
Y176 YQAEWDDYVPKLyEQ
K179 EWDDYVPKLyEQLsG
Y181-p DDYVPKLyEQLsGk_
S185-p PKLyEQLsGk_____
K187-a LyEQLsGk_______
K187-u LyEQLsGk_______
  rat

 
Q7 _MAADISQWAGPLSL
S13 SQWAGPLSLQEVDEP
D28 PQHALRVDYGGVTVD
T42 DELGKVLTPTQVMNR
T44 LGKVLTPTQVMNRPs
M47 VLTPTQVMNRPssIS
S51-p TQVMNRPssISWDGL
S52-p QVMNRPssISWDGLD
S54 MNRPssISWDGLDPG
P60 ISWDGLDPGKLYTLV
K62 WDGLDPGKLYTLVLT
S75 LTDPDAPSRKDPKFR
K77 DPDAPSRKDPKFREW
K80 APSRKDPKFREWHHF
F81 PSRKDPKFREWHHFL
S98 NMKGNDISSGTVLSE
S99 MKGNDISSGTVLSEY
S104 ISSGTVLSEYVGSGP
Y106 SGTVLSEYVGSGPPK
K113 YVGSGPPKDTGLHRY
T115 GSGPPKDTGLHRYVW
Y120 KDTGLHRYVWLVYEQ
Y125 HRYVWLVYEQEQPLN
N132 YEQEQPLNCDEPILS
N132 YEQEQPLNCDEPILS
N132 YEQEQPLNCDEPILS
S153-p RGKFKVEsFRKKYHL
F169 APVAGTCFQAEWDDS
S176 FQAEWDDSVPKLHDQ
K179 EWDDSVPKLHDQLAG
H181 DDSVPKLHDQLAGK_
A185 PKLHDQLAGK_____
K187 LHDQLAGK_______
K187 LHDQLAGK_______
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