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

Overview
Spinophilin actin-binding regulatory subunit of protein phosphatase 1 (PP1). The actin-binding domain of spinophilin is necessary and sufficient for targeting of spinophilin to dendrites and dendritic spines. May play a role in establishing a signaling complex for dopaminergic neurotransmission through D2 receptors by linking receptors downstream signaling molecules and the actin cytoskeleton. Interacts with p14-ARF. Contains one PDZ/DHR domain. Note: This description may include information from UniProtKB.
Protein type: Protein phosphatase, regulatory subunit; Adaptor/scaffold
Cellular Component: nucleoplasm; cortical actin cytoskeleton; adherens junction; lamellipodium; cytoplasm; dendritic spine; plasma membrane; synapse; protein phosphatase type 1 complex; filopodium
Molecular Function: protein binding; protein phosphatase inhibitor activity; actin binding; protein phosphatase 1 binding
Biological Process: cell migration; regulation of cell growth by extracellular stimulus; regulation of protein amino acid phosphorylation; filopodium formation; RNA splicing; calcium-mediated signaling; regulation of exit from mitosis; actin filament organization; regulation of cell proliferation; negative regulation of catalytic activity; dendrite development; negative regulation of cell growth; cell cycle arrest
Reference #:  Q96SB3 (UniProtKB)
Alt. Names/Synonyms: FLJ30345; NEB2; neurabin II; Neurabin-2; Neurabin-II; PPP1R6; PPP1R9; PPP1R9B; Protein phosphatase 1 regulatory subunit 9B; protein phosphatase 1, regulatory (inhibitor) subunit 9B; protein phosphatase 1, regulatory subunit 9B; protein phosphatase 1, regulatory subunit 9B, spinophilin; SPINO; Spinophilin; SPL; Spn
Gene Symbols: PPP1R9B
Molecular weight: 89,192 Da
Basal Isoelectric point: 4.91  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Spinophilin

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

 
1 0 S15 GPGGPLRSASPHRsA
1 0 S17 GGPLRSASPHRsAyE
0 2 S21-p RSASPHRsAyEAGIQ
0 37 Y23-p ASPHRsAyEAGIQAL
0 1 S87-p LAEAPRAsERGVRLs
6 4 S94-p sERGVRLsLPRAssL
1 4 S99-p RLsLPRAssLNENVD
3 17 S100-p LsLPRAssLNENVDH
0 1 T115-p SALLKLGtSVSERVS
3 1 G175 LLRQERAGLQDRKLD
0 10 S190-p VVVRFNGstEALDKL
0 5 T191-p VVRFNGstEALDKLD
1 5 S203-p KLDADAVsPTVSQLS
0 1 S210 sPTVSQLSAVFEKAD
0 1 S246-p SKLVSKRsRVFQPPP
0 5 S304-p KPVEVEEsGEsEAEs
0 2 S307-p EVEEsGEsEAEsAPG
0 3 S311-p sGEsEAEsAPGEVIQ
1 0 Y396 DLVDVSAYSGLGEDS
0 2 S436-p CVEIPGLsEEEDPAP
0 1 S444-p EEEDPAPsRKIHFST
0 1 S478-p DVDPMAAsAEyELEK
1 1 Y481-p PMAAsAEyELEKRVE
0 2 S656-p AENEDALsPVDMEPE
0 1 K675-ub KFKELQIkHAVTEAE
0 1 K687-ub EAEIQQLkRKLQSLE
0 1 S710-p EKAQLEQsVEENKER
0 38 Y746-p LRETQAQyQALERKY
0 1 K798 EMDKLLDKISELEGN
  mouse

 
S15-p GPGGPLRsAsPHRSA
S17-p GGPLRsAsPHRSAYE
S21 RsAsPHRSAYEAGIQ
Y23 AsPHRSAYEAGIQAL
S87 MAEAPRASDRGVRLs
S94-p SDRGVRLsLPRAssL
S99-p RLsLPRAssLNENVD
S100-p LsLPRAssLNENVDH
T115 SALLKLGTSVSERVS
G177 LLRQERAGLQDRKLD
S192-p VVVRFNGstEALDKL
T193-p VVRFNGstEALDKLD
S205-p KLDADAVsPTVSQLs
S212-p sPTVSQLsAVFEKAD
S248 SKLVTKRSRVFQPPP
S305 KPVEVEESGESEAES
S308 EVEESGESEAESAPG
S312 SGESEAESAPGEVIQ
Y398-p DLVDVSAySGLGEDS
S438 CVEIPGLSEEEDPAP
S446 EEEDPAPSRKIHFST
S480 DVDPMAASAEyELEK
Y483-p PMAASAEyELEKRVE
S658 AENEDALSPVEMEPE
K677 KFKELQIKHAVTEAE
K689 EAEIQQLKRKLQSLE
S712 EKAQLEQSVEENKER
Y748 LRETQAQYQALERKY
K800-ub EMDKLLDkISELEGN
  rat

 
S15 GPGGPLRSASPHRSA
S17 GGPLRSASPHRSAYE
S21 RSASPHRSAYEAGIQ
Y23 ASPHRSAYEAGIQAL
S87 MAEAPRASDRGVRLs
S94-p SDRGVRLsLPRAssL
S99-p RLsLPRAssLNENVD
S100-p LsLPRAssLNENVDH
T115 SALLKLGTSVSERVS
S177-p LLRQERAsLQDRKLD
S192 VVVRFNGSTEALDKL
T193 VVRFNGSTEALDKLD
S205 KLDADAVSPTVSQLS
S212 SPTVSQLSAVFEKAD
S248 SKLVTKRSRVFQPPP
S305 KPVEVEESGESEAES
S308 EVEESGESEAESAPG
S312 SGESEAESAPGEVIQ
Y398 DLVDVSAYSGLGEDS
S438 CVEIPGLSEEEDPAP
S446 EEEDPAPSRKIHFST
S480 DVDPMAASAEYELEK
Y483 PMAASAEYELEKRVE
S658 AENEDALSPVEMEPE
K677 KFKELQIKHAVTEAE
K689 EAEIQQLKRKLQSLE
S712 EKAQLEQSVEENKER
Y748 LRETQAQYQALERKY
K800 EMDKLLDKISELEGN
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