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Spinophilin (human)

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: Adaptor/scaffold; Protein phosphatase, regulatory subunit Cellular Component: nucleoplasm; cytoskeleton; adherens junction; lamellipodium; cytoplasm; dendritic spine; plasma membrane; synapse; protein phosphatase type 1 complex; filopodium Molecular Function: protein binding; actin binding; protein phosphatase inhibitor activity; protein phosphatase 1 binding Biological Process: nervous system development; regulation of cell growth by extracellular stimulus; cell migration; filopodium formation; RNA splicing; regulation of exit from mitosis; negative regulation of cell growth; cell differentiation; cell cycle arrest; regulation of cell proliferation 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®

Select Structure to View Below Spinophilin 2G5M - B=492-602 (rat) 3EGG - D/C=417-583 (rat) 3EGH - D/C=417-583 (rat)

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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

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	40		Y23-p	ASPHRsAyEAGIQAL
0	1		S87-p	LAEAPRAsERGVRLs
5	3		S94-p	sERGVRLsLPRAssL
1	3		S99-p	RLsLPRAssLNENVD
3	14		S100-p	LsLPRAssLNENVDH
0	1		T115-p	SALLKLGtSVSERVS
2	1		G175	LLRQERAGLQDRKLD
0	7		S190-p	VVVRFNGstEALDKL
0	3		T191-p	VVRFNGstEALDKLD
1	3		S203-p	KLDADAVsPTVSQLS
0	1		S210	sPTVSQLSAVFEKAD
0	1		S246-p	SKLVSKRsRVFQPPP
0	4		S304-p	KPVEVEEsGEsEAEs
0	1		S307-p	EVEEsGEsEAEsAPG
0	3		S311-p	sGEsEAEsAPGEVIQ
1	0		Y396	DLVDVSAYSGLGEDS
0	1		S436-p	CVEIPGLsEEEDPAP
1	0		Y481	PMAASAEYELEKRVE
0	1		S656-p	AENEDALsPVDMEPE
0	1		K675-u	KFKELQIkHAVTEAE
0	1		K687-u	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
Y483-p	PMAASAEyELEKRVE
S658	AENEDALSPVEMEPE
K677	KFKELQIKHAVTEAE
K689	EAEIQQLKRKLQSLE
S712	EKAQLEQSVEENKER
Y748	LRETQAQYQALERKY
K800-u	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
Y483	PMAASAEYELEKRVE
S658	AENEDALSPVEMEPE
K677	KFKELQIKHAVTEAE
K689	EAEIQQLKRKLQSLE
S712	EKAQLEQSVEENKER
Y748	LRETQAQYQALERKY
K800	EMDKLLDKISELEGN

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