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PLXNA1 (human)

Overview PLXNA1 Coreceptor for SEMA3A, SEMA3C, SEMA3F and SEMA6D. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down- stream signaling events in the cytoplasm. Interacts directly with NRP1 and NRP2. Interacts with FARP2, RND1 and KDR/VEGFR2. Binding of SEMA3A leads to dissociation of FARP2. Detected in fetal brain, lung, liver and kidney. Belongs to the plexin family. Note: This description may include information from UniProtKB. Protein type: Receptor, misc.; Membrane protein, integral; Motility/polarity/chemotaxis Cellular Component: cytoplasm; integral to membrane; plasma membrane; nucleus Molecular Function: semaphorin receptor activity; receptor activity Biological Process: axon guidance; multicellular organismal development Reference #:  Q9UIW2 (UniProtKB) Alt. Names/Synonyms: DKFZp761P19121; NOV; NOVP; plexin 1; plexin A1; Plexin-A1; PLXA1; PLXN1; PLXNA1; Semaphorin receptor NOV Gene Symbols: PLXNA1 Molecular weight: 211,067 Da Basal Isoelectric point: 6.49  Predict pI for various phosphorylation states CST Pathways:  Regulation of Actin Dynamics Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below PLXNA1 3RYT - A/B=1269-1894 (mouse)

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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
0	1		Y122	NKLLLLDYAANRLLA
0	1		T446	AYDYRGRTVVFAGTR
0	1		S454	VVFAGTRSGRIRKIL
0	1		K1041-u	QLTNPEVkYNYTEDP
0	1		Y1097-p	RENGCLVyNDTTMVC
0	1		K1353	EVQANVEKSLTLFGQ
0	1		T1356	ANVEKSLTLFGQLLT
0	1		T1363	TLFGQLLTKKHFLLT
0	1		Y1403-p	ALQGEMEyATGVLKQ
0	2		K1418-u	LLSDLIEkNLESKNH
0	1		K1454-a	FLLYKFLkECAGEPL
0	1		Y1486-p	AITGEARySLSEDKL
0	1		Y1500-p	LIRQQIDyKTLTLNC
0	56		Y1608-p	VPKQTSAyNISNSSt
0	1		T1615-p	yNISNSStFTKSLSR
0	1		K1618	SNSStFTKSLSRyEs
0	1		Y1623-p	FTKSLSRyEsMLRTA
0	3		S1625-p	KSLSRyEsMLRTASs
0	1		S1631	EsMLRTASsPDsLRS
0	2		S1632-p	sMLRTASsPDsLRSR
0	5		S1635-p	RTASsPDsLRSRTPM
0	1		T1644	RSRTPMITPDLESGT
0	2		Y1817-p	KSWVERYyADIAKMP
0	1		S1844	EQSRLHLSQFNSMSA

	mouse
Y120-p	NKLLLLDyAANRLLA
T444-p	AYDYQGRtVVFAGTR
S452-p	VVFAGTRsGRIRKIL
K1039	QLSNPEVKYNYTEDP
Y1095	RENSCMVYNDTTMVC
K1351-u	EVQANVEkSLtLFGQ
T1354-p	ANVEkSLtLFGQLLt
T1361-p	tLFGQLLtKKHFLLT
Y1401	ALQGEMEYATGVLKQ
K1416-u	LLSDLIEkNLESKNH
K1452	FLLYKFLKECAGEPL
Y1484	AITGEARYSLSEDKL
Y1498	LIRQQIDYKTLTLNC
Y1606	VPKQTSAYNISNSST
T1613	YNISNSSTFTkSLSR
K1616-u	SNSSTFTkSLSRYEs
Y1621	FTkSLSRYEsMLRTA
S1623-p	kSLSRYEsMLRTAss
S1629-p	EsMLRTAssPDsLRS
S1630-p	sMLRTAssPDsLRSR
S1633-p	RTAssPDsLRSRTPM
T1642-p	RSRTPMItPDLESGT
Y1815	KSWVERYYADIAKMP
S1842-p	EQSRLHLsQFNSMSA

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