PLXA4_HUMAN - dbPTM
PLXA4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLXA4_HUMAN
UniProt AC Q9HCM2
Protein Name Plexin-A4
Gene Name PLXNA4
Organism Homo sapiens (Human).
Sequence Length 1894
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Coreceptor for SEMA3A. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance in the developing nervous system. 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 (By similarity)..
Protein Sequence MKAMPWNWTCLLSHLLMVGMGSSTLLTRQPAPLSQKQRSFVTFRGEPAEGFNHLVVDERTGHIYLGAVNRIYKLSSDLKVLVTHETGPDEDNPKCYPPRIVQTCNEPLTTTNNVNKMLLIDYKENRLIACGSLYQGICKLLRLEDLFKLGEPYHKKEHYLSGVNESGSVFGVIVSYSNLDDKLFIATAVDGKPEYFPTISSRKLTKNSEADGMFAYVFHDEFVASMIKIPSDTFTIIPDFDIYYVYGFSSGNFVYFLTLQPEMVSPPGSTTKEQVYTSKLVRLCKEDTAFNSYVEVPIGCERSGVEYRLLQAAYLSKAGAVLGRTLGVHPDDDLLFTVFSKGQKRKMKSLDESALCIFILKQINDRIKERLQSCYRGEGTLDLAWLKVKDIPCSSALLTIDDNFCGLDMNAPLGVSDMVRGIPVFTEDRDRMTSVIAYVYKNHSLAFVGTKSGKLKKIRVDGPRGNALQYETVQVVDPGPVLRDMAFSKDHEQLYIMSERQLTRVPVESCGQYQSCGECLGSGDPHCGWCVLHNTCTRKERCERSKEPRRFASEMKQCVRLTVHPNNISVSQYNVLLVLETYNVPELSAGVNCTFEDLSEMDGLVVGNQIQCYSPAAKEVPRIITENGDHHVVQLQLKSKETGMTFASTSFVFYNCSVHNSCLSCVESPYRCHWCKYRHVCTHDPKTCSFQEGRVKLPEDCPQLLRVDKILVPVEVIKPITLKAKNLPQPQSGQRGYECILNIQGSEQRVPALRFNSSSVQCQNTSYSYEGMEINNLPVELTVVWNGHFNIDNPAQNKVHLYKCGAMRESCGLCLKADPDFACGWCQGPGQCTLRQHCPAQESQWLELSGAKSKCTNPRITEIIPVTGPREGGTKVTIRGENLGLEFRDIASHVKVAGVECSPLVDGYIPAEQIVCEMGEAKPSQHAGFVEICVAVCRPEFMARSSQLYYFMTLTLSDLKPSRGPMSGGTQVTITGTNLNAGSNVVVMFGKQPCLFHRRSPSYIVCNTTSSDEVLEMKVSVQVDRAKIHQDLVFQYVEDPTIVRIEPEWSIVSGNTPIAVWGTHLDLIQNPQIRAKHGGKEHINICEVLNATEMTCQAPALALGPDHQSDLTERPEEFGFILDNVQSLLILNKTNFTYYPNPVFEAFGPSGILELKPGTPIILKGKNLIPPVAGGNVKLNYTVLVGEKPCTVTVSDVQLLCESPNLIGRHKVMARVGGMEYSPGMVYIAPDSPLSLPAIVSIAVAGGLLIIFIVAVLIAYKRKSRESDLTLKRLQMQMDNLESRVALECKEAFAELQTDIHELTSDLDGAGIPFLDYRTYTMRVLFPGIEDHPVLRDLEVPGYRQERVEKGLKLFAQLINNKVFLLSFIRTLESQRSFSMRDRGNVASLIMTVLQSKLEYATDVLKQLLADLIDKNLESKNHPKLLLRRTESVAEKMLTNWFTFLLYKFLKECAGEPLFSLFCAIKQQMEKGPIDAITGEARYSLSEDKLIRQQIDYKTLVLSCVSPDNANSPEVPVKILNCDTITQVKEKILDAIFKNVPCSHRPKAADMDLEWRQGSGARMILQDEDITTKIENDWKRLNTLAHYQVPDGSVVALVSKQVTAYNAVNNSTVSRTSASKYENMIRYTGSPDSLRSRTPMITPDLESGVKMWHLVKNHEHGDQKEGDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETIFSTAHRGSALPLAIKYMFDFLDEQADKHGIHDPHVRHTWKSNCLPLRFWVNMIKNPQFVFDIHKNSITDACLSVVAQTFMDSCSTSEHRLGKDSPSNKLLYAKDIPSYKNWVERYYSDIGKMPAISDQDMNAYLAEQSRMHMNEFNTMSALSEIFSYVGKYSEEILGPLDHDDQCGKQKLAYKLEQVITLMSLDS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
75PhosphorylationVNRIYKLSSDLKVLV
HHHHEECCCCCEEEE		20.0422210691
76PhosphorylationNRIYKLSSDLKVLVT
HHHEECCCCCEEEEE		58.3522210691
159PhosphorylationPYHKKEHYLSGVNES
CCCCCCCCCCCCCCC		12.03-
166PhosphorylationYLSGVNESGSVFGVI
CCCCCCCCCCEEEEE		31.03-
344AcetylationTVFSKGQKRKMKSLD
EECCCCCCCCCCCCC		63.7630591413
461 (in isoform 2)Phosphorylation-52.08-
462 (in isoform 2)Phosphorylation-15.79-
466 (in isoform 2)Phosphorylation-38.46-
488PhosphorylationVLRDMAFSKDHEQLY
HHHCCCCCCCHHHEE		27.86-
649PhosphorylationTGMTFASTSFVFYNC
CCCCEEEEEEEEEEC		23.8222798277
655N-linked_GlycosylationSTSFVFYNCSVHNSC
EEEEEEEECEECCCH		10.50UniProtKB CARBOHYD
657PhosphorylationSFVFYNCSVHNSCLS
EEEEEECEECCCHHH		23.8322798277
668PhosphorylationSCLSCVESPYRCHWC
CHHHHCCCCCCCCEE		13.5622798277
811S-palmitoylationCGAMRESCGLCLKAD
CCCCHHHCCEEEECC		4.0629575903
814S-palmitoylationMRESCGLCLKADPDF
CHHHCCEEEECCCCC		1.9129575903
877PhosphorylationREGGTKVTIRGENLG
CCCCEEEEECCEECC		13.4024719451
946PhosphorylationPEFMARSSQLYYFMT
HHHHHCCCHHEEEEE		20.7417525332
957PhosphorylationYFMTLTLSDLKPSRG
EEEEEEHHHCCCCCC		35.3425332170
967PhosphorylationKPSRGPMSGGTQVTI
CCCCCCCCCCCEEEE		36.8925278378
970PhosphorylationRGPMSGGTQVTITGT
CCCCCCCCEEEEEEE		24.3225278378
973PhosphorylationMSGGTQVTITGTNLN
CCCCCEEEEEEEECC		11.7325278378
975PhosphorylationGGTQVTITGTNLNAG
CCCEEEEEEEECCCC		28.7025332170
977PhosphorylationTQVTITGTNLNAGSN
CEEEEEEEECCCCCC		28.0825278378
983PhosphorylationGTNLNAGSNVVVMFG
EEECCCCCCEEEEEC		24.8425278378
1002PhosphorylationLFHRRSPSYIVCNTT
EEECCCCCEEEEECC		28.83-
1003PhosphorylationFHRRSPSYIVCNTTS
EECCCCCEEEEECCC		10.76-
1007N-linked_GlycosylationSPSYIVCNTTSSDEV
CCCEEEEECCCCHHH		35.18UniProtKB CARBOHYD
1009PhosphorylationSYIVCNTTSSDEVLE
CEEEEECCCCHHHEE		16.55-
1132N-linked_GlycosylationVQSLLILNKTNFTYY
HHHEEEEECCCCCCC		41.95UniProtKB CARBOHYD
1138PhosphorylationLNKTNFTYYPNPVFE
EECCCCCCCCCHHHH		16.88-
1139PhosphorylationNKTNFTYYPNPVFEA
ECCCCCCCCCHHHHH		8.09-
1180N-linked_GlycosylationAGGNVKLNYTVLVGE
CCCCEEEEEEEEECC		25.39UniProtKB CARBOHYD
1232PhosphorylationMVYIAPDSPLSLPAI
EEEECCCCCCCHHHH		27.04-
1235PhosphorylationIAPDSPLSLPAIVSI
ECCCCCCCHHHHHHH		35.37-
1270PhosphorylationKSRESDLTLKRLQMQ
HCCCCHHHHHHHHHH		34.9128060719
1350AcetylationYRQERVEKGLKLFAQ
CCHHHHHHHHHHHHH		67.6819608861
1419PhosphorylationLIDKNLESKNHPKLL
HHHHCCCCCCCHHHH		41.7620886841
1424UbiquitinationLESKNHPKLLLRRTE
CCCCCCHHHHHHCCH		44.19-
1483PhosphorylationAITGEARYSLSEDKL
EECCCEECCCCHHHH		22.4728102081
1484PhosphorylationITGEARYSLSEDKLI
ECCCEECCCCHHHHH		21.6228102081
1489UbiquitinationRYSLSEDKLIRQQID
ECCCCHHHHHHHHCC		41.59-
1497PhosphorylationLIRQQIDYKTLVLSC
HHHHHCCCCEEEEEC		13.91-
1543PhosphorylationIFKNVPCSHRPKAAD
HHHCCCCCCCCCCCC		19.2324719451
1605PhosphorylationVSKQVTAYNAVNNST
EECEEEEECCCCCCC		8.3525884760
1621PhosphorylationSRTSASKYENMIRYT
CCCCCHHHHHCHHHC		15.2722210691
1627PhosphorylationKYENMIRYTGSPDSL
HHHHCHHHCCCCHHH		12.4323403867
1628PhosphorylationYENMIRYTGSPDSLR
HHHCHHHCCCCHHHH		22.7223403867
1630PhosphorylationNMIRYTGSPDSLRSR
HCHHHCCCCHHHHCC		20.1028355574
1633PhosphorylationRYTGSPDSLRSRTPM
HHCCCCHHHHCCCCC		29.1219664994
1636PhosphorylationGSPDSLRSRTPMITP
CCCHHHHCCCCCCCC		45.8820639409
1642PhosphorylationRSRTPMITPDLESGV
HCCCCCCCCCHHHCC		12.4224719451
1647PhosphorylationMITPDLESGVKMWHL
CCCCCHHHCCCEEEH		57.0725599653
1670PhosphorylationQKEGDRGSKMVSEIY
CCCCCHHHHHHHHHH		20.6224719451
1677PhosphorylationSKMVSEIYLTRLLAT
HHHHHHHHHHHHHCC		9.66-
1685UbiquitinationLTRLLATKGTLQKFV
HHHHHCCHHHHHHHH		44.27-
1767PhosphorylationDIHKNSITDACLSVV
ECCCCCHHHHHHHHH		19.8429116813
1791UbiquitinationTSEHRLGKDSPSNKL
CCCCCCCCCCCCCCE		60.67-
1795PhosphorylationRLGKDSPSNKLLYAK
CCCCCCCCCCEEEEC		51.0228857561
1797UbiquitinationGKDSPSNKLLYAKDI
CCCCCCCCEEEECCC		44.18-
1800PhosphorylationSPSNKLLYAKDIPSY
CCCCCEEEECCCHHH		23.26-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PLXA4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLXA4_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PLXA4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
QORL1_HUMANCRYZL1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLXA4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1350, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-946, AND MASSSPECTROMETRY.

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