PLXA2_HUMAN - dbPTM
PLXA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLXA2_HUMAN
UniProt AC O75051
Protein Name Plexin-A2
Gene Name PLXNA2
Organism Homo sapiens (Human).
Sequence Length 1894
Subcellular Localization Cell membrane
Single-pass type I membrane protein.
Protein Description Coreceptor for SEMA3A and SEMA6A. Necessary for signaling by SEMA6A and 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 (By similarity)..
Protein Sequence MEQRRPWPRALEVDSRSVVLLSVVWVLLAPPAAGMPQFSTFHSENRDWTFNHLTVHQGTGAVYVGAINRVYKLTGNLTIQVAHKTGPEEDNKSCYPPLIVQPCSEVLTLTNNVNKLLIIDYSENRLLACGSLYQGVCKLLRLDDLFILVEPSHKKEHYLSSVNKTGTMYGVIVRSEGEDGKLFIGTAVDGKQDYFPTLSSRKLPRDPESSAMLDYELHSDFVSSLIKIPSDTLALVSHFDIFYIYGFASGGFVYFLTVQPETPEGVAINSAGDLFYTSRIVRLCKDDPKFHSYVSLPFGCTRAGVEYRLLQAAYLAKPGDSLAQAFNITSQDDVLFAIFSKGQKQYHHPPDDSALCAFPIRAINLQIKERLQSCYQGEGNLELNWLLGKDVQCTKAPVPIDDNFCGLDINQPLGGSTPVEGLTLYTTSRDRMTSVASYVYNGYSVVFVGTKSGKLKKIRADGPPHGGVQYEMVSVLKDGSPILRDMAFSIDQRYLYVMSERQVTRVPVESCEQYTTCGECLSSGDPHCGWCALHNMCSRRDKCQQAWEPNRFAASISQCVSLAVHPSSISVSEHSRLLSLVVSDAPDLSAGIACAFGNLTEVEGQVSGSQVICISPGPKDVPVIPLDQDWFGLELQLRSKETGKIFVSTEFKFYNCSAHQLCLSCVNSAFRCHWCKYRNLCTHDPTTCSFQEGRINISEDCPQLVPTEEILIPVGEVKPITLKARNLPQPQSGQRGYECVLNIQGAIHRVPALRFNSSSVQCQNSSYQYDGMDISNLAVDFAVVWNGNFIIDNPQDLKVHLYKCAAQRESCGLCLKADRKFECGWCSGERRCTLHQHCTSPSSPWLDWSSHNVKCSNPQITEILTVSGPPEGGTRVTIHGVNLGLDFSEIAHHVQVAGVPCTPLPGEYIIAEQIVCEMGHALVGTTSGPVRLCIGECKPEFMTKSHQQYTFVNPSVLSLNPIRGPESGGTMVTITGHYLGAGSSVAVYLGNQTCEFYGRSMSEIVCVSPPSSNGLGPVPVSVSVDRAHVDSNLQFEYIDDPRVQRIEPEWSIASGHTPLTITGFNLDVIQEPRIRVKFNGKESVNVCKVVNTTTLTCLAPSLTTDYRPGLDTVERPDEFGFVFNNVQSLLIYNDTKFIYYPNPTFELLSPTGVLDQKPGSPIILKGKNLCPPASGGAKLNYTVLIGETPCAVTVSETQLLCEPPNLTGQHKVMVHVGGMVFSPGSVSVISDSLLTLPAIVSIAAGGSLLLIIVIIVLIAYKRKSRENDLTLKRLQMQMDNLESRVALECKEAFAELQTDINELTSDLDRSGIPYLDYRTYAMRVLFPGIEDHPVLRELEVQGNGQQHVEKALKLFAQLINNKVFLLTFIRTLELQRSFSMRDRGNVASLIMTGLQGRLEYATDVLKQLLSDLIDKNLENKNHPKLLLRRTESVAEKMLTNWFAFLLHKFLKECAGEPLFMLYCAIKQQMEKGPIDAITGEARYSLSEDKLIRQQIEYKTLILNCVNPDNENSPEIPVKVLNCDTITQVKEKILDAVYKNVPYSQRPRAVDMDLEWRQGRIARVVLQDEDITTKIEGDWKRLNTLMHYQVSDRSVVALVPKQTSSYNIPASASISRTSISRYDSSFRYTGSPDSLRSRAPMITPDLESGVKVWHLVKNHDHGDQKEGDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETLFSTVHRGSALPLAIKYMFDFLDEQADRHSIHDTDVRHTWKSNCLPLRFWVNVIKNPQFVFDIHKGSITDACLSVVAQTFMDSCSTSEHRLGKDSPSNKLLYAKDIPSYKSWVERYYADIAKLPAISDQDMNAYLAEQSRLHAVEFNMLSALNEIYSYVSKYSEELIGALEQDEQARRQRLAYKVEQLINAMSIES
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
15PhosphorylationPRALEVDSRSVVLLS
CCCCCCCCHHHHEEE
31.4724719451
49PhosphorylationHSENRDWTFNHLTVH
CCCCCCEEEEEEEEE
20.8829978859
54PhosphorylationDWTFNHLTVHQGTGA
CEEEEEEEEECCCCE
14.3729978859
59PhosphorylationHLTVHQGTGAVYVGA
EEEEECCCCEEEEEE
18.5229978859
63PhosphorylationHQGTGAVYVGAINRV
ECCCCEEEEEECCEE
7.8229978859
76N-linked_GlycosylationRVYKLTGNLTIQVAH
EEEEEECCEEEEEEE
28.86UniProtKB CARBOHYD
91N-linked_GlycosylationKTGPEEDNKSCYPPL
CCCCCCCCCCCCCCE
41.23UniProtKB CARBOHYD
138AcetylationSLYQGVCKLLRLDDL
HHHHHHHHHHCCCCE
48.4219828253
154AcetylationILVEPSHKKEHYLSS
EEECCCCCCCEEEEC
65.287978527
197PhosphorylationGKQDYFPTLSSRKLP
CCCCCCCCCCCCCCC
29.4026471730
199PhosphorylationQDYFPTLSSRKLPRD
CCCCCCCCCCCCCCC
30.4926471730
200PhosphorylationDYFPTLSSRKLPRDP
CCCCCCCCCCCCCCC
36.2326471730
224PhosphorylationLHSDFVSSLIKIPSD
ECHHHHHHHCCCCHH
28.8924719451
293PhosphorylationDDPKFHSYVSLPFGC
CCCCCCCEECCCCCC
5.86-
295PhosphorylationPKFHSYVSLPFGCTR
CCCCCEECCCCCCCC
23.30-
327N-linked_GlycosylationDSLAQAFNITSQDDV
CCHHHHCCCCCCCCE
39.38UniProtKB CARBOHYD
340PhosphorylationDVLFAIFSKGQKQYH
CEEEEEEECCCCCCC
29.7524719451
434PhosphorylationTSRDRMTSVASYVYN
CCCCCCHHHHHHHHC
13.32-
444PhosphorylationSYVYNGYSVVFVGTK
HHHHCCEEEEEEEEC
17.13-
470PhosphorylationPPHGGVQYEMVSVLK
CCCCCCEEEEEEEEC
12.0020363803
474PhosphorylationGVQYEMVSVLKDGSP
CCEEEEEEEECCCCC
22.0320363803
598N-linked_GlycosylationGIACAFGNLTEVEGQ
HEEEECCCCEEEEEE
37.02UniProtKB CARBOHYD
696N-linked_GlycosylationSFQEGRINISEDCPQ
CCCCCCEECCCCCCC
30.30UniProtKB CARBOHYD
756N-linked_GlycosylationRVPALRFNSSSVQCQ
ECCEEECCCCCEEEC
34.25UniProtKB CARBOHYD
811S-palmitoylationCAAQRESCGLCLKAD
HHHCCCCCCEEEECC
4.0629575903
814S-palmitoylationQRESCGLCLKADRKF
CCCCCCEEEECCCCE
1.9129575903
850PhosphorylationSPWLDWSSHNVKCSN
CCCCCCCCCCEECCC
18.15-
1205N-linked_GlycosylationQLLCEPPNLTGQHKV
EEEECCCCCCCCCEE
62.03UniProtKB CARBOHYD
1222PhosphorylationHVGGMVFSPGSVSVI
EECCEEECCCCEEEE
19.5526074081
1225PhosphorylationGMVFSPGSVSVISDS
CEEECCCCEEEECCC
18.0126074081
1227PhosphorylationVFSPGSVSVISDSLL
EECCCCEEEECCCCC
18.5426074081
1230PhosphorylationPGSVSVISDSLLTLP
CCCEEEECCCCCCHH
20.9926074081
1232PhosphorylationSVSVISDSLLTLPAI
CEEEECCCCCCHHHH
20.6326074081
1235PhosphorylationVISDSLLTLPAIVSI
EECCCCCCHHHHHHH
35.6726074081
1264PhosphorylationLIAYKRKSRENDLTL
HHHHHHHCCCCCHHH
49.19-
1272UbiquitinationRENDLTLKRLQMQMD
CCCCHHHHHHHHHHH
45.91-
1388PhosphorylationRDRGNVASLIMTGLQ
CCCCCHHHHHHHCCH
17.72-
1424UbiquitinationLENKNHPKLLLRRTE
CCCCCCHHHHHHCCH
44.19-
1451AcetylationFLLHKFLKECAGEPL
HHHHHHHHHHCCCHH
54.6119827435
1483PhosphorylationAITGEARYSLSEDKL
EECCCEECCCCHHHH
22.4728102081
1484PhosphorylationITGEARYSLSEDKLI
ECCCEECCCCHHHHH
21.6228102081
1489UbiquitinationRYSLSEDKLIRQQIE
ECCCCHHHHHHHHHH
41.59-
1524PhosphorylationVKVLNCDTITQVKEK
EEEECCCCHHHHHHH
28.29-
1593PhosphorylationHYQVSDRSVVALVPK
EEECCCCEEEEEEEC
26.4025999147
1605PhosphorylationVPKQTSSYNIPASAS
EECCCCCCCCCCCCE
19.5125884760
1610PhosphorylationSSYNIPASASISRTS
CCCCCCCCCEECCCE
19.7324719451
1612PhosphorylationYNIPASASISRTSIS
CCCCCCCEECCCEEE
20.7123403867
1614PhosphorylationIPASASISRTSISRY
CCCCCEECCCEEECC
27.3220639409
1621PhosphorylationSRTSISRYDSSFRYT
CCCEEECCCCCCCCC
17.2423403867
1623PhosphorylationTSISRYDSSFRYTGS
CEEECCCCCCCCCCC
23.5723403867
1624PhosphorylationSISRYDSSFRYTGSP
EEECCCCCCCCCCCC
15.7324719451
1627PhosphorylationRYDSSFRYTGSPDSL
CCCCCCCCCCCCHHH
17.2823403867
1628PhosphorylationYDSSFRYTGSPDSLR
CCCCCCCCCCCHHHH
27.2523403867
1630PhosphorylationSSFRYTGSPDSLRSR
CCCCCCCCCHHHHHC
20.1028355574
1633PhosphorylationRYTGSPDSLRSRAPM
CCCCCCHHHHHCCCC
29.1219664994
1636PhosphorylationGSPDSLRSRAPMITP
CCCHHHHHCCCCCCC
37.7823403867
1670PhosphorylationQKEGDRGSKMVSEIY
CCCCCHHHHHHHHHH
20.6224719451
1677PhosphorylationSKMVSEIYLTRLLAT
HHHHHHHHHHHHHHC
9.66-
1685UbiquitinationLTRLLATKGTLQKFV
HHHHHHCHHHHHHHH
44.27-
1791UbiquitinationTSEHRLGKDSPSNKL
CCCCCCCCCCCCCCE
60.67-
1795PhosphorylationRLGKDSPSNKLLYAK
CCCCCCCCCCEEEEC
51.0228857561
1797UbiquitinationGKDSPSNKLLYAKDI
CCCCCCCCEEEECCC
44.18-
1800PhosphorylationSPSNKLLYAKDIPSY
CCCCCEEEECCCHHH
23.26-
1806PhosphorylationLYAKDIPSYKSWVER
EEECCCHHHHHHHHH
45.59-
1807PhosphorylationYAKDIPSYKSWVERY
EECCCHHHHHHHHHH
12.04-
1814PhosphorylationYKSWVERYYADIAKL
HHHHHHHHHHHHHHC
6.90-
1815PhosphorylationKSWVERYYADIAKLP
HHHHHHHHHHHHHCC
12.20-
1825PhosphorylationIAKLPAISDQDMNAY
HHHCCCCCHHHHHHH
31.18-
1832PhosphorylationSDQDMNAYLAEQSRL
CHHHHHHHHHHHHHH
11.0525307156
1837PhosphorylationNAYLAEQSRLHAVEF
HHHHHHHHHHHHHHH
28.4525307156
1848PhosphorylationAVEFNMLSALNEIYS
HHHHHHHHHHHHHHH
21.6825907765
1854PhosphorylationLSALNEIYSYVSKYS
HHHHHHHHHHHHHHC
6.4325907765
1855PhosphorylationSALNEIYSYVSKYSE
HHHHHHHHHHHHHCH
25.3925907765
1856PhosphorylationALNEIYSYVSKYSEE
HHHHHHHHHHHHCHH
7.5625907765
1858PhosphorylationNEIYSYVSKYSEELI
HHHHHHHHHHCHHHH
20.0425907765
1860PhosphorylationIYSYVSKYSEELIGA
HHHHHHHHCHHHHHH
17.51-
1861PhosphorylationYSYVSKYSEELIGAL
HHHHHHHCHHHHHHH
28.47-

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
1605YPhosphorylationKinaseFYNP06241
PSP
1677YPhosphorylationKinaseFYNP06241
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLXA2_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 PLXA2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBP2L_HUMANUBAP2Lphysical
12421765
FNBP4_HUMANFNBP4physical
12421765
CEMIP_HUMANCEMIPphysical
12421765
IFT80_HUMANIFT80physical
12421765
SYF1_HUMANXAB2physical
26344197

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 PLXA2_HUMAN

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Related Literatures of Post-Translational Modification

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