SYNJ2_HUMAN - dbPTM
SYNJ2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYNJ2_HUMAN
UniProt AC O15056
Protein Name Synaptojanin-2
Gene Name SYNJ2
Organism Homo sapiens (Human).
Sequence Length 1496
Subcellular Localization Cytoplasm . Cell membrane . Membrane raft . Cell projection, axon . Cytoplasm, cytoskeleton . Localizes at nerve terminals in brain and at bundles of microtubules surrounding the nucleus in the elongating spermatids corresponding to the manchette (By
Protein Description Inositol 5-phosphatase which may be involved in distinct membrane trafficking and signal transduction pathways. May mediate the inhibitory effect of Rac1 on endocytosis..
Protein Sequence MALSKGLRLLGRLGAEGDCSVLLEARGRDDCLLFEAGTVATLAPEEKEVIKGQYGKLTDAYGCLGELRLKSGGTSLSFLVLVTGCTSVGRIPDAEIYKITATDFYPLQEEAKEEERLIALKKILSSGVFYFSWPNDGSRFDLTVRTQKQGDDSSEWGNSFFWNQLLHVPLRQHQVSCCDWLLKIICGVVTIRTVYASHKQAKACLVSRVSCERTGTRFHTRGVNDDGHVSNFVETEQMIYMDDGVSSFVQIRGSVPLFWEQPGLQVGSHHLRLHRGLEANAPAFDRHMVLLKEQYGQQVVVNLLGSRGGEEVLNRAFKKLLWASCHAGDTPMINFDFHQFAKGGKLEKLETLLRPQLKLHWEDFDVFTKGENVSPRFQKGTLRMNCLDCLDRTNTVQSFIALEVLHLQLKTLGLSSKPIVDRFVESFKAMWSLNGHSLSKVFTGSRALEGKAKVGKLKDGARSMSRTIQSNFFDGVKQEAIKLLLVGDVYGEEVADKGGMLLDSTALLVTPRILKAMTERQSEFTNFKRIRIAMGTWNVNGGKQFRSNVLRTAELTDWLLDSPQLSGATDSQDDSSPADIFAVGFEEMVELSAGNIVNASTTNKKMWGEQLQKAISRSHRYILLTSAQLVGVCLYIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVGIRFQFHSTSFCFICSHLTAGQSQVKERNEDYKEITQKLCFPMGRNVFSHDYVFWCGDFNYRIDLTYEEVFYFVKRQDWKKLLEFDQLQLQKSSGKIFKDFHEGAINFGPTYKYDVGSAAYDTSDKCRTPAWTDRVLWWRKKHPFDKTAGELNLLDSDLDVDTKVRHTWSPGALQYYGRAELQASDHRPVLAIVEVEVQEVDVGARERVFQEVSSFQGPLDATVVVNLQSPTLEEKNEFPEDLRTELMQTLGSYGTIVLVRINQGQMLVTFADSHSALSVLDVDGMKVKGRAVKIRPKTKDWLKGLREEIIRKRDSMAPVSPTANSCLLEENFDFTSLDYESEGDILEDDEDYLVDEFNQPGVSDSELGGDDLSDVPGPTALAPPSKSPALTKKKQHPTYKDDADLVELKRELEAVGEFRHRSPSRSLSVPNRPRPPQPPQRPPPPTGLMVKKSASDASISSGTHGQYSILQTARLLPGAPQQPPKARTGISKPYNVKQIKTTNAQEAEAAIRCLLEARGGASEEALSAVAPRDLEASSEPEPTPGAAKPETPQAPPLLPRRPPPRVPAIKKPTLRRTGKPLSPEEQFEQQTVHFTIGPPETSVEAPPVVTAPRVPPVPKPRTFQPGKAAERPSHRKPASDEAPPGAGASVPPPLEAPPLVPKVPPRRKKSAPAAFHLQVLQSNSQLLQGLTYNSSDSPSGHPPAAGTVFPQGDFLSTSSATSPDSDGTKAMKPEAAPLLGDYQDPFWNLLHHPKLLNNTWLSKSSDPLDSGTRSPKRDPIDPVSAGASAAKAELPPDHEHKTLGHWVTISDQEKRTALQVFDPLAKT
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
4Phosphorylation----MALSKGLRLLG
----CCCHHHHHHHH		31.56-
5Ubiquitination---MALSKGLRLLGR
---CCCHHHHHHHHH		63.92-
51UbiquitinationPEEKEVIKGQYGKLT
HHHHHHHCCCCCCHH		45.17-
56UbiquitinationVIKGQYGKLTDAYGC
HHCCCCCCHHHHCCC		43.19-
61PhosphorylationYGKLTDAYGCLGELR
CCCHHHHCCCEEEEE		15.92-
112 (in isoform 3)Ubiquitination-69.7821906983
112 (in isoform 2)Ubiquitination-69.7821890473
112 (in isoform 1)Ubiquitination-69.7821890473
112UbiquitinationYPLQEEAKEEERLIA
ECCHHHHHHHHHHHH		69.7821906983
130PhosphorylationILSSGVFYFSWPNDG
HHHCCCEEEECCCCC		8.3622817900
220PhosphorylationRTGTRFHTRGVNDDG
CCCCCEEECCCCCCC		26.8023403867
235PhosphorylationHVSNFVETEQMIYMD
CCCCCEEEEEEEEEC		26.6423403867
240PhosphorylationVETEQMIYMDDGVSS
EEEEEEEEECCCHHH		6.8023403867
247PhosphorylationYMDDGVSSFVQIRGS
EECCCHHHEEEEECC		27.3423403867
268PhosphorylationQPGLQVGSHHLRLHR
CCCCCCCCHHHHHCC		14.6327251275
348UbiquitinationAKGGKLEKLETLLRP
HCCCCHHHHHHHHCH		63.16-
369UbiquitinationEDFDVFTKGENVSPR
HCCEEEECCCCCCHH		53.41-
374PhosphorylationFTKGENVSPRFQKGT
EECCCCCCHHHCCCC		23.1821712546
393PhosphorylationCLDCLDRTNTVQSFI
HHHHHHCCCHHHHHH		34.6025072903
395PhosphorylationDCLDRTNTVQSFIAL
HHHHCCCHHHHHHHH		21.2225072903
398PhosphorylationDRTNTVQSFIALEVL
HCCCHHHHHHHHHHH		17.8125072903
411PhosphorylationVLHLQLKTLGLSSKP
HHHHHHHHCCCCCCH		34.3525072903
415PhosphorylationQLKTLGLSSKPIVDR
HHHHCCCCCCHHHHH		34.2225072903
416PhosphorylationLKTLGLSSKPIVDRF
HHHCCCCCCHHHHHH		47.7125072903
477UbiquitinationSNFFDGVKQEAIKLL
HCCCCCCCHHHHHHH		48.20-
490PhosphorylationLLLVGDVYGEEVADK
HHHHHCCCCHHHHHC		24.45-
504PhosphorylationKGGMLLDSTALLVTP
CCCEECCHHHHHHCH		18.62-
505PhosphorylationGGMLLDSTALLVTPR
CCEECCHHHHHHCHH		22.4623403867
510PhosphorylationDSTALLVTPRILKAM
CHHHHHHCHHHHHHH		13.5624719451
515UbiquitinationLVTPRILKAMTERQS
HHCHHHHHHHHHCHH		33.47-
543UbiquitinationTWNVNGGKQFRSNVL
CEECCCCHHHHHCHH		47.89-
547PhosphorylationNGGKQFRSNVLRTAE
CCCHHHHHCHHHHHH		32.3625404012
616PhosphorylationEQLQKAISRSHRYIL
HHHHHHHHHHHHHHH		32.3722673903
618PhosphorylationLQKAISRSHRYILLT
HHHHHHHHHHHHHHC		12.9122673903
779PhosphorylationGAINFGPTYKYDVGS
CCCCCCCCEECCCCC		32.7828348404
781UbiquitinationINFGPTYKYDVGSAA
CCCCCCEECCCCCCE		37.14-
825PhosphorylationGELNLLDSDLDVDTK
CHHCCCCCCCCCCCC		39.7918491316
838PhosphorylationTKVRHTWSPGALQYY
CCCEECCCCCHHHHE		18.0125159151
891PhosphorylationFQGPLDATVVVNLQS
CCCCCCEEEEEECCC		17.3222468782
898PhosphorylationTVVVNLQSPTLEEKN
EEEEECCCCCHHHCC		24.0222468782
918PhosphorylationLRTELMQTLGSYGTI
HHHHHHHHHHCCCEE		21.08-
921PhosphorylationELMQTLGSYGTIVLV
HHHHHHHCCCEEEEE		24.41-
922PhosphorylationLMQTLGSYGTIVLVR
HHHHHHCCCEEEEEE		19.2527762562
947PhosphorylationADSHSALSVLDVDGM
ECCCCCCEEEECCCC		21.9822210691
989PhosphorylationRDSMAPVSPTANSCL
CCCCCCCCCCCHHCC		18.5726074081
991PhosphorylationSMAPVSPTANSCLLE
CCCCCCCCCHHCCEE		30.8526074081
994PhosphorylationPVSPTANSCLLEENF
CCCCCCHHCCEECCC		12.0426074081
1032PhosphorylationEFNQPGVSDSELGGD
CCCCCCCCHHHCCCC		41.1424275569
1078UbiquitinationDADLVELKRELEAVG
HHHHHHHHHHHHHHH		30.26-
1079 (in isoform 2)Phosphorylation-67.3729507054
1095PhosphorylationRHRSPSRSLSVPNRP
CCCCCCCCCCCCCCC		29.3624719451
1097PhosphorylationRSPSRSLSVPNRPRP
CCCCCCCCCCCCCCC		36.4526657352
1120AcetylationPPTGLMVKKSASDAS
CCCCEEEECCCCCCC		27.3525953088
1122PhosphorylationTGLMVKKSASDASIS
CCEEEECCCCCCCCC		27.5621945579
1124PhosphorylationLMVKKSASDASISSG
EEEECCCCCCCCCCC		40.5823401153
1127PhosphorylationKKSASDASISSGTHG
ECCCCCCCCCCCCCC		28.1721945579
1129PhosphorylationSASDASISSGTHGQY
CCCCCCCCCCCCCCC		21.8821945579
1130PhosphorylationASDASISSGTHGQYS
CCCCCCCCCCCCCCH		46.1421945579
1132PhosphorylationDASISSGTHGQYSIL
CCCCCCCCCCCCHHH		25.4421945579
1136PhosphorylationSSGTHGQYSILQTAR
CCCCCCCCHHHHHHH		11.4121945579
1137PhosphorylationSGTHGQYSILQTARL
CCCCCCCHHHHHHHC		14.6721945579
1141PhosphorylationGQYSILQTARLLPGA
CCCHHHHHHHCCCCC		15.4221945579
1169UbiquitinationPYNVKQIKTTNAQEA
CCCCEECCCCCHHHH		46.96-
1191PhosphorylationLEARGGASEEALSAV
HHHCCCCCHHHHHHH		38.9620058876
1196PhosphorylationGASEEALSAVAPRDL
CCCHHHHHHHCCCCC		27.9526074081
1207PhosphorylationPRDLEASSEPEPTPG
CCCCCCCCCCCCCCC		65.3124719451
1212PhosphorylationASSEPEPTPGAAKPE
CCCCCCCCCCCCCCC		32.4624719451
1220PhosphorylationPGAAKPETPQAPPLL
CCCCCCCCCCCCCCC		29.2722199227
1246PhosphorylationKKPTLRRTGKPLSPE
CCCCCCCCCCCCCHH		43.0228348404
1251PhosphorylationRRTGKPLSPEEQFEQ
CCCCCCCCHHHHHHC		38.5028464451
1260PhosphorylationEEQFEQQTVHFTIGP
HHHHHCCEEEEEECC		18.6827251275
1318PhosphorylationAPPGAGASVPPPLEA
CCCCCCCCCCCCCCC		33.95-
1387 (in isoform 2)Ubiquitination-18.0121890473
1411PhosphorylationAAPLLGDYQDPFWNL
HCCCCCCCCCCHHHH		17.0228796482
1428PhosphorylationHPKLLNNTWLSKSSD
CHHHHCCCCCCCCCC		27.0624719451
1431PhosphorylationLLNNTWLSKSSDPLD
HHCCCCCCCCCCCCC		23.2723186163
1432UbiquitinationLNNTWLSKSSDPLDS
HCCCCCCCCCCCCCC		52.3821890473
1432 (in isoform 1)Ubiquitination-52.3821890473
1433PhosphorylationNNTWLSKSSDPLDSG
CCCCCCCCCCCCCCC		36.2825849741
1434PhosphorylationNTWLSKSSDPLDSGT
CCCCCCCCCCCCCCC		47.1623927012
1439PhosphorylationKSSDPLDSGTRSPKR
CCCCCCCCCCCCCCC		50.1525159151
1441PhosphorylationSDPLDSGTRSPKRDP
CCCCCCCCCCCCCCC		31.7425159151
1443PhosphorylationPLDSGTRSPKRDPID
CCCCCCCCCCCCCCC		34.3125159151
1453PhosphorylationRDPIDPVSAGASAAK
CCCCCCCCCCHHHHH		26.7728555341
1496PhosphorylationVFDPLAKT-------
HCCCCCCC-------		37.9322199227
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
490YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYNJ2_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 SYNJ2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYJ2B_HUMANSYNJ2BPphysical
10357812
RAC1_HUMANRAC1physical
11084340
ITSN2_HUMANITSN2physical
12421765
SH3K1_HUMANSH3KBP1physical
15090612
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYNJ2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1191, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-130, AND MASSSPECTROMETRY.

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