SYNJ1_RAT - dbPTM
SYNJ1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYNJ1_RAT
UniProt AC Q62910
Protein Name Synaptojanin-1
Gene Name Synj1
Organism Rattus norvegicus (Rat).
Sequence Length 1574
Subcellular Localization Cytoplasm, perinuclear region .
Protein Description Phosphatase that acts on various phosphoinositides, including phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)-bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate (By similarity). Has a role in clathrin-mediated endocytosis. [PubMed: 9428629 Hydrolyzes PIP2 bound to actin regulatory proteins resulting in the rearrangement of actin filaments downstream of tyrosine kinase and ASH/GRB2 (By similarity]
Protein Sequence MAFSKGFRIYHKLDPPPFSLIVETRHKEECLMFESGAVAVLSSAEKEAIKGTYAKVLDAYGLLGVLRLNLGDTMLHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRVDASDEDRISEVRKVLNSGNFYFAWSASGVSLDLSLNAHRSMQEHTTDNRFFWNQSLHLHLKHYGVNCDDWLLRLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLDDCVSSFIQIRGSVPLFWEQPGLQVGSHRVRMSRGFEANAPAFDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLKASEHASDIHMVSFDYHQMVKGGKAEKLHSVLKPQVQKFLDYGFFYFDGSAVQRCQSGTVRTNCLDCLDRTNSVQAFLGLEMLAKQLEALGLAEKPQLVTRFQEVFRSMWSVNGDSISKIYAGTGALEGKAKLKDGARSVTRTIQNNFFDSSKQEAIDVLLLGNTLNSDLADKARALLTTGSLRVSEQTLQSASSKVLKNMCENFYKYSKPKKIRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWAVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNEDFVEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRAELKTSDHRPVVALIDIDIFEVEAEERQKIYKEVIAVQGPPDGTVLVSIKSSAQENTFFDDALIDELLQQFAHFGEVILIRFVEDKMWVTFLEGSSALNVLSLNGKELLNRTITITLKSPDWIKTLEEEMSLEKISVTLPSSTSSTLLGEDAEVSADFDMEGDVDDYSAEVEELLPQHLQPSSSSGLGTSPSSSPRTSPCQSPTAPEYSAPSLPIRPSRAPSRTPGPLSSQGAPVDTQPAAQKESSQTIEPKRPPPPRPVAPPARPAPPQRPPPPSGARSPAPARKEFGGVGAPPSPGVTRREMEAPKSPGTARKDNIGRNQPSPQAGLAGPGPSGYGAARPTIPARAGVISAPQSQARVSAGRLTPESQSKPLETSKGPAVLPEPLKPQAAFPPQPSLPTPAQKLQDPLVPIAAPMPPSIPQSNLETPPLPPPRSRSSQSLPSDSSPQLQQEQPTGQQVKINGACGVKQEPTLKSDPFEDLSLSVLAVSKAQPSAQISPVLTPDPKMLIQLPSASQSKVNSLSSVSCMLTMPPVPEQSKSQESVGSSANPFPSLPTRNPFTDRTAAPGNPFRVQSQESEATSWLSKEEPVSNSPFPPLMPLSHDMSKPSSSLDGFEDNFDLQSQSTVKTSNPKGWVTFDEDEDFPTKGKSRSVYPDSLGNTAASFDDDWSKGTNVSFCVLPARRPPPPPPPVPLLPPGTTSSAGPSTTLSSKASPTLDFTER
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
5Acetylation---MAFSKGFRIYHK
---CCCCCCEEEEEC
56.4622902405
60PhosphorylationYAKVLDAYGLLGVLR
HHHHHHHHHHHHHEE
14.15-
295AcetylationTLKDLYGKQIVVNLL
HHHHHHCCCCEEEHH
24.2422902405
305AcetylationVVNLLGSKEGEHMLS
EEEHHCCCHHHHHHH
68.8622902405
352AcetylationEKLHSVLKPQVQKFL
HHHHHHHHHHHHHHH
31.1122902405
414AcetylationEALGLAEKPQLVTRF
HHCCCCCCHHHHHHH
32.2422902405
499PhosphorylationKARALLTTGSLRVSE
HHHHHHHHCCCCCCH
25.4127097102
501PhosphorylationRALLTTGSLRVSEQT
HHHHHHCCCCCCHHH
15.7727097102
515UbiquitinationTLQSASSKVLKNMCE
HHHHHCHHHHHHHHH
49.44-
577UbiquitinationGIQEFQDKRSKPTDI
CHHHHHHCCCCCCCE
48.03-
659UbiquitinationDVAVDTVKTGMGGAT
EEEECCCCCCCCCCC
41.26-
744 (in isoform 6)Phosphorylation-55.3926437020
747 (in isoform 6)Phosphorylation-44.6626437020
783PhosphorylationGKVTFAPTYKYDLFS
CCEEECCEECEECCC
29.26-
784PhosphorylationKVTFAPTYKYDLFSE
CEEECCEECEECCCC
13.39-
786PhosphorylationTFAPTYKYDLFSEDY
EECCEECEECCCCCC
13.89-
820PhosphorylationRKWPFDRSAEDLDLL
CCCCCCCCHHHHHHH
37.5422673903
830PhosphorylationDLDLLNASFQDESKI
HHHHHCCCCCCCCCE
23.5123984901
835PhosphorylationNASFQDESKILYTWT
CCCCCCCCCEEEEEC
33.0323984901
982PhosphorylationKTLEEEMSLEKISVT
HHHHHHHCCCEEEEE
36.3325403869
1048PhosphorylationSPSSSPRTSPCQSPT
CCCCCCCCCCCCCCC
40.1727097102
1049PhosphorylationPSSSPRTSPCQSPTA
CCCCCCCCCCCCCCC
25.5930411139
1053PhosphorylationPRTSPCQSPTAPEYS
CCCCCCCCCCCCCCC
30.8223712012
1055PhosphorylationTSPCQSPTAPEYSAP
CCCCCCCCCCCCCCC
61.1527097102
1059PhosphorylationQSPTAPEYSAPSLPI
CCCCCCCCCCCCCCC
14.7427097102
1060PhosphorylationSPTAPEYSAPSLPIR
CCCCCCCCCCCCCCC
31.8528551015
1063PhosphorylationAPEYSAPSLPIRPSR
CCCCCCCCCCCCCCC
46.6328551015
1073PhosphorylationIRPSRAPSRTPGPLS
CCCCCCCCCCCCCCC
48.0428432305
1075PhosphorylationPSRAPSRTPGPLSSQ
CCCCCCCCCCCCCCC
36.6128432305
1080PhosphorylationSRTPGPLSSQGAPVD
CCCCCCCCCCCCCCC
24.6128432305
1081PhosphorylationRTPGPLSSQGAPVDT
CCCCCCCCCCCCCCC
40.0728432305
1131PhosphorylationPPPSGARSPAPARKE
CCCCCCCCCCCCCHH
25.5325403869
1144 (in isoform 5)Phosphorylation-15.4926437020
1144 (in isoform 4)Phosphorylation-15.4926437020
1147 (in isoform 4)Phosphorylation-32.9726437020
1147PhosphorylationGGVGAPPSPGVTRRE
CCCCCCCCCCCCHHH
32.9728551015
1147 (in isoform 5)Phosphorylation-32.9726437020
1151PhosphorylationAPPSPGVTRREMEAP
CCCCCCCCHHHCCCC
29.8928551015
1160PhosphorylationREMEAPKSPGTARKD
HHCCCCCCCCCCCCC
27.7428551015
1175PhosphorylationNIGRNQPSPQAGLAG
CCCCCCCCCCCCCCC
21.6329779826
1186PhosphorylationGLAGPGPSGYGAARP
CCCCCCCCCCCCCCC
51.0323984901
1188PhosphorylationAGPGPSGYGAARPTI
CCCCCCCCCCCCCCC
14.1323984901
1194PhosphorylationGYGAARPTIPARAGV
CCCCCCCCCCCCCCC
33.7623984901
1198MethylationARPTIPARAGVISAP
CCCCCCCCCCCEECC
26.90-
1212PhosphorylationPQSQARVSAGRLTPE
CHHHHHHCCCCCCHH
21.3228432305
1217PhosphorylationRVSAGRLTPESQSKP
HHCCCCCCHHHHCCC
24.5329779826
1220PhosphorylationAGRLTPESQSKPLET
CCCCCHHHHCCCCCC
40.7430240740
1222PhosphorylationRLTPESQSKPLETSK
CCCHHHHCCCCCCCC
45.5825403869
1227PhosphorylationSQSKPLETSKGPAVL
HHCCCCCCCCCCCCC
43.3428432305
1228PhosphorylationQSKPLETSKGPAVLP
HCCCCCCCCCCCCCC
26.6628432305
1287PhosphorylationPPLPPPRSRSSQSLP
CCCCCCCCCCCCCCC
42.1427097102
1289PhosphorylationLPPPRSRSSQSLPSD
CCCCCCCCCCCCCCC
33.6927097102
1290PhosphorylationPPPRSRSSQSLPSDS
CCCCCCCCCCCCCCC
23.7627097102
1292PhosphorylationPRSRSSQSLPSDSSP
CCCCCCCCCCCCCCH
44.1727097102
1295PhosphorylationRSSQSLPSDSSPQLQ
CCCCCCCCCCCHHHH
56.2527097102
1297PhosphorylationSQSLPSDSSPQLQQE
CCCCCCCCCHHHHCC
48.5327097102
1298PhosphorylationQSLPSDSSPQLQQEQ
CCCCCCCCHHHHCCC
22.9627097102
1346PhosphorylationAVSKAQPSAQISPVL
EEECCCCCCCCCCCC
22.2623984901
1350PhosphorylationAQPSAQISPVLTPDP
CCCCCCCCCCCCCCH
9.2528689409
1354PhosphorylationAQISPVLTPDPKMLI
CCCCCCCCCCHHHEE
26.3628689409
1427PhosphorylationGNPFRVQSQESEATS
CCCCEEECCCHHCCC
32.8128432305
1489PhosphorylationSNPKGWVTFDEDEDF
CCCCCEEEECCCCCC
20.8928432305
1516PhosphorylationSLGNTAASFDDDWSK
CCCCCCCCCCCCCCC
27.0928432305
1566PhosphorylationTTLSSKASPTLDFTE
CCCCCCCCCCCCCCC
23.3529779826
1568PhosphorylationLSSKASPTLDFTER-
CCCCCCCCCCCCCC-
36.1422673903
1572PhosphorylationASPTLDFTER-----
CCCCCCCCCC-----
30.4328689409

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
1018YPhosphorylationKinaseEPHB2A0A0G2JY48
GPS
1059YPhosphorylationKinaseEPHB2A0A0G2JY48
GPS
1144SPhosphorylationKinaseCDK5Q03114
PSP
1160SPhosphorylationKinaseCDK5Q03114
PSP
1172YPhosphorylationKinaseEPHB2A0A0G2JY48
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYNJ1_RAT !!

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 SYNJ1_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EPS15_HUMANEPS15physical
9428629

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYNJ1_RAT

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Related Literatures of Post-Translational Modification

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