EGFLA_HUMAN - dbPTM
EGFLA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EGFLA_HUMAN
UniProt AC Q63HQ2
Protein Name Pikachurin
Gene Name EGFLAM
Organism Homo sapiens (Human).
Sequence Length 1017
Subcellular Localization Secreted, extracellular space, extracellular matrix . Cell junction, synapse . Detected in the synaptic cleft of the ribbon synapse around the postsynaptic terminals of bipolar cells. Colocalizes with BSN, CTBP2 and DAG1 in photoreceptor synaptic ter
Protein Description Involved in both the retinal photoreceptor ribbon synapse formation and physiological functions of visual perception. Necessary for proper bipolar dendritic tip apposition to the photoreceptor ribbon synapse. Promotes matrix assembly and cell adhesiveness (By similarity)..
Protein Sequence MDLIRGVLLRLLLLASSLGPGAVSLRAAIRKPGKVGPPLDIKLGALNCTAFSIQWKMPRHPGSPILGYTVFYSEVGADKSLQEQLHSVPLSRDIPTTEEVIGDLKPGTEYRVSIAAYSQAGKGRLSSPRHVTTLSQDSCLPPAAPQQPHVIVVSDSEVALSWKPGASEGSAPIQYYSVEFIRPDFDKKWTSIHERIQMDSMVIKGLDPDTNYQFAVRAMNSHGPSPRSWPSDIIRTLCPEEAGSGRYGPRYITDMGAGEDDEGFEDDLDLDISFEEVKPLPATKGGNKKFLVESKKMSISNPKTISRLIPPTSASLPVTTVAPQPIPIQRKGKNGVAIMSRLFDMPCDETLCSADSFCVNDYTWGGSRCQCTLGKGGESCSEDIVIQYPQFFGHSYVTFEPLKNSYQAFQITLEFRAEAEDGLLLYCGENEHGRGDFMSLAIIRRSLQFRFNCGTGVAIIVSETKIKLGGWHTVMLYRDGLNGLLQLNNGTPVTGQSQGQYSKITFRTPLYLGGAPSAYWLVRATGTNRGFQGCVQSLAVNGRRIDMRPWPLGKALSGADVGECSSGICDEASCIHGGTCTAIKADSYICLCPLGFKGRHCEDAFTLTIPQFRESLRSYAATPWPLEPQHYLSFMEFEITFRPDSGDGVLLYSYDTGSKDFLSINLAGGHVEFRFDCGSGTGVLRSEDPLTLGNWHELRVSRTAKNGILQVDKQKIVEGMAEGGFTQIKCNTDIFIGGVPNYDDVKKNSGVLKPFSGSIQKIILNDRTIHVKHDFTSGVNVENAAHPCVRAPCAHGGSCRPRKEGYDCDCPLGFEGLHCQKECGNYCLNTIIEAIEIPQFIGRSYLTYDNPDILKRVSGSRSNVFMRFKTTAKDGLLLWRGDSPMRPNSDFISLGLRDGALVFSYNLGSGVASIMVNGSFNDGRWHRVKAVRDGQSGKITVDDYGARTGKSPGMMRQLNINGALYVGGMKEIALHTNRQYMRGLVGCISHFTLSTDYHISLVEDAVDGKNINTCGAK
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
31AcetylationSLRAAIRKPGKVGPP
HHHHHHCCCCCCCCC
52.5919413330
47N-linked_GlycosylationDIKLGALNCTAFSIQ
EEEECCCCCEEEEEE
22.13UniProtKB CARBOHYD
50UbiquitinationLGALNCTAFSIQWKM
ECCCCCEEEEEEECC
9.8222817900
54UbiquitinationNCTAFSIQWKMPRHP
CCEEEEEEECCCCCC
32.3222817900
55UbiquitinationCTAFSIQWKMPRHPG
CEEEEEEECCCCCCC
9.3921890473
55 (in isoform 4)Ubiquitination-9.3921890473
73UbiquitinationLGYTVFYSEVGADKS
CEEEEEEECCCCCHH
17.8421963094
80PhosphorylationSEVGADKSLQEQLHS
ECCCCCHHHHHHHHC
35.5127251275
87PhosphorylationSLQEQLHSVPLSRDI
HHHHHHHCCCCCCCC
33.7429449344
91PhosphorylationQLHSVPLSRDIPTTE
HHHCCCCCCCCCCCH
23.1029449344
113PhosphorylationPGTEYRVSIAAYSQA
CCCEEEEEEEEECCC
9.4924719451
117PhosphorylationYRVSIAAYSQAGKGR
EEEEEEEECCCCCCC
7.7224719451
126PhosphorylationQAGKGRLSSPRHVTT
CCCCCCCCCCCCEEE
36.6117081983
127PhosphorylationAGKGRLSSPRHVTTL
CCCCCCCCCCCEEEC
30.4625137130
200PhosphorylationHERIQMDSMVIKGLD
HHHHCCCCEEECCCC
15.0327251275
221PhosphorylationFAVRAMNSHGPSPRS
HHHHHHHCCCCCCCC
19.4125002506
225PhosphorylationAMNSHGPSPRSWPSD
HHHCCCCCCCCCCHH
37.2225002506
228PhosphorylationSHGPSPRSWPSDIIR
CCCCCCCCCCHHHHH
46.8825002506
231PhosphorylationPSPRSWPSDIIRTLC
CCCCCCCHHHHHHHC
34.8725002506
273PhosphorylationDDLDLDISFEEVKPL
CCCCCCCCEEEEECC
26.69-
283PhosphorylationEVKPLPATKGGNKKF
EEECCCCCCCCCCEE
28.43-
284UbiquitinationVKPLPATKGGNKKFL
EECCCCCCCCCCEEE
67.9122817900
288UbiquitinationPATKGGNKKFLVESK
CCCCCCCCEEEEEEE
48.4522817900
289 (in isoform 2)Ubiquitination-48.1821890473
289 (in isoform 1)Ubiquitination-48.1821890473
289UbiquitinationATKGGNKKFLVESKK
CCCCCCCEEEEEEEE
48.1822817900
294PhosphorylationNKKFLVESKKMSISN
CCEEEEEEEECCCCC
30.0525404012
298PhosphorylationLVESKKMSISNPKTI
EEEEEECCCCCCCCH
31.57-
312O-linked_GlycosylationISRLIPPTSASLPVT
HHHHCCCCCCCCCCE
31.41OGP
319O-linked_GlycosylationTSASLPVTTVAPQPI
CCCCCCCEEECCCCC
17.39OGP
446PhosphorylationSLAIIRRSLQFRFNC
HHHHHHHHHCEEECC
19.3729970186
473PhosphorylationIKLGGWHTVMLYRDG
EEECCEEEEEEEECC
10.9122468782
527UbiquitinationWLVRATGTNRGFQGC
EEHHHCCCCCCCCHH
19.8629967540
554AcetylationMRPWPLGKALSGADV
CCCCCCCCCCCCCCC
54.5619819087
615PhosphorylationTIPQFRESLRSYAAT
EHHHHHHHHHHHCCC
25.4822210691
631PhosphorylationWPLEPQHYLSFMEFE
CCCCCHHEEEEEEEE
9.9722210691
633PhosphorylationLEPQHYLSFMEFEIT
CCCHHEEEEEEEEEE
18.5122210691
696UbiquitinationPLTLGNWHELRVSRT
CCCCCCCEEEEEEEE
28.3621963094
703PhosphorylationHELRVSRTAKNGILQ
EEEEEEEECCCCCEE
34.1822210691
715AcetylationILQVDKQKIVEGMAE
CEEECHHHHHHHHHC
55.2319828367
729AcetylationEGGFTQIKCNTDIFI
CCCCCEEEECCCEEE
16.187491961
749PhosphorylationYDDVKKNSGVLKPFS
HHHHHHCCCCCCCCC
38.8828258704
761UbiquitinationPFSGSIQKIILNDRT
CCCCCEEEEEECCCE
30.0029967540
930UbiquitinationGRWHRVKAVRDGQSG
CCEEEEEEEECCCCC
9.9421963094
938UbiquitinationVRDGQSGKITVDDYG
EECCCCCEEEECCCH
40.2121963094
940PhosphorylationDGQSGKITVDDYGAR
CCCCCEEEECCCHHC
22.7423403867
944PhosphorylationGKITVDDYGARTGKS
CEEEECCCHHCCCCC
14.2823403867
948PhosphorylationVDDYGARTGKSPGMM
ECCCHHCCCCCCCCC
48.7223403867
951PhosphorylationYGARTGKSPGMMRQL
CHHCCCCCCCCCCEE
28.2023403867

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 EGFLA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EGFLA_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 EGFLA_HUMAN !!

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

Oops, there are no PPI records of EGFLA_HUMAN !!

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 EGFLA_HUMAN

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Related Literatures of Post-Translational Modification

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