SE1L3_HUMAN - dbPTM
SE1L3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SE1L3_HUMAN
UniProt AC Q68CR1
Protein Name Protein sel-1 homolog 3
Gene Name SEL1L3
Organism Homo sapiens (Human).
Sequence Length 1132
Subcellular Localization Membrane
Single-pass membrane protein .
Protein Description
Protein Sequence MQRRGAGLGWPRQQQQQPPPLAVGPRAAAMVPSGGVPQGLGGRSACALLLLCYLNVVPSLGRQTSLTTSVIPKAEQSVAYKDFIYFTVFEGNVRNVSEVSVEYLCSQPCVVNLEAVVSSEFRSSIPVYKKRWKNEKHLHTSRTQIVHVKFPSIMVYRDDYFIRHSISVSAVIVRAWITHKYSGRDWNVKWEENLLHAVAKNYTLLQTIPPFERPFKDHQVCLEWNMGYIWNLRANRIPQCPLENDVVALLGFPYASSGENTGIVKKFPRFRNRELEATRRQRMDYPVFTVSLWLYLLHYCKANLCGILYFVDSNEMYGTPSVFLTEEGYLHIQMHLVKGEDLAVKTKFIIPLKEWFRLDISFNGGQIVVTTSIGQDLKSYHNQTISFREDFHYNDTAGYFIIGGSRYVAGIEGFFGPLKYYRLRSLHPAQIFNPLLEKQLAEQIKLYYERCAEVQEIVSVYASAAKHGGERQEACHLHNSYLDLQRRYGRPSMCRAFPWEKELKDKHPSLFQALLEMDLLTVPRNQNESVSEIGGKIFEKAVKRLSSIDGLHQISSIVPFLTDSSCCGYHKASYYLAVFYETGLNVPRDQLQGMLYSLVGGQGSERLSSMNLGYKHYQGIDNYPLDWELSYAYYSNIATKTPLDQHTLQGDQAYVETIRLKDDEILKVQTKEDGDVFMWLKHEATRGNAAAQQRLAQMLFWGQQGVAKNPEAAIEWYAKGALETEDPALIYDYAIVLFKGQGVKKNRRLALELMKKAASKGLHQAVNGLGWYYHKFKKNYAKAAKYWLKAEEMGNPDASYNLGVLHLDGIFPGVPGRNQTLAGEYFHKAAQGGHMEGTLWCSLYYITGNLETFPRDPEKAVVWAKHVAEKNGYLGHVIRKGLNAYLEGSWHEALLYYVLAAETGIEVSQTNLAHICEERPDLARRYLGVNCVWRYYNFSVFQIDAPSFAYLKMGDLYYYGHQNQSQDLELSVQMYAQAALDGDSQGFFNLALLIEEGTIIPHHILDFLEIDSTLHSNNISILQELYERCWSHSNEESFSPCSLAWLYLHLRLLWGAILHSALIYFLGTFLLSILIAWTVQYFQSVSASDPPPRPSQASPDTATSTASPAVTPAADASDQDQPTVTNNPEPRG
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
80PhosphorylationKAEQSVAYKDFIYFT
CHHHHHHCCCEEEEE		14.66-
81UbiquitinationAEQSVAYKDFIYFTV
HHHHHHCCCEEEEEE		36.10-
160PhosphorylationIMVYRDDYFIRHSIS
EEEECCCCCHHCCCC		12.75-
200AcetylationNLLHAVAKNYTLLQT
HHHHHHHHCCCEECC		43.8419824931
201N-linked_GlycosylationLLHAVAKNYTLLQTI
HHHHHHHCCCEECCC		25.86UniProtKB CARBOHYD
285 (in isoform 3)Ubiquitination-7.6121906983
285PhosphorylationTRRQRMDYPVFTVSL
HHHHCCCCHHHHHHH		7.6126074081
289PhosphorylationRMDYPVFTVSLWLYL
CCCCHHHHHHHHHHH		14.9326074081
291PhosphorylationDYPVFTVSLWLYLLH
CCHHHHHHHHHHHHH		15.6926074081
295PhosphorylationFTVSLWLYLLHYCKA
HHHHHHHHHHHHHHH		8.8126074081
299PhosphorylationLWLYLLHYCKANLCG
HHHHHHHHHHHHCCC		8.8026074081
345UbiquitinationKGEDLAVKTKFIIPL
CCCCEEEEEEEEEEC		40.15-
346PhosphorylationGEDLAVKTKFIIPLK
CCCEEEEEEEEEECH		25.29-
382N-linked_GlycosylationQDLKSYHNQTISFRE
CCHHHHCCCEEEEEC		32.24UniProtKB CARBOHYD
384PhosphorylationLKSYHNQTISFREDF
HHHHCCCEEEEECCC		24.7324719451
386PhosphorylationSYHNQTISFREDFHY
HHCCCEEEEECCCCC		22.9529496963
399PhosphorylationHYNDTAGYFIIGGSR
CCCCCCEEEEECCCE		6.80-
403 (in isoform 2)Ubiquitination-24.1721906983
407PhosphorylationFIIGGSRYVAGIEGF
EEECCCEEEEECEEC		9.06-
420PhosphorylationGFFGPLKYYRLRSLH
ECCCCHHHHHHHHCC		11.08-
438UbiquitinationIFNPLLEKQLAEQIK
HHHHHHHHHHHHHHH		51.052190698
438 (in isoform 1)Ubiquitination-51.0521906983
447PhosphorylationLAEQIKLYYERCAEV
HHHHHHHHHHHHHHH		9.77-
448PhosphorylationAEQIKLYYERCAEVQ
HHHHHHHHHHHHHHH		13.82-
461PhosphorylationVQEIVSVYASAAKHG
HHHHHHHHHHHHHCC		6.32-
488PhosphorylationYLDLQRRYGRPSMCR
HHHHHHHHCCCHHHH		21.4829449344
492PhosphorylationQRRYGRPSMCRAFPW
HHHHCCCHHHHCCCC		29.2029449344
521PhosphorylationLLEMDLLTVPRNQNE
HHHCCCCCCCCCCCC		35.4424719451
527N-linked_GlycosylationLTVPRNQNESVSEIG
CCCCCCCCCCHHHHC		47.24UniProtKB CARBOHYD
608PhosphorylationGQGSERLSSMNLGYK
CCCHHHHHHCCCCCC		33.4918669648
615AcetylationSSMNLGYKHYQGIDN
HHCCCCCCCCCCCCC		33.757933653
634PhosphorylationWELSYAYYSNIATKT
EEEEEEEECCCCCCC		6.2522461510
635PhosphorylationELSYAYYSNIATKTP
EEEEEEECCCCCCCC		14.7522461510
661UbiquitinationYVETIRLKDDEILKV
EEEEEEECCCCEEEE		53.97-
667UbiquitinationLKDDEILKVQTKEDG
ECCCCEEEEEECCCC		37.65-
859UbiquitinationTFPRDPEKAVVWAKH
CCCCCHHHHHHHHHH		52.44-
865UbiquitinationEKAVVWAKHVAEKNG
HHHHHHHHHHHHHCC		23.93-
937N-linked_GlycosylationNCVWRYYNFSVFQID
EEEEEECCCEEEEEE		17.49UniProtKB CARBOHYD
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 SE1L3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SE1L3_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 SE1L3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MINY1_HUMANFAM63Aphysical
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 SE1L3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608, AND MASSSPECTROMETRY.

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