UN13D_HUMAN - dbPTM
UN13D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UN13D_HUMAN
UniProt AC Q70J99
Protein Name Protein unc-13 homolog D
Gene Name UNC13D
Organism Homo sapiens (Human).
Sequence Length 1090
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. Late endosome. Recycling endosome. Lysosome. Colocalizes with cytotoxic granules at the plasma membrane. Localizes to endosomal exocytic vesicles.
Protein Description Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse. Regulates assembly of recycling and late endosomal structures, leading to the formation of an endosomal exocytic compartment that fuses with perforin-containing granules at the immunologic synapse and licences them for exocytosis. Regulates Ca(2+)-dependent secretory lysosome exocytosis in mast cells..
Protein Sequence MATLLSHPQQRPPFLRQAIKIRRRRVRDLQDPPPQMAPEIQPPSHHFSPEQRALLYEDALYTVLHRLGHPEPNHVTEASELLRYLQEAFHVEPEEHQQTLQRVRELEKPIFCLKATVKQAKGILGKDVSGFSDPYCLLGIEQGVGVPGGSPGSRHRQKAVVRHTIPEEETHRTQVITQTLNPVWDETFILEFEDITNASFHLDMWDLDTVESVRQKLGELTDLHGLRRIFKEARKDKGQDDFLGNVVLRLQDLRCREDQWYPLEPRTETYPDRGQCHLQFQLIHKRRATSASRSQPSYTVHLHLLQQLVSHEVTQHEAGSTSWDGSLSPQAATVLFLHATQKDLSDFHQSMAQWLAYSRLYQSLEFPSSCLLHPITSIEYQWIQGRLKAEQQEELAASFSSLLTYGLSLIRRFRSVFPLSVSDSPARLQSLLRVLVQMCKMKAFGELCPNTAPLPQLVTEALQTGTTEWFHLKQQHHQPMVQGIPEAGKALLGLVQDVIGDLHQCQRTWDKIFHNTLKIHLFSMAFRELQWLVAKRVQDHTTVVGDVVSPEMGESLFQLYISLKELCQLRMSSSERDGVLALDNFHRWFQPAIPSWLQKTYNEALARVQRAVQMDELVPLGELTKHSTSAVDLSTCFAQISHTARQLDWPDPEEAFMITVKFVEDTCRLALVYCSLIKARARELSSGQKDQGQAANMLCVVVNDMEQLRLVIGKLPAQLAWEALEQRVGAVLEQGQLQNTLHAQLQSALAGLGHEIRTGVRTLAEQLEVGIAKHIQKLVGVRESVLPEDAILPLMKFLEVELCYMNTNLVQENFSSLLTLLWTHTLTVLVEAAASQRSSSLASNRLKIALQNLEICFHAEGCGLPPKALHTATFQALQRDLELQAASSRELIRKYFCSRIQQQAETTSEELGAVTVKASYRASEQKLRVELLSASSLLPLDSNGSSDPFVQLTLEPRHEFPELAARETQKHKKDLHPLFDETFEFLVPAEPCRKAGACLLLTVLDYDTLGADDLEGEAFLPLREVPGLSGSEEPGEVPQTRLPLTYPAPNGDPILQLLEGRKGDREAQVFVRLRRHRAKQASQHALRPAP
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
34UbiquitinationRDLQDPPPQMAPEIQ
HHCCCCCCCCCCCCC		41.8024816145
44O-linked_GlycosylationAPEIQPPSHHFSPEQ
CCCCCCCCCCCCHHH		35.9629351928
56PhosphorylationPEQRALLYEDALYTV
HHHHHHHHHHHHHHH		16.77-
61PhosphorylationLLYEDALYTVLHRLG
HHHHHHHHHHHHHCC		9.12-
62PhosphorylationLYEDALYTVLHRLGH
HHHHHHHHHHHHCCC		19.90-
79PhosphorylationPNHVTEASELLRYLQ
CCCCHHHHHHHHHHH		23.6528857561
108AcetylationQRVRELEKPIFCLKA
HHHHHCCCCEEEEHH		56.9126822725
108UbiquitinationQRVRELEKPIFCLKA
HHHHHCCCCEEEEHH		56.9129967540
126UbiquitinationQAKGILGKDVSGFSD
HHHCCCCCCCCCCCC		52.0629967540
129PhosphorylationGILGKDVSGFSDPYC
CCCCCCCCCCCCCCC		44.2326552605
132PhosphorylationGKDVSGFSDPYCLLG
CCCCCCCCCCCCCCE		41.0026552605
135PhosphorylationVSGFSDPYCLLGIEQ
CCCCCCCCCCCEEEC		10.7526552605
150PhosphorylationGVGVPGGSPGSRHRQ
CCCCCCCCCCHHHHH		31.8125159151
153PhosphorylationVPGGSPGSRHRQKAV
CCCCCCCHHHHHHHE		28.4430266825
216UbiquitinationTVESVRQKLGELTDL
HHHHHHHHHHHCCCH		48.14-
235UbiquitinationRIFKEARKDKGQDDF
HHHHHHHHCCCCCCH		71.49-
237UbiquitinationFKEARKDKGQDDFLG
HHHHHHCCCCCCHHH		62.6024816145
285UbiquitinationLQFQLIHKRRATSAS
EEEEEEECCCCCCCC		36.26-
308UbiquitinationHLHLLQQLVSHEVTQ
HHHHHHHHHHCCCCC		2.4821890473
396UbiquitinationAEQQEELAASFSSLL
HHHHHHHHHHHHHHH		12.3521987572
405PhosphorylationSFSSLLTYGLSLIRR
HHHHHHHHHHHHHHH		18.95-
430PhosphorylationDSPARLQSLLRVLVQ
CCHHHHHHHHHHHHH		33.6824719451
440UbiquitinationRVLVQMCKMKAFGEL
HHHHHHHCCHHHHHC		37.79-
473UbiquitinationTTEWFHLKQQHHQPM
CCCHHHHHHHHCCCC		39.0629967540
510UbiquitinationHQCQRTWDKIFHNTL
HHHHHHHHHHHHHHH		33.2921890473
511AcetylationQCQRTWDKIFHNTLK
HHHHHHHHHHHHHHH		38.5419608861
511UbiquitinationQCQRTWDKIFHNTLK
HHHHHHHHHHHHHHH		38.5422817900
511 (in isoform 1)Ubiquitination-38.5421890473
511 (in isoform 3)Ubiquitination-38.5421890473
541PhosphorylationAKRVQDHTTVVGDVV
HHHCCCCCEEEECCC		29.58-
542PhosphorylationKRVQDHTTVVGDVVS
HHCCCCCEEEECCCC		15.13-
549PhosphorylationTVVGDVVSPEMGESL
EEEECCCCHHHHHHH		18.26-
570UbiquitinationLKELCQLRMSSSERD
HHHHHHHHCCCCCCC		9.3223503661
574UbiquitinationCQLRMSSSERDGVLA
HHHHCCCCCCCCEEE		29.3723503661
598UbiquitinationPAIPSWLQKTYNEAL
CCCHHHHHHHHHHHH		29.7721987572
599UbiquitinationAIPSWLQKTYNEALA
CCHHHHHHHHHHHHH		51.2921987572
614SulfoxidationRVQRAVQMDELVPLG
HHHHHHHCCCEEEHH		3.3021406390
625UbiquitinationVPLGELTKHSTSAVD
EEHHHHCCCCCCCCC		48.4629967540
627PhosphorylationLGELTKHSTSAVDLS
HHHHCCCCCCCCCHH		26.1327080861
628PhosphorylationGELTKHSTSAVDLST
HHHCCCCCCCCCHHH		22.0327080861
629PhosphorylationELTKHSTSAVDLSTC
HHCCCCCCCCCHHHH		29.3427080861
634PhosphorylationSTSAVDLSTCFAQIS
CCCCCCHHHHHHHHH		20.7527080861
675PhosphorylationRLALVYCSLIKARAR
HHHHHHHHHHHHHHH		18.5524719451
678UbiquitinationLVYCSLIKARARELS
HHHHHHHHHHHHHHH		36.79-
689UbiquitinationRELSSGQKDQGQAAN
HHHHCCCCCHHHHHH		56.39-
713UbiquitinationEQLRLVIGKLPAQLA
HHHHHHHCCHHHHHH		20.2621987572
714UbiquitinationQLRLVIGKLPAQLAW
HHHHHHCCHHHHHHH		39.9221987572
714 (in isoform 3)Ubiquitination-39.92-
737UbiquitinationAVLEQGQLQNTLHAQ
HHHHCCCHHHHHHHH		5.6123503661
772UbiquitinationEQLEVGIAKHIQKLV
HHHHHHHHHHHHHHH		7.4623503661
773 (in isoform 3)Ubiquitination-39.04-
773AcetylationQLEVGIAKHIQKLVG
HHHHHHHHHHHHHHC		39.0425953088
773UbiquitinationQLEVGIAKHIQKLVG
HHHHHHHHHHHHHHC		39.0423503661
776UbiquitinationVGIAKHIQKLVGVRE
HHHHHHHHHHHCCCC		32.5223503661
777AcetylationGIAKHIQKLVGVRES
HHHHHHHHHHCCCCC		44.5325953088
777UbiquitinationGIAKHIQKLVGVRES
HHHHHHHHHHCCCCC		44.5323503661
784PhosphorylationKLVGVRESVLPEDAI
HHHCCCCCCCCHHCH		20.5628122231
894UbiquitinationSSRELIRKYFCSRIQ
CHHHHHHHHHHHHHH		35.37-
895PhosphorylationSRELIRKYFCSRIQQ
HHHHHHHHHHHHHHH		10.4426074081
898PhosphorylationLIRKYFCSRIQQQAE
HHHHHHHHHHHHHCC		23.6326074081
906PhosphorylationRIQQQAETTSEELGA
HHHHHCCCCHHHHCC		38.3426074081
907PhosphorylationIQQQAETTSEELGAV
HHHHCCCCHHHHCCE		26.1626074081
908PhosphorylationQQQAETTSEELGAVT
HHHCCCCHHHHCCEE		36.1726074081
915PhosphorylationSEELGAVTVKASYRA
HHHHCCEEEEHHHHC		18.7626074081
917 (in isoform 3)Ubiquitination-23.42-
917UbiquitinationELGAVTVKASYRASE
HHCCEEEEHHHHCCC		23.4223503661
919PhosphorylationGAVTVKASYRASEQK
CCEEEEHHHHCCCCH		14.9426074081
920PhosphorylationAVTVKASYRASEQKL
CEEEEHHHHCCCCHH		18.3026074081
923PhosphorylationVKASYRASEQKLRVE
EEHHHHCCCCHHHHE		31.4026074081
939UbiquitinationLSASSLLPLDSNGSS
EHHHHCCCCCCCCCC		39.1423503661
940UbiquitinationSASSLLPLDSNGSSD
HHHHCCCCCCCCCCC		13.0723503661
972UbiquitinationARETQKHKKDLHPLF
HHHHHHHHHCCHHHC		55.8329967540
973UbiquitinationRETQKHKKDLHPLFD
HHHHHHHHCCHHHCC		66.3029967540
1029PhosphorylationLREVPGLSGSEEPGE
HHCCCCCCCCCCCCC		46.3028270605
1031PhosphorylationEVPGLSGSEEPGEVP
CCCCCCCCCCCCCCC		35.1028270605
1079UbiquitinationRLRRHRAKQASQHAL
HHHHHHHHHHHHHHC		46.48-
1082PhosphorylationRHRAKQASQHALRPA
HHHHHHHHHHHCCCC		21.7223917254
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 UN13D_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UN13D_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 UN13D_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RB27A_HUMANRAB27Aphysical
14699162
LMNA_HUMANLMNAphysical
16248985
XRN2_HUMANXRN2physical
22939629
VP37B_HUMANVPS37Bphysical
22939629
ANXA5_HUMANANXA5physical
26344197
DPYL2_HUMANDPYSL2physical
26344197
Drug and Disease Associations
Kegg Disease
H00109 Familial hemophagocytic lymphohistiocytosis (FHPL), including the following three diseases: Perforin
OMIM Disease
608898Familial hemophagocytic lymphohistiocytosis 3 (FHL3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UN13D_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-511, AND MASS SPECTROMETRY.
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-150, AND MASSSPECTROMETRY.

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