SCYL2_HUMAN - dbPTM
SCYL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCYL2_HUMAN
UniProt AC Q6P3W7
Protein Name SCY1-like protein 2
Gene Name SCYL2
Organism Homo sapiens (Human).
Sequence Length 929
Subcellular Localization Cytoplasm, perinuclear region. Cytoplasmic vesicle, clathrin-coated vesicle. Golgi apparatus, trans-Golgi network membrane. Endosome membrane. According to PubMed:15809293, plasma membrane-associated in clathrin-coated vesicles. According to PubMed:1
Protein Description Component of AP2-containing clathrin coated structures at the plasma membrane or of endocytic coated vesicles. According to PubMed:15809293, probable serine/threonine-protein kinase that phosphorylates, in vitro, the beta2-subunit of the plasma membrane adapter complex AP2 and other proteins in presence of poly-L-lysine. According to PubMed:16914521, has no detectable kinase activity in vitro. May regulate clathrin-dependent trafficking between the TGN and/or the endosomal system..
Protein Sequence MESMLNKLKSTVTKVTADVTSAVMGNPVTREFDVGRHIASGGNGLAWKIFNGTKKSTKQEVAVFVFDKKLIDKYQKFEKDQIIDSLKRGVQQLTRLRHPRLLTVQHPLEESRDCLAFCTEPVFASLANVLGNWENLPSPISPDIKDYKLYDVETKYGLLQVSEGLSFLHSSVKMVHGNITPENIILNKSGAWKIMGFDFCVSSTNPSEQEPKFPCKEWDPNLPSLCLPNPEYLAPEYILSVSCETASDMYSLGTVMYAVFNKGKPIFEVNKQDIYKSFSRQLDQLSRLGSSSLTNIPEEVREHVKLLLNVTPTVRPDADQMTKIPFFDDVGAVTLQYFDTLFQRDNLQKSQFFKGLPKVLPKLPKRVIVQRILPCLTSEFVNPDMVPFVLPNVLLIAEECTKEEYVKLILPELGPVFKQQEPIQILLIFLQKMDLLLTKTPPDEIKNSVLPMVYRALEAPSIQIQELCLNIIPTFANLIDYPSMKNALIPRIKNACLQTSSLAVRVNSLVCLGKILEYLDKWFVLDDILPFLQQIPSKEPAVLMGILGIYKCTFTHKKLGITKEQLAGKVLPHLIPLSIENNLNLNQFNSFISVIKEMLNRLESEHKTKLEQLHIMQEQQKSLDIGNQMNVSEEMKVTNIGNQQIDKVFNNIGADLLTGSESENKEDGLQNKHKRASLTLEEKQKLAKEQEQAQKLKSQQPLKPQVHTPVATVKQTKDLTDTLMDNMSSLTSLSVSTPKSSASSTFTSVPSMGIGMMFSTPTDNTKRNLTNGLNANMGFQTSGFNMPVNTNQNFYSSPSTVGVTKMTLGTPPTLPNFNALSVPPAGAKQTQQRPTDMSALNNLFGPQKPKVSMNQLSQQKPNQWLNQFVPPQGSPTMGSSVMGTQMNVIGQSAFGMQGNPFFNPQNFAQPPTTMTNSSSASNDLKDLFG
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
7Acetylation-MESMLNKLKSTVTK
-CHHHHHHHHHHHHH		54.0225953088
9AcetylationESMLNKLKSTVTKVT
HHHHHHHHHHHHHHH		45.778273287
24SulfoxidationADVTSAVMGNPVTRE
HHCHHHHCCCCEEEE		4.2521406390
56PhosphorylationIFNGTKKSTKQEVAV
HHCCCCCCCCCEEEE		42.2526670566
57PhosphorylationFNGTKKSTKQEVAVF
HCCCCCCCCCEEEEE		45.7026670566
79UbiquitinationDKYQKFEKDQIIDSL
HHHHHHCHHHHHHHH		59.05-
148UbiquitinationSPDIKDYKLYDVETK
CCCCCCCEEEECCCC		51.18-
154PhosphorylationYKLYDVETKYGLLQV
CEEEECCCCCCEEHH		29.4322210691
156PhosphorylationLYDVETKYGLLQVSE
EEECCCCCCEEHHHH		22.0422210691
171PhosphorylationGLSFLHSSVKMVHGN
HHHHHHHCEEEECCC		18.2722210691
275PhosphorylationEVNKQDIYKSFSRQL
EECHHHHHHHHHHHH		14.6322817900
277PhosphorylationNKQDIYKSFSRQLDQ
CHHHHHHHHHHHHHH		16.1022817900
279PhosphorylationQDIYKSFSRQLDQLS
HHHHHHHHHHHHHHH		26.6322817900
290PhosphorylationDQLSRLGSSSLTNIP
HHHHHHCCCCCCCCC		22.7325850435
291PhosphorylationQLSRLGSSSLTNIPE
HHHHHCCCCCCCCCH		27.8025850435
292PhosphorylationLSRLGSSSLTNIPEE
HHHHCCCCCCCCCHH		40.6925850435
294PhosphorylationRLGSSSLTNIPEEVR
HHCCCCCCCCCHHHH		32.8026471730
350PhosphorylationQRDNLQKSQFFKGLP
HCCCCCHHHHHCCCC		21.1822817900
354AcetylationLQKSQFFKGLPKVLP
CCHHHHHCCCCCCCC		61.9126051181
438PhosphorylationQKMDLLLTKTPPDEI
HHHHHHHCCCCHHHH		32.6118669648
440PhosphorylationMDLLLTKTPPDEIKN
HHHHHCCCCHHHHHH		34.5118669648
499PhosphorylationIKNACLQTSSLAVRV
HHHHHHHCCCHHHHH		13.8222210691
500PhosphorylationKNACLQTSSLAVRVN
HHHHHHCCCHHHHHH		15.4722210691
501PhosphorylationNACLQTSSLAVRVNS
HHHHHCCCHHHHHHH		24.6022210691
508PhosphorylationSLAVRVNSLVCLGKI
CHHHHHHHHHHHHHH		21.2320068231
537PhosphorylationPFLQQIPSKEPAVLM
HHHHHCCCCCCHHHH		51.8124719451
553PhosphorylationILGIYKCTFTHKKLG
HHHEEECCCCCCCCC		27.6720068231
622PhosphorylationIMQEQQKSLDIGNQM
HHHHHHHHCCCCCCC		27.2629507054
632PhosphorylationIGNQMNVSEEMKVTN
CCCCCCCCHHHCCCC		23.8821815630
658PhosphorylationNIGADLLTGSESENK
HHCCCHHCCCCCCCC		46.0623186163
660PhosphorylationGADLLTGSESENKED
CCCHHCCCCCCCCCC		32.4925159151
662PhosphorylationDLLTGSESENKEDGL
CHHCCCCCCCCCCCC		48.4423186163
677PhosphorylationQNKHKRASLTLEEKQ
CCHHHHHHCCHHHHH		26.3923401153
679PhosphorylationKHKRASLTLEEKQKL
HHHHHHCCHHHHHHH		29.6329255136
683UbiquitinationASLTLEEKQKLAKEQ
HHCCHHHHHHHHHHH		43.27-
6832-HydroxyisobutyrylationASLTLEEKQKLAKEQ
HHCCHHHHHHHHHHH		43.27-
688TrimethylationEEKQKLAKEQEQAQK
HHHHHHHHHHHHHHH		71.07-
688MethylationEEKQKLAKEQEQAQK
HHHHHHHHHHHHHHH		71.07-
698PhosphorylationEQAQKLKSQQPLKPQ
HHHHHHHHCCCCCCC		44.4723403867
703UbiquitinationLKSQQPLKPQVHTPV
HHHCCCCCCCCCCCC		39.84-
703MalonylationLKSQQPLKPQVHTPV
HHHCCCCCCCCCCCC		39.8432601280
708PhosphorylationPLKPQVHTPVATVKQ
CCCCCCCCCCCCCEE		22.1725159151
712PhosphorylationQVHTPVATVKQTKDL
CCCCCCCCCEECCCC		28.5923403867
714UbiquitinationHTPVATVKQTKDLTD
CCCCCCCEECCCCHH		48.14-
728PhosphorylationDTLMDNMSSLTSLSV
HHHHHHHHHHHEEEE		28.5727251275
729PhosphorylationTLMDNMSSLTSLSVS
HHHHHHHHHHEEEEC		25.5427251275
731PhosphorylationMDNMSSLTSLSVSTP
HHHHHHHHEEEECCC		29.5727251275
732PhosphorylationDNMSSLTSLSVSTPK
HHHHHHHEEEECCCC		24.7630576142
732O-linked_GlycosylationDNMSSLTSLSVSTPK
HHHHHHHEEEECCCC		24.7630059200
734O-linked_GlycosylationMSSLTSLSVSTPKSS
HHHHHEEEECCCCCC		17.4930059200
734PhosphorylationMSSLTSLSVSTPKSS
HHHHHEEEECCCCCC		17.4930576142
736PhosphorylationSLTSLSVSTPKSSAS
HHHEEEECCCCCCCC		35.3030576142
736O-linked_GlycosylationSLTSLSVSTPKSSAS
HHHEEEECCCCCCCC		35.3030059200
737PhosphorylationLTSLSVSTPKSSASS
HHEEEECCCCCCCCC		32.3622199227
740O-linked_GlycosylationLSVSTPKSSASSTFT
EEECCCCCCCCCCCC		32.1330059200
741O-linked_GlycosylationSVSTPKSSASSTFTS
EECCCCCCCCCCCCC		37.9930059200
745O-linked_GlycosylationPKSSASSTFTSVPSM
CCCCCCCCCCCCCCC		28.5630059200
751PhosphorylationSTFTSVPSMGIGMMF
CCCCCCCCCCEEEEE		27.7321712546
759PhosphorylationMGIGMMFSTPTDNTK
CCEEEEEECCCCCCC		18.6425159151
760PhosphorylationGIGMMFSTPTDNTKR
CEEEEEECCCCCCCC		20.9525159151
795PhosphorylationVNTNQNFYSSPSTVG
CCCCCCCCCCCCCCC		18.78-
807PhosphorylationTVGVTKMTLGTPPTL
CCCCEEEECCCCCCC		24.4822199227
810PhosphorylationVTKMTLGTPPTLPNF
CEEEECCCCCCCCCC		29.2522199227
813PhosphorylationMTLGTPPTLPNFNAL
EECCCCCCCCCCCCC		56.9325159151
848UbiquitinationNNLFGPQKPKVSMNQ
HHHHCCCCCCCCHHH		50.36-
857PhosphorylationKVSMNQLSQQKPNQW
CCCHHHHHCCCCCHH		22.3225159151
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 SCYL2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCYL2_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 SCYL2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CLH1_HUMANCLTCphysical
25852190
THOC4_HUMANALYREFphysical
25852190
PCBP2_HUMANPCBP2physical
26344197
PIMT_HUMANPCMT1physical
26344197
GORS2_HUMANGORASP2physical
27173435
SHLB1_HUMANSH3GLB1physical
27173435
CDK5_HUMANCDK5physical
27173435
PRCC_HUMANPRCCphysical
27173435
SEPT7_HUMANSEPT7physical
27173435
CHRD1_HUMANCHORDC1physical
27173435
SARNP_HUMANSARNPphysical
27173435
UBAP2_HUMANUBAP2physical
27173435
COPZ1_HUMANCOPZ1physical
27173435
SEP11_HUMANSEPT11physical
27173435
PDLI1_HUMANPDLIM1physical
27173435
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 SCYL2_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 THR-438; THR-440 ANDSER-677, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND MASSSPECTROMETRY.

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