SCFD1_HUMAN - dbPTM
SCFD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCFD1_HUMAN
UniProt AC Q8WVM8
Protein Name Sec1 family domain-containing protein 1
Gene Name SCFD1
Organism Homo sapiens (Human).
Sequence Length 642
Subcellular Localization Cytoplasm. Endoplasmic reticulum membrane
Peripheral membrane protein. Golgi apparatus, Golgi stack membrane
Peripheral membrane protein.
Protein Description Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with COG4. Involved in vesicular transport between the endoplasmic reticulum and the Golgi (By similarity)..
Protein Sequence MAAAAAATAAAAASIRERQTVALKRMLNFNVPHIKNSTGEPVWKVLIYDRFGQDIISPLLSVKELRDMGITLHLLLHSDRDPIPDVPAVYFVMPTEENIDRMCQDLRNQLYESYYLNFISAISRSKLEDIANAALAASAVTQVAKVFDQYLNFITLEDDMFVLCNQNKELVSYRAINRPDITDTEMETVMDTIVDSLFCFFVTLGAVPIIRCSRGTAAEMVAVKLDKKLRENLRDARNSLFTGDTLGAGQFSFQRPLLVLVDRNIDLATPLHHTWTYQALVHDVLDFHLNRVNLEESSGVENSPAGARPKRKNKKSYDLTPVDKFWQKHKGSPFPEVAESVQQELESYRAQEDEVKRLKSIMGLEGEDEGAISMLSDNTAKLTSAVSSLPELLEKKRLIDLHTNVATAVLEHIKARKLDVYFEYEEKIMSKTTLDKSLLDIISDPDAGTPEDKMRLFLIYYISTQQAPSEADLEQYKKALTDAGCNLNPLQYIKQWKAFTKMASAPASYGSTTTKPMGLLSRVMNTGSQFVMEGVKNLVLKQQNLPVTRILDNLMEMKSNPETDDYRYFDPKMLRGNDSSVPRNKNPFQEAIVFVVGGGNYIEYQNLVDYIKGKQGKHILYGCSELFNATQFIKQLSQLGQK
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
2Acetylation------MAAAAAATA
------CHHHHHHHH		13.0519413330
14PhosphorylationATAAAAASIRERQTV
HHHHHHHHHHHHHHH		19.9028464451
24MethylationERQTVALKRMLNFNV
HHHHHHHHHHHCCCC		26.48115977587
242-HydroxyisobutyrylationERQTVALKRMLNFNV
HHHHHHHHHHHCCCC		26.48-
37PhosphorylationNVPHIKNSTGEPVWK
CCCCCCCCCCCEEEE		32.55-
57PhosphorylationRFGQDIISPLLSVKE
CCCCCCHHHHCCHHH		15.1619060867
61PhosphorylationDIISPLLSVKELRDM
CCHHHHCCHHHHHHC		38.5324719451
63UbiquitinationISPLLSVKELRDMGI
HHHHCCHHHHHHCCC		47.8821890473
113PhosphorylationLRNQLYESYYLNFIS
HHHHHHHHHHHHHHH		12.91-
114PhosphorylationRNQLYESYYLNFISA
HHHHHHHHHHHHHHH		10.47-
115PhosphorylationNQLYESYYLNFISAI
HHHHHHHHHHHHHHH		12.40-
125PhosphorylationFISAISRSKLEDIAN
HHHHHCHHHHHHHHH		34.5025278378
126UbiquitinationISAISRSKLEDIANA
HHHHCHHHHHHHHHH		55.5821906983
138O-linked_GlycosylationANAALAASAVTQVAK
HHHHHHHHHHHHHHH		20.0528510447
138PhosphorylationANAALAASAVTQVAK
HHHHHHHHHHHHHHH		20.0525278378
141O-linked_GlycosylationALAASAVTQVAKVFD
HHHHHHHHHHHHHHH		19.6228510447
141PhosphorylationALAASAVTQVAKVFD
HHHHHHHHHHHHHHH		19.6225278378
220SulfoxidationSRGTAAEMVAVKLDK
CCCCHHHHHHHHHCH		1.6921406390
252PhosphorylationTLGAGQFSFQRPLLV
CCCCCCCCCCCCEEE		16.7525627689
257UbiquitinationQFSFQRPLLVLVDRN
CCCCCCCEEEEEECC		5.8621890473
257UbiquitinationQFSFQRPLLVLVDRN
CCCCCCCEEEEEECC		5.8621890473
297PhosphorylationNRVNLEESSGVENSP
HCCCCHHHCCCCCCC		24.0229255136
298PhosphorylationRVNLEESSGVENSPA
CCCCHHHCCCCCCCC		50.5729255136
303PhosphorylationESSGVENSPAGARPK
HHCCCCCCCCCCCCC		11.5619664994
315MalonylationRPKRKNKKSYDLTPV
CCCCCCCCCCCCCCH		64.7426320211
315UbiquitinationRPKRKNKKSYDLTPV
CCCCCCCCCCCCCCH		64.74-
316PhosphorylationPKRKNKKSYDLTPVD
CCCCCCCCCCCCCHH		26.0328355574
317PhosphorylationKRKNKKSYDLTPVDK
CCCCCCCCCCCCHHH		24.6923403867
320PhosphorylationNKKSYDLTPVDKFWQ
CCCCCCCCCHHHHHH		20.5421815630
324AcetylationYDLTPVDKFWQKHKG
CCCCCHHHHHHHHCC		49.0521466224
324UbiquitinationYDLTPVDKFWQKHKG
CCCCCHHHHHHHHCC		49.0521890473
328AcetylationPVDKFWQKHKGSPFP
CHHHHHHHHCCCCCH		37.5721466224
330UbiquitinationDKFWQKHKGSPFPEV
HHHHHHHCCCCCHHH		69.03-
330AcetylationDKFWQKHKGSPFPEV
HHHHHHHCCCCCHHH		69.0321466224
332PhosphorylationFWQKHKGSPFPEVAE
HHHHHCCCCCHHHHH		28.3321712546
360PhosphorylationDEVKRLKSIMGLEGE
HHHHHHHHHHCCCCC		23.5428348404
362SulfoxidationVKRLKSIMGLEGEDE
HHHHHHHHCCCCCCH		6.9121406390
373PhosphorylationGEDEGAISMLSDNTA
CCCHHHHHHCCCCHH		17.0927251275
376PhosphorylationEGAISMLSDNTAKLT
HHHHHHCCCCHHHHH		21.8527251275
379PhosphorylationISMLSDNTAKLTSAV
HHHCCCCHHHHHHHH		30.11-
383PhosphorylationSDNTAKLTSAVSSLP
CCCHHHHHHHHHCHH		17.5925850435
384PhosphorylationDNTAKLTSAVSSLPE
CCHHHHHHHHHCHHH		36.7928348404
387PhosphorylationAKLTSAVSSLPELLE
HHHHHHHHCHHHHHH		26.3525850435
388PhosphorylationKLTSAVSSLPELLEK
HHHHHHHCHHHHHHH		41.1525850435
395UbiquitinationSLPELLEKKRLIDLH
CHHHHHHHCCCHHCH		43.0721906983
396UbiquitinationLPELLEKKRLIDLHT
HHHHHHHCCCHHCHH		42.96-
417UbiquitinationLEHIKARKLDVYFEY
HHHHHHCCCEEEEEE		54.63-
427UbiquitinationVYFEYEEKIMSKTTL
EEEEEHHHHCCCCCC		31.5921890473
427UbiquitinationVYFEYEEKIMSKTTL
EEEEEHHHHCCCCCC		31.5921890473
427UbiquitinationVYFEYEEKIMSKTTL
EEEEEHHHHCCCCCC		31.59-
431UbiquitinationYEEKIMSKTTLDKSL
EHHHHCCCCCCCHHH		28.31-
434UbiquitinationKIMSKTTLDKSLLDI
HHCCCCCCCHHHHHH		10.6521890473
434UbiquitinationKIMSKTTLDKSLLDI
HHCCCCCCCHHHHHH		10.6521890473
436UbiquitinationMSKTTLDKSLLDIIS
CCCCCCCHHHHHHHC		46.2221906983
443PhosphorylationKSLLDIISDPDAGTP
HHHHHHHCCCCCCCH		43.34-
494UbiquitinationLNPLQYIKQWKAFTK
CCHHHHHHHHHHHHH		45.2121906983
500PhosphorylationIKQWKAFTKMASAPA
HHHHHHHHHHHCCCH		25.4422210691
501UbiquitinationKQWKAFTKMASAPAS
HHHHHHHHHHCCCHH		26.4721890473
504PhosphorylationKAFTKMASAPASYGS
HHHHHHHCCCHHCCC		31.1421406692
508PhosphorylationKMASAPASYGSTTTK
HHHCCCHHCCCCCCC		29.0320068231
509PhosphorylationMASAPASYGSTTTKP
HHCCCHHCCCCCCCC		19.7320068231
511PhosphorylationSAPASYGSTTTKPMG
CCCHHCCCCCCCCCC		17.8521406692
512PhosphorylationAPASYGSTTTKPMGL
CCHHCCCCCCCCCCH		33.8421406692
513PhosphorylationPASYGSTTTKPMGLL
CHHCCCCCCCCCCHH		34.2221406692
514PhosphorylationASYGSTTTKPMGLLS
HHCCCCCCCCCCHHH		32.9921406692
515UbiquitinationSYGSTTTKPMGLLSR
HCCCCCCCCCCHHHH		30.8021906983
521PhosphorylationTKPMGLLSRVMNTGS
CCCCCHHHHHHHCCC		28.0721406692
526PhosphorylationLLSRVMNTGSQFVME
HHHHHHHCCCHHHHH		21.8024173317
528PhosphorylationSRVMNTGSQFVMEGV
HHHHHCCCHHHHHHH		20.5717525332
536UbiquitinationQFVMEGVKNLVLKQQ
HHHHHHHHHHHHHCC		56.2621906983
536AcetylationQFVMEGVKNLVLKQQ
HHHHHHHHHHHHHCC		56.2630592183
541MalonylationGVKNLVLKQQNLPVT
HHHHHHHHCCCCCHH		42.2126320211
541UbiquitinationGVKNLVLKQQNLPVT
HHHHHHHHCCCCCHH		42.21-
548PhosphorylationKQQNLPVTRILDNLM
HCCCCCHHHHHHHHH		15.2820068231
555SulfoxidationTRILDNLMEMKSNPE
HHHHHHHHHHHCCCC		6.2421406390
558UbiquitinationLDNLMEMKSNPETDD
HHHHHHHHCCCCCCC		33.502190698
572UbiquitinationDYRYFDPKMLRGNDS
CCCCCCHHHHCCCCC		53.03-
575MethylationYFDPKMLRGNDSSVP
CCCHHHHCCCCCCCC		38.07115493403
637PhosphorylationTQFIKQLSQLGQK--
HHHHHHHHHHCCC--		22.3628857561
642UbiquitinationQLSQLGQK-------
HHHHHCCC-------		61.58-
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 SCFD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCFD1_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 SCFD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ODO2_HUMANDLSTphysical
16169070
DKKL1_HUMANDKKL1physical
19176879
KAT5_HUMANKAT5physical
19176879
APBP2_HUMANAPPBP2physical
19176879
VPP1_HUMANATP6V0A1physical
22939629
SNP23_HUMANSNAP23physical
22939629
VAMP2_HUMANVAMP2physical
22939629
RM09_HUMANMRPL9physical
26344197
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 SCFD1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-303, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-303, AND MASS SPECTROMETRY.
"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-303, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory