CFDP1_HUMAN - dbPTM
CFDP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CFDP1_HUMAN
UniProt AC Q9UEE9
Protein Name Craniofacial development protein 1
Gene Name CFDP1
Organism Homo sapiens (Human).
Sequence Length 299
Subcellular Localization Chromosome, centromere, kinetochore .
Protein Description May play a role during embryogenesis..
Protein Sequence MEEFDSEDFSTSEEDEDYVPSGGEYSEDDVNELVKEDEVDGEEQTQKTQGKKRKAQSIPARKRRQGGLSLEEEEEEDANSESEGSSSEEEDDAAEQEKGIGSEDARKKKEDELWASFLNDVGPKSKVPPSTQVKKGEETEETSSSKLLVKAEELEKPKETEKVKITKVFDFAGEEVRVTKEVDATSKEAKSFFKQNEKEKPQANVPSALPSLPAGSGLKRSSGMSSLLGKIGAKKQKMSTLEKSKLDWESFKEEEGIGEELAIHNRGKEGYIERKAFLDRVDHRQFEIERDLRLSKMKP
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
57PhosphorylationGKKRKAQSIPARKRR
CHHHHHHCCCHHHHH		35.0928555341
80PhosphorylationEEEEDANSESEGSSS
HHHHHCCCCCCCCCC		44.1920363803
82PhosphorylationEEDANSESEGSSSEE
HHHCCCCCCCCCCHH		47.2625137130
85PhosphorylationANSESEGSSSEEEDD
CCCCCCCCCCHHHHH		27.0025137130
86PhosphorylationNSESEGSSSEEEDDA
CCCCCCCCCHHHHHH		53.2620363803
87PhosphorylationSESEGSSSEEEDDAA
CCCCCCCCHHHHHHH		51.2120363803
102PhosphorylationEQEKGIGSEDARKKK
HHHHCCCCHHHHHHH		30.3125849741
116PhosphorylationKEDELWASFLNDVGP
HHHHHHHHHHHCCCC		20.7725159151
124UbiquitinationFLNDVGPKSKVPPST
HHHCCCCCCCCCCCC		57.91-
130PhosphorylationPKSKVPPSTQVKKGE
CCCCCCCCCCCCCCC		25.9622468782
131PhosphorylationKSKVPPSTQVKKGEE
CCCCCCCCCCCCCCC		43.0622798277
139PhosphorylationQVKKGEETEETSSSK
CCCCCCCCCCCCHHC		34.5223312004
142PhosphorylationKGEETEETSSSKLLV
CCCCCCCCCHHCEEE		27.9023312004
143PhosphorylationGEETEETSSSKLLVK
CCCCCCCCHHCEEEE		35.5730576142
144PhosphorylationEETEETSSSKLLVKA
CCCCCCCHHCEEEEH		38.6222468782
145PhosphorylationETEETSSSKLLVKAE
CCCCCCHHCEEEEHH		27.3923312004
146AcetylationTEETSSSKLLVKAEE
CCCCCHHCEEEEHHH		48.0325953088
146UbiquitinationTEETSSSKLLVKAEE
CCCCCHHCEEEEHHH		48.03-
150SumoylationSSSKLLVKAEELEKP
CHHCEEEEHHHHCCC		50.4828112733
150SumoylationSSSKLLVKAEELEKP
CHHCEEEEHHHHCCC		50.48-
156AcetylationVKAEELEKPKETEKV
EEHHHHCCCCCCCCE		74.2025953088
167AcetylationTEKVKITKVFDFAGE
CCCEEEEEEEECCCC		44.3626822725
167 (in isoform 1)Ubiquitination-44.3621890473
167 (in isoform 2)Ubiquitination-44.3621890473
167UbiquitinationTEKVKITKVFDFAGE
CCCEEEEEEEECCCC		44.3621890473
177MethylationDFAGEEVRVTKEVDA
ECCCCEEEEEEEECC		33.40-
1802-HydroxyisobutyrylationGEEVRVTKEVDATSK
CCEEEEEEEECCCHH		53.54-
180UbiquitinationGEEVRVTKEVDATSK
CCEEEEEEEECCCHH		53.54-
187AcetylationKEVDATSKEAKSFFK
EEECCCHHHHHHHHH		58.2925953088
194MethylationKEAKSFFKQNEKEKP
HHHHHHHHHCCCCCC		50.64-
200AcetylationFKQNEKEKPQANVPS
HHHCCCCCCCCCCCC		54.2023236377
207PhosphorylationKPQANVPSALPSLPA
CCCCCCCCCCCCCCC		37.8523186163
211PhosphorylationNVPSALPSLPAGSGL
CCCCCCCCCCCCCCC		48.0821712546
216PhosphorylationLPSLPAGSGLKRSSG
CCCCCCCCCCCCCCC		42.9625159151
219UbiquitinationLPAGSGLKRSSGMSS
CCCCCCCCCCCCHHH		54.48-
219MethylationLPAGSGLKRSSGMSS
CCCCCCCCCCCCHHH		54.4824129315
219AcetylationLPAGSGLKRSSGMSS
CCCCCCCCCCCCHHH		54.4825953088
221PhosphorylationAGSGLKRSSGMSSLL
CCCCCCCCCCHHHHH		29.6525159151
222PhosphorylationGSGLKRSSGMSSLLG
CCCCCCCCCHHHHHH		42.4125159151
224SulfoxidationGLKRSSGMSSLLGKI
CCCCCCCHHHHHHHH		2.3821406390
225PhosphorylationLKRSSGMSSLLGKIG
CCCCCCHHHHHHHHH		22.7428857561
226PhosphorylationKRSSGMSSLLGKIGA
CCCCCHHHHHHHHHH		20.7923401153
230AcetylationGMSSLLGKIGAKKQK
CHHHHHHHHHHHHHH		37.6325953088
237TrimethylationKIGAKKQKMSTLEKS
HHHHHHHHCHHHHHH		43.63-
237MethylationKIGAKKQKMSTLEKS
HHHHHHHHCHHHHHH		43.63-
239PhosphorylationGAKKQKMSTLEKSKL
HHHHHHCHHHHHHCC		36.5524719451
244PhosphorylationKMSTLEKSKLDWESF
HCHHHHHHCCCHHHH		29.1325159151
245UbiquitinationMSTLEKSKLDWESFK
CHHHHHHCCCHHHHH		62.63-
250PhosphorylationKSKLDWESFKEEEGI
HHCCCHHHHHCCCCC		37.0528355574
268AcetylationLAIHNRGKEGYIERK
HHCCCCCCCCEEEEC		44.748276399
271PhosphorylationHNRGKEGYIERKAFL
CCCCCCCEEEECHHH		10.7427642862
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 CFDP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CFDP1_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 CFDP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
DMAP1_HUMANDMAP1physical
22939629
SRCAP_HUMANSRCAPphysical
22939629
RUVB1_HUMANRUVBL1physical
26344197
RUVB2_HUMANRUVBL2physical
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 CFDP1_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-116 AND SER-250, ANDMASS SPECTROMETRY.

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