CE024_HUMAN - dbPTM
CE024_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CE024_HUMAN
UniProt AC Q7Z6I8
Protein Name UPF0461 protein C5orf24
Gene Name C5orf24
Organism Homo sapiens (Human).
Sequence Length 188
Subcellular Localization
Protein Description
Protein Sequence MMHPVASSNPAFCGPGKPSCLNEDAMRAADQFDIYSSQQSKYSHTVNHKPMVCQRQDPLNETHLQTTSGRSIEIKDELKKKKNLNRSGKRGRPSGTTKSAGYRTSTGRPLGTTKAAGFKTSPGRPLGTTKAAGYKVSPGRPPGSIKALSRLADLGYGCGTAAFPYPMMHGRAVHGVEETSSEVKPPNE
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
17AcetylationPAFCGPGKPSCLNED
CCCCCCCCHHHCCHH		36.5725953088
35PhosphorylationAADQFDIYSSQQSKY
HHHHHCCCCCCCHHC		12.2421945579
36PhosphorylationADQFDIYSSQQSKYS
HHHHCCCCCCCHHCC		23.2321945579
37PhosphorylationDQFDIYSSQQSKYSH
HHHCCCCCCCHHCCC		18.4421945579
40PhosphorylationDIYSSQQSKYSHTVN
CCCCCCCHHCCCCCC		26.3921945579
41 (in isoform 2)Ubiquitination-46.5721890473
41 (in isoform 1)Ubiquitination-46.5721890473
41UbiquitinationIYSSQQSKYSHTVNH
CCCCCCHHCCCCCCC		46.5721890473
49AcetylationYSHTVNHKPMVCQRQ
CCCCCCCCCCEEECC		29.6123749302
49UbiquitinationYSHTVNHKPMVCQRQ
CCCCCCCCCCEEECC		29.6129967540
71PhosphorylationLQTTSGRSIEIKDEL
CCCCCCCCEECHHHH		28.2627134283
75SumoylationSGRSIEIKDELKKKK
CCCCEECHHHHHHHH		32.15-
75UbiquitinationSGRSIEIKDELKKKK
CCCCEECHHHHHHHH		32.1532015554
75SumoylationSGRSIEIKDELKKKK
CCCCEECHHHHHHHH		32.1528112733
94PhosphorylationSGKRGRPSGTTKSAG
CCCCCCCCCCCCCCC		47.62-
96PhosphorylationKRGRPSGTTKSAGYR
CCCCCCCCCCCCCCC		35.07-
97PhosphorylationRGRPSGTTKSAGYRT
CCCCCCCCCCCCCCC		26.9122210691
102PhosphorylationGTTKSAGYRTSTGRP
CCCCCCCCCCCCCCC		15.5022210691
104PhosphorylationTKSAGYRTSTGRPLG
CCCCCCCCCCCCCCC		23.3529209046
105PhosphorylationKSAGYRTSTGRPLGT
CCCCCCCCCCCCCCC		21.6225627689
106PhosphorylationSAGYRTSTGRPLGTT
CCCCCCCCCCCCCCC		36.2829209046
112PhosphorylationSTGRPLGTTKAAGFK
CCCCCCCCCCCCCCC		32.5729209046
113PhosphorylationTGRPLGTTKAAGFKT
CCCCCCCCCCCCCCC		19.5229209046
114UbiquitinationGRPLGTTKAAGFKTS
CCCCCCCCCCCCCCC		35.7623000965
119AcetylationTTKAAGFKTSPGRPL
CCCCCCCCCCCCCCC		47.3725953088
119UbiquitinationTTKAAGFKTSPGRPL
CCCCCCCCCCCCCCC		47.3723000965
120PhosphorylationTKAAGFKTSPGRPLG
CCCCCCCCCCCCCCC		37.5825159151
121PhosphorylationKAAGFKTSPGRPLGT
CCCCCCCCCCCCCCC		26.4125159151
128PhosphorylationSPGRPLGTTKAAGYK
CCCCCCCCCCCCCCC		32.5723403867
129PhosphorylationPGRPLGTTKAAGYKV
CCCCCCCCCCCCCCC		19.5223403867
134PhosphorylationGTTKAAGYKVSPGRP
CCCCCCCCCCCCCCC		11.9523403867
137PhosphorylationKAAGYKVSPGRPPGS
CCCCCCCCCCCCCCH		19.9325159151
137 (in isoform 2)Phosphorylation-19.9325159151
144PhosphorylationSPGRPPGSIKALSRL
CCCCCCCHHHHHHHH		27.0425159151
146UbiquitinationGRPPGSIKALSRLAD
CCCCCHHHHHHHHHH		45.0023000965
146 (in isoform 1)Ubiquitination-45.0021890473
179PhosphorylationAVHGVEETSSEVKPP
CCCCCCCCCCCCCCC		24.8523663014
180PhosphorylationVHGVEETSSEVKPPN
CCCCCCCCCCCCCCC		27.9923663014
181PhosphorylationHGVEETSSEVKPPNE
CCCCCCCCCCCCCCC		54.5523663014
184UbiquitinationEETSSEVKPPNE---
CCCCCCCCCCCC---		51.1933845483
184SumoylationEETSSEVKPPNE---
CCCCCCCCCCCC---		51.1928112733
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 CE024_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CE024_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 CE024_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PKNX2_HUMANPKNOX2physical
28514442
GOPC_HUMANGOPCphysical
28514442
STK11_HUMANSTK11physical
28514442
STRAA_HUMANSTRADAphysical
28514442
CHFR_HUMANCHFRphysical
28514442
PBX2_HUMANPBX2physical
28514442
PBX3_HUMANPBX3physical
28514442
MEIS1_HUMANMEIS1physical
28514442
CAB39_HUMANCAB39physical
28514442
DCA16_HUMANDCAF16physical
28514442
2ABD_HUMANPPP2R2Dphysical
28514442
PBX1_HUMANPBX1physical
28514442
MK09_HUMANMAPK9physical
28514442
PKNX1_HUMANPKNOX1physical
28514442
WIPI3_HUMANWDR45Bphysical
28514442
AEDO_HUMANADOphysical
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 CE024_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-37, AND MASSSPECTROMETRY.

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