DCAF1_ARATH - dbPTM
DCAF1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCAF1_ARATH
UniProt AC Q9M086
Protein Name DDB1- and CUL4-associated factor homolog 1
Gene Name DCAF1
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 1883
Subcellular Localization Nucleus .
Protein Description Component of the CUL4-RBX1-DDB1-DCAF1 E3 ubiquitin-protein ligase complex, DCAF1 may function as the substrate recognition module within this complex. Appears to be required for plant embryogenesis and to affect several other developmental processes including leaf, shoot, and flower development..
Protein Sequence MDGQEHAEVPNSMVEDDQSVVAAEAIAELANSTGEPNPEEGEEQSVEDELIAKAQKLMEDITSVANNPNPNILHALSQLLESQESLFLEENGHFSNARGSHNSGKLCILIRENDEFFELISSTFLSENSYSTAVKAASARLLMNCSLTWMYPHVFDDAVTENFKNWVMEEAVKFPGEDSAKKEASDFEMLKTYSTGLLALSLASRGQIVEDVLTSGLSAKLMHYLRVRVLKEPSTSRIHTTETKHVSLKTKEEGRSRVRKIVDTVEGDHVLETDSGREMGQTDVQPDGEFEIDGRDVFNVSGVVDCKIKPGDDNSVRDDPSRHRLNRSKSRGRGRVHEGAPDTEVLLASPRLGRLLVRDRDLSKISDGRNAEDVTVCLGKMKSGIMEIEREDNDECFQGCIIGTKNITDLVKRAVGAAETEARAAHAPDDAAKAAGDAAAELVKTAALEEFKSSGSEEAAVSAATRAAITVIDAAEVSRNPTCVTSDQTTDVSEVSLPDIESLAQLQEKYCIQCLEILGEYVEVLGPVLHEKGVDVCIVLLERTSQLDDRSTVSPLLPDVMKLICALAAHRKFAAMFVERRGILKLLAVPRVSETFYGLSSCLYTIGSLQGIMERVCALPLVVIHQVVKLAIELLDCSQDQARKNSALFFAAAFVFRAILDAFDAQDSLQKLLAILKDAASVRTGANTDRSAPEVMTSSEKQMAFHTCFALRQYFRAHLLLLVDSIRPSRISRGGVPSSMKPNIRAAYKPLDISNEAVDAIFLQLQKDRRLGPTFVKAQWPAVNNFLASSGHVTMLELCQTPPVDRYLHDLLQYAFGVLHIVTSIPDGRKAIAHATLSNNRAGIAVILDAANISNSIVDPEIIQPALNVLINLVCPPPSLSNKPPLAQNHQPVPGQATTRPSTDVAVGTQSTGNAPQTPVAPASSGLVGDRRIFLGAGTGSAGLAAKLEQVYRQAREAVRGNDGIKILLKLLQPRIYVNPPATPDCLRALACRVLLGLARDDTIAQILTKLEVGKSLSELIRDSGGQSSGTDQGRWQAELAQVALELIGIVTNSGHATTLTASDAATPTLRRIERAAIAAATPITYDSKELLLLIHEHLQASGLGDTASALLKEAQLTPLPSSASPSSIAYSTTQEMSTPLAQEQWPSGRANSGFFTSKPKVCAHDEDPNSRSNAALSAKKKHLASSTLEMPTPVAQQQWPSGRANCGFCPSIPKINARDEDPSSRGNAAPSAKKKQLTFSPSFSSQSRKQSFSHDALPQSTQRINCCSNSDPALADTSETAAELVLKNDLDADAQFKTPISFPRKRKLSELRDSSVPGKRIDLGERRNSTFADGSGLQTPASALDANQSGSSRLGQMTPASQLRLPSDPQPSNPERLSLDSLVVQYLKHQHRQCLAPITTLPPVSLLHPHVCPEPKRLLEAPLNMTGRLGTRELQSFYSGVHGNRRDRQFVFSRFKSWRSFRDETALFTCIALLGGTNHIAVGSHAGEIKIFEASSGSMLESVSGHQAPVTLVQPYVSRDTQLLLSSSSSDVQLWDASSITGGPRHSFDGCKAAKFSNSGLQFAALSCEASRKDVLLYDVQTCSPCQKLTDTVTSSRSNPYSLVHFSPCDTLILWNGVLWDRRIPEKVRRFDQFTDYGGGGFHPSRNEVIINSEIWDMRTFKLLRSVPSLDQTAITFNSRGDVIYAMLRRNIEDVMSAVHTRRVKHPLFAAFRTLDAINYSDIATIPVDRCLLDFATEPTDSFLGLITMEDQEDMFSSARMYEIGRRRPTDDDSDPDDDDETEDEDEDDEEEDDLDRILGLAGDNSDSGDDDLSSEDNEDSVSDFDEEADILIDGDFMEELIEGENEDDGNGEDEDDDDDGEMQDFMSSGEEDDYRDNIRSS
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
343PhosphorylationVHEGAPDTEVLLASP
CCCCCCCHHHHCCCH		27.2523776212
349PhosphorylationDTEVLLASPRLGRLL
CHHHHCCCHHHHHHE		15.5530291188
1052PhosphorylationLELIGIVTNSGHATT
HHHHCHHCCCCCCEE		23.0325368622
1054PhosphorylationLIGIVTNSGHATTLT
HHCHHCCCCCCEEEE		23.6925368622
1058PhosphorylationVTNSGHATTLTASDA
HCCCCCCEEEEHHHC		19.3625368622
1059PhosphorylationTNSGHATTLTASDAA
CCCCCCEEEEHHHCC		23.9325368622
1061PhosphorylationSGHATTLTASDAATP
CCCCEEEEHHHCCCH		23.2525368622
1063PhosphorylationHATTLTASDAATPTL
CCEEEEHHHCCCHHH		23.6525368622
1067PhosphorylationLTASDAATPTLRRIE
EEHHHCCCHHHHHHH		20.6625368622
1069PhosphorylationASDAATPTLRRIERA
HHHCCCHHHHHHHHH		28.6625368622
1153PhosphorylationWPSGRANSGFFTSKP
CCCCCCCCCCCCCCC		35.6725561503
1241PhosphorylationKKKQLTFSPSFSSQS
HHCCCEECCCCCCHH		17.8823776212
1243PhosphorylationKQLTFSPSFSSQSRK
CCCEECCCCCCHHHC		36.2430291188
1245PhosphorylationLTFSPSFSSQSRKQS
CEECCCCCCHHHCCC		31.6323776212
1246PhosphorylationTFSPSFSSQSRKQSF
EECCCCCCHHHCCCC		30.1123776212
1248PhosphorylationSPSFSSQSRKQSFSH
CCCCCCHHHCCCCCC		43.3123776212
1252PhosphorylationSSQSRKQSFSHDALP
CCHHHCCCCCCCCCC		31.5830589143
1254PhosphorylationQSRKQSFSHDALPQS
HHHCCCCCCCCCCCC		26.2125561503
1261PhosphorylationSHDALPQSTQRINCC
CCCCCCCCCCCCCCC		25.2719880383
1262PhosphorylationHDALPQSTQRINCCS
CCCCCCCCCCCCCCC		19.3319880383
1310PhosphorylationFPRKRKLSELRDSSV
CCCCCCHHHHHCCCC		37.3119880383
1330PhosphorylationDLGERRNSTFADGSG
CCCCCCCCCCCCCCC		24.0824243849
1331PhosphorylationLGERRNSTFADGSGL
CCCCCCCCCCCCCCC		26.7924243849
1336PhosphorylationNSTFADGSGLQTPAS
CCCCCCCCCCCCCHH		36.5624243849
1340PhosphorylationADGSGLQTPASALDA
CCCCCCCCCHHHHCC		26.3524243849
1343PhosphorylationSGLQTPASALDANQS
CCCCCCHHHHCCCCC		30.4824243849
1350PhosphorylationSALDANQSGSSRLGQ
HHHCCCCCCCCCCCC		40.2124243849
1771PhosphorylationEIGRRRPTDDDSDPD
HCCCCCCCCCCCCCC		50.6923776212
1775PhosphorylationRRPTDDDSDPDDDDE
CCCCCCCCCCCCCCC		59.0223776212
1783PhosphorylationDPDDDDETEDEDEDD
CCCCCCCCCCCCCCC		56.5923776212
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 DCAF1_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCAF1_ARATH !!
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 DCAF1_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDB1A_ARATHDDB1Aphysical
18552200
CUL4_ARATHCUL4physical
18552200
CSN5A_ARATHCSN5Aphysical
18552200
CSN7_ARATHFUS5physical
18552200
ABI5_ARATHABI5physical
24563203
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DCAF1_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana.";
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.;
J. Proteomics 72:439-451(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND MASSSPECTROMETRY.

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