RFWD3_HUMAN - dbPTM
RFWD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RFWD3_HUMAN
UniProt AC Q6PCD5
Protein Name E3 ubiquitin-protein ligase RFWD3 {ECO:0000305}
Gene Name RFWD3 {ECO:0000312|HGNC:HGNC:25539}
Organism Homo sapiens (Human).
Sequence Length 774
Subcellular Localization Nucleus . Nucleus, PML body . Cytoplasm . In undamaged cells, found both in the cytoplasm and in the nucleus, partially associated with PML nuclear bodies (PubMed:21558276). In response to replication block, such as that caused by hydroxyurea treatme
Protein Description E3 ubiquitin-protein ligase required for the repair of DNA interstrand cross-links (ICL) in response to DNA damage. [PubMed: 21504906]
Protein Sequence MAHEAMEYDVQVQLNHAEQQPAPAGMASSQGGPALLQPVPADVVSSQGVPSILQPAPAEVISSQATPPLLQPAPQLSVDLTEVEVLGEDTVENINPRTSEQHRQGSDGNHTIPASSLHSMTNFISGLQRLHGMLEFLRPSSSNHSVGPMRTRRRVSASRRARAGGSQRTDSARLRAPLDAYFQVSRTQPDLPATTYDSETRNPVSEELQVSSSSDSDSDSSAEYGGVVDQAEESGAVILEEQLAGVSAEQEVTCIDGGKTLPKQPSPQKSEPLLPSASMDEEEGDTCTICLEQWTNAGDHRLSALRCGHLFGYRCISTWLKGQVRKCPQCNKKARHSDIVVLYARTLRALDTSEQERMKSSLLKEQMLRKQAELESAQCRLQLQVLTDKCTRLQRRVQDLQKLTSHQSQNLQQPRGSQAWVLSCSPSSQGQHKHKYHFQKTFTVSQAGNCRIMAYCDALSCLVISQPSPQASFLPGFGVKMLSTANMKSSQYIPMHGKQIRGLAFSSYLRGLLLSASLDNTIKLTSLETNTVVQTYNAGRPVWSCCWCLDEANYIYAGLANGSILVYDVRNTSSHVQELVAQKARCPLVSLSYMPRAASAAFPYGGVLAGTLEDASFWEQKMDFSHWPHVLPLEPGGCIDFQTENSSRHCLVTYRPDKNHTTIRSVLMEMSYRLDDTGNPICSCQPVHTFFGGPTCKLLTKNAIFQSPENDGNILVCTGDEAANSALLWDAASGSLLQDLQTDQPVLDICPFEVNRNSYLATLTEKMVHIYKWE
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
46PhosphorylationVPADVVSSQGVPSIL
CCCCHHCCCCCCCCC		21.2428575658
63PhosphorylationAPAEVISSQATPPLL
CCHHHHHCCCCCCCC		16.8328575658
181PhosphorylationLRAPLDAYFQVSRTQ
CCCCHHHEEEEECCC		8.3327642862
185PhosphorylationLDAYFQVSRTQPDLP
HHHEEEEECCCCCCC		20.8728555341
253PhosphorylationVSAEQEVTCIDGGKT
CCCCCEEEEEECCCC		11.7326074081
260PhosphorylationTCIDGGKTLPKQPSP
EEEECCCCCCCCCCC		52.1226074081
263UbiquitinationDGGKTLPKQPSPQKS
ECCCCCCCCCCCCCC		77.3329967540
266PhosphorylationKTLPKQPSPQKSEPL
CCCCCCCCCCCCCCC		37.1525849741
270PhosphorylationKQPSPQKSEPLLPSA
CCCCCCCCCCCCCCC		38.9226074081
276PhosphorylationKSEPLLPSASMDEEE
CCCCCCCCCCCCCCC		32.7126074081
278PhosphorylationEPLLPSASMDEEEGD
CCCCCCCCCCCCCCC		30.9826074081
321UbiquitinationRCISTWLKGQVRKCP
HHHHHHHCCCCCCCC		38.5722505724
337PhosphorylationCNKKARHSDIVVLYA
CCCCCCCCCEEHEEH		24.3929214152
352PhosphorylationRTLRALDTSEQERMK
HHHHHCCCCHHHHHH		34.7123403867
353PhosphorylationTLRALDTSEQERMKS
HHHHCCCCHHHHHHH		36.6323403867
359UbiquitinationTSEQERMKSSLLKEQ
CCHHHHHHHHHHHHH		43.0122817900
360PhosphorylationSEQERMKSSLLKEQM
CHHHHHHHHHHHHHH		19.5129116813
361PhosphorylationEQERMKSSLLKEQML
HHHHHHHHHHHHHHH		32.0024719451
364UbiquitinationRMKSSLLKEQMLRKQ
HHHHHHHHHHHHHHH		51.7121906983
364AcetylationRMKSSLLKEQMLRKQ
HHHHHHHHHHHHHHH		51.7112650403
370UbiquitinationLKEQMLRKQAELESA
HHHHHHHHHHHHHHH		50.3133845483
370AcetylationLKEQMLRKQAELESA
HHHHHHHHHHHHHHH		50.3112650411
376PhosphorylationRKQAELESAQCRLQL
HHHHHHHHHHHHHHH		35.9430377224
387PhosphorylationRLQLQVLTDKCTRLQ
HHHHHHHHHHHHHHH		34.2630377224
389UbiquitinationQLQVLTDKCTRLQRR
HHHHHHHHHHHHHHH		32.0723000965
391PhosphorylationQVLTDKCTRLQRRVQ
HHHHHHHHHHHHHHH		39.9124043423
402UbiquitinationRRVQDLQKLTSHQSQ
HHHHHHHHHHHHHCC		62.1121890473
402UbiquitinationRRVQDLQKLTSHQSQ
HHHHHHHHHHHHHCC		62.1121963094
402UbiquitinationRRVQDLQKLTSHQSQ
HHHHHHHHHHHHHCC		62.1121890473
404PhosphorylationVQDLQKLTSHQSQNL
HHHHHHHHHHHCCCC		31.0626714015
405PhosphorylationQDLQKLTSHQSQNLQ
HHHHHHHHHHCCCCC		29.9326714015
408PhosphorylationQKLTSHQSQNLQQPR
HHHHHHHCCCCCCCC		18.6626714015
417PhosphorylationNLQQPRGSQAWVLSC
CCCCCCCCEEEEEEE		20.2923312004
423PhosphorylationGSQAWVLSCSPSSQG
CCEEEEEEECCCCCC		11.7022199227
425PhosphorylationQAWVLSCSPSSQGQH
EEEEEEECCCCCCCC		25.1725159151
427PhosphorylationWVLSCSPSSQGQHKH
EEEEECCCCCCCCCC		20.9917525332
428PhosphorylationVLSCSPSSQGQHKHK
EEEECCCCCCCCCCE		41.5417525332
433UbiquitinationPSSQGQHKHKYHFQK
CCCCCCCCCEEEEEE		33.6321963094
435UbiquitinationSQGQHKHKYHFQKTF
CCCCCCCEEEEEEEE		45.2722817900
440UbiquitinationKHKYHFQKTFTVSQA
CCEEEEEEEEEECCC		44.6621963094
488MethylationMLSTANMKSSQYIPM
EEEECCCCCCCEECC		46.9282987989
488UbiquitinationMLSTANMKSSQYIPM
EEEECCCCCCCEECC		46.9229967540
488SumoylationMLSTANMKSSQYIPM
EEEECCCCCCCEECC		46.92-
488SumoylationMLSTANMKSSQYIPM
EEEECCCCCCCEECC		46.92-
489PhosphorylationLSTANMKSSQYIPMH
EEECCCCCCCEECCC		16.3530631047
490PhosphorylationSTANMKSSQYIPMHG
EECCCCCCCEECCCC		22.8330631047
498UbiquitinationQYIPMHGKQIRGLAF
CEECCCCCCCCHHHH		28.0727667366
525PhosphorylationLDNTIKLTSLETNTV
CCCEEEEEECCCCCE		26.6823879269
526PhosphorylationDNTIKLTSLETNTVV
CCEEEEEECCCCCEE		34.3423879269
529PhosphorylationIKLTSLETNTVVQTY
EEEEECCCCCEEEEE		41.2923879269
531PhosphorylationLTSLETNTVVQTYNA
EEECCCCCEEEEECC		29.4923879269
583UbiquitinationVQELVAQKARCPLVS
HHHHHHHHCCCCEEE		28.2321906983
583UbiquitinationVQELVAQKARCPLVS
HHHHHHHHCCCCEEE		28.2321890473
583UbiquitinationVQELVAQKARCPLVS
HHHHHHHHCCCCEEE		28.2321890473
599UbiquitinationSYMPRAASAAFPYGG
CCCCCHHHHCCCCCC		21.1021963094
638UbiquitinationLPLEPGGCIDFQTEN
ECCCCCCEEEEECCC		3.1521963094
642UbiquitinationPGGCIDFQTENSSRH
CCCEEEEECCCCCCE		44.1222817900
658UbiquitinationLVTYRPDKNHTTIRS
EEEECCCCCCCCHHH		54.0021963094
661PhosphorylationYRPDKNHTTIRSVLM
ECCCCCCCCHHHHHH		33.0617081983
697UbiquitinationFFGGPTCKLLTKNAI
CCCCCCEEEEECCCE		49.3521963094
701UbiquitinationPTCKLLTKNAIFQSP
CCEEEEECCCEECCC		44.3322817900
707UbiquitinationTKNAIFQSPENDGNI
ECCCEECCCCCCCCE		24.3521890473
713UbiquitinationQSPENDGNILVCTGD
CCCCCCCCEEEECCC		27.5522505724
766UbiquitinationYLATLTEKMVHIYKW
EEEECHHHHEEEEEC		40.7721906983
766UbiquitinationYLATLTEKMVHIYKW
EEEECHHHHEEEEEC		40.7721890473
766UbiquitinationYLATLTEKMVHIYKW
EEEECHHHHEEEEEC		40.7721890473
772SumoylationEKMVHIYKWE-----
HHHEEEEECC-----		44.22-
772SumoylationEKMVHIYKWE-----
HHHEEEEECC-----		44.22-
772UbiquitinationEKMVHIYKWE-----
HHHEEEEECC-----		44.2222505724
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
46SPhosphorylationKinaseATMQ13315
Uniprot
46SPhosphorylationKinaseATRQ13535
Uniprot
63SPhosphorylationKinaseATMQ13315
Uniprot
63SPhosphorylationKinaseATRQ13535
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
46SPhosphorylation

20173098
63SPhosphorylation

20173098
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 RFWD3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RFA2_HUMANRPA2physical
21558276
RFA1_HUMANRPA1physical
21558276
RFA3_HUMANRPA3physical
21558276
P53_HUMANTP53physical
20173098
MDM2_HUMANMDM2physical
20173098
RFA2_HUMANRPA2physical
21504906
RFA3_HUMANRPA3physical
21504906
RFA1_HUMANRPA1physical
21504906
COA1_HUMANCOA1physical
21504906
A4_HUMANAPPphysical
21832049
CALX_HUMANCANXphysical
26496610
TCPZ_HUMANCCT6Aphysical
26496610
GSLG1_HUMANGLG1physical
26496610
CH60_HUMANHSPD1physical
26496610
MBNL1_HUMANMBNL1physical
26496610
PFD1_HUMANPFDN1physical
26496610
PFD2_HUMANPFDN2physical
26496610
TCPA_HUMANTCP1physical
26496610
ENPL_HUMANHSP90B1physical
26496610
TCPG_HUMANCCT3physical
26496610
VA0D1_HUMANATP6V0D1physical
26496610
HYOU1_HUMANHYOU1physical
26496610
TCPH_HUMANCCT7physical
26496610
TCPD_HUMANCCT4physical
26496610
TCPB_HUMANCCT2physical
26496610
TCPQ_HUMANCCT8physical
26496610
TCPE_HUMANCCT5physical
26496610
LYAR_HUMANLYARphysical
26496610
RFA1_HUMANRPA1physical
28575657
RFA1_HUMANRPA1physical
28575658
RFA2_HUMANRPA2physical
28575658
RFA3_HUMANRPA3physical
28575658
RAD51_HUMANRAD51physical
28575658
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 RFWD3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"RFWD3-Mdm2 ubiquitin ligase complex positively regulates p53stability in response to DNA damage.";
Fu X., Yucer N., Liu S., Li M., Yi P., Mu J.J., Yang T., Chu J.,Jung S.Y., O'Malley B.W., Gu W., Qin J., Wang Y.;
Proc. Natl. Acad. Sci. U.S.A. 107:4579-4584(2010).
Cited for: FUNCTION, INTERACTION WITH MDM2 AND TP53, SUBCELLULAR LOCATION,PHOSPHORYLATION AT SER-46 AND SER-63, AND MUTAGENESIS OF SER-46;SER-63 AND CYS-315.
"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-427 AND SER-428, ANDMASS SPECTROMETRY.

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