ABCF3_HUMAN - dbPTM
ABCF3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABCF3_HUMAN
UniProt AC Q9NUQ8
Protein Name ATP-binding cassette sub-family F member 3
Gene Name ABCF3
Organism Homo sapiens (Human).
Sequence Length 709
Subcellular Localization
Protein Description Displays an antiviral effect against flaviviruses such as west Nile virus (WNV) in the presence of OAS1B..
Protein Sequence MATCAEILRSEFPEIDGQVFDYVTGVLHSGSADFESVDDLVEAVGELLQEVSGDSKDDAGIRAVCQRMYNTLRLAEPQSQGNSQVLLDAPIQLSKITENYDCGTKLPGLLKREQSSTVNAKKLEKAEARLKAKQEKRSEKDTLKTSNPLVLEEASASQAGSRKESRLESSGKNKSYDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLLHVEQEVAGDDTPALQSVLESDSVREDLLRRERELTAQIAAGRAEGSEAAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIDRFRYNANRASQVQSKLKMLEKLPELKPVDKESEVVMKFPDGFEKFSPPILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLARKFPGRPEEEYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVTRVEGGFDQYRALLQEQFRREGFL
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------MATCAEILR
------CCCHHHHHH		16.0422223895
3Phosphorylation-----MATCAEILRS
-----CCCHHHHHHH		15.7920860994
79PhosphorylationLRLAEPQSQGNSQVL
HHHCCCCCCCCCEEE		51.2623663014
83PhosphorylationEPQSQGNSQVLLDAP
CCCCCCCCEEEEECC		28.6123663014
95UbiquitinationDAPIQLSKITENYDC
ECCEEHHHHCCCCCC		63.34-
97PhosphorylationPIQLSKITENYDCGT
CEEHHHHCCCCCCCC		23.1626552605
100PhosphorylationLSKITENYDCGTKLP
HHHHCCCCCCCCCCC		13.3328796482
104PhosphorylationTENYDCGTKLPGLLK
CCCCCCCCCCCCHHH		35.4228796482
111UbiquitinationTKLPGLLKREQSSTV
CCCCCHHHHHHCCCC		59.95-
115PhosphorylationGLLKREQSSTVNAKK
CHHHHHHCCCCCHHH		24.1930576142
116PhosphorylationLLKREQSSTVNAKKL
HHHHHHCCCCCHHHH		35.7511660005
117PhosphorylationLKREQSSTVNAKKLE
HHHHHCCCCCHHHHH		24.0326699800
144UbiquitinationRSEKDTLKTSNPLVL
HCHHHHCCCCCCCHH		52.58-
145PhosphorylationSEKDTLKTSNPLVLE
CHHHHCCCCCCCHHH		36.5325159151
146PhosphorylationEKDTLKTSNPLVLEE
HHHHCCCCCCCHHHH		34.5625159151
155PhosphorylationPLVLEEASASQAGSR
CCHHHHHCHHHCCCC		31.5623882029
157PhosphorylationVLEEASASQAGSRKE
HHHHHCHHHCCCCCH		20.3323917254
161PhosphorylationASASQAGSRKESRLE
HCHHHCCCCCHHHHH		43.1028857561
165PhosphorylationQAGSRKESRLESSGK
HCCCCCHHHHHCCCC		45.2423882029
169PhosphorylationRKESRLESSGKNKSY
CCHHHHHCCCCCCCC		49.3223882029
170PhosphorylationKESRLESSGKNKSYD
CHHHHHCCCCCCCCE		44.4023882029
174UbiquitinationLESSGKNKSYDVRIE
HHCCCCCCCCEEEEE		54.61-
218PhosphorylationRNGLGKTTLLKMLAT
CCCCCHHHHHHHHHH		33.3150558673
225PhosphorylationTLLKMLATRSLRVPA
HHHHHHHHCCCCCCE		19.4820068231
272PhosphorylationLRRERELTAQIAAGR
HHHHHHHHHHHHHHC		16.2636012617
283PhosphorylationAAGRAEGSEAAELAE
HHHCCCCCHHHHHHH		18.6325159151
288 (in isoform 2)Ubiquitination-4.4321906983
294 (in isoform 1)Ubiquitination-39.1921906983
294UbiquitinationELAEIYAKLEEIEAD
HHHHHHHHHHHHHHC		39.1922053931
294UbiquitinationELAEIYAKLEEIEAD
HHHHHHHHHHHHHHC		39.19-
302UbiquitinationLEEIEADKAPARASV
HHHHHHCCCHHHHHH		64.42-
317PhosphorylationILAGLGFTPKMQQQP
HHHHCCCCHHHHCCC		21.8726270265
319UbiquitinationAGLGFTPKMQQQPTR
HHCCCCHHHHCCCCC		46.40-
319AcetylationAGLGFTPKMQQQPTR
HHCCCCHHHHCCCCC		46.4025953088
329PhosphorylationQQPTREFSGGWRMRL
CCCCCCCCHHHHHHH		31.4826270265
411PhosphorylationGYRGDFETFIKSKQE
CCCCCHHHHHHHHHH		30.5624719451
427PhosphorylationLLNQQREYEAQQQYR
HHHHHHHHHHHHHHH		20.8228796482
433PhosphorylationEYEAQQQYRQHIQVF
HHHHHHHHHHHHHHH		14.1146156943
452PhosphorylationRYNANRASQVQSKLK
HHCCHHHHHHHHHHH		27.8728450419
457UbiquitinationRASQVQSKLKMLEKL
HHHHHHHHHHHHHHC		34.73-
457MalonylationRASQVQSKLKMLEKL
HHHHHHHHHHHHHHC		34.7326320211
457AcetylationRASQVQSKLKMLEKL
HHHHHHHHHHHHHHC		34.7325953088
463UbiquitinationSKLKMLEKLPELKPV
HHHHHHHHCCCCCCC		66.44-
468UbiquitinationLEKLPELKPVDKESE
HHHCCCCCCCCCCCC		41.14-
479UbiquitinationKESEVVMKFPDGFEK
CCCCEEEECCCCHHH		41.98-
512PhosphorylationHVIFSRLSVSADLES
CEEEEEEEECCCCCC		16.9620068231
514PhosphorylationIFSRLSVSADLESRI
EEEEEEECCCCCCCE		16.8220068231
519PhosphorylationSVSADLESRICVVGE
EECCCCCCCEEEECC		33.9520068231
531UbiquitinationVGENGAGKSTMLKLL
ECCCCCCHHHHHHHH		42.07-
536UbiquitinationAGKSTMLKLLLGDLA
CCHHHHHHHHHHCCH		26.68-
616UbiquitinationASLSGGQKSRVAFAQ
HHCCCCCCHHEEEEE		43.43-
657MethylationGRALNNFRGGVILVS
HHHHHHCCCCEEEEE		42.98-
686PhosphorylationVCEGGGVTRVEGGFD
EECCCCCEEEECCHH		32.0720068231
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 ABCF3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABCF3_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 ABCF3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACINU_HUMANACIN1physical
16169070
IDLC_HUMANDNALI1physical
16169070
LTOR1_HUMANLAMTOR1physical
16169070
TOE1_HUMANTOE1physical
16169070
VATB2_HUMANATP6V1B2physical
22939629
HNRPF_HUMANHNRNPFphysical
22863883
CCD33_HUMANCCDC33physical
25416956
ABCF2_HUMANABCF2physical
26344197
NLRP9_HUMANNLRP9physical
26344197
TRI27_HUMANTRIM27physical
21516116
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 ABCF3_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-283, AND MASSSPECTROMETRY.

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