ABCF2_HUMAN - dbPTM
ABCF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABCF2_HUMAN
UniProt AC Q9UG63
Protein Name ATP-binding cassette sub-family F member 2
Gene Name ABCF2
Organism Homo sapiens (Human).
Sequence Length 623
Subcellular Localization
Protein Description
Protein Sequence MPSDLAKKKAAKKKEAAKARQRPRKGHEENGDVVTEPQVAEKNEANGRETTEVDLLTKELEDFEMKKAAARAVTGVLASHPNSTDVHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLTREMPPSDKTPLHCVMEVDTERAMLEKEAERLAHEDAECEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYVKTRLELEENQMKRFHWEQDQIAHMKNYIARFGHGSAKLARQAQSKEKTLQKMMASGLTERVVSDKTLSFYFPPCGKIPPPVIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQEQLDLDLSPLEYMMKCYPEIKEKEEMRKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTITKWPGDILAYKEHLKSKLVDEEPQLTKRTHNV
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
3O-linked_Glycosylation-----MPSDLAKKKA
-----CCHHHHHHHH		43.9130379171
7Acetylation-MPSDLAKKKAAKKK
-CCHHHHHHHHHHHH		63.2091109
8AcetylationMPSDLAKKKAAKKKE
CCHHHHHHHHHHHHH		41.8891113
9AcetylationPSDLAKKKAAKKKEA
CHHHHHHHHHHHHHH		53.5291117
35PhosphorylationEENGDVVTEPQVAEK
CCCCCCCCCHHHHCC		41.6226074081
42AcetylationTEPQVAEKNEANGRE
CCHHHHCCCHHCCCC		50.8026051181
50PhosphorylationNEANGRETTEVDLLT
CHHCCCCCCHHHHHH		27.2226074081
51PhosphorylationEANGRETTEVDLLTK
HHCCCCCCHHHHHHH		29.2926074081
57PhosphorylationTTEVDLLTKELEDFE
CCHHHHHHHHHHHHH		29.7526074081
65SulfoxidationKELEDFEMKKAAARA
HHHHHHHHHHHHHHH		5.6421406390
662-HydroxyisobutyrylationELEDFEMKKAAARAV
HHHHHHHHHHHHHHH		31.87-
66UbiquitinationELEDFEMKKAAARAV
HHHHHHHHHHHHHHH		31.87-
125PhosphorylationGLNGIGKSMLLSAIG
ECCCCCHHHHHHHHC		14.9521406692
129PhosphorylationIGKSMLLSAIGKREV
CCHHHHHHHHCCCCC		17.5563756007
1332-HydroxyisobutyrylationMLLSAIGKREVPIPE
HHHHHHCCCCCCCCC		38.99-
133AcetylationMLLSAIGKREVPIPE
HHHHHHCCCCCCCCC		38.9925953088
133UbiquitinationMLLSAIGKREVPIPE
HHHHHHCCCCCCCCC		38.99-
145PhosphorylationIPEHIDIYHLTREMP
CCCCEEEEHHCCCCC		6.2428152594
148PhosphorylationHIDIYHLTREMPPSD
CEEEEHHCCCCCCCC		15.9828152594
156AcetylationREMPPSDKTPLHCVM
CCCCCCCCCCCEEEE		57.2826051181
174UbiquitinationTERAMLEKEAERLAH
HHHHHHHHHHHHHHH		59.2621890473
174AcetylationTERAMLEKEAERLAH
HHHHHHHHHHHHHHH		59.2625953088
174UbiquitinationTERAMLEKEAERLAH
HHHHHHHHHHHHHHH		59.2621906983
188AcetylationHEDAECEKLMELYER
HCHHHHHHHHHHHHH		65.8726051181
188UbiquitinationHEDAECEKLMELYER
HCHHHHHHHHHHHHH		65.87-
203UbiquitinationLEELDADKAEMRASR
HHHHCCHHHHHHHHH		48.2221890473
203AcetylationLEELDADKAEMRASR
HHHHCCHHHHHHHHH		48.2226051181
203UbiquitinationLEELDADKAEMRASR
HHHHCCHHHHHHHHH		48.2221906983
206SulfoxidationLDADKAEMRASRILH
HCCHHHHHHHHHHHH		5.3221406390
218PhosphorylationILHGLGFTPAMQRKK
HHHHCCCCHHHHHHH		14.3523917254
227AcetylationAMQRKKLKDFSGGWR
HHHHHHHCCCCCCHH		66.6526051181
227UbiquitinationAMQRKKLKDFSGGWR
HHHHHHHCCCCCCHH		66.65-
230PhosphorylationRKKLKDFSGGWRMRV
HHHHCCCCCCHHHHH		46.6726270265
304AcetylationHMHNKKLKYYTGNYD
HHCCCCCEEECCCHH		45.1219608861
304MalonylationHMHNKKLKYYTGNYD
HHCCCCCEEECCCHH		45.1226320211
304UbiquitinationHMHNKKLKYYTGNYD
HHCCCCCEEECCCHH		45.1219608861
305PhosphorylationMHNKKLKYYTGNYDQ
HCCCCCEEECCCHHH		19.3928152594
306PhosphorylationHNKKLKYYTGNYDQY
CCCCCEEECCCHHHH		13.4483473
315UbiquitinationGNYDQYVKTRLELEE
CCHHHHHHHHHHHHH		24.0021890473
315AcetylationGNYDQYVKTRLELEE
CCHHHHHHHHHHHHH		24.0026051181
315UbiquitinationGNYDQYVKTRLELEE
CCHHHHHHHHHHHHH		24.0021906983
325SulfoxidationLELEENQMKRFHWEQ
HHHHHHHHHHCCCCH		5.1921406390
326UbiquitinationELEENQMKRFHWEQD
HHHHHHHHHCCCCHH		41.9921890473
326MethylationELEENQMKRFHWEQD
HHHHHHHHHCCCCHH		41.99-
326UbiquitinationELEENQMKRFHWEQD
HHHHHHHHHCCCCHH		41.9921906983
327MethylationLEENQMKRFHWEQDQ
HHHHHHHHCCCCHHH		24.26-
339UbiquitinationQDQIAHMKNYIARFG
HHHHHHHHHHHHHHC		36.4121890473
339UbiquitinationQDQIAHMKNYIARFG
HHHHHHHHHHHHHHC		36.4121906983
341PhosphorylationQIAHMKNYIARFGHG
HHHHHHHHHHHHCCH		7.1645281997
349PhosphorylationIARFGHGSAKLARQA
HHHHCCHHHHHHHHH		19.2928985074
351UbiquitinationRFGHGSAKLARQAQS
HHCCHHHHHHHHHHH		44.36-
351AcetylationRFGHGSAKLARQAQS
HHCCHHHHHHHHHHH		44.3625953088
351UbiquitinationRFGHGSAKLARQAQS
HHCCHHHHHHHHHHH		44.36-
359UbiquitinationLARQAQSKEKTLQKM
HHHHHHHHHHHHHHH		51.67-
362PhosphorylationQAQSKEKTLQKMMAS
HHHHHHHHHHHHHHC		35.2029449344
365UbiquitinationSKEKTLQKMMASGLT
HHHHHHHHHHHCCCC		33.4821890473
365UbiquitinationSKEKTLQKMMASGLT
HHHHHHHHHHHCCCC		33.4821906983
369PhosphorylationTLQKMMASGLTERVV
HHHHHHHCCCCCCHH		19.2120860994
372PhosphorylationKMMASGLTERVVSDK
HHHHCCCCCCHHCCC		25.8582570245
377PhosphorylationGLTERVVSDKTLSFY
CCCCCHHCCCEEEEE		30.4582570251
379UbiquitinationTERVVSDKTLSFYFP
CCCHHCCCEEEEECC		43.81-
380PhosphorylationERVVSDKTLSFYFPP
CCHHCCCEEEEECCC		32.4028851738
382PhosphorylationVVSDKTLSFYFPPCG
HHCCCEEEEECCCCC		24.1128555341
384PhosphorylationSDKTLSFYFPPCGKI
CCCEEEEECCCCCCC		16.2923917254
402PhosphorylationVIMVQNVSFKYTKDG
EEEEECCEEEECCCC		24.4620873877
404AcetylationMVQNVSFKYTKDGPC
EEECCEEEECCCCCE		44.5025953088
406PhosphorylationQNVSFKYTKDGPCIY
ECCEEEECCCCCEEE		24.2146156925
407AcetylationNVSFKYTKDGPCIYN
CCEEEECCCCCEEEC		58.5626051181
436UbiquitinationVGPNGAGKSTLLKLL
ECCCCCCHHHHHHHH		39.4721890473
436UbiquitinationVGPNGAGKSTLLKLL
ECCCCCCHHHHHHHH		39.4721890473
437PhosphorylationGPNGAGKSTLLKLLT
CCCCCCHHHHHHHHH		24.3022210691
438PhosphorylationPNGAGKSTLLKLLTG
CCCCCHHHHHHHHHC		39.3322210691
441UbiquitinationAGKSTLLKLLTGELL
CCHHHHHHHHHCCCC		44.56-
441UbiquitinationAGKSTLLKLLTGELL
CCHHHHHHHHHCCCC		44.56-
444PhosphorylationSTLLKLLTGELLPTD
HHHHHHHHCCCCCCC		38.7622210691
453SulfoxidationELLPTDGMIRKHSHV
CCCCCCCCCCCCCCC		2.7421406390
456UbiquitinationPTDGMIRKHSHVKIG
CCCCCCCCCCCCCCC		38.24-
461UbiquitinationIRKHSHVKIGRYHQH
CCCCCCCCCCCHHHH		33.74-
465PhosphorylationSHVKIGRYHQHLQEQ
CCCCCCCHHHHHHHH		10.7172505
482PhosphorylationLDLSPLEYMMKCYPE
CCCCHHHHHHHHCHH		15.3672509
487PhosphorylationLEYMMKCYPEIKEKE
HHHHHHHCHHHHHHH		9.8122817900
503PhosphorylationMRKIIGRYGLTGKQQ
HHHHHHHHCCCCCCC		15.9820068231
506PhosphorylationIIGRYGLTGKQQVSP
HHHHHCCCCCCCCCC		37.6620068231
508UbiquitinationGRYGLTGKQQVSPIR
HHHCCCCCCCCCCCC		32.1121890473
508AcetylationGRYGLTGKQQVSPIR
HHHCCCCCCCCCCCC		32.1126051181
508UbiquitinationGRYGLTGKQQVSPIR
HHHCCCCCCCCCCCC		32.1121906983
512PhosphorylationLTGKQQVSPIRNLSD
CCCCCCCCCCCCCCC		15.4021815630
518PhosphorylationVSPIRNLSDGQKCRV
CCCCCCCCCCCCHHH		43.1536012605
522UbiquitinationRNLSDGQKCRVCLAW
CCCCCCCCHHHHHHH		29.5421890473
522AcetylationRNLSDGQKCRVCLAW
CCCCCCCCHHHHHHH		29.5425953088
522UbiquitinationRNLSDGQKCRVCLAW
CCCCCCCCHHHHHHH		29.5421906983
588UbiquitinationQEIWVCEKQTITKWP
HHHHCCCCCCCCCCC		47.84-
588AcetylationQEIWVCEKQTITKWP
HHHHCCCCCCCCCCC		47.8426051181
588UbiquitinationQEIWVCEKQTITKWP
HHHHCCCCCCCCCCC		47.8421890473
593UbiquitinationCEKQTITKWPGDILA
CCCCCCCCCCCCHHH		47.76-
601PhosphorylationWPGDILAYKEHLKSK
CCCCHHHHHHHHHHH		17.2920049867
602UbiquitinationPGDILAYKEHLKSKL
CCCHHHHHHHHHHHC		32.8121890473
602AcetylationPGDILAYKEHLKSKL
CCCHHHHHHHHHHHC		32.8126051181
602UbiquitinationPGDILAYKEHLKSKL
CCCHHHHHHHHHHHC		32.8121890473
606UbiquitinationLAYKEHLKSKLVDEE
HHHHHHHHHHCCCCC		47.67-
606UbiquitinationLAYKEHLKSKLVDEE
HHHHHHHHHHCCCCC		47.67-
607PhosphorylationAYKEHLKSKLVDEEP
HHHHHHHHHCCCCCC		37.2727251275
608AcetylationYKEHLKSKLVDEEPQ
HHHHHHHHCCCCCCH		51.44-
608UbiquitinationYKEHLKSKLVDEEPQ
HHHHHHHHCCCCCCH		51.4421890473
608AcetylationYKEHLKSKLVDEEPQ
HHHHHHHHCCCCCCH		51.4423236377
608UbiquitinationYKEHLKSKLVDEEPQ
HHHHHHHHCCCCCCH		51.4421906983
617PhosphorylationVDEEPQLTKRTHNV-
CCCCCHHHCCCCCC-		17.1521406692
617 (in isoform 2)Phosphorylation-17.1524719451
618UbiquitinationDEEPQLTKRTHNV--
CCCCHHHCCCCCC--		64.9821890473
618AcetylationDEEPQLTKRTHNV--
CCCCHHHCCCCCC--		64.9825953088
618UbiquitinationDEEPQLTKRTHNV--
CCCCHHHCCCCCC--		64.9821906983
620 (in isoform 2)Phosphorylation-21.25-
625 (in isoform 2)Phosphorylation-24719451
627 (in isoform 2)Phosphorylation--
630 (in isoform 2)Phosphorylation-24719451
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 ABCF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABCF2_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 ABCF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIR6_HUMANSIRT6physical
22939629
PP1RA_HUMANPPP1R10physical
22939629
ECHA_HUMANHADHAphysical
21988832
ROA2_HUMANHNRNPA2B1physical
22863883
DDX3X_HUMANDDX3Xphysical
26344197
DKC1_HUMANDKC1physical
26344197
IF2G_HUMANEIF2S3physical
26344197
IF2P_HUMANEIF5Bphysical
26344197
C1TC_HUMANMTHFD1physical
26344197
WDR36_HUMANWDR36physical
26344197
SAHH3_HUMANAHCYL2physical
28514442
GNL1_HUMANGNL1physical
28514442
PGES2_HUMANPTGES2physical
28514442
SAHH2_HUMANAHCYL1physical
28514442
NUDC1_HUMANNUDCD1physical
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 ABCF2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-304, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND MASSSPECTROMETRY.

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