ABCF1_MOUSE - dbPTM
ABCF1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABCF1_MOUSE
UniProt AC Q6P542
Protein Name ATP-binding cassette sub-family F member 1
Gene Name Abcf1
Organism Mus musculus (Mouse).
Sequence Length 837
Subcellular Localization Cytoplasm . Nucleus, nucleoplasm . Nucleus envelope .
Protein Description Required for efficient Cap- and IRES-mediated mRNA translation initiation. Not involved in the ribosome biogenesis (By similarity)..
Protein Sequence MPKGPKQQPPEPEWIGDGEGTSPADKVVKKGKKDKKTKKTFFEELAVEDKQAGEEEKLQKEKEQQQQQQQQKKKRDTRKGRRKKDVDDDSDERVLMERLKQLSVPASDEEDEVPAPIPRGRKKAKGGNVFEALIQDDSEEEEEEEENRVLKPAKPEKNRINKAVAEEPPGLRSKKGKEEKSKGKAKSKPAAADSEGEEEEEDTAKEKEPPQQGKDRDKKEAEQGSGEEKEEKEGDLKANDPYANLSKKEKKKLKKQMDYERQVESLKAANAAENDFSVSQAEVSSRQAMLENASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLRLLEEERRLQGQLEQGDDTAAEKLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKELKAGGKSTKQAEKQTKEVLTRKQQKCRRKNQDEESQEPPELLKRPKEYTVRFTFPDPPPLSPPVLGLHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQYAEQLHMEETPTEYLQRSFNLPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKGAVIVVSHDARLITETNCQLWVVEEQGVSQIDGDFDDYKREVLEALGEVMVNRPRD
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
21PhosphorylationWIGDGEGTSPADKVV
CCCCCCCCCHHHHHH		27.5123684622
22PhosphorylationIGDGEGTSPADKVVK
CCCCCCCCHHHHHHH		29.0225521595
90PhosphorylationKKDVDDDSDERVLME
CCCCCCCCHHHHHHH		48.6526824392
103PhosphorylationMERLKQLSVPASDEE
HHHHHHCCCCCCCCC		24.4624925903
107PhosphorylationKQLSVPASDEEDEVP
HHCCCCCCCCCCCCC		39.2124925903
138PhosphorylationEALIQDDSEEEEEEE
HHHHCCCCHHHHHHH		56.0227087446
162AcetylationPEKNRINKAVAEEPP
CCCCCCCHHHHCCCC		41.707613245
173PhosphorylationEEPPGLRSKKGKEEK
CCCCCCCCCCCHHHH		43.7026824392
187PhosphorylationKSKGKAKSKPAAADS
HCCCCCCCCCCCCCC		49.0525159016
194PhosphorylationSKPAAADSEGEEEEE
CCCCCCCCCCHHHHC		42.6527087446
203PhosphorylationGEEEEEDTAKEKEPP
CHHHHCHHHHHCCCC		42.8025521595
225PhosphorylationKKEAEQGSGEEKEEK
HHHHHCCCCCCHHHH		42.6027087446
242PhosphorylationDLKANDPYANLSKKE
CCCCCCCCCCCCHHH		15.8125159016
246PhosphorylationNDPYANLSKKEKKKL
CCCCCCCCHHHHHHH		41.3025159016
265PhosphorylationDYERQVESLKAANAA
CHHHHHHHHHHHHHH		35.9923737553
279PhosphorylationAENDFSVSQAEVSSR
HCCCCCHHHHHHHHH		23.6029514104
297AcetylationLENASDIKLEKFSIS
HHCHHCCCCEEEEEE		56.4315611783
300AcetylationASDIKLEKFSISAHG
HHCCCCEEEEEECCC		55.6415611793
324PhosphorylationYIVAGRRYGLVGPNG
EEEECCCCCCCCCCC		17.2851457439
332UbiquitinationGLVGPNGKGKTTLLK
CCCCCCCCCHHHHHH		64.9722790023
339AcetylationKGKTTLLKHIANRAL
CCHHHHHHHHHHHHH		35.7622826441
357GlutathionylationPNIDVLLCEQEVVAD
CCCCEEEECCEEECC		4.4224333276
399PhosphorylationQLEQGDDTAAEKLEK
HHHCCCHHHHHHHHH		32.2925367039
403UbiquitinationGDDTAAEKLEKVYEE
CCHHHHHHHHHHHHH		58.1622790023
408PhosphorylationAEKLEKVYEELRATG
HHHHHHHHHHHHHHC		18.1125367039
414PhosphorylationVYEELRATGAAAAEA
HHHHHHHHCHHHHHH		22.4036012601
492PhosphorylationYLQGWRKTLLIVSHD
HHHHHCCEEEEEECC		20.4428285833
497PhosphorylationRKTLLIVSHDQGFLD
CCEEEEEECCCCCHH		17.8528285833
507GlutathionylationQGFLDDVCTDIIHLD
CCCHHHHCCEEEECC		3.4924333276
543PhosphorylationQKELLKQYEKQEKKL
HHHHHHHHHHHHHHH		24.4127742792
587PhosphorylationRKNQDEESQEPPELL
HCCCCHHHCCCHHHH		37.48-
605PhosphorylationKEYTVRFTFPDPPPL
CEEEEEEECCCCCCC		24.5622942356
613PhosphorylationFPDPPPLSPPVLGLH
CCCCCCCCCCEEEEE		32.6926239621
623PhosphorylationVLGLHGVTFGYEGQK
EEEEECEEECCCCCC		18.8826643407
626PhosphorylationLHGVTFGYEGQKPLF
EECEEECCCCCCCCC		16.8226643407
657PhosphorylationGPNGVGKSTLLLLLT
CCCCCCHHHHHHHHH		20.5429138745
658PhosphorylationPNGVGKSTLLLLLTG
CCCCCHHHHHHHHHC		25.5522817900
668PhosphorylationLLLTGKLTPTNGEMR
HHHHCCCCCCCCCHH		31.3922817900
670PhosphorylationLTGKLTPTNGEMRKN
HHCCCCCCCCCHHHC		51.0922817900
733GlutathionylationHAHTIQICKLSGGQK
CCEEEEEEECCCCCE		1.7624333276
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
107SPhosphorylationKinaseCK2-FAMILY-GPS
107SPhosphorylationKinaseCK2-Uniprot
138SPhosphorylationKinaseCK2-FAMILY-GPS
138SPhosphorylationKinaseCK2-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
107SPhosphorylation

15345747
138SPhosphorylation

15345747
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 ABCF1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ABCF1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ABCF1_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-107 ANDSER-194, AND MASS SPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND SER-194, ANDMASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-138 ANDSER-194, AND MASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-107 ANDSER-138, AND MASS SPECTROMETRY.

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