dbPTM

ABCF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ABCF1_HUMAN
UniProt AC	Q8NE71
Protein Name	ATP-binding cassette sub-family F member 1
Gene Name	ABCF1
Organism	Homo sapiens (Human).
Sequence Length	845
Subcellular Localization	Isoform 2: Cytoplasm . Nucleus, nucleoplasm . Nucleus envelope .
Protein Description	Isoform 2 is required for efficient Cap- and IRES-mediated mRNA translation initiation. Isoform 2 is not involved in the ribosome biogenesis..
Protein Sequence	MPKAPKQQPPEPEWIGDGESTSPSDKVVKKGKKDKKIKKTFFEELAVEDKQAGEEEKVLKEKEQQQQQQQQQQKKKRDTRKGRRKKDVDDDGEEKELMERLKKLSVPTSDEEDEVPAPKPRGGKKTKGGNVFAALIQDQSEEEEEEEKHPPKPAKPEKNRINKAVSEEQQPALKGKKGKEEKSKGKAKPQNKFAALDNEEEDKEEEIIKEKEPPKQGKEKAKKAEQGSEEEGEGEEEEEEGGESKADDPYAHLSKKEKKKLKKQMEYERQVASLKAANAAENDFSVSQAEMSSRQAMLENASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLKLLEEERRLQGQLEQGDDTAAERLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKELKAGGKSTKQAEKQTKEALTRKQQKCRRKNQDEESQEAPELLKRPKEYTVRFTFPDPPPLSPPVLGLHGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLKIGFFNQQYAEQLRMEETPTEYLQRGFNLPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDARLITETNCQLWVVEEQSVSQIDGDFEDYKREVLEALGEVMVSRPRE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Ubiquitination	--MPKAPKQQPPEPE --CCCCCCCCCCCCC	67.44	-
20	Phosphorylation	EWIGDGESTSPSDKV CCCCCCCCCCHHHHH	39.45	22167270
21	Phosphorylation	WIGDGESTSPSDKVV CCCCCCCCCHHHHHH	40.11	22167270
22	Phosphorylation	IGDGESTSPSDKVVK CCCCCCCCHHHHHHH	31.52	19664994
24	Phosphorylation	DGESTSPSDKVVKKG CCCCCCHHHHHHHCC	50.24	22167270
26	Ubiquitination	ESTSPSDKVVKKGKK CCCCHHHHHHHCCCC	53.95	-
39	Ubiquitination	KKDKKIKKTFFEELA CCCHHHHHHHHHHHH	54.78	21890473
39	Ubiquitination	KKDKKIKKTFFEELA CCCHHHHHHHHHHHH	54.78	21890473
39 (in isoform 1)	Ubiquitination	-	54.78	21890473
39 (in isoform 2)	Ubiquitination	-	54.78	21890473
50	Acetylation	EELAVEDKQAGEEEK HHHHHHCHHCCHHHH	28.66	26051181
50	Ubiquitination	EELAVEDKQAGEEEK HHHHHHCHHCCHHHH	28.66	-
79	Phosphorylation	QQKKKRDTRKGRRKK HHHHHHHHHHHCCCC	38.01	26657352
95	Acetylation	VDDDGEEKELMERLK CCCCHHHHHHHHHHH	52.42	26051181
98	Sulfoxidation	DGEEKELMERLKKLS CHHHHHHHHHHHHCC	2.71	21406390
105	Phosphorylation	MERLKKLSVPTSDEE HHHHHHCCCCCCCCC	34.62	29255136
108	Phosphorylation	LKKLSVPTSDEEDEV HHHCCCCCCCCCCCC	46.80	29255136
109	Phosphorylation	KKLSVPTSDEEDEVP HHCCCCCCCCCCCCC	36.63	19664994
140	Phosphorylation	AALIQDQSEEEEEEE EHEECCCCHHHHHHH	56.09	29255136
163	Acetylation	PEKNRINKAVSEEQQ CCCCCHHHHCCHHHH	48.03	7613249
163	Methylation	PEKNRINKAVSEEQQ CCCCCHHHHCCHHHH	48.03	-
166	Phosphorylation	NRINKAVSEEQQPAL CCHHHHCCHHHHHHH	40.03	23401153
174	Acetylation	EEQQPALKGKKGKEE HHHHHHHCCCCCHHH	71.44	26051181
174	Methylation	EEQQPALKGKKGKEE HHHHHHHCCCCCHHH	71.44	-
174	Ubiquitination	EEQQPALKGKKGKEE HHHHHHHCCCCCHHH	71.44	-
176	Methylation	QQPALKGKKGKEEKS HHHHHCCCCCHHHHC	57.68	-
209	Ubiquitination	DKEEEIIKEKEPPKQ HHHHHHHHHCCCCCC	69.28	-
228	Phosphorylation	AKKAEQGSEEEGEGE HHHHHHCCCCCCCCH	41.34	22167270
237 (in isoform 2)	Ubiquitination	-	67.42	21890473
244	Phosphorylation	EEEEGGESKADDPYA HHHCCCCCCCCCHHH	36.10	22167270
250	Phosphorylation	ESKADDPYAHLSKKE CCCCCCHHHCCCHHH	17.41	23927012
254	Phosphorylation	DDPYAHLSKKEKKKL CCHHHCCCHHHHHHH	31.64	23927012
255	Ubiquitination	DPYAHLSKKEKKKLK CHHHCCCHHHHHHHH	71.90	-
263	Ubiquitination	KEKKKLKKQMEYERQ HHHHHHHHHHHHHHH	66.37	-
267	Phosphorylation	KLKKQMEYERQVASL HHHHHHHHHHHHHHH	15.86	19664994
273	Phosphorylation	EYERQVASLKAANAA HHHHHHHHHHHHHHH	31.39	46156889
275	Methylation	ERQVASLKAANAAEN HHHHHHHHHHHHHHC	42.85	-
275	Ubiquitination	ERQVASLKAANAAEN HHHHHHHHHHHHHHC	42.85	21906983
275 (in isoform 1)	Ubiquitination	-	42.85	21890473
285	Phosphorylation	NAAENDFSVSQAEMS HHHHCCCCHHHHHHH	24.59	24719451
287	Phosphorylation	AENDFSVSQAEMSSR HHCCCCHHHHHHHHH	23.60	21815630
291	Sulfoxidation	FSVSQAEMSSRQAML CCHHHHHHHHHHHHH	5.03	21406390
292	Phosphorylation	SVSQAEMSSRQAMLE CHHHHHHHHHHHHHH	17.55	24532841
293	Phosphorylation	VSQAEMSSRQAMLEN HHHHHHHHHHHHHHC	27.40	21815630
297	Sulfoxidation	EMSSRQAMLENASDI HHHHHHHHHHCHHCC	3.50	21406390
305	Acetylation	LENASDIKLEKFSIS HHCHHCCCCEEEEEE	56.43	26051181
305	Ubiquitination	LENASDIKLEKFSIS HHCHHCCCCEEEEEE	56.43	-
308	Ubiquitination	ASDIKLEKFSISAHG HHCCCCEEEEEECCC	55.64	-
332	Phosphorylation	YIVAGRRYGLVGPNG EEEECCCCCCCCCCC	17.28	51457443
343	Phosphorylation	GPNGKGKTTLLKHIA CCCCCCHHHHHHHHH	31.20	46156901
344	Phosphorylation	PNGKGKTTLLKHIAN CCCCCHHHHHHHHHH	33.31	46156907
347	Acetylation	KGKTTLLKHIANRAL CCHHHHHHHHHHHHH	35.76	25953088
347	Malonylation	KGKTTLLKHIANRAL CCHHHHHHHHHHHHH	35.76	26320211
347	Ubiquitination	KGKTTLLKHIANRAL CCHHHHHHHHHHHHH	35.76	-
389	Ubiquitination	RADTKRLKLLEEERR HHCHHHHHHHHHHHH	55.87	-
407	Phosphorylation	QLEQGDDTAAERLEK HHHCCCHHHHHHHHH	32.29	46156913
413 (in isoform 2)	Ubiquitination	-	46.85	21890473
414	Ubiquitination	TAAERLEKVYEELRA HHHHHHHHHHHHHHH	55.50	-
416	Phosphorylation	AERLEKVYEELRATG HHHHHHHHHHHHHHC	18.11	28796482
422	Phosphorylation	VYEELRATGAAAAEA HHHHHHHHCHHHHHH	22.40	20068231
430	2-Hydroxyisobutyrylation	GAAAAEAKARRILAG CHHHHHHHHHHHHHH	33.65	-
430	Ubiquitination	GAAAAEAKARRILAG CHHHHHHHHHHHHHH	33.65	-
451	Ubiquitination	MQNRPTQKFSGGWRM HCCCCCCCCCCCHHH	43.93	21890473
451	Acetylation	MQNRPTQKFSGGWRM HCCCCCCCCCCCHHH	43.93	26051181
451	Ubiquitination	MQNRPTQKFSGGWRM HCCCCCCCCCCCHHH	43.93	21890473
451 (in isoform 1)	Ubiquitination	-	43.93	21890473
453	Phosphorylation	NRPTQKFSGGWRMRV CCCCCCCCCCHHHHH	43.35	26270265
533	Phosphorylation	LHYYRGNYMTFKKMY HHHHHCCHHHHHHHH	10.60	26657352
537	Methylation	RGNYMTFKKMYQQKQ HCCHHHHHHHHHHHH	27.71	-
540	Phosphorylation	YMTFKKMYQQKQKEL HHHHHHHHHHHHHHH	19.37	26074081
549	Ubiquitination	QKQKELLKQYEKQEK HHHHHHHHHHHHHHH	64.56	-
551	Phosphorylation	QKELLKQYEKQEKKL HHHHHHHHHHHHHHH	24.41	46156919
573	Ubiquitination	KSTKQAEKQTKEALT HHHHHHHHHHHHHHH	67.30	17370265
576	Ubiquitination	KQAEKQTKEALTRKQ HHHHHHHHHHHHHHH	38.20	-
580	Phosphorylation	KQTKEALTRKQQKCR HHHHHHHHHHHHHHH	42.75	20071362
582	Ubiquitination	TKEALTRKQQKCRRK HHHHHHHHHHHHHHC	52.42	17370265
589	Acetylation	KQQKCRRKNQDEESQ HHHHHHHCCCCHHHH	39.34	26051181
589	Ubiquitination	KQQKCRRKNQDEESQ HHHHHHHCCCCHHHH	39.34	-
595	Phosphorylation	RKNQDEESQEAPELL HCCCCHHHHHHHHHH	31.13	23401153
603	Malonylation	QEAPELLKRPKEYTV HHHHHHHHCCCEEEE	78.32	26320211
603	Ubiquitination	QEAPELLKRPKEYTV HHHHHHHHCCCEEEE	78.32	-
613	Phosphorylation	KEYTVRFTFPDPPPL CEEEEEEECCCCCCC	24.56	29255136
621	Phosphorylation	FPDPPPLSPPVLGLH CCCCCCCCCCEEEEE	32.69	29255136
631	Phosphorylation	VLGLHGVTFGYQGQK EEEEECEEECCCCCC	18.88	27732954
634	Phosphorylation	LHGVTFGYQGQKPLF EECEEECCCCCCCCC	12.79	27732954
650	Sulfoxidation	NLDFGIDMDSRICIV CCCCCCCCCCCEEEE	4.81	21406390
651 (in isoform 2)	Ubiquitination	-	30.89	21890473
652	Phosphorylation	DFGIDMDSRICIVGP CCCCCCCCCEEEECC	19.53	46156895
665	Phosphorylation	GPNGVGKSTLLLLLT CCCCCCHHHHHHHHH	20.54	22496350
666	Phosphorylation	PNGVGKSTLLLLLTG CCCCCHHHHHHHHHC	25.55	21406692
672	Phosphorylation	STLLLLLTGKLTPTH HHHHHHHHCCCCCCC	32.04	21406692
676	Phosphorylation	LLLTGKLTPTHGEMR HHHHCCCCCCCCHHH	29.63	20068231
678	Phosphorylation	LTGKLTPTHGEMRKN HHCCCCCCCCHHHHC	36.96	20068231
682	Sulfoxidation	LTPTHGEMRKNHRLK CCCCCCHHHHCCEEE	9.77	30846556
689	Ubiquitination	MRKNHRLKIGFFNQQ HHHCCEEEEEEECHH	40.51	21890473
689	Ubiquitination	MRKNHRLKIGFFNQQ HHHCCEEEEEEECHH	40.51	21890473
689 (in isoform 1)	Ubiquitination	-	40.51	21890473
697	Phosphorylation	IGFFNQQYAEQLRME EEEECHHHHHHHCCC	11.44	28152594
703	Sulfoxidation	QYAEQLRMEETPTEY HHHHHHCCCCCHHHH	8.09	30846556
710	Phosphorylation	MEETPTEYLQRGFNL CCCCHHHHHHHCCCC	15.60	110754775
733	Phosphorylation	LGRFGLESHAHTIQI HHHCCCCCCCEEEEE	30.89	20068231
742	Acetylation	AHTIQICKLSGGQKA CEEEEEEECCCCCEE	47.52	26051181
748	2-Hydroxyisobutyrylation	CKLSGGQKARVVFAE EECCCCCEEEEEEEE	41.24	-
748	Ubiquitination	CKLSGGQKARVVFAE EECCCCCEEEEEEEE	41.24	-

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
109	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
109	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
109	S	Phosphorylation	Kinase	CK2	-	Uniprot
140	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
140	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
140	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
109	S	Phosphorylation	17081983
Isoform 2 phosphorylation on Ser-109 and Ser-140 by CK2 inhibits association of EIF2 with ribosomes.
140	S	Phosphorylation	17081983
Isoform 2 phosphorylation on Ser-109 and Ser-140 by CK2 inhibits association of EIF2 with ribosomes.

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
DHX9_HUMAN	DHX9	physical	22863883
DC1I2_HUMAN	DYNC1I2	physical	22863883
ROA0_HUMAN	HNRNPA0	physical	22863883
ROA2_HUMAN	HNRNPA2B1	physical	22863883
HNRPM_HUMAN	HNRNPM	physical	22863883
HNRPU_HUMAN	HNRNPU	physical	22863883
IF2B3_HUMAN	IGF2BP3	physical	22863883
ILF2_HUMAN	ILF2	physical	22863883
MTAP2_HUMAN	MAP2	physical	22863883
MRE11_HUMAN	MRE11A	physical	22863883
NMT1_HUMAN	NMT1	physical	22863883
PRS8_HUMAN	PSMC5	physical	22863883
PRS10_HUMAN	PSMC6	physical	22863883
PSD13_HUMAN	PSMD13	physical	22863883
PSMD7_HUMAN	PSMD7	physical	22863883
PSMD8_HUMAN	PSMD8	physical	22863883
PTBP1_HUMAN	PTBP1	physical	22863883
RL27A_HUMAN	RPL27A	physical	22863883
TBL1R_HUMAN	TBL1XR1	physical	22863883
FTM_HUMAN	RPGRIP1L	physical	27173435

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 ABCF1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108; SER-109; SER-140;SER-166 AND SER-228, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-24; THR-108;SER-109 AND SER-140, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-228, ANDMASS SPECTROMETRY.	18318008 [Abstract]
"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-24; SER-105; THR-108;SER-109; SER-140; SER-166 AND SER-228, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASSSPECTROMETRY.	18088087 [Abstract]
"The N-terminal region of ABC50 interacts with eukaryotic initiationfactor eIF2 and is a target for regulatory phosphorylation by CK2."; Paytubi S., Morrice N.A., Boudeau J., Proud C.G.; Biochem. J. 409:223-231(2008). Cited for: INTERACTION WITH EIF2S1, ASSOCIATION WITH RIBOSOMES, PHOSPHORYLATIONAT SER-109 AND SER-140, PHOSPHORYLATION, MASS SPECTROMETRY, ANDMUTAGENESIS OF SER-109 AND SER-140.	17894550 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108 AND SER-109, ANDMASS SPECTROMETRY.	18187866 [Abstract]
"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-595, AND MASSSPECTROMETRY.	17525332 [Abstract]
"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-140 AND SER-228, ANDMASS SPECTROMETRY.	17287340 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; THR-108; SER-109;SER-140 AND SER-228, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; THR-108 ANDSER-109, AND MASS SPECTROMETRY.	16083285 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108 AND SER-109, ANDMASS SPECTROMETRY.	15302935 [Abstract]
Ubiquitylation
Reference	PubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry."; Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; Proteomics 7:868-874(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-573 AND LYS-582, AND MASSSPECTROMETRY.	17370265 [Abstract]

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