dbPTM

TRFE_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRFE_HUMAN	Jmol._Canvas2D (Jmol) "myJmol"[x]
UniProt AC	P02787
Protein Name	Serotransferrin
Gene Name	TF
Organism	Homo sapiens (Human).
Sequence Length	698
Subcellular Localization	Secreted.
Protein Description	Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation..
Protein Sequence	MRLAVGALLVCAVLGLCLAVPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEAPTDECKPVKWCALSHHERLKCDEWSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGKCGLVPVLAENYNKSDNCEDTPEAGYFAIAVVKKSASDLTWDNLKGKKSCHTAVGRTAGWNIPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYTGAFRCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTRKPVEEYANCHLARAPNHAVVTRKDKEACVHKILRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAKLHDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
36	Phosphorylation	AVSEHEATKCQSFRD EECCCHHHHCHHHHH	29.39	-
37	Acetylation	VSEHEATKCQSFRDH ECCCHHHHCHHHHHH	37.01	7679221
37	Malonylation	VSEHEATKCQSFRDH ECCCHHHHCHHHHHH	37.01	26320211
42	Methylation	ATKCQSFRDHMKSVI HHHCHHHHHHHHHCC	37.87	-
47	Phosphorylation	SFRDHMKSVIPSDGP HHHHHHHHCCCCCCC	20.08	21406692
51	Phosphorylation	HMKSVIPSDGPSVAC HHHHCCCCCCCCEEE	44.04	21406692
51	O-linked_Glycosylation	HMKSVIPSDGPSVAC HHHHCCCCCCCCEEE	44.04	UniProtKB CARBOHYD
55	Phosphorylation	VIPSDGPSVACVKKA CCCCCCCCEEEEEEH	28.07	21406692
58	S-nitrosylation	SDGPSVACVKKASYL CCCCCEEEEEEHHHH	4.29	25040305
61	Glycation	PSVACVKKASYLDCI CCEEEEEEHHHHHHH	23.36	-
63	Phosphorylation	VACVKKASYLDCIRA EEEEEEHHHHHHHHH	34.80	-
64	Phosphorylation	ACVKKASYLDCIRAI EEEEEHHHHHHHHHH	16.06	22817900
122	Malonylation	YAVAVVKKDSGFQMN EEEEEEECCCCCCCH	45.58	26320211
122	Glycation	YAVAVVKKDSGFQMN EEEEEEECCCCCCCH	45.58	-
136	Phosphorylation	NQLRGKKSCHTGLGR HHCCCCCCCCCCCCH	18.02	-
137	S-nitrosylation	QLRGKKSCHTGLGRS HCCCCCCCCCCCCHH	4.59	25040305
139	Phosphorylation	RGKKSCHTGLGRSAG CCCCCCCCCCCHHCC	38.13	-
144	Phosphorylation	CHTGLGRSAGWNIPI CCCCCCHHCCCCCCE	29.36	30087585
155	Phosphorylation	NIPIGLLYCDLPEPR CCCEEEEECCCCCCC	6.75	-
207	Phosphorylation	TLNQYFGYSGAFKCL HHHHHCCCCCHHHHH	8.27	21253578
213	S-nitrosylation	GYSGAFKCLKDGAGD CCCCHHHHHCCCCCC	4.63	25040305
215	Glycation	SGAFKCLKDGAGDVA CCHHHHHCCCCCCEE	64.68	-
225	Acetylation	AGDVAFVKHSTIFEN CCCEEEEECHHHHHH	25.94	27178108
225	Glycation	AGDVAFVKHSTIFEN CCCEEEEECHHHHHH	25.94	-
227	Phosphorylation	DVAFVKHSTIFENLA CEEEEECHHHHHHHC	19.92	28857561
246	S-nitrosylation	RDQYELLCLDNTRKP HHHHHEEEECCCCCC	7.58	25040305
257	Phosphorylation	TRKPVDEYKDCHLAQ CCCCCHHHCCCCCCC	13.99	-
258	Glycation	RKPVDEYKDCHLAQV CCCCHHHCCCCCCCC	52.40	-
260	S-nitrosylation	PVDEYKDCHLAQVPS CCHHHCCCCCCCCCC	2.18	25040305
297	Glycation	QEHFGKDKSKEFQLF HHHHCCCCCCCEEEC	67.90	-
298	Phosphorylation	EHFGKDKSKEFQLFS HHHCCCCCCCEEECC	47.77	24719451
299	Glycation	HFGKDKSKEFQLFSS HHCCCCCCCEEECCC	69.18	-
305	Phosphorylation	SKEFQLFSSPHGKDL CCCEEECCCCCCCCC	52.10	24719451
306	Phosphorylation	KEFQLFSSPHGKDLL CCEEECCCCCCCCCE	17.37	24719451
310	Malonylation	LFSSPHGKDLLFKDS ECCCCCCCCCEECCC	42.01	26320211
315	Glycation	HGKDLLFKDSAHGFL CCCCCEECCCCCCCC	51.23	-
336	Nitration	DAKMYLGYEYVTAIR CCHHCCCHHHHHHHH	11.07	-
340	Phosphorylation	YLGYEYVTAIRNLRE CCCHHHHHHHHHHCC	18.57	-
349	Phosphorylation	IRNLREGTCPEAPTD HHHHCCCCCCCCCCC	21.82	-
355	Phosphorylation	GTCPEAPTDECKPVK CCCCCCCCCCCCCCC	52.02	-
355	O-linked_Glycosylation	GTCPEAPTDECKPVK CCCCCCCCCCCCCCC	52.02	OGP
359	Acetylation	EAPTDECKPVKWCAL CCCCCCCCCCCEECC	51.29	20167786
364	S-nitrosylation	ECKPVKWCALSHHER CCCCCCEECCCCCHH	1.95	25040305
373	Malonylation	LSHHERLKCDEWSVN CCCCHHCCCCCCCCC	45.95	26320211
374	S-nitrosylation	SHHERLKCDEWSVNS CCCHHCCCCCCCCCC	7.30	25040305
389	Phosphorylation	VGKIECVSAETTEDC CCEEEEEECCCHHHH	31.85	28270605
392	Phosphorylation	IECVSAETTEDCIAK EEEEECCCHHHHHHH	34.89	28270605
393	Phosphorylation	ECVSAETTEDCIAKI EEEECCCHHHHHHHH	22.72	28270605
396	S-nitrosylation	SAETTEDCIAKIMNG ECCCHHHHHHHHHCC	2.37	25040305
409	O-linked_Glycosylation	NGEADAMSLDGGFVY CCCCCEEECCCCEEE	25.65	OGP
430	N-linked_Glycosylation	LVPVLAENYNKSDNC CHHHHHCCCCCCCCC	39.82	18514042
432	N-linked_Glycosylation	PVLAENYNKSDNCED HHHHCCCCCCCCCCC	49.27	15084671
432	N-linked_Glycosylation	PVLAENYNKSDNCED HHHHCCCCCCCCCCC	49.27	15084671
453	Acetylation	FAIAVVKKSASDLTW EEEEEEECCHHHCCC	39.38	27178108
454	Phosphorylation	AIAVVKKSASDLTWD EEEEEECCHHHCCCC	27.56	24275569
456	Phosphorylation	AVVKKSASDLTWDNL EEEECCHHHCCCCCC	40.00	29507054
468	Phosphorylation	DNLKGKKSCHTAVGR CCCCCCCCCCCCCCH	18.02	-
476	Phosphorylation	CHTAVGRTAGWNIPM CCCCCCHHHCCCCCH	24.48	-
487	Phosphorylation	NIPMGLLYNKINHCR CCCHHHHHCCCCCCC	21.32	30631047
491	N-linked_Glycosylation	GLLYNKINHCRFDEF HHHHCCCCCCCHHHH	29.80	15536627
503	S-nitrosylation	DEFFSEGCAPGSKKD HHHHCCCCCCCCCCC	3.47	25040305
508	Acetylation	EGCAPGSKKDSSLCK CCCCCCCCCCCHHHH	67.52	7668159
520	Phosphorylation	LCKLCMGSGLNLCEP HHHHHCCCCCCCCCC	17.14	27251275
525	S-nitrosylation	MGSGLNLCEPNNKEG CCCCCCCCCCCCCCC	8.76	25040305
533	Phosphorylation	EPNNKEGYYGYTGAF CCCCCCCCCCCCCEE	8.53	21253578
534	Phosphorylation	PNNKEGYYGYTGAFR CCCCCCCCCCCCEEE	17.95	27251275
534	Nitration	PNNKEGYYGYTGAFR CCCCCCCCCCCCEEE	17.95	-
536	Phosphorylation	NKEGYYGYTGAFRCL CCCCCCCCCCEEEEE	5.96	27273156
537	Phosphorylation	KEGYYGYTGAFRCLV CCCCCCCCCEEEEEE	20.05	27130503
546	Acetylation	AFRCLVEKGDVAFVK EEEEEEECCCEEEEE	53.59	26051181
553	Acetylation	KGDVAFVKHQTVPQN CCCEEEEEECCCCCC	24.44	27178108
553	Malonylation	KGDVAFVKHQTVPQN CCCEEEEEECCCCCC	24.44	26320211
553	Glycation	KGDVAFVKHQTVPQN CCCEEEEEECCCCCC	24.44	-
571	Acetylation	KNPDPWAKNLNEKDY CCCCHHHHCCCHHCE	59.09	27178108
582	S-nitrosylation	EKDYELLCLDGTRKP HHCEEEEEECCCCCC	5.21	25040305
593	Phosphorylation	TRKPVEEYANCHLAR CCCCHHHHHCCHHCC	6.93	-
596	S-nitrosylation	PVEEYANCHLARAPN CHHHHHCCHHCCCCC	1.80	25040305
630	N-linked_Glycosylation	QQHLFGSNVTDCSGN CHHHHCCCCCCCCCC	40.88	15084671
630	N-linked_Glycosylation	QQHLFGSNVTDCSGN CHHHHCCCCCCCCCC	40.88	15084671
643	Phosphorylation	GNFCLFRSETKDLLF CCEEEEECCCCCEEC	42.14	24275569
645	Phosphorylation	FCLFRSETKDLLFRD EEEEECCCCCEECCC	30.98	23312004
646	Acetylation	CLFRSETKDLLFRDD EEEECCCCCEECCCC	42.18	27178108
654	Phosphorylation	DLLFRDDTVCLAKLH CEECCCCEEEEEECC	19.87	-
659	Malonylation	DDTVCLAKLHDRNTY CCEEEEEECCCCCHH	33.15	26320211
659	Acetylation	DDTVCLAKLHDRNTY CCEEEEEECCCCCHH	33.15	27178108
659	Glycation	DDTVCLAKLHDRNTY CCEEEEEECCCCCHH	33.15	-
666	Phosphorylation	KLHDRNTYEKYLGEE ECCCCCHHHHHCCHH	17.61	22817900
668	Acetylation	HDRNTYEKYLGEEYV CCCCHHHHHCCHHHH	35.05	27178108
668	Glycation	HDRNTYEKYLGEEYV CCCCHHHHHCCHHHH	35.05	-
669	Phosphorylation	DRNTYEKYLGEEYVK CCCHHHHHCCHHHHH	14.17	-
674	Phosphorylation	EKYLGEEYVKAVGNL HHHCCHHHHHHHCCH	11.71	-
676	Glycation	YLGEEYVKAVGNLRK HCCHHHHHHHCCHHH	36.13	-
683	Glycation	KAVGNLRKCSTSSLL HHHCCHHHCCHHHHH	35.39	-
683	Malonylation	KAVGNLRKCSTSSLL HHHCCHHHCCHHHHH	35.39	26320211
684	S-nitrosylation	AVGNLRKCSTSSLLE HHCCHHHCCHHHHHH	4.30	25040305
685	Phosphorylation	VGNLRKCSTSSLLEA HCCHHHCCHHHHHHH	34.07	9272172
686	Phosphorylation	GNLRKCSTSSLLEAC CCHHHCCHHHHHHHH	31.63	29116813
687	Phosphorylation	NLRKCSTSSLLEACT CHHHCCHHHHHHHHH	11.60	29116813
688	Phosphorylation	LRKCSTSSLLEACTF HHHCCHHHHHHHHHC	36.74	23312004
694	Phosphorylation	SSLLEACTFRRP--- HHHHHHHHCCCC---	27.50	-

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
389	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
685	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TRFE_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
58	S-nitrosylation	55 (3)	S ⇒ R	rs8177318	Mean corpuscular hemoglobin concentration Mean corpuscular volume	27863252
63	Phosphorylation	55 (8)	S ⇒ R	rs8177318	Mean corpuscular hemoglobin concentration Mean corpuscular volume	27863252
64	Phosphorylation	55 (9)	S ⇒ R	rs8177318	Mean corpuscular hemoglobin concentration Mean corpuscular volume	27863252
340	Phosphorylation	343 (3)	R ⇒ W	rs150854910	Mean corpuscular volume	27863252
349	Phosphorylation	343 (6)	R ⇒ W	rs150854910	Mean corpuscular volume	27863252
582	S-nitrosylation	589 (7)	P ⇒ S	rs1049296	Alcohol consumption (transferrin glycosylation)	21665994
593	Phosphorylation	589 (4)	P ⇒ S	rs1049296	Alcohol consumption (transferrin glycosylation)	21665994
596	S-nitrosylation	589 (7)	P ⇒ S	rs1049296	Alcohol consumption (transferrin glycosylation)	21665994

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IGF1_HUMAN	IGF1	physical	11749962
IGF2_HUMAN	IGF2	physical	11749962
TIM_HUMAN	TIMELESS	physical	21988832

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
209300	Atransferrinemia (ATRAF)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TRFE_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Enrichment of glycopeptides for glycan structure and attachment siteidentification."; Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,Brinkmalm G., Larson G.; Nat. Methods 6:809-811(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630, STRUCTUREOF CARBOHYDRATES, AND MASS SPECTROMETRY.	19838169 [Abstract]
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry."; Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.; J. Proteome Res. 5:1493-1503(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-630, AND MASSSPECTROMETRY.	16740002 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630, AND MASSSPECTROMETRY.	16335952 [Abstract]
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry."; Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; Proteomics 4:454-465(2004). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630, AND MASSSPECTROMETRY.	14760718 [Abstract]
"A proteomic analysis of human bile."; Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; Mol. Cell. Proteomics 3:715-728(2004). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630, AND MASSSPECTROMETRY.	15084671 [Abstract]
Phosphorylation
Reference	PubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-536, AND MASSSPECTROMETRY.	18083107 [Abstract]