Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Serotransferrin  

UniProtKB / Swiss-Prot ID :  TRFE_HUMAN

Gene Name (Synonyms) : 
TF PRO1400  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Secreted. 

Protein Function :  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 MRLAVGALLVCAVLGLCLAVPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRA...
Predicted Secondary Structure CCCHHHHHHHHHHHHHHHCCCCCEEEEEECCHHHHHHHHHHHHHHHHCCCCCCCEEEEECCCCHHHHHHH...
Protein Variant
LocationDescription
42R -> L (in dbSNP:rs41298293). VAR_034569
55S -> R (in dbSNP:rs8177318). VAR_029280
76A -> V (in dbSNP:rs41298977). VAR_034570
77D -> N (in ATRAF). VAR_038810
142G -> S (in dbSNP:rs1799830). VAR_011997
277G -> S (in allele TF*C3; associated witha reduction in total iron binding
296D -> G (in allele TF*D1;dbSNP:rs8177238).
319H -> R (in allele TF*CHI). VAR_007545
377W -> C (in dbSNP:rs1804498). VAR_011999
448I -> V (in dbSNP:rs2692696). VAR_058199
477A -> P (in ATRAF). VAR_012997
562G -> V (in dbSNP:rs41296590). VAR_034571
589P -> S (in allele TF*C2;dbSNP:rs1049296).
645T -> P (in dbSNP:rs1130537). VAR_012001
646K -> E (in allele TF*BV). VAR_012998
671G -> E (in allele TF*B2). VAR_012999
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
51O-linked (GalNAc...)./FTId=CAR_000073.SVIPSDGPS
HCCCCCCCE
44.04UniProtKB
Link
207PhosphotyrosineQYFGYSGAF
CCCCHHHHH
8.27Phosphositeplus
Link
359N6-acetyllysineTDECKPVKW
CCCCCCEEE
51.29Phosphositeplus
Link-
430N-linked (GlcNAc...)VLAENYNKS
EEEEEECCC
39.82SysPTM
Link-
432N-linked (Glc...)AENYNKSDN
EEEECCCCC
49.27HPRD
Link-
432N-linked (GlcNAc...)AENYNKSDN
EEEECCCCC
49.27SysPTM
Link-
432N-linked (GlcNAc...) (complex).AENYNKSDN
EEEECCCCC
49.27UniProtKB
Link-
533PhosphotyrosineNKEGYYGYT
CCCCCCCCH
8.53Phosphositeplus
Link-
536PhosphotyrosineGYYGYTGAF
CCCCCHHHH
5.96HPRD
Link-
536PhosphotyrosineGYYGYTGAF
CCCCCHHHH
5.96PhosphoELM
Link-
536PhosphotyrosineGYYGYTGAF
CCCCCHHHH
5.96Phosphositeplus
Link-
536Phosphotyrosine.GYYGYTGAF
CCCCCHHHH
5.96UniProtKB
Link-
630N-linked (Glc...)LFGSNVTDC
HHCCCCCCC
40.88HPRD
Link-
630N-linked (GlcNAc...)LFGSNVTDC
HHCCCCCCC
40.88SysPTM
Link-
630N-linked (GlcNAc...) (complex).LFGSNVTDC
HHCCCCCCC
40.88UniProtKB
Link-
666PhosphotyrosineDRNTYEKYL
CCCCHHHHC
17.61Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
Q9BV28_HUMANphysical interactionMINT-65349MINT16169070
APOA1_HUMANphysical interactionEBI-1221355
intact15174051
HEP2_HUMANphysical interactionEBI-1221355
intact15174051
RENT1_HUMANphysical interactionEBI-1221355
intact15174051
FINC_HUMANphysical interactionEBI-1221355
intact15174051
TTHY_HUMANphysical interactionEBI-1221355
intact15174051
IGHG1_HUMANphysical interactionEBI-1221355
intact15174051
KAC_HUMANphysical interactionEBI-1221355
intact15174051
K2C72_HUMANphysical interactionEBI-1221355
intact15174051
CATL1_HUMANphysical interactionEBI-1221355
intact15174051
RYR1_HUMANphysical interactionEBI-1221355
intact15174051
ALBU_HUMANphysical interactionEBI-1221355
intact15174051
KV201_HUMANphysical interactionEBI-1221355
intact15174051
SETX_HUMANphysical interactionEBI-1221355
intact15174051
CALR_HUMANin vivoHPRD:01811HPRD9312001
CALX_HUMANin vivoHPRD:01811HPRD9312001
IBP5_HUMANin vitroHPRD:01811HPRD11297622
IBP6_HUMANin vitroHPRD:01811HPRD11297622
IBP1_HUMANin vitroHPRD:01811HPRD11297622
IBP2_HUMANin vitroHPRD:01811HPRD11297622
IBP3_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:01811HPRD11749962
11297622
IBP4_HUMANin vitroHPRD:01811HPRD11297622
TBB3_HUMANyeast 2-hybridHPRD:01811HPRD16169070
TFR2_HUMANENSP00000264998STRING
IL2_HUMANENSP00000264998STRING
TBP_HUMANENSP00000264998STRING
TTHY_HUMANENSP00000264998STRING
TBPL2_HUMANENSP00000264998STRING
TBPL2_HUMANENSP00000264998STRING
INS_HUMANENSP00000264998STRING
INS_HUMANENSP00000264998STRING
S40A1_HUMANENSP00000264998STRING
CERU_HUMANENSP00000264998STRING
EGF_HUMANENSP00000264998STRING
HEMO_HUMANENSP00000264998STRING
PMM2_HUMANENSP00000264998STRING
RAB5A_HUMANENSP00000264998STRING
IBP3_HUMANENSP00000264998STRING
ALBU_HUMANENSP00000264998STRING
ALBU_HUMANENSP00000264998STRING
PRS6A_HUMANENSP00000264998STRING
HFE_HUMANENSP00000264998STRING
CALR_HUMANENSP00000264998STRING
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Disease Reference
Kegg disease
OMIM disease
209300Atransferrinemia (ATRAF)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
"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.
Phosphorylation
ReferencePubMed
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures