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AFP (human)

Overview AFP Binds copper, nickel, and fatty acids as well as, and bilirubin less well than, serum albumin. Only a small percentage (less than 2%) of the human AFP shows estrogen-binding properties. Dimeric and trimeric forms have been found in addition to the monomeric form. Plasma. Synthesized by the fetal liver and yolk sac. Belongs to the ALB/AFP/VDB family. Note: This description may include information from UniProtKB. Protein type: Secreted, signal peptide; Secreted Cellular Component: extracellular space; cytoplasm Molecular Function: metal ion binding Biological Process: response to organic substance; organ regeneration; transport; pancreas development; progesterone metabolic process; liver development; ovulation from ovarian follicle Reference #:  P02771 (UniProtKB) Alt. Names/Synonyms: AFP; Alpha-1-fetoprotein; Alpha-fetoglobulin; Alpha-fetoprotein; FETA; HPAFP Gene Symbols: AFP Molecular weight: 68,678 Da Basal Isoelectric point: 5.48  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below AFP 3MRK - P=137-145 (human)

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	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		Y164	TFMNKFIYEIARRHP
0	1		T248-p	TKLSQKFtKVNFTEI
0	5		S368-p	RHPQLAVsVILRVAK
0	5		K413-a	QESQALAkRsCGLFQ
0	2		S415-p	SQALAkRsCGLFQKL

	mouse
Y160-p	VFMNRFIyEVSRRNP
T244	IKLSQKLTEANFTEI
S364	THPNLPVSVILRIAK
K409	EESQALSKQSCALYQ
S411	SQALSKQSCALYQTL

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