AFAM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AFAM_HUMAN
• UniProt AC: P43652
• Protein Name: Afamin
• Gene Name: AFM
• Organism: Homo sapiens (Human).
• Sequence Length: 599
• Subcellular Localization: Secreted .
• Protein Description: Functions as carrier for hydrophobic molecules in body fluids (Probable). Essential for the solubility and activity of lipidated Wnt family members, including WNT1, WNT2B, WNT3, WNT3A, WNT5A, WNT7A, WNT7B, WNT8, WNT9A, WNT9B, WNT10A and WNT10B. [PubMed: 26902720 Binds vitamin E]
• Protein Sequence: MKLLKLTGFIFFLFFLTESLTLPTQPRDIENFNSTQKFIEDNIEYITIIAFAQYVQEATFEEMEKLVKDMVEYKDRCMADKTLPECSKLPNNVLQEKICAMEGLPQKHNFSHCCSKVDAQRRLCFFYNKKSDVGFLPPFPTLDPEEKCQAYESNRESLLNHFLYEVARRNPFVFAPTLLTVAVHFEEVAKSCCEEQNKVNCLQTRAIPVTQYLKAFSSYQKHVCGALLKFGTKVVHFIYIAILSQKFPKIEFKELISLVEDVSSNYDGCCEGDVVQCIRDTSKVMNHICSKQDSISSKIKECCEKKIPERGQCIINSNKDDRPKDLSLREGKFTDSENVCQERDADPDTFFAKFTFEYSRRHPDLSIPELLRIVQIYKDLLRNCCNTENPPGCYRYAEDKFNETTEKSLKMVQQECKHFQNLGKDGLKYHYLIRLTKIAPQLSTEELVSLGEKMVTAFTTCCTLSEEFACVDNLADLVFGELCGVNENRTINPAVDHCCKTNFAFRRPCFESLKADKTYVPPPFSQDLFTFHADMCQSQNEELQRKTDRFLVNLVKLKHELTDEELQSLFTNFANVVDKCCKAESPEVCFNEESPKIGN

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
33	N-linked_Glycosylation	PRDIENFNSTQKFIE CCCCCCCCHHHHHHH	56.58	18638581
33	N-linked_Glycosylation	PRDIENFNSTQKFIE CCCCCCCCHHHHHHH	56.58	17623646
109	N-linked_Glycosylation	EGLPQKHNFSHCCSK CCCCCCCCCCHHCCH	47.34	19838169
141	O-linked_Glycosylation	GFLPPFPTLDPEEKC CCCCCCCCCCHHHHH	44.14	OGP
212	Phosphorylation	RAIPVTQYLKAFSSY CCCCHHHHHHHHHHH	10.78	7280931
219	Phosphorylation	YLKAFSSYQKHVCGA HHHHHHHHHHHHHHH	22.00	7280943
246	Acetylation	YIAILSQKFPKIEFK HHHHHCCCCCCCCHH	61.33	30586615
294	Phosphorylation	HICSKQDSISSKIKE HHHHCCHHHHHHHHH	23.13	22210691
317	Phosphorylation	RGQCIINSNKDDRPK CCCEEECCCCCCCCC	34.54	46156023
327	Phosphorylation	DDRPKDLSLREGKFT CCCCCCCCCCCCCCC	35.20	24719451
332	Glycation	DLSLREGKFTDSENV CCCCCCCCCCCCCCH	40.10	-
366	Phosphorylation	SRRHPDLSIPELLRI HHHCCCCCHHHHHHH	43.40	24114839
383	N-linked_Glycosylation	IYKDLLRNCCNTENP HHHHHHHHHCCCCCC	34.36	17623646
383	N-linked_Glycosylation	IYKDLLRNCCNTENP HHHHHHHHHCCCCCC	34.36	19838169
402	N-linked_Glycosylation	RYAEDKFNETTEKSL HHHHHHCCHHHHHHH	51.99	26902720
402	N-linked_Glycosylation	RYAEDKFNETTEKSL HHHHHHCCHHHHHHH	51.99	18638581
488	N-linked_Glycosylation	ELCGVNENRTINPAV HHCCCCCCCCCCHHH	40.99	16335952

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of AFAM_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AFAM_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
402	N-linked Glycosylation	395 (7)	R ⇒ H	rs41265665	Blood protein levels	28240269
402	N-linked Glycosylation	395 (7)	R ⇒ H	rs41265665	Blood protein levels	28240269

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
POTEI_HUMAN	POTEI	physical	28514442
GBP1_HUMAN	GBP1	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
ACTA_HUMAN	ACTA2	physical	28514442

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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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-109; ASN-383 AND ASN-402,STRUCTURE OF CARBOHYDRATES, AND MASS SPECTROMETRY.
PubMed: 19838169

"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-33 AND ASN-402, AND MASSSPECTROMETRY.
PubMed: 19159218

"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-33, AND MASS SPECTROMETRY.
PubMed: 16740002

"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-33; ASN-402 AND ASN-488,AND MASS SPECTROMETRY.
PubMed: 16335952

"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-402, AND MASSSPECTROMETRY.
PubMed: 14760718