dbPTM

APOH_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	APOH_HUMAN
UniProt AC	P02749
Protein Name	Beta-2-glycoprotein 1
Gene Name	APOH
Organism	Homo sapiens (Human).
Sequence Length	345
Subcellular Localization	Secreted.
Protein Description	Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells..
Protein Sequence	MISPVLILFSSFLCHVAIAGRTCPKPDDLPFSTVVPLKTFYEPGEEITYSCKPGYVSRGGMRKFICPLTGLWPINTLKCTPRVCPFAGILENGAVRYTTFEYPNTISFSCNTGFYLNGADSAKCTEEGKWSPELPVCAPIICPPPSIPTFATLRVYKPSAGNNSLYRDTAVFECLPQHAMFGNDTITCTTHGNWTKLPECREVKCPFPSRPDNGFVNYPAKPTLYYKDKATFGCHDGYSLDGPEEIECTKLGNWSAMPSCKASCKVPVKKATVVYQGERVKIQEKFKNGMLHGDKVSFFCKNKEKKCSYTEDAQCIDGTIEVPKCFKEHSSLAFWKTDASDVKPC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
32	O-linked_Glycosylation	KPDDLPFSTVVPLKT CCCCCCCCEEEEECE	20.53	OGP
33	O-linked_Glycosylation	PDDLPFSTVVPLKTF CCCCCCCEEEEECEE	26.38	UniProtKB CARBOHYD
39	Phosphorylation	STVVPLKTFYEPGEE CEEEEECEEECCCCC	38.85	28258704
48	Phosphorylation	YEPGEEITYSCKPGY ECCCCCEEEEECCCE	16.80	28258704
55	Phosphorylation	TYSCKPGYVSRGGMR EEEECCCEECCCCCC	12.09	23909892
57	Phosphorylation	SCKPGYVSRGGMRKF EECCCEECCCCCCEE	19.41	23909892
125	Phosphorylation	GADSAKCTEEGKWSP CCCCCCCCCCCCCCC	36.04	27251275
131	Phosphorylation	CTEEGKWSPELPVCA CCCCCCCCCCCCEEE	16.39	27251275
149	O-linked_Glycosylation	CPPPSIPTFATLRVY CCCCCCCCEEEEEEE	25.00	9155091
162	N-linked_Glycosylation	VYKPSAGNNSLYRDT EECCCCCCCCCCCCE	34.33	15084671
162	N-linked_Glycosylation	VYKPSAGNNSLYRDT EECCCCCCCCCCCCE	34.33	15084671
183	N-linked_Glycosylation	PQHAMFGNDTITCTT CCHHCCCCCEEEEEC	31.80	18638581
183	N-linked_Glycosylation	PQHAMFGNDTITCTT CCHHCCCCCEEEEEC	31.80	6587378
193	N-linked_Glycosylation	ITCTTHGNWTKLPEC EEEECCCCCCCCCCC	35.32	6587378
193	N-linked_Glycosylation	ITCTTHGNWTKLPEC EEEECCCCCCCCCCC	35.32	18638581
253	N-linked_Glycosylation	IECTKLGNWSAMPSC EEEEECCCCCCCCCC	39.71	15084671
253	N-linked_Glycosylation	IECTKLGNWSAMPSC EEEEECCCCCCCCCC	39.71	15084671
272	Phosphorylation	KVPVKKATVVYQGER CCCCCEEEEEECCCE	21.27	26091039
272	O-linked_Glycosylation	KVPVKKATVVYQGER CCCCCEEEEEECCCE	21.27	OGP
300	S-nitrosylation	GDKVSFFCKNKEKKC CCEEEEEECCCCCCC	4.47	24105792
301	Methylation	DKVSFFCKNKEKKCS CEEEEEECCCCCCCC	66.93	-
330	Phosphorylation	PKCFKEHSSLAFWKT CCHHHHCCCCEEEEC	28.30	28348404
331	Phosphorylation	KCFKEHSSLAFWKTD CHHHHCCCCEEEECC	26.14	28348404

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
188	N	Glycosylation		6587378
PubMed:6587378 also reports glycosylation on 'Asn-188' for their allele.

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
149	O-linked Glycosylation	154 (5)	R ⇒ H	rs8178847	Blood protein levels	28240269
156	N-linked Glycosylation	154 (2)	R ⇒ H	rs8178847	Blood protein levels	28240269
162	N-linked Glycosylation	154 (8)	R ⇒ H	rs8178847	Blood protein levels	28240269

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LRP8_HUMAN	LRP8	physical	12807892
LRP2_HUMAN	LRP2	physical	9727058
FLNA_HUMAN	FLNA	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.

Regulatory Network of APOH_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-162, STRUCTURE OFCARBOHYDRATES, 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-162; ASN-183; ASN-193 ANDASN-253, AND MASS SPECTROMETRY.	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-162 AND ASN-253, 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-162; ASN-183; ASN-193 ANDASN-253, AND MASS SPECTROMETRY.	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-162; ASN-183 AND ASN-193,AND MASS SPECTROMETRY.	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-162 AND ASN-253, AND MASSSPECTROMETRY.	15084671 [Abstract]
"Complete amino acid sequence of human plasma beta 2-glycoprotein I."; Lozier J., Takahashi N., Putnam F.W.; Proc. Natl. Acad. Sci. U.S.A. 81:3640-3644(1984). Cited for: PROTEIN SEQUENCE OF 20-345, GLYCOSYLATION AT ASN-162; ASN-183; ASN-193AND ASN-253, AND DISULFIDE BONDS.	6587378 [Abstract]

show