dbPTM

APOD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	APOD_HUMAN
UniProt AC	P05090
Protein Name	Apolipoprotein D
Gene Name	APOD
Organism	Homo sapiens (Human).
Sequence Length	189
Subcellular Localization	Secreted.
Protein Description	APOD occurs in the macromolecular complex with lecithin-cholesterol acyltransferase. It is probably involved in the transport and binding of bilin. Appears to be able to transport a variety of ligands in a number of different contexts..
Protein Sequence	MVMLLLLLSALAGLFGAAEGQAFHLGKCPNPPVQENFDVNKYLGRWYEIEKIPTTFENGRCIQANYSLMENGKIKVLNQELRADGTVNQIEGEATPVNLTEPAKLEVKFSWFMPSAPYWILATDYENYALVYSCTCIIQLFHVDFAWILARNPNLPPETVDSLKNILTSNNIDVKKMTVTDQVNCPKLS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21	Pyrrolidone_carboxylic_acid	LFGAAEGQAFHLGKC HHCHHHHCCEECCCC	32.15	-
21	Pyrrolidone_carboxylic_acid	LFGAAEGQAFHLGKC HHCHHHHCCEECCCC	32.15	3453108
21	Pyrrolidone_carboxylic_acid	LFGAAEGQAFHLGKC HHCHHHHCCEECCCC	32.15	3453108
65	N-linked_Glycosylation	NGRCIQANYSLMENG CCEEEEECEEEEECC	15.56	22171320
65	N-linked_Glycosylation	NGRCIQANYSLMENG CCEEEEECEEEEECC	15.56	22171320
67	O-linked_Glycosylation	RCIQANYSLMENGKI EEEEECEEEEECCCE	22.50	28657654
93	Sulfoxidation	TVNQIEGEATPVNLT CEEEECCEEECCCCC	36.26	22150111
98	N-linked_Glycosylation	EGEATPVNLTEPAKL CCEEECCCCCCCEEE	42.31	22171320
98	N-linked_Glycosylation	EGEATPVNLTEPAKL CCEEECCCCCCCEEE	42.31	22171320
168	Phosphorylation	DSLKNILTSNNIDVK HHHHHHHHHCCCCEE	26.13	30622161
169	Phosphorylation	SLKNILTSNNIDVKK HHHHHHHHCCCCEEE	25.16	30622161
178	Phosphorylation	NIDVKKMTVTDQVNC CCCEEECEECCCCCC	29.18	30622161
180	Phosphorylation	DVKKMTVTDQVNCPK CEEECEECCCCCCCC	16.14	30622161

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 APOD_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of APOD_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
Oops, there are no SNP-PTM records of APOD_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
APOD_HUMAN	APOD	physical	7918467
APOA2_HUMAN	APOA2	physical	7918467
VAPA_HUMAN	VAPA	physical	25416956
CD166_HUMAN	ALCAM	physical	28514442
CYR61_HUMAN	CYR61	physical	28514442
GDN_HUMAN	SERPINE2	physical	28514442
NECT2_HUMAN	PVRL2	physical	28514442
TOR1A_HUMAN	TOR1A	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 APOD_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Site-specific detection and structural characterization of theglycosylation of human plasma proteins lecithin:cholesterolacyltransferase and apolipoprotein D using HPLC/electrospray massspectrometry and sequential glycosidase digestion."; Schindler P.A., Settineri C.A., Collet X., Fielding C.J.,Burlingame A.L.; Protein Sci. 4:791-803(1995). Cited for: GLYCOSYLATION AT ASN-65 AND ASN-98.	7613477 [Abstract]
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD."; Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; Mol. Cell. Proteomics 0:0-0(2011). Cited for: GLYCOSYLATION AT ASN-65 AND ASN-98, STRUCTURE OF CARBOHYDRATES, ANDMASS SPECTROMETRY.	22171320 [Abstract]
"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-98, 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-65 AND ASN-98, AND MASSSPECTROMETRY.	19159218 [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-98, 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-98, AND MASS SPECTROMETRY.	14760718 [Abstract]
"Structure of human apolipoprotein D: locations of the intermolecularand intramolecular disulfide links."; Yang C.-Y., Gu Z.-W., Blanco-Vaca F., Gaskell S.J., Yang M.,Massey J.B., Gotto A.M. Jr., Pownall H.J.; Biochemistry 33:12451-12455(1994). Cited for: PROTEIN SEQUENCE OF 21-189, DISULFIDE BONDS, AND GLYCOSYLATION ATASN-65 AND ASN-98.	7918467 [Abstract]
Pyrrolidone carboxylic acid
Reference	PubMed
"Cloning and expression of human apolipoprotein D cDNA."; Drayna D.T., Fielding C., McLean J.W., Baer B., Castro G., Chen E.,Comstock L., Henzel W., Kohr W., Rhee L., Wion K.L., Lawn R.M.; J. Biol. Chem. 261:16535-16539(1986). Cited for: NUCLEOTIDE SEQUENCE [MRNA].	3453108 [Abstract]