dbPTM

APMAP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	APMAP_HUMAN
UniProt AC	Q9HDC9
Protein Name	Adipocyte plasma membrane-associated protein
Gene Name	APMAP
Organism	Homo sapiens (Human).
Sequence Length	416
Subcellular Localization	Membrane Single-pass type II membrane protein .
Protein Description	Exhibits strong arylesterase activity with beta-naphthyl acetate and phenyl acetate. May play a role in adipocyte differentiation..
Protein Sequence	MSEADGLRQRRPLRPQVVTDDDGQAPEAKDGSSFSGRVFRVTFLMLAVSLTVPLLGAMMLLESPIDPQPLSFKEPPLLLGVLHPNTKLRQAERLFENQLVGPESIAHIGDVMFTGTADGRVVKLENGEIETIARFGSGPCKTRDDEPVCGRPLGIRAGPNGTLFVADAYKGLFEVNPWKREVKLLLSSETPIEGKNMSFVNDLTVTQDGRKIYFTDSSSKWQRRDYLLLVMEGTDDGRLLEYDTVTREVKVLLDQLRFPNGVQLSPAEDFVLVAETTMARIRRVYVSGLMKGGADLFVENMPGFPDNIRPSSSGGYWVGMSTIRPNPGFSMLDFLSERPWIKRMIFKLFSQETVMKFVPRYSLVLELSDSGAFRRSLHDPDGLVATYISEVHEHDGHLYLGSFRSPFLCRLSLQAV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSEADGLRQ ------CCCCCCCCC	41.30	24719451
2	Acetylation	------MSEADGLRQ ------CCCCCCCCC	41.30	22814378
19	Phosphorylation	PLRPQVVTDDDGQAP CCCCCEEECCCCCCC	34.55	23401153
29	Ubiquitination	DGQAPEAKDGSSFSG CCCCCCCCCCCCCCC	62.04	22817900
29 (in isoform 1)	Ubiquitination	-	62.04	21890473
29 (in isoform 2)	Ubiquitination	-	62.04	21890473
71	Phosphorylation	PIDPQPLSFKEPPLL CCCCCCCCCCCCCEE	40.74	24719451
87	Ubiquitination	GVLHPNTKLRQAERL EEECCCHHHHHHHHH	48.60	33845483
123 (in isoform 2)	Ubiquitination	-	47.42	21890473
123	2-Hydroxyisobutyrylation	TADGRVVKLENGEIE CCCCEEEEEECCEEE	47.42	-
123 (in isoform 1)	Ubiquitination	-	47.42	21890473
123	Ubiquitination	TADGRVVKLENGEIE CCCCEEEEEECCEEE	47.42	21906983
137	Phosphorylation	ETIARFGSGPCKTRD EEEEEECCCCCCCCC	36.53	-
141	Ubiquitination	RFGSGPCKTRDDEPV EECCCCCCCCCCCCC	50.13	24816145
141	Acetylation	RFGSGPCKTRDDEPV EECCCCCCCCCCCCC	50.13	7674283
142	Phosphorylation	FGSGPCKTRDDEPVC ECCCCCCCCCCCCCC	46.15	-
160	N-linked_Glycosylation	LGIRAGPNGTLFVAD CEEEECCCCCEEEEE	55.98	17623646
160	N-linked_Glycosylation	LGIRAGPNGTLFVAD CEEEECCCCCEEEEE	55.98	17623646
162	O-linked_Glycosylation	IRAGPNGTLFVADAY EEECCCCCEEEEECC	24.54	30059200
179 (in isoform 2)	Ubiquitination	-	39.68	21890473
179	Ubiquitination	LFEVNPWKREVKLLL CEECCCCHHHHEEHH	39.68	23000965
179 (in isoform 1)	Ubiquitination	-	39.68	21890473
179	2-Hydroxyisobutyrylation	LFEVNPWKREVKLLL CEECCCCHHHHEEHH	39.68	-
183	Ubiquitination	NPWKREVKLLLSSET CCCHHHHEEHHCCCC	28.76	23000965
187	Phosphorylation	REVKLLLSSETPIEG HHHEEHHCCCCCCCC	26.54	23911959
188	O-linked_Glycosylation	EVKLLLSSETPIEGK HHEEHHCCCCCCCCC	45.52	OGP
188	Phosphorylation	EVKLLLSSETPIEGK HHEEHHCCCCCCCCC	45.52	23911959
195 (in isoform 1)	Ubiquitination	-	36.37	21890473
195 (in isoform 2)	Ubiquitination	-	36.37	21890473
195	Ubiquitination	SETPIEGKNMSFVND CCCCCCCCCCCCCCE	36.37	22817900
196	N-linked_Glycosylation	ETPIEGKNMSFVNDL CCCCCCCCCCCCCEE	42.03	12754519
198	Phosphorylation	PIEGKNMSFVNDLTV CCCCCCCCCCCEEEE	35.12	22210691
211	Ubiquitination	TVTQDGRKIYFTDSS EECCCCCEEEEECCC	47.49	32142685
213	Phosphorylation	TQDGRKIYFTDSSSK CCCCCEEEEECCCCC	11.94	28152594
215	Phosphorylation	DGRKIYFTDSSSKWQ CCCEEEEECCCCCCE	20.28	28152594
217	Phosphorylation	RKIYFTDSSSKWQRR CEEEEECCCCCCEEC	33.19	22461510
220	Acetylation	YFTDSSSKWQRRDYL EEECCCCCCEECCEE	49.66	25825284
220	Ubiquitination	YFTDSSSKWQRRDYL EEECCCCCCEECCEE	49.66	32142685
220	2-Hydroxyisobutyrylation	YFTDSSSKWQRRDYL EEECCCCCCEECCEE	49.66	-
242	Phosphorylation	DDGRLLEYDTVTREV CCCCEEECCCCCHHH	19.51	-
244	Phosphorylation	GRLLEYDTVTREVKV CCEEECCCCCHHHHH	23.91	-
250	Ubiquitination	DTVTREVKVLLDQLR CCCCHHHHHHHHHHC	23.55	24816145
250	2-Hydroxyisobutyrylation	DTVTREVKVLLDQLR CCCCHHHHHHHHHHC	23.55	-
265	Phosphorylation	FPNGVQLSPAEDFVL CCCCCCCCCHHCEEE	12.65	-
312	Phosphorylation	PDNIRPSSSGGYWVG CCCCCCCCCCCEEEE	35.37	30576142
342	2-Hydroxyisobutyrylation	LSERPWIKRMIFKLF HHCCHHHHHHHHHHH	31.85	-
342	Ubiquitination	LSERPWIKRMIFKLF HHCCHHHHHHHHHHH	31.85	22817900
347	Acetylation	WIKRMIFKLFSQETV HHHHHHHHHHCHHHH	37.38	7704525
347	Ubiquitination	WIKRMIFKLFSQETV HHHHHHHHHHCHHHH	37.38	22817900
347 (in isoform 1)	Ubiquitination	-	37.38	21890473
355	Sulfoxidation	LFSQETVMKFVPRYS HHCHHHHHHHCCCEE	3.49	21406390
402	Phosphorylation	DGHLYLGSFRSPFLC CCEEEEECCCCCCEE	18.19	24719451

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 APMAP_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of APMAP_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 APMAP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMAD3_HUMAN	SMAD3	physical	21988832
CALX_HUMAN	CANX	physical	26344197
CLGN_HUMAN	CLGN	physical	26344197
HNRDL_HUMAN	HNRNPDL	physical	26344197
INTU_HUMAN	INTU	physical	27173435

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 APMAP_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-160 AND ASN-196, 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-160 AND ASN-196, AND MASSSPECTROMETRY.	16335952 [Abstract]
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-160 AND ASN-196.	12754519 [Abstract]