AP1AR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AP1AR_HUMAN
• UniProt AC: Q63HQ0
• Protein Name: AP-1 complex-associated regulatory protein
• Gene Name: AP1AR
• Organism: Homo sapiens (Human).
• Sequence Length: 302
• Subcellular Localization: Golgi apparatus, trans-Golgi network. Late endosome. Early endosome. Localizes to the juxta-nuclear Golgi region and to tubular structures throughout the cytoplasm, which are highly mobile and cycle between the juxta-nuclear area and the cell periphe
• Protein Description: Necessary for adaptor protein complex 1 (AP-1)-dependent transport between the trans-Golgi network and endosomes. Regulates the membrane association of AP1G1/gamma1-adaptin, one of the subunits of the AP-1 adaptor complex. The direct interaction with AP1G1/gamma1-adaptin attenuates the release of the AP-1 complex from membranes. Regulates endosomal membrane traffic via association with AP-1 and KIF5B thus linking kinesin-based plus-end-directed microtubular transport to AP-1-dependent membrane traffic. May act as effector of AP-1 in calcium-induced endo-lysosome secretion. Inhibits Arp2/3 complex function; negatively regulates cell spreading, size and motility via intracellular sequestration of the Arp2/3 complex..
• Protein Sequence: MGNCCWTQCFGLLRKEAGRLQRVGGGGGSKYFRTCSRGEHLTIEFENLVESDEGESPGSSHRPLTEEEIVDLRERHYDSIAEKQKDLDKKIQKELALQEEKLRLEEEALYAAQREAARAAKQRKLLEQERQRIVQQYHPSNNGEYQSSGPEDDFESCLRNMKSQYEVFRSSRLSSDATVLTPNTESSCDLMTKTKSTSGNDDSTSLDLEWEDEEGMNRMLPMRERSKTEEDILRAALKYSNKKTGSNPTSASDDSNGLEWENDFVSAEMDDNGNSEYSGFVNPVLELSDSGIRHSDTDQQTR

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
29	Phosphorylation	RVGGGGGSKYFRTCS ECCCCCCCCCCEECC	27.70	23401153
30	Ubiquitination	VGGGGGSKYFRTCSR CCCCCCCCCCEECCC	52.24	-
31	Phosphorylation	GGGGGSKYFRTCSRG CCCCCCCCCEECCCC	10.45	23927012
42	Phosphorylation	CSRGEHLTIEFENLV CCCCCCEEEEEEECC	21.99	26471730
51	Phosphorylation	EFENLVESDEGESPG EEEECCCCCCCCCCC	33.22	26074081
56	Phosphorylation	VESDEGESPGSSHRP CCCCCCCCCCCCCCC	45.47	26074081
59	Phosphorylation	DEGESPGSSHRPLTE CCCCCCCCCCCCCCH	26.76	26074081
60	Phosphorylation	EGESPGSSHRPLTEE CCCCCCCCCCCCCHH	29.45	26074081
65	Phosphorylation	GSSHRPLTEEEIVDL CCCCCCCCHHHHHHH	43.99	26074081
77	Phosphorylation	VDLRERHYDSIAEKQ HHHHHHHHHHHHHHH	20.01	28796482
79	Phosphorylation	LRERHYDSIAEKQKD HHHHHHHHHHHHHHH	19.28	27642862
83	2-Hydroxyisobutyrylation	HYDSIAEKQKDLDKK HHHHHHHHHHHHHHH	54.34	-
83	Ubiquitination	HYDSIAEKQKDLDKK HHHHHHHHHHHHHHH	54.34	-
93	Ubiquitination	DLDKKIQKELALQEE HHHHHHHHHHHHHHH	59.16	-
101	Ubiquitination	ELALQEEKLRLEEEA HHHHHHHHHHHHHHH	37.85	-
110	Phosphorylation	RLEEEALYAAQREAA HHHHHHHHHHHHHHH	13.62	21945579
124	Ubiquitination	ARAAKQRKLLEQERQ HHHHHHHHHHHHHHH	55.73	-
137	Phosphorylation	RQRIVQQYHPSNNGE HHHHHHHHCCCCCCC	9.90	21945579
140	Phosphorylation	IVQQYHPSNNGEYQS HHHHHCCCCCCCCCC	29.61	21945579
145	Phosphorylation	HPSNNGEYQSSGPED CCCCCCCCCCCCCHH	18.33	21945579
147	Phosphorylation	SNNGEYQSSGPEDDF CCCCCCCCCCCHHHH	36.04	21945579
148	Phosphorylation	NNGEYQSSGPEDDFE CCCCCCCCCCHHHHH	42.73	21945579
156	Phosphorylation	GPEDDFESCLRNMKS CCHHHHHHHHHHHHH	20.60	21945579
162	Ubiquitination	ESCLRNMKSQYEVFR HHHHHHHHHHHHHHH	37.65	-
163	Phosphorylation	SCLRNMKSQYEVFRS HHHHHHHHHHHHHHH	27.50	25348954
165	Phosphorylation	LRNMKSQYEVFRSSR HHHHHHHHHHHHHCC	22.58	28797
170	Phosphorylation	SQYEVFRSSRLSSDA HHHHHHHHCCCCCCC	14.35	28450419
171	Phosphorylation	QYEVFRSSRLSSDAT HHHHHHHCCCCCCCE	32.74	28450419
174	Phosphorylation	VFRSSRLSSDATVLT HHHHCCCCCCCEEEC	25.68	25159151
175	Phosphorylation	FRSSRLSSDATVLTP HHHCCCCCCCEEECC	35.54	25159151
178	Phosphorylation	SRLSSDATVLTPNTE CCCCCCCEEECCCCC	22.49	25159151
181	Phosphorylation	SSDATVLTPNTESSC CCCCEEECCCCCCCC	15.34	25159151
184	Phosphorylation	ATVLTPNTESSCDLM CEEECCCCCCCCCEE	38.15	30576142
186	Phosphorylation	VLTPNTESSCDLMTK EECCCCCCCCCEEEC	33.94	30576142
187	Phosphorylation	LTPNTESSCDLMTKT ECCCCCCCCCEEECC	12.86	30576142
192	Phosphorylation	ESSCDLMTKTKSTSG CCCCCEEECCCCCCC	42.74	30576142
194	Phosphorylation	SCDLMTKTKSTSGND CCCEEECCCCCCCCC	22.51	46164867
196	Phosphorylation	DLMTKTKSTSGNDDS CEEECCCCCCCCCCC	32.79	21955146
197	Phosphorylation	LMTKTKSTSGNDDST EEECCCCCCCCCCCC	42.06	21955146
198	Phosphorylation	MTKTKSTSGNDDSTS EECCCCCCCCCCCCC	42.56	30576142
203	Phosphorylation	STSGNDDSTSLDLEW CCCCCCCCCCCCEEE	23.82	28450419
204	Phosphorylation	TSGNDDSTSLDLEWE CCCCCCCCCCCEEEE	40.06	30576142
205	Phosphorylation	SGNDDSTSLDLEWED CCCCCCCCCCEEEEC	24.68	28450419
226	Phosphorylation	MLPMRERSKTEEDIL CCCHHHCCCCHHHHH	38.89	27273156
228	Phosphorylation	PMRERSKTEEDILRA CHHHCCCCHHHHHHH	45.94	23401153
247	N-linked_Glycosylation	SNKKTGSNPTSASDD CCCCCCCCCCCCCCC	45.25	19349973
247	N-linked_Glycosylation	SNKKTGSNPTSASDD CCCCCCCCCCCCCCC	45.25	19349973
256	N-linked_Glycosylation	TSASDDSNGLEWEND CCCCCCCCCCEEECC	67.09	19349973
256	N-linked_Glycosylation	TSASDDSNGLEWEND CCCCCCCCCCEEECC	67.09	-
262	N-linked_Glycosylation	SNGLEWENDFVSAEM CCCCEEECCEEEEEE	49.44	19349973
262	N-linked_Glycosylation	SNGLEWENDFVSAEM CCCCEEECCEEEEEE	49.44	-

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

Oops, there are no upstream regulatory protein records of AP1AR_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AP1AR_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of AP1AR_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of AP1AR_HUMAN !!

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

"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-247, AND MASSSPECTROMETRY.
PubMed: 19349973

Phosphorylation

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-228, AND MASSSPECTROMETRY.
PubMed: 18669648