AN13A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AN13A_MOUSE
• UniProt AC: Q80UP5
• Protein Name: Ankyrin repeat domain-containing protein 13A
• Gene Name: Ankrd13a
• Organism: Mus musculus (Mouse).
• Sequence Length: 588
• Subcellular Localization: Cell membrane. Late endosome. Interaction with EGFR may enhance association with the cell membrane..
• Protein Description: Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Does not bind 'Lys-48'-linked ubiquitin. Positively regulates the internalization of ligand-activated EGFR by binding to the Ub moiety of ubiquitinated EGFR at the cell membrane (By similarity)..
• Protein Sequence: MSSARDTSSRFPLHLLVWNNDYEQLEKELRDQNAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMVYTVLQHRDYHNTSMALEGVPELLHKILEAPDFYVQMKWEFTSWVPLVSRICPNDVCRIWKSGAKLRVDITLLGFENMSWIRGRRSFIFKGGDNWAELMEVNHDDRVVTTEHFDLSQEMERLTLDLMKPKSREVERRLTSPVINTSLDTKNVAFERTKSGFWGWRTDKAEVVNGYEAKVYSVNNVSVITRIRTEHLTEEEKKRYKEDRNPLESLLGTVEHQFGAQGDLATECATVNNPTAITPDEYFDEDFDLKDRDIGRPKELTIRTQKFKATLWMCEEFPLSLVEQVIPIIDLMARTSAHFARLRDFIKLDFPPGFPVKIEIPLFHVLNARITFGNVNGCSTADESQGVEGTPAEAVSEATNFEVDQSVFEIPESYHIQDNGRNVHLQDEDYEIMQFAIQQSLLESSRSQDLSGPASNGGVSHTHSYEAQYERAIQESLLTNMEGRCPGGLSESSRFDSDLQLAMELSAKELAERELRLQEEEAELQQVLQLSLTEK

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
27	Ubiquitination	NDYEQLEKELRDQNA CCHHHHHHHHHHHCC	71.31	-
205	Phosphorylation	TTEHFDLSQEMERLT EECCCCHHHHHHHHH	26.41	17525332
217	Ubiquitination	RLTLDLMKPKSREVE HHHHHHHCCCCHHHH	57.50	22790023
219	Ubiquitination	TLDLMKPKSREVERR HHHHHCCCCHHHHHH	57.54	22790023
239	Ubiquitination	INTSLDTKNVAFERT CCCCCCCCCCEEEEE	49.44	22790023
247	Ubiquitination	NVAFERTKSGFWGWR CCEEEEECCCCCCEE	55.60	22790023
257	Ubiquitination	FWGWRTDKAEVVNGY CCCEECCCEEEECCE	45.92	22790023
400	Ubiquitination	ARLRDFIKLDFPPGF HHHHHHHCCCCCCCC	41.83	22790023
401	Ubiquitination	RLRDFIKLDFPPGFP HHHHHHCCCCCCCCC	7.59	27667366
410	Ubiquitination	FPPGFPVKIEIPLFH CCCCCCEEEEEEEEE	34.55	-
483	Phosphorylation	VHLQDEDYEIMQFAI EEECCCCHHHHHHHH	12.81	119635
500	Phosphorylation	SLLESSRSQDLSGPA HHHHHHCCCCCCCCC	29.96	30635358
504	Phosphorylation	SSRSQDLSGPASNGG HHCCCCCCCCCCCCC	51.53	30635358
508	Phosphorylation	QDLSGPASNGGVSHT CCCCCCCCCCCCCCC	38.86	30635358
513	Phosphorylation	PASNGGVSHTHSYEA CCCCCCCCCCCCHHH	26.41	30635358
515	Phosphorylation	SNGGVSHTHSYEAQY CCCCCCCCCCHHHHH	12.66	22817900
517	Phosphorylation	GGVSHTHSYEAQYER CCCCCCCCHHHHHHH	26.31	9668229
518	Phosphorylation	GVSHTHSYEAQYERA CCCCCCCHHHHHHHH	14.00	22817900
522	Phosphorylation	THSYEAQYERAIQES CCCHHHHHHHHHHHH	17.90	22817900
561	Ubiquitination	LAMELSAKELAEREL HHHHHHHHHHHHHHH	50.30	22790023
584	Phosphorylation	LQQVLQLSLTEK--- HHHHHHHHHCCC---	21.93	-

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

Oops, there are no upstream regulatory protein records of AN13A_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AN13A_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of AN13A_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of AN13A_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND MASSSPECTROMETRY.
PubMed: 17525332