dbPTM

SIDT2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SIDT2_HUMAN
UniProt AC	Q8NBJ9
Protein Name	SID1 transmembrane family member 2
Gene Name	SIDT2
Organism	Homo sapiens (Human).
Sequence Length	832
Subcellular Localization	Lysosome membrane Multi-pass membrane protein . Cell membrane . Mainly localizes to lysosomes and only partly to the plasma membrane (PubMed:28277980). Lysosomal localization is required for SIDT2-mediated intracellular degradation of endogenous RN
Protein Description	Mediates the translocation of RNA and DNA across the lysosomal membrane during RNA and DNA autophagy (RDA), a process in which RNA or DNA is directly imported into lysosomes in an ATP-dependent manner, and degraded. [PubMed: 27046251]
Protein Sequence	MFALGLPFLVLLVASVESHLGVLGPKNVSQKDAEFERTYVDEVNSELVNIYTFNHTVTRNRTEGVRVSVNVLNKQKGAPLLFVVRQKEAVVSFQVPLILRGMFQRKYLYQKVERTLCQPPTKNESEIQFFYVDVSTLSPVNTTYQLRVSRMDDFVLRTGEQFSFNTTAAQPQYFKYEFPEGVDSVIVKVTSNKAFPCSVISIQDVLCPVYDLDNNVAFIGMYQTMTKKAAITVQRKDFPSNSFYVVVVVKTEDQACGGSLPFYPFAEDEPVDQGHRQKTLSVLVSQAVTSEAYVSGMLFCLGIFLSFYLLTVLLACWENWRQKKKTLLVAIDRACPESGHPRVLADSFPGSSPYEGYNYGSFENVSGSTDGLVDSAGTGDLSYGYQGRSFEPVGTRPRVDSMSSVEEDDYDTLTDIDSDKNVIRTKQYLYVADLARKDKRVLRKKYQIYFWNIATIAVFYALPVVQLVITYQTVVNVTGNQDICYYNFLCAHPLGNLSAFNNILSNLGYILLGLLFLLIILQREINHNRALLRNDLCALECGIPKHFGLFYAMGTALMMEGLLSACYHVCPNYTNFQFDTSFMYMIAGLCMLKLYQKRHPDINASAYSAYACLAIVIFFSVLGVVFGKGNTAFWIVFSIIHIIATLLLSTQLYYMGRWKLDSGIFRRILHVLYTDCIRQCSGPLYVDRMVLLVMGNVINWSLAAYGLIMRPNDFASYLLAIGICNLLLYFAFYIIMKLRSGERIKLIPLLCIVCTSVVWGFALFFFFQGLSTWQKTPAESREHNRDCILLDFFDDHDIWHFLSSIAMFGSFLVLLTLDDDLDTVQRDKIYVF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
27	N-linked_Glycosylation	LGVLGPKNVSQKDAE HCCCCCCCCCHHHHH	41.63	UniProtKB CARBOHYD
54	N-linked_Glycosylation	LVNIYTFNHTVTRNR EEEEEEEECEEECCC	23.32	UniProtKB CARBOHYD
60	N-linked_Glycosylation	FNHTVTRNRTEGVRV EECEEECCCCCCEEE	45.95	UniProtKB CARBOHYD
107	Phosphorylation	RGMFQRKYLYQKVER CHHHHHHHHHHHHHH	16.90	-
109	Phosphorylation	MFQRKYLYQKVERTL HHHHHHHHHHHHHHC	11.82	19415658
111	Ubiquitination	QRKYLYQKVERTLCQ HHHHHHHHHHHHCCC	32.29	29967540
121	Phosphorylation	RTLCQPPTKNESEIQ HHCCCCCCCCCCCEE	53.86	-
123	N-linked_Glycosylation	LCQPPTKNESEIQFF CCCCCCCCCCCEEEE	61.58	UniProtKB CARBOHYD
125	Phosphorylation	QPPTKNESEIQFFYV CCCCCCCCCEEEEEE	49.76	29978859
131	Phosphorylation	ESEIQFFYVDVSTLS CCCEEEEEEEHHHCC	9.31	29978859
135	Phosphorylation	QFFYVDVSTLSPVNT EEEEEEHHHCCCCCC	21.11	29978859
136	Phosphorylation	FFYVDVSTLSPVNTT EEEEEHHHCCCCCCE	30.97	29978859
138	Phosphorylation	YVDVSTLSPVNTTYQ EEEHHHCCCCCCEEE	27.22	29978859
141	N-linked_Glycosylation	VSTLSPVNTTYQLRV HHHCCCCCCEEEEEE	30.04	UniProtKB CARBOHYD
142	Phosphorylation	STLSPVNTTYQLRVS HHCCCCCCEEEEEEE	27.41	29978859
143	Phosphorylation	TLSPVNTTYQLRVSR HCCCCCCEEEEEEEE	12.22	29978859
144	Phosphorylation	LSPVNTTYQLRVSRM CCCCCCEEEEEEEEC	11.96	29978859
149	Phosphorylation	TTYQLRVSRMDDFVL CEEEEEEEECCCEEE	18.56	29978859
165	N-linked_Glycosylation	TGEQFSFNTTAAQPQ CCCCEEECCCCCCCC	35.01	UniProtKB CARBOHYD
191	Phosphorylation	SVIVKVTSNKAFPCS EEEEEEECCCCCCEE	39.04	-
201	Phosphorylation	AFPCSVISIQDVLCP CCCEEEEEEECEEEE	16.43	-
228	Ubiquitination	MYQTMTKKAAITVQR EEECCCCEEEEEEEE	33.61	29967540
351	Phosphorylation	LADSFPGSSPYEGYN ECCCCCCCCCCCCCC	28.51	28348404
352	Phosphorylation	ADSFPGSSPYEGYNY CCCCCCCCCCCCCCC	37.10	28348404
354	Phosphorylation	SFPGSSPYEGYNYGS CCCCCCCCCCCCCCC	24.76	28348404
357	Phosphorylation	GSSPYEGYNYGSFEN CCCCCCCCCCCCEEC	8.02	28348404
359	Phosphorylation	SPYEGYNYGSFENVS CCCCCCCCCCEECCC	12.98	28348404
361	Phosphorylation	YEGYNYGSFENVSGS CCCCCCCCEECCCCC	21.01	28348404
366	Phosphorylation	YGSFENVSGSTDGLV CCCEECCCCCCCCCC	38.31	28348404
368	Phosphorylation	SFENVSGSTDGLVDS CEECCCCCCCCCCCC	18.80	28348404
369	Phosphorylation	FENVSGSTDGLVDSA EECCCCCCCCCCCCC	37.30	28348404
375	Phosphorylation	STDGLVDSAGTGDLS CCCCCCCCCCCCCCC	22.56	28348404
378	Phosphorylation	GLVDSAGTGDLSYGY CCCCCCCCCCCCCCC	27.52	25332170
382	Phosphorylation	SAGTGDLSYGYQGRS CCCCCCCCCCCCCCC	22.66	25332170
385	Phosphorylation	TGDLSYGYQGRSFEP CCCCCCCCCCCCCCC	10.28	25332170
389	Phosphorylation	SYGYQGRSFEPVGTR CCCCCCCCCCCCCCC	40.56	30266825
395	Phosphorylation	RSFEPVGTRPRVDSM CCCCCCCCCCCCCCC	37.42	28102081
401	Phosphorylation	GTRPRVDSMSSVEED CCCCCCCCCCCCCCC	20.08	28102081
403	Phosphorylation	RPRVDSMSSVEEDDY CCCCCCCCCCCCCCC	34.87	28102081
404	Phosphorylation	PRVDSMSSVEEDDYD CCCCCCCCCCCCCCC	25.55	10810093
410	Phosphorylation	SSVEEDDYDTLTDID CCCCCCCCCCCCCCC	24.13	27486199
412	Phosphorylation	VEEDDYDTLTDIDSD CCCCCCCCCCCCCCC	25.90	27486199
414	Phosphorylation	EDDYDTLTDIDSDKN CCCCCCCCCCCCCCC	32.76	28102081
418	Phosphorylation	DTLTDIDSDKNVIRT CCCCCCCCCCCEEHH	51.31	28102081
426	Ubiquitination	DKNVIRTKQYLYVAD CCCEEHHHEEEHHHH	27.39	33845483
428	Phosphorylation	NVIRTKQYLYVADLA CEEHHHEEEHHHHHH	11.10	25072903
430	Phosphorylation	IRTKQYLYVADLARK EHHHEEEHHHHHHHC	6.67	25072903
476	N-linked_Glycosylation	ITYQTVVNVTGNQDI EEEEEEEECCCCCCE	22.69	UniProtKB CARBOHYD
496	N-linked_Glycosylation	LCAHPLGNLSAFNNI EECCCCCCHHHHHHH	38.21	UniProtKB CARBOHYD
572	N-linked_Glycosylation	ACYHVCPNYTNFQFD HHHHHCCCCCCCCCC	51.65	UniProtKB CARBOHYD
603	N-linked_Glycosylation	QKRHPDINASAYSAY HHHCCCCCHHHHHHH	34.91	UniProtKB CARBOHYD

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 SIDT2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SIDT2_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 SIDT2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SIDT2_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.

Regulatory Network of SIDT2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-401; SER-403 ANDSER-404, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401; SER-403 ANDSER-404, AND MASS SPECTROMETRY.	17081983 [Abstract]