RNFT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RNFT1_HUMAN
• UniProt AC: Q5M7Z0
• Protein Name: E3 ubiquitin-protein ligase RNFT1 {ECO:0000305}
• Gene Name: RNFT1
• Organism: Homo sapiens (Human).
• Sequence Length: 435
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein .
• Protein Description: E3 ubiquitin-protein ligase that acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and subsequent proteasome-mediated degradation. Protects cells from ER stress-induced apoptosis..
• Protein Sequence: MPLFLLSLPTPPSASGHERRQRPEAKTSGSEKKYLRAMQANRSQLHSPPGTGSSEDASTPQCVHTRLTGEGSCPHSGDVHIQINSIPKECAENASSRNIRSGVHSCAHGCVHSRLRGHSHSEARLTDDTAAESGDHGSSSFSEFRYLFKWLQKSLPYILILSVKLVMQHITGISLGIGLLTTFMYANKSIVNQVFLRERSSKIQCAWLLVFLAGSSVLLYYTFHSQSLYYSLIFLNPTLDHLSFWEVFWIVGITDFILKFFFMGLKCLILLVPSFIMPFKSKGYWYMLLEELCQYYRTFVPIPVWFRYLISYGEFGNVTRWSLGILLALLYLILKLLEFFGHLRTFRQVLRIFFTQPSYGVAASKRQCSDVDDICSICQAEFQKPILLICQHIFCEECMTLWFNREKTCPLCRTVISDHINKWKDGATSSHLQIY

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
26	Ubiquitination	RRQRPEAKTSGSEKK CCCCCCCCCCCCHHH	41.37	-
30	Phosphorylation	PEAKTSGSEKKYLRA CCCCCCCCHHHHHHH	46.11	-
43	Phosphorylation	RAMQANRSQLHSPPG HHHHHCHHHHCCCCC	36.58	21712546
47	Phosphorylation	ANRSQLHSPPGTGSS HCHHHHCCCCCCCCC	41.19	25159151
51	Phosphorylation	QLHSPPGTGSSEDAS HHCCCCCCCCCCCCC	39.40	27251275
53	Phosphorylation	HSPPGTGSSEDASTP CCCCCCCCCCCCCCC	30.32	27251275
54	Phosphorylation	SPPGTGSSEDASTPQ CCCCCCCCCCCCCCC	40.62	21712546
58	Phosphorylation	TGSSEDASTPQCVHT CCCCCCCCCCCEEEE	53.60	25159151
59	Phosphorylation	GSSEDASTPQCVHTR CCCCCCCCCCEEEEE	21.06	25159151
65	Phosphorylation	STPQCVHTRLTGEGS CCCCEEEEEECCCCC	13.64	21712546
72	Phosphorylation	TRLTGEGSCPHSGDV EEECCCCCCCCCCCE	21.85	25159151
76	Phosphorylation	GEGSCPHSGDVHIQI CCCCCCCCCCEEEEE	23.10	25159151
149 (in isoform 3)	Ubiquitination	-	44.38	21890473
149 (in isoform 2)	Ubiquitination	-	44.38	21890473
149 (in isoform 1)	Ubiquitination	-	44.38	21890473
149	Ubiquitination	SEFRYLFKWLQKSLP HHHHHHHHHHHHHHC	44.38	22817900
153	Ubiquitination	YLFKWLQKSLPYILI HHHHHHHHHHCHHHH	52.36	22817900
162	Phosphorylation	LPYILILSVKLVMQH HCHHHHHHHHHHHHH	15.37	24719451
171	Phosphorylation	KLVMQHITGISLGIG HHHHHHHHHHHHHHH	26.74	-
174	Phosphorylation	MQHITGISLGIGLLT HHHHHHHHHHHHHHH	23.14	-
281	Phosphorylation	SFIMPFKSKGYWYML HHHCCCCCCCHHHHH	31.52	-
364	Phosphorylation	PSYGVAASKRQCSDV CCCCCCCCCCCCCCH	20.73	24260401
365	Ubiquitination	SYGVAASKRQCSDVD CCCCCCCCCCCCCHH	41.58	21963094

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

Oops, there are no upstream regulatory protein records of RNFT1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RNFT1_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 RNFT1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of RNFT1_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.