RN128_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RN128_HUMAN
• UniProt AC: Q8TEB7
• Protein Name: E3 ubiquitin-protein ligase RNF128
• Gene Name: RNF128
• Organism: Homo sapiens (Human).
• Sequence Length: 428
• Subcellular Localization: Endomembrane system; Single-pass membrane protein. Cytoplasm, cytoskeleton . Cytoplasm, perinuclear region. Localized in an asymmetric perinuclear punctate manner. Localizes to the internal pool of the transferrin recycling endosomal pathway. Partial
• Protein Description: E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains formation. Functions as an inhibitor of cytokine gene transcription. Inhibits IL2 and IL4 transcription, thereby playing an important role in the induction of the anergic phenotype, a long-term stable state of T-lymphocyte unresponsiveness to antigenic stimulation associated with the blockade of interleukin production. Ubiquitinates ARPC5 with 'Lys-48' linkages and COR1A with 'Lys-63' linkages leading to their degradation, down-regulation of these cytosleletal components results in impaired lamellipodium formation and reduced accumulation of F-actin at the immunological synapse. Functions in the patterning of the dorsal ectoderm; sensitizes ectoderm to respond to neural-inducing signals..
• Protein Sequence: MGPPPGAGVSCRGGCGFSRLLAWCFLLALSPQAPGSRGAEAVWTAYLNVSWRVPHTGVNRTVWELSEEGVYGQDSPLEPVAGVLVPPDGPGALNACNPHTNFTVPTVWGSTVQVSWLALIQRGGGCTFADKIHLAYERGASGAVIFNFPGTRNEVIPMSHPGAVDIVAIMIGNLKGTKILQSIQRGIQVTMVIEVGKKHGPWVNHYSIFFVSVSFFIITAATVGYFIFYSARRLRNARAQSRKQRQLKADAKKAIGRLQLRTLKQGDKEIGPDGDSCAVCIELYKPNDLVRILTCNHIFHKTCVDPWLLEHRTCPMCKCDILKALGIEVDVEDGSVSLQVPVSNEISNSASSHEEDNRSETASSGYASVQGTDEPPLEEHVQSTNESLQLVNHEANSVAVDVIPHVDNPTFEEDETPNQETAVREIKS

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
48	N-linked_Glycosylation	AVWTAYLNVSWRVPH EEEEEEEEEEEECCC	17.07	UniProtKB CARBOHYD
56	O-linked_Glycosylation	VSWRVPHTGVNRTVW EEEECCCCCCCCEEE	36.43	29351928
59	N-linked_Glycosylation	RVPHTGVNRTVWELS ECCCCCCCCEEEEEC	34.94	UniProtKB CARBOHYD
61	O-linked_Glycosylation	PHTGVNRTVWELSEE CCCCCCCEEEEECCC	25.43	29351928
101	N-linked_Glycosylation	NACNPHTNFTVPTVW HCCCCCCCCCCCCCC	27.79	UniProtKB CARBOHYD
182	Phosphorylation	KGTKILQSIQRGIQV CCHHHHHHHHCCCEE	19.76	29978859
185	Methylation	KILQSIQRGIQVTMV HHHHHHHCCCEEEEE	42.38	115387815
190	Phosphorylation	IQRGIQVTMVIEVGK HHCCCEEEEEEEECH	6.85	29978859
275	Ubiquitination	KEIGPDGDSCAVCIE EECCCCCCCEEEEEE	48.17	32015554
292	Ubiquitination	KPNDLVRILTCNHIF CCCCEEEEEECCCEE	2.66	29901268
301	Ubiquitination	TCNHIFHKTCVDPWL ECCCEECCCCCCHHH	32.63	32015554
318	Ubiquitination	HRTCPMCKCDILKAL CCCCCCCCCHHHHHH	28.79	29901268

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

Oops, there are no upstream regulatory protein records of RN128_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RN128_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 RN128_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
OTUB1_HUMAN	OTUB1	physical	14661020
CD40L_HUMAN	CD40LG	physical	18641297
GDIR1_MOUSE	Arhgdia	physical	17114425
GDIR2_MOUSE	Arhgdib	physical	17114425
RN128_HUMAN	RNF128	physical	12705856
UB2E1_HUMAN	UBE2E1	physical	12705856
UBE2H_HUMAN	UBE2H	physical	12705856
UB2D1_HUMAN	UBE2D1	physical	12705856
P53_HUMAN	TP53	physical	23370271
CEP76_HUMAN	CEP76	physical	25416956
TBK1_HUMAN	TBK1	physical	27776110
CD83_HUMAN	CD83	physical	19542455

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.