dbPTM

RNF11_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RNF11_HUMAN
UniProt AC	Q9Y3C5
Protein Name	RING finger protein 11
Gene Name	RNF11
Organism	Homo sapiens (Human).
Sequence Length	154
Subcellular Localization	Early endosome. Recycling endosome. Cytoplasm. Nucleus. Predominantly cytoplasmic, when unphosphorylated, and nuclear, when phosphorylated by PKB/AKT1.
Protein Description	Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for ubiquitination, leading to its degradation by the 26S proteasome..
Protein Sequence	MGNCLKSPTSDDISLLHESQSDRASFGEGTEPDQEPPPPYQEQVPVPVYHPTPSQTRLATQLTEEEQIRIAQRIGLIQHLPKGVYDPGRDGSEKKIRECVICMMDFVYGDPIRFLPCMHIYHLDCIDDWLMRSFTCPSCMEPVDAALLSSYETN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Myristoylation	------MGNCLKSPT ------CCCCCCCCC	33.29	20676133
2	N-myristoyl glycine	------MGNCLKSPT ------CCCCCCCCC	33.29	-
4	S-palmitoylation	----MGNCLKSPTSD ----CCCCCCCCCCC	4.13	20676133
4	S-nitrosylation	----MGNCLKSPTSD ----CCCCCCCCCCC	4.13	24105792
7	Phosphorylation	-MGNCLKSPTSDDIS -CCCCCCCCCCCCCH	22.06	30266825
9	Phosphorylation	GNCLKSPTSDDISLL CCCCCCCCCCCCHHH	52.45	30266825
10	Phosphorylation	NCLKSPTSDDISLLH CCCCCCCCCCCHHHC	36.35	30266825
14	Phosphorylation	SPTSDDISLLHESQS CCCCCCCHHHCHHHC	31.69	30266825
19	Phosphorylation	DISLLHESQSDRASF CCHHHCHHHCCHHCC	25.00	30266825
21	Phosphorylation	SLLHESQSDRASFGE HHHCHHHCCHHCCCC	38.04	30266825
25	Phosphorylation	ESQSDRASFGEGTEP HHHCCHHCCCCCCCC	34.38	23663014
30	Phosphorylation	RASFGEGTEPDQEPP HHCCCCCCCCCCCCC	39.79	23663014
40	Phosphorylation	DQEPPPPYQEQVPVP CCCCCCCCCCCCCCC	30.38	28060719
49	Phosphorylation	EQVPVPVYHPTPSQT CCCCCCCCCCCHHHH	8.94	30576142
52	Phosphorylation	PVPVYHPTPSQTRLA CCCCCCCCHHHHCHH	23.43	28060719
54	Phosphorylation	PVYHPTPSQTRLATQ CCCCCCHHHHCHHHC	46.81	28060719
56	Phosphorylation	YHPTPSQTRLATQLT CCCCHHHHCHHHCCC	31.80	30576142
82	Ubiquitination	GLIQHLPKGVYDPGR CHHHHCCCCCCCCCC	68.33	33845483
135	Phosphorylation	DWLMRSFTCPSCMEP HHHHHHCCCCCCCCC	25.42	16123141
151	Phosphorylation	DAALLSSYETN---- CHHHHHHHCCC----	24.32	27642862

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
135	T	Phosphorylation	Kinase	AKT1	P31749	Uniprot
135	T	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:19953087
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF2	Q9HAU4	PMID:14562029
-	K	Ubiquitination	E3 ubiquitin ligase	WWP1	Q9H0M0	PMID:18724389

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RNF11_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 RNF11_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EPS15_HUMAN	EPS15	physical	14755250
UBC_HUMAN	UBC	physical	14755250
ZN350_HUMAN	ZNF350	physical	14755250
STABP_HUMAN	STAMBP	physical	14755250
TAXB1_HUMAN	TAX1BP1	physical	19131965
STAT1_HUMAN	STAT1	physical	19131965
TNAP3_HUMAN	TNFAIP3	physical	19131965
RIPK1_HUMAN	RIPK1	physical	19131965
SMUF2_HUMAN	SMURF2	physical	14562029
UB2D1_HUMAN	UBE2D1	physical	14562029
UB2D2_HUMAN	UBE2D2	physical	14562029
UB2D3_HUMAN	UBE2D3	physical	14562029
GGA1_HUMAN	GGA1	physical	20676133
ITCH_HUMAN	ITCH	physical	20676133
SMUF2_HUMAN	SMURF2	physical	20676133
NEDD4_HUMAN	NEDD4	physical	20676133
WWP1_HUMAN	WWP1	physical	18724389
SMAD4_HUMAN	SMAD4	physical	19528490
TNAP3_HUMAN	TNFAIP3	physical	22507528
ITCH_HUMAN	ITCH	physical	22507528
UBE2N_HUMAN	UBE2N	physical	18615712
1433T_HUMAN	YWHAQ	physical	16123141
A4_HUMAN	APP	physical	21832049
ZFYV9_HUMAN	ZFYVE9	physical	23222715
STAM2_HUMAN	STAM2	physical	23222715
EPS15_HUMAN	EPS15	physical	23222715
HGS_HUMAN	HGS	physical	23222715
IKKE_HUMAN	IKBKE	physical	23308279
TBK1_HUMAN	TBK1	physical	23308279
WWP2_HUMAN	WWP2	physical	15231748
STAM2_HUMAN	STAM2	physical	15231748
RU17_HUMAN	SNRNP70	physical	15231748
UBC_HUMAN	UBC	physical	15231748
TNAP3_HUMAN	TNFAIP3	physical	15231748
UBP5_HUMAN	USP5	physical	15231748
NEDD4_HUMAN	NEDD4	physical	15231748
SYQ_HUMAN	QARS	physical	15231748
UBE2N_HUMAN	UBE2N	physical	15231748
UB2D2_HUMAN	UBE2D2	physical	15231748
RL40_HUMAN	UBA52	physical	15231748
ERCC6_HUMAN	ERCC6	physical	15231748
CACO2_HUMAN	CALCOCO2	physical	15231748
CBLB_HUMAN	CBLB	physical	15231748
TNIP1_HUMAN	TNIP1	physical	15231748
RS27A_HUMAN	RPS27A	physical	15231748
PTPRC_HUMAN	PTPRC	physical	15231748
ZFY16_HUMAN	ZFYVE16	physical	15231748
TAXB1_HUMAN	TAX1BP1	physical	15231748
GGA1_HUMAN	GGA1	physical	15231748
RN168_HUMAN	RNF168	physical	15231748
AN13A_HUMAN	ANKRD13A	physical	15231748
PDC6I_HUMAN	PDCD6IP	physical	15231748
CC127_HUMAN	CCDC127	physical	15231748
OPTN_HUMAN	OPTN	physical	15231748
DCNL1_HUMAN	DCUN1D1	physical	15231748
TM1L2_HUMAN	TOM1L2	physical	15231748
NED4L_HUMAN	NEDD4L	physical	15231748
WWP1_HUMAN	WWP1	physical	15231748
ASCC2_HUMAN	ASCC2	physical	15231748
EPN3_HUMAN	EPN3	physical	15231748
SMUF2_HUMAN	SMURF2	physical	15231748
SMUF1_HUMAN	SMURF1	physical	15231748
UBQL4_HUMAN	UBQLN4	physical	15231748
RN216_HUMAN	RNF216	physical	15231748
GGA3_HUMAN	GGA3	physical	15231748
UBQL2_HUMAN	UBQLN2	physical	15231748
RABX5_HUMAN	RABGEF1	physical	15231748
MYO6_HUMAN	MYO6	physical	15231748
POLI_HUMAN	POLI	physical	15231748
UB2D4_HUMAN	UBE2D4	physical	15231748
AUP1_HUMAN	AUP1	physical	15231748
EPN1_HUMAN	EPN1	physical	15231748
NEMO_HUMAN	IKBKG	physical	15231748
UBP5_HUMAN	USP5	physical	23751493
UBP7_HUMAN	USP7	physical	23751493
UBP2_HUMAN	USP2	physical	23751493
UBP14_HUMAN	USP14	physical	23751493
TF2H1_HUMAN	GTF2H1	physical	23751493
TF2H4_HUMAN	GTF2H4	physical	23751493
AP2M1_HUMAN	AP2M1	physical	23751493
AP2A1_HUMAN	AP2A1	physical	23751493
AP2B1_HUMAN	AP2B1	physical	23751493
AP2S1_HUMAN	AP2S1	physical	23751493
CSK21_HUMAN	CSNK2A1	physical	23751493
CSK2B_HUMAN	CSNK2B	physical	23751493
UBE2N_HUMAN	UBE2N	physical	23751493
UB2V2_HUMAN	UBE2V2	physical	23751493
UBE2O_HUMAN	UBE2O	physical	23751493
PSMD1_HUMAN	PSMD1	physical	23751493
PSMD2_HUMAN	PSMD2	physical	23751493
PSMD3_HUMAN	PSMD3	physical	23751493
PSMD4_HUMAN	PSMD4	physical	23751493
PSMD5_HUMAN	PSMD5	physical	23751493
PSMD6_HUMAN	PSMD6	physical	23751493
PSMD7_HUMAN	PSMD7	physical	23751493
PSMD8_HUMAN	PSMD8	physical	23751493
PSD10_HUMAN	PSMD10	physical	23751493
PSD11_HUMAN	PSMD11	physical	23751493
PSD12_HUMAN	PSMD12	physical	23751493
PSD13_HUMAN	PSMD13	physical	23751493
PSDE_HUMAN	PSMD14	physical	23751493
ZFYV9_HUMAN	ZFYVE9	physical	24377927
STAM2_HUMAN	STAM2	physical	24377927
EPS15_HUMAN	EPS15	physical	24377927
RNF11_HUMAN	RNF11	physical	19549727
UB2D1_HUMAN	UBE2D1	physical	19549727
UB2D2_HUMAN	UBE2D2	physical	19549727
UB2D3_HUMAN	UBE2D3	physical	19549727
UB2E1_HUMAN	UBE2E1	physical	19549727
UB2D4_HUMAN	UBE2D4	physical	21516116
UBB_HUMAN	UBB	physical	28514442
SOAT1_HUMAN	SOAT1	physical	28514442
VAMP3_HUMAN	VAMP3	physical	28514442
KC1G3_HUMAN	CSNK1G3	physical	28514442
BMPR2_HUMAN	BMPR2	physical	28514442
SDCB1_HUMAN	SDCBP	physical	28514442
TR10B_HUMAN	TNFRSF10B	physical	28514442
TNPO2_HUMAN	TNPO2	physical	28514442
AVR2A_HUMAN	ACVR2A	physical	28514442
STX4_HUMAN	STX4	physical	28514442

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 RNF11_HUMAN

Related Literatures of Post-Translational Modification

Myristoylation
Reference	PubMed
"Strategy for comprehensive identification of human N-myristoylatedproteins using an insect cell-free protein synthesis system."; Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,Tsunasawa S., Utsumi T.; Proteomics 10:1780-1793(2010). Cited for: MYRISTOYLATION AT GLY-2.	20213681 [Abstract]
Phosphorylation
Reference	PubMed
"Molecular characterization of ring finger protein 11."; Connor M.K., Azmi P.B., Subramaniam V., Li H., Seth A.K.; Mol. Cancer Res. 3:453-461(2005). Cited for: PROTEIN SEQUENCE OF 70-113 AND 132-154, PHOSPHORYLATION AT THR-135,SUBCELLULAR LOCATION, INTERACTION WITH 14-3-3, AND MUTAGENESIS OFTHR-135.	16123141 [Abstract]