RN157_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RN157_HUMAN
• UniProt AC: Q96PX1
• Protein Name: E3 ubiquitin ligase RNF157 {ECO:0000303|PubMed:25342469}
• Gene Name: RNF157
• Organism: Homo sapiens (Human).
• Sequence Length: 679
• Subcellular Localization: Cytoplasm .
• Protein Description: E3 ubiquitin ligase that ubiquitinates APBB1 for its degradation by the proteasome and thus prevents apoptosis and promotes survival of neurons. [PubMed: 25342469 Has a dual role in neurons as it is also required for dendrite growth and maintenance for which its ligase activity is not critical]
• Protein Sequence: MGALTSRQHAGVEEVDIPSNSVYRYPPKSGSYFASHFIMGGEKFDSTHPEGYLFGENSDLNFLGNRPVVFPYAAPPPQEPVKTLRSLVNIRKDTLRLVKCAEEVKSPGEEASKAKVHYNVEFTFDTDARVAITIYYQATEEFQNGIASYIPKDNSLQSETVQYKRGVCQQFCLPSHTVDPSEWAEEELGFDLDREVYPLVVHAVVDEGDEYFGHCHVLLGTFEKHTDGTFCVKPLKQKQVVDGVSYLLQEIYGIENKYNTQDSKVAEDEVSDNSAECVVCLSDVRDTLILPCRHLCLCNTCADTLRYQANNCPICRLPFRALLQIRAMRKKLGPLSPTSFNPIISSQTSDSEEHPSSENIPPGYEVVSLLEALNGPLTPSPAVPPLHVLGDGHLSGMLPSYGSDGHLPPVRTISPLDRLSDSSSQGLKLKKSLSKSTSQNSSVLHEEEDEHSCSESETQLSQRPSVQHLGEECGVTPESENLTLSSSGAIDQSSCTGTPLSSTISSPEGPASSSLAQSVMSMASSQISTDTVSSMSGSYIAPGTEEEGEALSSPQPASRAPSEEGEGLPAESPDSNFAGLPAGEQDAEGNDVIEEEDGSPTQEGQRTCAFLGMECDNNNDFDIASVKALDNKLCSEVCLPGAWQADDNAVSRNAQRRRLSSSSLEDSETRPCVWGPLAV

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
2	Myristoylation	------MGALTSRQH ------CCCCCCCCC	29.32	20213681
2	N-myristoyl glycine	------MGALTSRQH ------CCCCCCCCC	29.32	-
106	Phosphorylation	KCAEEVKSPGEEASK HHHHHCCCCCHHHHC	43.23	28270605
112	Phosphorylation	KSPGEEASKAKVHYN CCCCHHHHCCEEEEE	36.10	28270605
164	Ubiquitination	QSETVQYKRGVCQQF CCCCEECCCCCCHHH	26.11	32142685
245	Phosphorylation	KQVVDGVSYLLQEIY CCHHCHHHHHHHHHH	18.65	21955146
246	Phosphorylation	QVVDGVSYLLQEIYG CHHCHHHHHHHHHHC	14.71	21955146
252	Phosphorylation	SYLLQEIYGIENKYN HHHHHHHHCCCCCCC	15.99	21955146
518	Phosphorylation	ASSSLAQSVMSMASS CCHHHHHHHHHHHHC	17.74	24275569
521	Phosphorylation	SLAQSVMSMASSQIS HHHHHHHHHHHCCCC	14.72	24275569
528	Phosphorylation	SMASSQISTDTVSSM HHHHCCCCCCCHHHC	16.76	24275569
531	Phosphorylation	SSQISTDTVSSMSGS HCCCCCCCHHHCCCC	23.52	24275569
538	Phosphorylation	TVSSMSGSYIAPGTE CHHHCCCCEECCCCH	13.17	24275569
660	Phosphorylation	NAQRRRLSSSSLEDS HHHHHHHCCCCCCCC	26.77	28655764
661	Phosphorylation	AQRRRLSSSSLEDSE HHHHHHCCCCCCCCC	28.65	22817900
662	Phosphorylation	QRRRLSSSSLEDSET HHHHHCCCCCCCCCC	35.25	22817900
663	Phosphorylation	RRRLSSSSLEDSETR HHHHCCCCCCCCCCC	37.41	14702039
669	Phosphorylation	SSLEDSETRPCVWGP CCCCCCCCCCCCCCC	43.81	24719451

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

Oops, there are no upstream regulatory protein records of RN157_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
660	S	Phosphorylation	Phosphorylation at Ser-660, Ser-661, Ser-662 and Ser-663 downstream of the PI3K and MAPK pathways influences the E3 ligase activity and stability of RNF157 during the cell cycle in an anaphase-promoting complex/cyclosome-CDH1-dependent manner.	28655764
661	S	Phosphorylation	Phosphorylation at Ser-660, Ser-661, Ser-662 and Ser-663 downstream of the PI3K and MAPK pathways influences the E3 ligase activity and stability of RNF157 during the cell cycle in an anaphase-promoting complex/cyclosome-CDH1-dependent manner.	28655764
662	S	Phosphorylation	Phosphorylation at Ser-660, Ser-661, Ser-662 and Ser-663 downstream of the PI3K and MAPK pathways influences the E3 ligase activity and stability of RNF157 during the cell cycle in an anaphase-promoting complex/cyclosome-CDH1-dependent manner.	28655764
663	S	Phosphorylation	Phosphorylation at Ser-660, Ser-661, Ser-662 and Ser-663 downstream of the PI3K and MAPK pathways influences the E3 ligase activity and stability of RNF157 during the cell cycle in an anaphase-promoting complex/cyclosome-CDH1-dependent manner.	28655764

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RN157_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATRN_HUMAN	ATRN	physical	28655764
MEGF8_HUMAN	MEGF8	physical	28655764
TECR_HUMAN	TECR	physical	28655764
MSI2H_HUMAN	MSI2	physical	28655764
PLRG1_HUMAN	PLRG1	physical	28655764
BYST_HUMAN	BYSL	physical	28655764
MTEF3_HUMAN	MTERF3	physical	28655764
PSA1_HUMAN	PSMA1	physical	28655764
RT18B_HUMAN	MRPS18B	physical	28655764
PRP4_HUMAN	PRPF4	physical	28655764
FAKD2_HUMAN	FASTKD2	physical	28655764
TXTP_HUMAN	SLC25A1	physical	28655764
SMU1_HUMAN	SMU1	physical	28655764
CNOT9_HUMAN	RQCD1	physical	28655764
RT02_HUMAN	MRPS2	physical	28655764
MAGT1_HUMAN	MAGT1	physical	28655764
CHD1_HUMAN	CHD1	physical	28655764
FXR2_HUMAN	FXR2	physical	28655764
EMD_HUMAN	EMD	physical	28655764
PSMD8_HUMAN	PSMD8	physical	28655764
HDAC1_HUMAN	HDAC1	physical	28655764
RAN_HUMAN	RAN	physical	28655764
DHB12_HUMAN	HSD17B12	physical	28655764
TXND5_HUMAN	TXNDC5	physical	28655764
RM19_HUMAN	MRPL19	physical	28655764

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.

Related Literatures of Post-Translational Modification

Myristoylation

"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.
PubMed: 20213681