MAGB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MAGB2_HUMAN
• UniProt AC: O15479
• Protein Name: Melanoma-associated antigen B2
• Gene Name: MAGEB2
• Organism: Homo sapiens (Human).
• Sequence Length: 319
• Protein Description: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex..
• Protein Sequence: MPRGQKSKLRAREKRRKARDETRGLNVPQVTEAEEEEAPCCSSSVSGGAASSSPAAGIPQEPQRAPTTAAAAAAGVSSTKSKKGAKSHQGEKNASSSQASTSTKSPSEDPLTRKSGSLVQFLLYKYKIKKSVTKGEMLKIVGKRFREHFPEILKKASEGLSVVFGLELNKVNPNGHTYTFIDKVDLTDEESLLSSWDFPRRKLLMPLLGVIFLNGNSATEEEIWEFLNMLGVYDGEEHSVFGEPWKLITKDLVQEKYLEYKQVPSSDPPRFQFLWGPRAYAETSKMKVLEFLAKVNGTTPCAFPTHYEEALKDEEKAGV

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
42	Phosphorylation	EEEAPCCSSSVSGGA HHCCCCCCCCCCCCC	32.15	18669648
44	Phosphorylation	EAPCCSSSVSGGAAS CCCCCCCCCCCCCCC	12.19	18669648
51	Phosphorylation	SVSGGAASSSPAAGI CCCCCCCCCCCCCCC	30.71	18669648
53	Phosphorylation	SGGAASSSPAAGIPQ CCCCCCCCCCCCCCC	18.96	18669648
67	Phosphorylation	QEPQRAPTTAAAAAA CCCCCCCCHHHHHHH	28.25	23186163
77	Phosphorylation	AAAAAGVSSTKSKKG HHHHHCCCCCCCCCC	31.22	30266825
78	Phosphorylation	AAAAGVSSTKSKKGA HHHHCCCCCCCCCCC	37.13	30266825
79	Phosphorylation	AAAGVSSTKSKKGAK HHHCCCCCCCCCCCC	31.65	30266825
80	Ubiquitination	AAGVSSTKSKKGAKS HHCCCCCCCCCCCCC	63.33	21906983
81	Phosphorylation	AGVSSTKSKKGAKSH HCCCCCCCCCCCCCC	39.42	-
92	Ubiquitination	AKSHQGEKNASSSQA CCCCCCCCCCCCCCC	65.72	21906983
95	Phosphorylation	HQGEKNASSSQASTS CCCCCCCCCCCCCCC	39.66	24732914
96	Phosphorylation	QGEKNASSSQASTST CCCCCCCCCCCCCCC	24.86	23186163
97	Phosphorylation	GEKNASSSQASTSTK CCCCCCCCCCCCCCC	27.54	23186163
100	Phosphorylation	NASSSQASTSTKSPS CCCCCCCCCCCCCCC	18.43	24732914
101	Phosphorylation	ASSSQASTSTKSPSE CCCCCCCCCCCCCCC	43.35	24732914
102	Phosphorylation	SSSQASTSTKSPSED CCCCCCCCCCCCCCC	31.20	24732914
103	Phosphorylation	SSQASTSTKSPSEDP CCCCCCCCCCCCCCC	35.31	24732914
104	Ubiquitination	SQASTSTKSPSEDPL CCCCCCCCCCCCCCC	61.20	21906983
105	Phosphorylation	QASTSTKSPSEDPLT CCCCCCCCCCCCCCC	33.47	29116813
107	Phosphorylation	STSTKSPSEDPLTRK CCCCCCCCCCCCCCC	62.82	24732914
112	Phosphorylation	SPSEDPLTRKSGSLV CCCCCCCCCCCCHHH	41.25	23186163
114	Ubiquitination	SEDPLTRKSGSLVQF CCCCCCCCCCHHHHH	54.67	21906983
115	Phosphorylation	EDPLTRKSGSLVQFL CCCCCCCCCHHHHHH	30.26	28450419
117	Phosphorylation	PLTRKSGSLVQFLLY CCCCCCCHHHHHHHH	32.24	28450419
124	Phosphorylation	SLVQFLLYKYKIKKS HHHHHHHHHHHCCCC	17.89	26074081
131	Phosphorylation	YKYKIKKSVTKGEML HHHHCCCCCCHHHHH	29.98	29083192
133	Phosphorylation	YKIKKSVTKGEMLKI HHCCCCCCHHHHHHH	40.18	29083192
134	Ubiquitination	KIKKSVTKGEMLKIV HCCCCCCHHHHHHHH	51.20	-
139	Ubiquitination	VTKGEMLKIVGKRFR CCHHHHHHHHHHHHH	33.75	-
154	Ubiquitination	EHFPEILKKASEGLS HHHHHHHHHHHCCCE	52.54	-
155	Ubiquitination	HFPEILKKASEGLSV HHHHHHHHHHCCCEE	54.41	-
170	Ubiquitination	VFGLELNKVNPNGHT EEEEEEEEECCCCCE	56.89	-
191	Phosphorylation	VDLTDEESLLSSWDF CCCCCHHHHHHHCCC	32.34	27050516
250	Succinylation	EPWKLITKDLVQEKY CCCHHHCHHHHHHHH	41.91	23954790
250	Ubiquitination	EPWKLITKDLVQEKY CCCHHHCHHHHHHHH	41.91	-
250	2-Hydroxyisobutyrylation	EPWKLITKDLVQEKY CCCHHHCHHHHHHHH	41.91	-
256	Ubiquitination	TKDLVQEKYLEYKQV CHHHHHHHHHHHCCC	37.74	21906983
256	Acetylation	TKDLVQEKYLEYKQV CHHHHHHHHHHHCCC	37.74	26822725
261	Ubiquitination	QEKYLEYKQVPSSDP HHHHHHHCCCCCCCC	35.13	21906983
285	Ubiquitination	RAYAETSKMKVLEFL HHHHHHCHHHHHHHH	50.59	-
287	Ubiquitination	YAETSKMKVLEFLAK HHHHCHHHHHHHHHH	47.61	2190698
294	Ubiquitination	KVLEFLAKVNGTTPC HHHHHHHHHCCCCCC	38.08	-
307	Phosphorylation	PCAFPTHYEEALKDE CCCCCHHHHHHHHHH	20.24	27642862
312	Ubiquitination	THYEEALKDEEKAGV HHHHHHHHHHHHHCC	70.87	-
312	Acetylation	THYEEALKDEEKAGV HHHHHHHHHHHHHCC	70.87	-
316	Ubiquitination	EALKDEEKAGV---- HHHHHHHHHCC----	48.68	-

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

Oops, there are no upstream regulatory protein records of MAGB2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MAGB2_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 MAGB2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBP7_HUMAN	USP7	physical	17353931
RS3A_HUMAN	RPS3A	physical	17353931
RL23A_HUMAN	RPL23A	physical	17353931
RS19_HUMAN	RPS19	physical	17353931
RL31_HUMAN	RPL31	physical	17353931
RS14_HUMAN	RPS14	physical	17353931
RS16_HUMAN	RPS16	physical	17353931
RL26_HUMAN	RPL26	physical	17353931
RL36_HUMAN	RPL36	physical	17353931
RL34_HUMAN	RPL34	physical	17353931
RL21_HUMAN	RPL21	physical	17353931
RS9_HUMAN	RPS9	physical	17353931
CSK2B_HUMAN	CSNK2B	physical	17353931
LXN_HUMAN	LXN	physical	17353931
RL28_HUMAN	RPL28	physical	17353931
RS11_HUMAN	RPS11	physical	17353931
RS26_HUMAN	RPS26	physical	17353931
RL36A_HUMAN	RPL36A	physical	17353931
TIF1B_HUMAN	TRIM28	physical	20864041
ANM5_HUMAN	PRMT5	physical	23455924
RPGR1_HUMAN	RPGRIP1	physical	25416956
HDAC1_HUMAN	HDAC1	physical	26468294

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

Phosphorylation

"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-77 AND SER-105, AND MASSSPECTROMETRY.
PubMed: 18669648