dbPTM

SUN2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SUN2_MOUSE
UniProt AC	Q8BJS4
Protein Name	SUN domain-containing protein 2
Gene Name	Sun2
Organism	Mus musculus (Mouse).
Sequence Length	731
Subcellular Localization	Nucleus inner membrane Single-pass type II membrane protein . Nucleus envelope . Endosome membrane Single-pass type II membrane protein . Colocalizes with KASH5 at sites of telomere attachment in meiocytes.
Protein Description	As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Required for nuclear migration in retinal photoreceptor progenitors implicating association with cytoplasmic dynein-dynactin and kinesin motor complexes, and probably B-type lamins; SUN1 and SUN2 seem to act redundantly. The SUN1/2:KASH5 LINC complex couples telomeres to microtubules during meiosis; SUN1 and SUN2 seem to act at least partial redundantly. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for Rab5-GDP and participate in the activation of Rab5..
Protein Sequence	MSRRSQRLTRYSQDDNDGGSSSSGASSVAGSQGTVFKDSPLRTLKRKSSNMKHLSPAPQLGPSSDSHTSYYSESVVRESYIGSPRAVSLARSALLDDHLHSEPYWSGDLRGRRRRGTGGSESSKANGLTAESKASEDFFGSSSGYSSEDDLAGYTDSDQHSSGSRLRSAASRAGSFVWTLVTFPGRLFGLLYWWIGTTWYRLTTAASLLDVFVLTRSRHFSLNLKSFLWFLLLLLLLTGLTYGAWHFYPLGLQTLQPAVVSWWAAKESRKQPEVWESRDASQHFQAEQRVLSRVHSLERRLEALAADFSSNWQKEAIRLERLELRQGAAGHGGGSSLSHEDALSLLEGLVSRREATLKEDLRRDTVAHIQEELATLRAEHHQDSEDLFKKIVQASQESEARVQQLKTEWKSMTQEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVESQFPDWIRQFLLGDRGARSGLLQRDEMHAQLQELENKILTKMAEMQGKSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQRYSEDRIGMVDYALESGGASVISTRCSETYETKTALLSLFGIPLWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALSPNSTISSAPKDFAIFGFDEDLQQEGTLLGTFAYDQDGEPIQTFYFQASKMATYQVVELRILTNWGHPEYTCIYRFRVHGEPAH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MSRRSQRLTRYS ---CCHHHHHCCCCC	20.67	26745281
9	Phosphorylation	SRRSQRLTRYSQDDN CHHHHHCCCCCCCCC	29.74	27742792
11	Phosphorylation	RSQRLTRYSQDDNDG HHHHCCCCCCCCCCC	12.87	27742792
12	Phosphorylation	SQRLTRYSQDDNDGG HHHCCCCCCCCCCCC	24.68	25521595
20	Phosphorylation	QDDNDGGSSSSGASS CCCCCCCCCCCCCCC	32.35	27742792
21	Phosphorylation	DDNDGGSSSSGASSV CCCCCCCCCCCCCCC	31.62	25619855
22	Phosphorylation	DNDGGSSSSGASSVA CCCCCCCCCCCCCCC	34.19	25619855
23	Phosphorylation	NDGGSSSSGASSVAG CCCCCCCCCCCCCCC	40.08	25619855
26	Phosphorylation	GSSSSGASSVAGSQG CCCCCCCCCCCCCCC	28.95	25619855
27	Phosphorylation	SSSSGASSVAGSQGT CCCCCCCCCCCCCCC	18.56	25619855
31	Phosphorylation	GASSVAGSQGTVFKD CCCCCCCCCCCEECC	18.72	25619855
34	Phosphorylation	SVAGSQGTVFKDSPL CCCCCCCCEECCCHH	18.35	25619855
39	Phosphorylation	QGTVFKDSPLRTLKR CCCEECCCHHHHHCH	26.82	25521595
43	Phosphorylation	FKDSPLRTLKRKSSN ECCCHHHHHCHHCCC	44.29	29550500
55	Phosphorylation	SSNMKHLSPAPQLGP CCCCCCCCCCCCCCC	20.80	26824392
63	Phosphorylation	PAPQLGPSSDSHTSY CCCCCCCCCCCCCCC	45.00	25619855
64	Phosphorylation	APQLGPSSDSHTSYY CCCCCCCCCCCCCCC	46.39	25619855
66	Phosphorylation	QLGPSSDSHTSYYSE CCCCCCCCCCCCCCC	30.52	25619855
68	Phosphorylation	GPSSDSHTSYYSESV CCCCCCCCCCCCCCH	23.52	25619855
69	Phosphorylation	PSSDSHTSYYSESVV CCCCCCCCCCCCCHH	19.36	25619855
70	Phosphorylation	SSDSHTSYYSESVVR CCCCCCCCCCCCHHC	16.50	25619855
71	Phosphorylation	SDSHTSYYSESVVRE CCCCCCCCCCCHHCH	13.01	25619855
72	Phosphorylation	DSHTSYYSESVVRES CCCCCCCCCCHHCHH	18.37	25619855
74	Phosphorylation	HTSYYSESVVRESYI CCCCCCCCHHCHHHC	21.70	25619855
79	Phosphorylation	SESVVRESYIGSPRA CCCHHCHHHCCCHHH	16.10	-
80	Phosphorylation	ESVVRESYIGSPRAV CCHHCHHHCCCHHHH	12.44	22802335
83	Phosphorylation	VRESYIGSPRAVSLA HCHHHCCCHHHHHHH	11.14	24453211
88	Phosphorylation	IGSPRAVSLARSALL CCCHHHHHHHHHHHH	18.48	24453211
92	Phosphorylation	RAVSLARSALLDDHL HHHHHHHHHHHCCCC	20.05	25159016
101	Phosphorylation	LLDDHLHSEPYWSGD HHCCCCCCCCCCCCC	46.77	25159016
104	Phosphorylation	DHLHSEPYWSGDLRG CCCCCCCCCCCCCCC	14.25	26643407
106	Phosphorylation	LHSEPYWSGDLRGRR CCCCCCCCCCCCCCC	19.31	25159016
117	Phosphorylation	RGRRRRGTGGSESSK CCCCCCCCCCCCCHH	36.24	27087446
120	Phosphorylation	RRRGTGGSESSKANG CCCCCCCCCCHHHCC	35.33	27087446
122	Phosphorylation	RGTGGSESSKANGLT CCCCCCCCHHHCCCC	38.54	27087446
123	Phosphorylation	GTGGSESSKANGLTA CCCCCCCHHHCCCCC	31.56	21082442
129	Phosphorylation	SSKANGLTAESKASE CHHHCCCCCCCHHCC	29.76	25159016
132	Phosphorylation	ANGLTAESKASEDFF HCCCCCCCHHCCCCC	30.93	25159016
135	Phosphorylation	LTAESKASEDFFGSS CCCCCHHCCCCCCCC	41.24	28833060
141	Phosphorylation	ASEDFFGSSSGYSSE HCCCCCCCCCCCCCH	19.04	28833060
142	Phosphorylation	SEDFFGSSSGYSSED CCCCCCCCCCCCCHH	28.32	28833060
143	Phosphorylation	EDFFGSSSGYSSEDD CCCCCCCCCCCCHHH	43.37	28833060
145	Phosphorylation	FFGSSSGYSSEDDLA CCCCCCCCCCHHHHC	15.80	28833060
146	Phosphorylation	FGSSSGYSSEDDLAG CCCCCCCCCHHHHCC	30.67	28833060
147	Phosphorylation	GSSSGYSSEDDLAGY CCCCCCCCHHHHCCC	36.24	26688217
154	Phosphorylation	SEDDLAGYTDSDQHS CHHHHCCCCCCCCCC	11.19	28833060
155	Phosphorylation	EDDLAGYTDSDQHSS HHHHCCCCCCCCCCC	28.27	28833060
157	Phosphorylation	DLAGYTDSDQHSSGS HHCCCCCCCCCCCCH	31.22	28833060
161	Phosphorylation	YTDSDQHSSGSRLRS CCCCCCCCCCHHHHH	30.66	28833060
162	Phosphorylation	TDSDQHSSGSRLRSA CCCCCCCCCHHHHHH	38.37	28833060
164	Phosphorylation	SDQHSSGSRLRSAAS CCCCCCCHHHHHHHH	30.04	28833060
203	Phosphorylation	GTTWYRLTTAASLLD HHHHHHHHHHHHHHH	12.85	22871156
215	Phosphorylation	LLDVFVLTRSRHFSL HHHHHHHHCCCCCCC	22.69	22871156
264	Phosphorylation	PAVVSWWAAKESRKQ HHHHHHHHHHHHCCC	11.46	24719451
281	Phosphorylation	VWESRDASQHFQAEQ HHHCCCHHHHHHHHH	28.60	28833060
395	Phosphorylation	FKKIVQASQESEARV HHHHHHHHHHHHHHH	19.86	28464351
411	Phosphorylation	QLKTEWKSMTQEAFQ HHHHHHHHHCHHHHH	28.30	21189417
420	Phosphorylation	TQEAFQESSVKELGR CHHHHHHHHHHHHHH	29.64	21189417
455	Phosphorylation	SVADEVGLLPQKIQA CHHHHHCCCHHHHHH	8.34	24719451
476	Phosphorylation	SQFPDWIRQFLLGDR HHCCHHHHHHHHCCC	19.55	24719451
485	Phosphorylation	FLLGDRGARSGLLQR HHHCCCCHHCCCCHH	11.89	24719451
487	Phosphorylation	LGDRGARSGLLQRDE HCCCCHHCCCCHHHH	33.00	-
497	Ubiquitination	LQRDEMHAQLQELEN CHHHHHHHHHHHHHH	15.52	27667366
508	Phosphorylation	ELENKILTKMAEMQG HHHHHHHHHHHHHCC	23.42	-
515	Ubiquitination	TKMAEMQGKSAREAA HHHHHHCCHHHHHHH	25.28	27667366
517	Phosphorylation	MAEMQGKSAREAAAS HHHHCCHHHHHHHHH	39.11	-
545	Ubiquitination	TEEQVHRIVKQALQR CHHHHHHHHHHHHHH	2.47	27667366
547	Ubiquitination	EQVHRIVKQALQRYS HHHHHHHHHHHHHHC	27.73	22790023
650	N-linked_Glycosylation	VPKALSPNSTISSAP CCCCCCCCCCCCCCC	48.70	19656770

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
Oops, there are no upstream regulatory protein records of SUN2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SUN2_MOUSE !!

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 SUN2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
LMNA_MOUSE	Lmna	physical	16380439
SYNE2_MOUSE	Syne2	physical	16380439

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SUN2_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:identification, glycosite occupancy, and membrane orientation."; Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,Wollscheid B.; Mol. Cell. Proteomics 8:2555-2569(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-650, AND MASSSPECTROMETRY.	19656770 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASSSPECTROMETRY.	17242355 [Abstract]