dbPTM

SUN2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SUN2_HUMAN
UniProt AC	Q9UH99
Protein Name	SUN domain-containing protein 2
Gene Name	SUN2
Organism	Homo sapiens (Human).
Sequence Length	717
Subcellular Localization	Nucleus inner membrane Single-pass type II membrane protein . Nucleus envelope . Endosome membrane Single-pass type II membrane protein .
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	MSRRSQRLTRYSQGDDDGSSSSGGSSVAGSQSTLFKDSPLRTLKRKSSNMKRLSPAPQLGPSSDAHTSYYSESLVHESWFPPRSSLEELHGDANWGEDLRVRRRRGTGGSESSRASGLVGRKATEDFLGSSSGYSSEDDYVGYSDVDQQSSSSRLRSAVSRAGSLLWMVATSPGRLFRLLYWWAGTTWYRLTTAASLLDVFVLTRRFSSLKTFLWFLLPLLLLTCLTYGAWYFYPYGLQTFHPALVSWWAAKDSRRPDEGWEARDSSPHFQAEQRVMSRVHSLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREAALKEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRIGLADYALESGGASVISTRCSETYETKTALLSLFGIPLWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALSPNSTISSAPKDFAIFGFDEDLQQEGTLLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEPAH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MSRRSQRLTRYS ---CCHHHHHCHHCC	20.67	27282143
9	Phosphorylation	SRRSQRLTRYSQGDD CHHHHHCHHCCCCCC	29.74	23401153
9 (in isoform 2)	Phosphorylation	-	29.74	27251275
11	Phosphorylation	RSQRLTRYSQGDDDG HHHHCHHCCCCCCCC	10.50	23927012
12 (in isoform 2)	Phosphorylation	-	25.13	27251275
12	Phosphorylation	SQRLTRYSQGDDDGS HHHCHHCCCCCCCCC	25.13	23927012
19	Phosphorylation	SQGDDDGSSSSGGSS CCCCCCCCCCCCCCC	33.76	23927012
20	Phosphorylation	QGDDDGSSSSGGSSV CCCCCCCCCCCCCCC	33.77	23401153
21	Phosphorylation	GDDDGSSSSGGSSVA CCCCCCCCCCCCCCC	34.40	23927012
22	Phosphorylation	DDDGSSSSGGSSVAG CCCCCCCCCCCCCCC	49.47	23927012
22 (in isoform 2)	Phosphorylation	-	49.47	27251275
25	Phosphorylation	GSSSSGGSSVAGSQS CCCCCCCCCCCCCCC	25.76	23927012
26	Phosphorylation	SSSSGGSSVAGSQST CCCCCCCCCCCCCCC	21.18	22167270
30	Phosphorylation	GGSSVAGSQSTLFKD CCCCCCCCCCCCCCC	15.95	23401153
30 (in isoform 2)	Phosphorylation	-	15.95	27251275
32	Phosphorylation	SSVAGSQSTLFKDSP CCCCCCCCCCCCCCC	28.86	22167270
33	Phosphorylation	SVAGSQSTLFKDSPL CCCCCCCCCCCCCCC	28.69	22167270
38 (in isoform 2)	Phosphorylation	-	26.82	27251275
38	Phosphorylation	QSTLFKDSPLRTLKR CCCCCCCCCCHHHHH	26.82	22167270
42	Phosphorylation	FKDSPLRTLKRKSSN CCCCCCHHHHHHCCC	44.29	23401153
54	Phosphorylation	SSNMKRLSPAPQLGP CCCCCCCCCCCCCCC	24.05	23927012
62	Phosphorylation	PAPQLGPSSDAHTSY CCCCCCCCCCCCCHH	38.77	29978859
63	Phosphorylation	APQLGPSSDAHTSYY CCCCCCCCCCCCHHC	41.78	28464451
67	Phosphorylation	GPSSDAHTSYYSESL CCCCCCCCHHCCCCC	21.83	23927012
68	Phosphorylation	PSSDAHTSYYSESLV CCCCCCCHHCCCCCC	16.53	27080861
69	Phosphorylation	SSDAHTSYYSESLVH CCCCCCHHCCCCCCC	16.50	27080861
71	Phosphorylation	DAHTSYYSESLVHES CCCCHHCCCCCCCCC	16.69	26657352
73	Phosphorylation	HTSYYSESLVHESWF CCHHCCCCCCCCCCC	29.74	-
84	Phosphorylation	ESWFPPRSSLEELHG CCCCCCCHHHHHHHC	45.08	23663014
85 (in isoform 2)	Phosphorylation	-	40.87	27251275
85	Phosphorylation	SWFPPRSSLEELHGD CCCCCCHHHHHHHCC	40.87	23663014
107	Phosphorylation	RVRRRRGTGGSESSR CHHHHCCCCCCHHHH	36.24	27273156
110	Phosphorylation	RRRGTGGSESSRASG HHCCCCCCHHHHHCC	35.33	23401153
112	Phosphorylation	RGTGGSESSRASGLV CCCCCCHHHHHCCCC	27.16	27273156
113	Phosphorylation	GTGGSESSRASGLVG CCCCCHHHHHCCCCC	28.02	23401153
116 (in isoform 2)	Phosphorylation	-	31.39	27251275
116	Phosphorylation	GSESSRASGLVGRKA CCHHHHHCCCCCCCC	31.39	23401153
124 (in isoform 2)	Phosphorylation	-	38.84	-
124	Phosphorylation	GLVGRKATEDFLGSS CCCCCCCCHHHCCCC	38.84	28450419
130 (in isoform 2)	Phosphorylation	-	24.39	22210691
130	Phosphorylation	ATEDFLGSSSGYSSE CCHHHCCCCCCCCCC	24.39	28796482
131	Phosphorylation	TEDFLGSSSGYSSED CHHHCCCCCCCCCCC	26.45	23401153
132	Phosphorylation	EDFLGSSSGYSSEDD HHHCCCCCCCCCCCC	43.37	28796482
134	Phosphorylation	FLGSSSGYSSEDDYV HCCCCCCCCCCCCCC	15.80	28796482
135	Phosphorylation	LGSSSGYSSEDDYVG CCCCCCCCCCCCCCC	30.67	28796482
136 (in isoform 2)	Phosphorylation	-	36.24	22210691
136	Phosphorylation	GSSSGYSSEDDYVGY CCCCCCCCCCCCCCC	36.24	28796482
140	Phosphorylation	GYSSEDDYVGYSDVD CCCCCCCCCCCCCCC	14.22	26657352
143	Phosphorylation	SEDDYVGYSDVDQQS CCCCCCCCCCCCCCC	7.52	28796482
144	Phosphorylation	EDDYVGYSDVDQQSS CCCCCCCCCCCCCCC	25.81	28796482
150	Phosphorylation	YSDVDQQSSSSRLRS CCCCCCCCCHHHHHH	26.93	28450419
151	Phosphorylation	SDVDQQSSSSRLRSA CCCCCCCCHHHHHHH	28.17	28450419
152 (in isoform 2)	Phosphorylation	-	25.40	-
152	Phosphorylation	DVDQQSSSSRLRSAV CCCCCCCHHHHHHHH	25.40	28450419
153	Phosphorylation	VDQQSSSSRLRSAVS CCCCCCHHHHHHHHH	36.96	28450419
154 (in isoform 2)	Phosphorylation	-	35.75	-
157	Phosphorylation	SSSSRLRSAVSRAGS CCHHHHHHHHHHHHH	37.30	22210691
160	Phosphorylation	SRLRSAVSRAGSLLW HHHHHHHHHHHHHHH	19.01	22210691
266	Phosphorylation	EGWEARDSSPHFQAE CCCCCCCCCCCHHHH	39.97	23401153
267	Phosphorylation	GWEARDSSPHFQAEQ CCCCCCCCCCHHHHH	27.04	21712546
282	Phosphorylation	RVMSRVHSLERRLEA HHHHHHHHHHHHHHH	29.12	24719451
300	Ubiquitination	EFSSNWQKEAMRLER HHCHHHHHHHHHHHH	38.77	21906983
324	Phosphorylation	QGGGGGLSHEDTLAL CCCCCCCCHHHHHHH	28.27	22210691
328	Phosphorylation	GGLSHEDTLALLEGL CCCCHHHHHHHHHHH	15.79	22210691
335	Ubiquitination	TLALLEGLVSRREAA HHHHHHHHHHHHHHH	2.00	21906983
344	Ubiquitination	SRREAALKEDFRRET HHHHHHHHHHHHHHH	50.97	-
375	Ubiquitination	QDSEDLFKKIVRASQ HCCHHHHHHHHHHHH	49.22	-
381	Phosphorylation	FKKIVRASQESEARI HHHHHHHHHHHHHHH	24.74	-
392	Ubiquitination	EARIQQLKSEWQSMT HHHHHHHHHHHHHCC	41.83	21906983
399	O-linked_Glycosylation	KSEWQSMTQESFQES HHHHHHCCHHHHHHH	34.14	OGP
409	Ubiquitination	SFQESSVKELRRLED HHHHHHHHHHHHHHH	53.64	21906983
427	Ubiquitination	GLQQELAALALKQSS HHHHHHHHHHHHCCH	13.14	21906983
444	Ubiquitination	EEVGLLPQQIQAVRD HHHCCCHHHHHHHHH	53.64	21906983
491	Ubiquitination	QLRELESKILTHVAE HHHHHHHHHHHHHHH	32.15	-
502	Ubiquitination	HVAEMQGKSAREAAA HHHHHCCCCHHHHHH	24.85	2190698
510	Phosphorylation	SAREAAASLSLTLQK CHHHHHHHHHHEEEE	17.48	22985185
514	Phosphorylation	AAASLSLTLQKEGVI HHHHHHHEEEECCCC	24.62	19413330
533	Ubiquitination	EQVHHIVKQALQRYS HHHHHHHHHHHHHHC	29.29	-
537	Ubiquitination	HIVKQALQRYSEDRI HHHHHHHHHHCCCCC	45.33	21906983
549	Phosphorylation	DRIGLADYALESGGA CCCCHHHHHHHCCCC	13.89	-
553	Phosphorylation	LADYALESGGASVIS HHHHHHHCCCCEEEE	43.29	27251275
557	Phosphorylation	ALESGGASVISTRCS HHHCCCCEEEECCCC	24.21	27251275
560	Phosphorylation	SGGASVISTRCSETY CCCCEEEECCCCCCC	13.98	27251275
561	Phosphorylation	GGASVISTRCSETYE CCCEEEECCCCCCCC	25.27	27251275
564	Phosphorylation	SVISTRCSETYETKT EEEECCCCCCCCHHH	29.68	27251275
566	Phosphorylation	ISTRCSETYETKTAL EECCCCCCCCHHHHH	15.46	27251275
567	Phosphorylation	STRCSETYETKTALL ECCCCCCCCHHHHHH	19.97	27251275
569	Phosphorylation	RCSETYETKTALLSL CCCCCCCHHHHHHHH	24.23	27251275
574 (in isoform 2)	Phosphorylation	-	3.76	27251275
581 (in isoform 2)	Phosphorylation	-	7.19	27251275
622	O-linked_Glycosylation	LSARIRPTAVTLEHV EEEEECCCEEEHHCC	24.74	OGP
634	O-linked_Glycosylation	EHVPKALSPNSTISS HCCCCCCCCCCCCCC	27.22	30379171
636	N-linked_Glycosylation	VPKALSPNSTISSAP CCCCCCCCCCCCCCC	48.70	19159218
637	Phosphorylation	PKALSPNSTISSAPK CCCCCCCCCCCCCCC	30.42	23312004
638	Phosphorylation	KALSPNSTISSAPKD CCCCCCCCCCCCCCC	31.36	23312004
640	Phosphorylation	LSPNSTISSAPKDFA CCCCCCCCCCCCCEE	22.12	23312004
641	O-linked_Glycosylation	SPNSTISSAPKDFAI CCCCCCCCCCCCEEE	44.75	30379171
641	Phosphorylation	SPNSTISSAPKDFAI CCCCCCCCCCCCEEE	44.75	23312004
683	O-linked_Glycosylation	TFHFQAPTMATYQVV EEEEECCCCCEEEEE	23.58	OGP

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
12	S	Phosphorylation	Kinase	ATR	Q13535	PSP
12	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
12	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
12	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
54	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
54	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
54	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
116	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
116	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
116	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SUN2_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 SUN2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SYNE1_HUMAN	SYNE1	physical	22632968
SYNE2_HUMAN	SYNE2	physical	22632968
FBW1B_HUMAN	FBXW11	physical	28514442
FKB14_HUMAN	FKBP14	physical	28514442
DHRS4_HUMAN	DHRS4	physical	28514442
RAB5A_HUMAN	RAB5A	physical	28514442
RAB5C_HUMAN	RAB5C	physical	28514442
PK3CA_HUMAN	PIK3CA	physical	28514442
UGPA_HUMAN	UGP2	physical	28514442
PI42C_HUMAN	PIP4K2C	physical	28514442
PI42B_HUMAN	PIP4K2B	physical	28514442
MAP2_HUMAN	METAP2	physical	28514442
POTEF_HUMAN	POTEF	physical	28514442
PI42A_HUMAN	PIP4K2A	physical	28514442
ZO1_HUMAN	TJP1	physical	28514442
CHMP6_HUMAN	CHMP6	physical	28514442
ACADS_HUMAN	ACADS	physical	28514442
LMNA_HUMAN	LMNA	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 SUN2_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-636, AND MASSSPECTROMETRY.	19159218 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, AND MASSSPECTROMETRY.	17081983 [Abstract]
"A mass spectrometry-based proteomic approach for identification ofserine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies: identification of a novel protein, Frigg, as aprotein kinase A substrate."; Gronborg M., Kristiansen T.Z., Stensballe A., Andersen J.S., Ohara O.,Mann M., Jensen O.N., Pandey A.; Mol. Cell. Proteomics 1:517-527(2002). Cited for: PHOSPHORYLATION AT SER-12; SER-54 AND SER-116.	12239280 [Abstract]