CLIP2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CLIP2_MOUSE
• UniProt AC: Q9Z0H8
• Protein Name: CAP-Gly domain-containing linker protein 2
• Gene Name: Clip2
• Organism: Mus musculus (Mouse).
• Sequence Length: 1047
• Subcellular Localization: Cytoplasm . Cytoplasm, cytoskeleton . Localizes preferentially to the ends of tyrosinated microtubules.
• Protein Description: Seems to link microtubules to dendritic lamellar body (DLB), a membranous organelle predominantly present in bulbous dendritic appendages of neurons linked by dendrodendritic gap junctions. May operate in the control of brain-specific organelle translocations (By similarity)..
• Protein Sequence: MQKPSGLKPPGRGGKHSSPVGRPSVGSASSSVVASTSGSKEGSPLHKQASGPSSSGAATTVSEKPGPKAAEVGDDFLGDFVVGERVWVNGVKPGVVQYLGETQFAPGQWAGVVLDDPVGKNDGAVGGVRYFECPALQGIFTRPSKLTRQPTAEGSGSDTHSVESLTAQNLSLHSGTATPPLTGRVIPLRESVLNSSVKTGNESGSNLSDSGSVKRGDKDLHLGDRVLVGGTKTGVVRYVGETDFAKGEWCGVELDEPLGKNDGAVAGTRYFQCPPKFGLFAPIHKVIRIGFPSTSPAKAKKTKRMAMGVSALTHSPSSSSISSVSSVASSVGGRPSRSGLLTETSSRYARKISGTTALQEALKEKQQHIEQLLAERDLERAEVAKATSHICEVEKEIALLKAQHEQYVAEAEEKLQRARLLVENVRKEKVDLSNQLEEERRKVEDLQFRVEEESITKGDLETQTQLEHARIGELEQSLLLEKAQAERLLRELADNRLTTVAEKSRVLQLEEELSLRRGEIEELQHCLLQSGPPPADHPEAAETLRLRERLLSASKEHQRDSTLLQDKYEHMLKTYQTEVDKLRAANEKYAQEVADLKAKVQQATTENMGLMDNWKSKLDSLASDHQKSLEDLKATLNSGPGAQQKEIGELKALVEGIKMEHQLELGNLQAKHDLETAMHGKEKEGLRQKLQEVQEELAGLQQHWREQLEEQASQHRLELQEAQDQCRDAQLRAQELEGLDVEYRGQAQAIEFLKEQISLAEKKMLDYEMLQRAEAQSRQEAERLREKLLVAENRLQAAESLCSAQHSHVIESSDLSEETIRMKETVEGLQDKLNKRDKEVTALTSQMDMLRAQVSALENKCKSGEKKIDSLLKEKRRLEAELEAVSRKTHDASGQLVHISQELLRKERSLNELRVLLLEANRHSPGPERDLSREVHKAEWRIKEQKLKDDIRGLREKLTGLDKEKSLSEQRRYSLIDPASPPELLKLQHQLVSTEDALRDALNQAQQVERLVEALRGCSDRTQTISNSGSANGIHQPDKAHKQEDKH

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
17	Phosphorylation	PGRGGKHSSPVGRPS CCCCCCCCCCCCCCC	39.56	26160508
18	Phosphorylation	GRGGKHSSPVGRPSV CCCCCCCCCCCCCCC	24.27	26160508
24	Phosphorylation	SSPVGRPSVGSASSS CCCCCCCCCCCCCCC	37.44	26160508
27	Phosphorylation	VGRPSVGSASSSVVA CCCCCCCCCCCCEEE	23.87	26160508
29	Phosphorylation	RPSVGSASSSVVAST CCCCCCCCCCEEECC	25.50	26160508
30	Phosphorylation	PSVGSASSSVVASTS CCCCCCCCCEEECCC	27.20	26160508
31	Phosphorylation	SVGSASSSVVASTSG CCCCCCCCEEECCCC	20.37	26643407
35	Phosphorylation	ASSSVVASTSGSKEG CCCCEEECCCCCCCC	16.11	26643407
36	Phosphorylation	SSSVVASTSGSKEGS CCCEEECCCCCCCCC	27.63	26643407
37	Phosphorylation	SSVVASTSGSKEGSP CCEEECCCCCCCCCC	38.28	26643407
39	Phosphorylation	VVASTSGSKEGSPLH EEECCCCCCCCCCCC	27.57	26643407
43	Phosphorylation	TSGSKEGSPLHKQAS CCCCCCCCCCCCCCC	25.94	25521595
50	Phosphorylation	SPLHKQASGPSSSGA CCCCCCCCCCCCCCC	49.06	21082442
53	Phosphorylation	HKQASGPSSSGAATT CCCCCCCCCCCCCCC	40.43	20415495
54	Phosphorylation	KQASGPSSSGAATTV CCCCCCCCCCCCCCC	35.60	20415495
55	Phosphorylation	QASGPSSSGAATTVS CCCCCCCCCCCCCCC	36.47	22942356
59	Phosphorylation	PSSSGAATTVSEKPG CCCCCCCCCCCCCCC	27.48	25195567
60	Phosphorylation	SSSGAATTVSEKPGP CCCCCCCCCCCCCCC	19.80	25195567
62	Phosphorylation	SGAATTVSEKPGPKA CCCCCCCCCCCCCCH	37.50	20415495
133	S-palmitoylation	GGVRYFECPALQGIF CCEEEEECCCCCCCC	1.39	28680068
147	Phosphorylation	FTRPSKLTRQPTAEG CCCCHHCCCCCCCCC	30.87	26643407
151	Phosphorylation	SKLTRQPTAEGSGSD HHCCCCCCCCCCCCC	29.06	26643407
155	Phosphorylation	RQPTAEGSGSDTHSV CCCCCCCCCCCCCCC	26.99	26643407
157	Phosphorylation	PTAEGSGSDTHSVES CCCCCCCCCCCCCHH	40.82	26643407
159	Phosphorylation	AEGSGSDTHSVESLT CCCCCCCCCCCHHHE	20.11	26643407
161	Phosphorylation	GSGSDTHSVESLTAQ CCCCCCCCCHHHEEC	29.67	26643407
164	Phosphorylation	SDTHSVESLTAQNLS CCCCCCHHHEECCCC	28.94	26643407
166	Phosphorylation	THSVESLTAQNLSLH CCCCHHHEECCCCCC	35.16	26643407
171	Phosphorylation	SLTAQNLSLHSGTAT HHEECCCCCCCCCCC	31.42	26643407
174	Phosphorylation	AQNLSLHSGTATPPL ECCCCCCCCCCCCCC	43.03	26643407
176	Phosphorylation	NLSLHSGTATPPLTG CCCCCCCCCCCCCCC	30.30	24719451
178	Phosphorylation	SLHSGTATPPLTGRV CCCCCCCCCCCCCCE	25.85	26643407
182	Phosphorylation	GTATPPLTGRVIPLR CCCCCCCCCCEEECC	28.81	26643407
191	Phosphorylation	RVIPLRESVLNSSVK CEEECCHHHHCCCCC	26.02	29514104
195	Phosphorylation	LRESVLNSSVKTGNE CCHHHHCCCCCCCCC	32.14	29176673
196	Phosphorylation	RESVLNSSVKTGNES CHHHHCCCCCCCCCC	26.93	27149854
199	Phosphorylation	VLNSSVKTGNESGSN HHCCCCCCCCCCCCC	42.98	27087446
203	Phosphorylation	SVKTGNESGSNLSDS CCCCCCCCCCCCCCC	52.07	25521595
205	Phosphorylation	KTGNESGSNLSDSGS CCCCCCCCCCCCCCC	43.83	25521595
208	Phosphorylation	NESGSNLSDSGSVKR CCCCCCCCCCCCCCC	33.70	25521595
210	Phosphorylation	SGSNLSDSGSVKRGD CCCCCCCCCCCCCCC	29.59	27742792
212	Phosphorylation	SNLSDSGSVKRGDKD CCCCCCCCCCCCCCC	28.54	25521595
293	Phosphorylation	VIRIGFPSTSPAKAK EHHCCCCCCCHHHCH	38.98	25521595
294	Phosphorylation	IRIGFPSTSPAKAKK HHCCCCCCCHHHCHH	38.68	25521595
295	Phosphorylation	RIGFPSTSPAKAKKT HCCCCCCCHHHCHHH	27.48	25521595
310	Phosphorylation	KRMAMGVSALTHSPS HHHHCCHHHHHCCCC	16.31	21183079
313	Phosphorylation	AMGVSALTHSPSSSS HCCHHHHHCCCCCCC	21.74	21183079
315	Phosphorylation	GVSALTHSPSSSSIS CHHHHHCCCCCCCCC	22.65	19060867
317	Phosphorylation	SALTHSPSSSSISSV HHHHCCCCCCCCCCH	45.96	19060867
318	Phosphorylation	ALTHSPSSSSISSVS HHHCCCCCCCCCCHH	31.33	19060867
319	Phosphorylation	LTHSPSSSSISSVSS HHCCCCCCCCCCHHH	35.71	22807455
320	Phosphorylation	THSPSSSSISSVSSV HCCCCCCCCCCHHHH	28.56	20415495
322	Phosphorylation	SPSSSSISSVSSVAS CCCCCCCCCHHHHHH	27.00	20415495
323	Phosphorylation	PSSSSISSVSSVASS CCCCCCCCHHHHHHH	25.09	20415495
336	Phosphorylation	SSVGGRPSRSGLLTE HHCCCCCCCCCCCCH	37.40	29899451
338	Phosphorylation	VGGRPSRSGLLTETS CCCCCCCCCCCCHHC	37.82	-
344	Phosphorylation	RSGLLTETSSRYARK CCCCCCHHCHHHHHH	27.11	29176673
345	Phosphorylation	SGLLTETSSRYARKI CCCCCHHCHHHHHHH	13.44	29176673
346	Phosphorylation	GLLTETSSRYARKIS CCCCHHCHHHHHHHH	36.41	29176673
353	Phosphorylation	SRYARKISGTTALQE HHHHHHHHCHHHHHH	32.87	26824392
355	Phosphorylation	YARKISGTTALQEAL HHHHHHCHHHHHHHH	11.34	26824392
355	O-linked_Glycosylation	YARKISGTTALQEAL HHHHHHCHHHHHHHH	11.34	29562282
356	O-linked_Glycosylation	ARKISGTTALQEALK HHHHHCHHHHHHHHH	28.97	29562282
356	Phosphorylation	ARKISGTTALQEALK HHHHHCHHHHHHHHH	28.97	27742792
498	Phosphorylation	ELADNRLTTVAEKSR HHHHCCCCHHHHHHH	18.91	-
499	Phosphorylation	LADNRLTTVAEKSRV HHHCCCCHHHHHHHH	23.47	-
514	Phosphorylation	LQLEEELSLRRGEIE HHHHHHHHCCCCCHH	24.10	27149854
552	Phosphorylation	RLRERLLSASKEHQR HHHHHHHHHCHHHHH	34.78	20531401
567	Acetylation	DSTLLQDKYEHMLKT HCHHHHHHHHHHHHH	39.31	2413469
589	Phosphorylation	LRAANEKYAQEVADL HHHHHHHHHHHHHHH	13.82	28059163
628	Phosphorylation	LASDHQKSLEDLKAT HHHHHHHHHHHHHHH	30.35	22324799
802	S-palmitoylation	LQAAESLCSAQHSHV HHHHHHHHHHHCCCC	4.39	28680068
860	Acetylation	QVSALENKCKSGEKK HHHHHHHHHHHCHHH	33.39	7721579
862	Acetylation	SALENKCKSGEKKID HHHHHHHHHCHHHHH	64.20	7721591
870	Phosphorylation	SGEKKIDSLLKEKRR HCHHHHHHHHHHHHH	38.79	29899451
873	Acetylation	KKIDSLLKEKRRLEA HHHHHHHHHHHHHHH	67.49	19862125
889	Phosphorylation	LEAVSRKTHDASGQL HHHHHHHCCCCCCCH	24.71	22807455
909	Phosphorylation	ELLRKERSLNELRVL HHHHHCCCHHHHHHH	36.32	29899451
924	Phosphorylation	LLEANRHSPGPERDL HHHHCCCCCCCCCHH	28.45	25521595
973	Phosphorylation	SLSEQRRYSLIDPAS CCCHHHCHHCCCCCC	15.26	25521595
974	Phosphorylation	LSEQRRYSLIDPASP CCHHHCHHCCCCCCC	19.62	25521595
980	Phosphorylation	YSLIDPASPPELLKL HHCCCCCCCHHHHHH	46.50	21082442

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

Oops, there are no upstream regulatory protein records of CLIP2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CLIP2_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CLIP2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CLIP2_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND MASSSPECTROMETRY.
PubMed: 19367708

"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASSSPECTROMETRY.
PubMed: 17114649