dbPTM

DESM_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DESM_MOUSE
UniProt AC	P31001
Protein Name	Desmin
Gene Name	Des
Organism	Mus musculus (Mouse).
Sequence Length	469
Subcellular Localization	Cytoplasm, myofibril, sarcomere, Z line . Cytoplasm . Cell membrane, sarcolemma . Nucleus . Localizes in the intercalated disks which occur at the Z line of cardiomyocytes (By similarity). Localizes in the nucleus exclusively in differentiating cardi
Protein Description	Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity (By similarity). In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures. [PubMed: 25394388 May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction]
Protein Sequence	MSQAYSSSQRVSSYRRTFGGAPGFSLGSPLSSPVFPRAGFGTKGSSSSMTSRVYQVSRTSGGAGGLGSLRSSRLGTTRAPSYGAGELLDFSLADAVNQEFLATRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAELYEEEMRELRRQVEVLTNQRARVDVERDNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEANGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRINLPIQTFSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSQAYSSSQ ------CCCCCCCHH	24.42	27742792
5	Phosphorylation	---MSQAYSSSQRVS ---CCCCCCCHHCHH	11.05	26160508
6	Phosphorylation	--MSQAYSSSQRVSS --CCCCCCCHHCHHH	26.91	17381546
7	Phosphorylation	-MSQAYSSSQRVSSY -CCCCCCCHHCHHHH	20.15	17381546
8	Phosphorylation	MSQAYSSSQRVSSYR CCCCCCCHHCHHHHH	18.96	17381546
12	Phosphorylation	YSSSQRVSSYRRTFG CCCHHCHHHHHCCCC	24.68	26160508
13	Phosphorylation	SSSQRVSSYRRTFGG CCHHCHHHHHCCCCC	21.57	27742792
16	Methylation	QRVSSYRRTFGGAPG HCHHHHHCCCCCCCC	26.61	24129315
17	Phosphorylation	RVSSYRRTFGGAPGF CHHHHHCCCCCCCCC	20.03	27180971
25	Phosphorylation	FGGAPGFSLGSPLSS CCCCCCCCCCCCCCC	37.42	28542873
28	Phosphorylation	APGFSLGSPLSSPVF CCCCCCCCCCCCCCC	28.14	26824392
31	Phosphorylation	FSLGSPLSSPVFPRA CCCCCCCCCCCCCCC	35.66	23926118
32	Phosphorylation	SLGSPLSSPVFPRAG CCCCCCCCCCCCCCC	32.53	26824392
37	Asymmetric dimethylarginine	LSSPVFPRAGFGTKG CCCCCCCCCCCCCCC	35.56	-
37	Methylation	LSSPVFPRAGFGTKG CCCCCCCCCCCCCCC	35.56	24129315
43	Methylation	PRAGFGTKGSSSSMT CCCCCCCCCCCCCCC	58.12	-
43	Ubiquitination	PRAGFGTKGSSSSMT CCCCCCCCCCCCCCC	58.12	22790023
45	Phosphorylation	AGFGTKGSSSSMTSR CCCCCCCCCCCCCEE	28.71	23737553
46	Phosphorylation	GFGTKGSSSSMTSRV CCCCCCCCCCCCEEE	34.79	23737553
47	Phosphorylation	FGTKGSSSSMTSRVY CCCCCCCCCCCEEEE	26.31	23737553
48	Phosphorylation	GTKGSSSSMTSRVYQ CCCCCCCCCCEEEEE	28.20	23737553
50	Phosphorylation	KGSSSSMTSRVYQVS CCCCCCCCEEEEEEE	18.48	23737553
51	Phosphorylation	GSSSSMTSRVYQVSR CCCCCCCEEEEEEEC	15.88	21082442
57	Phosphorylation	TSRVYQVSRTSGGAG CEEEEEEECCCCCCC	17.83	23737553
58	ADP-ribosylation	SRVYQVSRTSGGAGG EEEEEEECCCCCCCC	33.77	-
58	ADP-ribosylation	SRVYQVSRTSGGAGG EEEEEEECCCCCCCC	33.77	-
59	Phosphorylation	RVYQVSRTSGGAGGL EEEEEECCCCCCCCC	24.98	24899341
60	Phosphorylation	VYQVSRTSGGAGGLG EEEEECCCCCCCCCH	33.83	24899341
68	Phosphorylation	GGAGGLGSLRSSRLG CCCCCCHHHHCCCCC	26.17	27742792
70	Methylation	AGGLGSLRSSRLGTT CCCCHHHHCCCCCCC	33.99	24129315
71	Phosphorylation	GGLGSLRSSRLGTTR CCCHHHHCCCCCCCC	25.71	28464351
76	Phosphorylation	LRSSRLGTTRAPSYG HHCCCCCCCCCCCCC	20.08	22817900
77	Phosphorylation	RSSRLGTTRAPSYGA HCCCCCCCCCCCCCH	24.04	9875213
81	Phosphorylation	LGTTRAPSYGAGELL CCCCCCCCCCHHHHH	34.90	27180971
82	Phosphorylation	GTTRAPSYGAGELLD CCCCCCCCCHHHHHH	15.22	28059163
91	Phosphorylation	AGELLDFSLADAVNQ HHHHHHCHHHHHHCH	23.47	-
108	Ubiquitination	LATRTNEKVELQELN HHHCCCCCCCHHHHH	42.98	22790023
124	Ubiquitination	RFANYIEKVRFLEQQ HHHHHHHHHHHHHHH	29.20	22790023
192	Ubiquitination	DLQRLKAKLQEEIQL HHHHHHHHHHHHHHH	49.46	22790023
240	Ubiquitination	EEIAFLKKVHEEEIR HHHHHHHHHCHHHHH	51.47	22790023
286	Ubiquitination	QYETIAAKNISEAEE HHHHHHHCCHHHHHH	45.88	22790023
289	Phosphorylation	TIAAKNISEAEEWYK HHHHCCHHHHHHHHH	39.90	27742792
296	Ubiquitination	SEAEEWYKSKVSDLT HHHHHHHHHHHHHHH	44.89	22790023
297	Phosphorylation	EAEEWYKSKVSDLTQ HHHHHHHHHHHHHHH	23.69	27742792
300	Phosphorylation	EWYKSKVSDLTQAAN HHHHHHHHHHHHHHH	30.55	24899341
303	Phosphorylation	KSKVSDLTQAANKNN HHHHHHHHHHHHHCH	22.58	27742792
308	Ubiquitination	DLTQAANKNNDALRQ HHHHHHHHCHHHHHH	53.02	22790023
317	Ubiquitination	NDALRQAKQEMMEYR HHHHHHHHHHHHHHH	38.15	22790023
329	Phosphorylation	EYRHQIQSYTCEIDA HHHHHHHHCCCHHHH	24.84	27742792
330	Phosphorylation	YRHQIQSYTCEIDAL HHHHHHHCCCHHHHH	10.07	-
332	S-nitrosocysteine	HQIQSYTCEIDALKG HHHHHCCCHHHHHCC	3.07	-
332	S-nitrosylation	HQIQSYTCEIDALKG HHHHHCCCHHHHHCC	3.07	21278135
338	Ubiquitination	TCEIDALKGTNDSLM CCHHHHHCCCCHHHH	66.46	22790023
340	Phosphorylation	EIDALKGTNDSLMRQ HHHHHCCCCHHHHHH	33.98	23737553
343	Phosphorylation	ALKGTNDSLMRQMRE HHCCCCHHHHHHHHH	26.57	23737553
357	Phosphorylation	ELEDRFASEANGYQD HHHHHHHHHHCCCHH	34.23	27742792
362	Phosphorylation	FASEANGYQDNIARL HHHHHCCCHHHHHHH	16.70	-
387	Phosphorylation	MARHLREYQDLLNVK HHHHHHHHHHHHCHH	10.82	25367039
406	Ubiquitination	VEIATYRKLLEGEES HHHHHHHHHHCCCCC	47.19	-
413	Phosphorylation	KLLEGEESRINLPIQ HHHCCCCCCCCCCCC	33.87	28066266
421	Phosphorylation	RINLPIQTFSALNFR CCCCCCCCEECCCCC	21.93	23984901
423	Phosphorylation	NLPIQTFSALNFRET CCCCCCEECCCCCCC	34.92	23737553
430	Phosphorylation	SALNFRETSPEQRGS ECCCCCCCCHHHCCC	45.38	24899341
431	Phosphorylation	ALNFRETSPEQRGSE CCCCCCCCHHHCCCC	22.99	27742792
437	Phosphorylation	TSPEQRGSEVHTKKT CCHHHCCCCCEECEE	38.34	24899341
441	Phosphorylation	QRGSEVHTKKTVMIK HCCCCCEECEEEEEE	39.14	24899341
444	Phosphorylation	SEVHTKKTVMIKTIE CCCEECEEEEEEEEE	19.50	22817900
448	Ubiquitination	TKKTVMIKTIETRDG ECEEEEEEEEECCCC	25.92	22790023
459	O-linked_Glycosylation	TRDGEVVSEATQQQH CCCCCEECHHHHHHH	27.04	30016717
459	Phosphorylation	TRDGEVVSEATQQQH CCCCCEECHHHHHHH	27.04	27742792
462	Phosphorylation	GEVVSEATQQQHEVL CCEECHHHHHHHHCC	23.90	27742792

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
7	S	Phosphorylation	Kinase	CDK1	P06493	PSP
7	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot
12	S	Phosphorylation	Kinase	AURKB	O70126	Uniprot
17	T	Phosphorylation	Kinase	AURKB	O70126	Uniprot
17	T	Phosphorylation	Kinase	ROCK_GROUP	-	PhosphoELM
17	T	Phosphorylation	Kinase	ROCK-SUBFAMILY	-	GPS
17	T	Phosphorylation	Kinase	ROCK1	P70335	Uniprot
28	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot
28	S	Phosphorylation	Kinase	CDK1	P06493	PSP
32	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot
32	S	Phosphorylation	Kinase	CDK1	P06493	PSP
60	S	Phosphorylation	Kinase	AURKB	O70126	Uniprot
76	T	Phosphorylation	Kinase	ROCK1	P70335	Uniprot
76	T	Phosphorylation	Kinase	ROCK-SUBFAMILY	-	GPS
76	T	Phosphorylation	Kinase	ROCK_GROUP	-	PhosphoELM
77	T	Phosphorylation	Kinase	ROCK1	P70335	Uniprot
77	T	Phosphorylation	Kinase	ROCK-SUBFAMILY	-	GPS
77	T	Phosphorylation	Kinase	ROCK_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
7	S	Phosphorylation	27565725
Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1, phosphorylation at Ser-60 by AURKB and phosphorylation at Thr-76 by ROCK1 contribute to efficient separation of desmin intermediate filaments during mitosis.
28	S	Phosphorylation	21183079
Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1, phosphorylation at Ser-60 by AURKB and phosphorylation at Thr-76 by ROCK1 contribute to efficient separation of desmin intermediate filaments during mitosis.
32	S	Phosphorylation	21183079
Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1, phosphorylation at Ser-60 by AURKB and phosphorylation at Thr-76 by ROCK1 contribute to efficient separation of desmin intermediate filaments during mitosis.
60	S	Phosphorylation	27565725
Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1, phosphorylation at Ser-60 by AURKB and phosphorylation at Thr-76 by ROCK1 contribute to efficient separation of desmin intermediate filaments during mitosis.
76	T	Phosphorylation	27565725
Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1, phosphorylation at Ser-60 by AURKB and phosphorylation at Thr-76 by ROCK1 contribute to efficient separation of desmin intermediate filaments during mitosis.

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 DESM_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of DESM_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of DESM_MOUSE

Related Literatures of Post-Translational Modification

show

show

show

show

show