dbPTM

DESM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DESM_HUMAN
UniProt AC	P17661
Protein Name	Desmin
Gene Name	DES
Organism	Homo sapiens (Human).
Sequence Length	470
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 (PubMed:24200904, PubMed:26724190). Localizes in the nucleus exclusively in di
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. [PubMed: 25358400 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]
Protein Sequence	MSQAYSSSQRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGFGSKGSSSSVTSRVYQVSRTSGGAGGLGSLRASRLGTTRTPSSYGAGELLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRINLPIQTYSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSQAYSSSQ ------CCCCCCCHH	24.42	27499020
5	Phosphorylation	---MSQAYSSSQRVS ---CCCCCCCHHCHH	11.05	29116813
6	Phosphorylation	--MSQAYSSSQRVSS --CCCCCCCHHCHHH	26.91	24719451
7	Phosphorylation	-MSQAYSSSQRVSSY -CCCCCCCHHCHHHH	20.15	-
12	Phosphorylation	YSSSQRVSSYRRTFG CCCHHCHHHHHCCCC	24.68	12686604
13	Phosphorylation	SSSQRVSSYRRTFGG CCHHCHHHHHCCCCC	21.57	22817900
16	Methylation	QRVSSYRRTFGGAPG HCHHHHHCCCCCCCC	26.61	-
17	Phosphorylation	RVSSYRRTFGGAPGF CHHHHHCCCCCCCCC	20.03	21082442
28	Phosphorylation	APGFPLGSPLSSPVF CCCCCCCCCCCCCCC	30.28	24670416
31	Phosphorylation	FPLGSPLSSPVFPRA CCCCCCCCCCCCCCC	35.66	26657352
32	Phosphorylation	PLGSPLSSPVFPRAG CCCCCCCCCCCCCCC	32.53	27499020
37	Asymmetric dimethylarginine	LSSPVFPRAGFGSKG CCCCCCCCCCCCCCC	35.56	-
37	Methylation	LSSPVFPRAGFGSKG CCCCCCCCCCCCCCC	35.56	-
42	Phosphorylation	FPRAGFGSKGSSSSV CCCCCCCCCCCCCCC	31.42	23312004
43	Methylation	PRAGFGSKGSSSSVT CCCCCCCCCCCCCCC	64.29	-
45	Phosphorylation	AGFGSKGSSSSVTSR CCCCCCCCCCCCCEE	30.68	26657352
46	Phosphorylation	GFGSKGSSSSVTSRV CCCCCCCCCCCCEEE	34.99	30242111
47	Phosphorylation	FGSKGSSSSVTSRVY CCCCCCCCCCCEEEE	30.44	27251275
48	Phosphorylation	GSKGSSSSVTSRVYQ CCCCCCCCCCEEEEE	31.21	30242111
50	Phosphorylation	KGSSSSVTSRVYQVS CCCCCCCCEEEEEEE	16.86	27251275
51	Phosphorylation	GSSSSVTSRVYQVSR CCCCCCCEEEEEEEC	20.00	23312004
54	Phosphorylation	SSVTSRVYQVSRTSG CCCCEEEEEEECCCC	11.33	19651622
57	Phosphorylation	TSRVYQVSRTSGGAG CEEEEEEECCCCCCC	17.83	26437602
58	ADP-ribosylation	SRVYQVSRTSGGAGG EEEEEEECCCCCCCC	33.77	-
58	ADP-ribosylation	SRVYQVSRTSGGAGG EEEEEEECCCCCCCC	33.77	-
59	Phosphorylation	RVYQVSRTSGGAGGL EEEEEECCCCCCCCH	24.98	26657352
60	Phosphorylation	VYQVSRTSGGAGGLG EEEEECCCCCCCCHH	33.83	21082442
68	Phosphorylation	GGAGGLGSLRASRLG CCCCCHHHHCHHHCC	21.52	28857561
70	Methylation	AGGLGSLRASRLGTT CCCHHHHCHHHCCCC	32.01	-
72	Phosphorylation	GLGSLRASRLGTTRT CHHHHCHHHCCCCCC	22.92	24670416
76	Phosphorylation	LRASRLGTTRTPSSY HCHHHCCCCCCCCCC	20.07	10574968
77	Phosphorylation	RASRLGTTRTPSSYG CHHHCCCCCCCCCCC	30.65	10574968
79	Phosphorylation	SRLGTTRTPSSYGAG HHCCCCCCCCCCCHH	25.98	26657352
81	Phosphorylation	LGTTRTPSSYGAGEL CCCCCCCCCCCHHHH	35.26	26657352
82	Phosphorylation	GTTRTPSSYGAGELL CCCCCCCCCCHHHHH	28.87	26657352
83	Phosphorylation	TTRTPSSYGAGELLD CCCCCCCCCHHHHHH	18.48	26657352
92	Phosphorylation	AGELLDFSLADAVNQ HHHHHHCHHHHHCCH	23.47	26657352
106	Phosphorylation	QEFLTTRTNEKVELQ HHHHHCCCCCCEEHH	45.71	23911959
109	Ubiquitination	LTTRTNEKVELQELN HHCCCCCCEEHHHHH	42.98	20639865
109	Acetylation	LTTRTNEKVELQELN HHCCCCCCEEHHHHH	42.98	132853
122	Phosphorylation	LNDRFANYIEKVRFL HHHHHHHHHHHHHHH	13.66	-
149	Phosphorylation	RLKGREPTRVAELYE HHCCCCCCHHHHHHH	32.78	26437602
155	Phosphorylation	PTRVAELYEEELREL CCHHHHHHHHHHHHH	16.89	-
170	Phosphorylation	RRQVEVLTNQRARVD HHHHHHHHHCCCCCC	34.19	24719451
219	Phosphorylation	RADVDAATLARIDLE HHCCCHHHHHHHCHH	23.75	27499020
231	Phosphorylation	DLERRIESLNEEIAF CHHHHHHHHHHHHHH	33.84	27499020
240	Acetylation	NEEIAFLKKVHEEEI HHHHHHHHHHCHHHH	46.42	19608861
241	Acetylation	EEIAFLKKVHEEEIR HHHHHHHHHCHHHHH	51.47	30585705
281	Phosphorylation	LRDIRAQYETIAAKN HHHHHHHHHHHHHCC	17.66	-
290	Phosphorylation	TIAAKNISEAEEWYK HHHHCCHHHHHHHHH	39.90	26657352
296	Phosphorylation	ISEAEEWYKSKVSDL HHHHHHHHHHHHHHH	14.52	-
298	Phosphorylation	EAEEWYKSKVSDLTQ HHHHHHHHHHHHHHH	23.69	26437602
301	Phosphorylation	EWYKSKVSDLTQAAN HHHHHHHHHHHHHHH	30.55	26657352
304	Phosphorylation	KSKVSDLTQAANKNN HHHHHHHHHHHHHCH	22.58	26437602
315	Methylation	NKNNDALRQAKQEMM HHCHHHHHHHHHHHH	35.81	-
324	Phosphorylation	AKQEMMEYRHQIQSY HHHHHHHHHHHHHHC	8.76	-
330	Phosphorylation	EYRHQIQSYTCEIDA HHHHHHHHCCCHHHH	24.84	26657352
331	Phosphorylation	YRHQIQSYTCEIDAL HHHHHHHCCCHHHHH	10.07	23312004
332	Phosphorylation	RHQIQSYTCEIDALK HHHHHHCCCHHHHHC	14.65	23312004
339	Acetylation	TCEIDALKGTNDSLM CCHHHHHCCCCHHHH	66.46	7672175
341	Phosphorylation	EIDALKGTNDSLMRQ HHHHHCCCCHHHHHH	33.98	22210691
344	Phosphorylation	ALKGTNDSLMRQMRE HHCCCCHHHHHHHHH	26.57	22210691
358	Phosphorylation	ELEDRFASEASGYQD HHHHHHHHHHCCCHH	30.86	26657352
361	Phosphorylation	DRFASEASGYQDNIA HHHHHHHCCCHHHHH	33.70	26657352
363	Phosphorylation	FASEASGYQDNIARL HHHHHCCCHHHHHHH	15.36	24248375
386	Methylation	DEMARHLREYQDLLN HHHHHHHHHHHHHHC	34.16	-
388	Phosphorylation	MARHLREYQDLLNVK HHHHHHHHHHHHCHH	10.82	21253578
407	Ubiquitination	VEIATYRKLLEGEES HHHHHHHHHHCCCCC	47.19	2190698
407	Acetylation	VEIATYRKLLEGEES HHHHHHHHHHCCCCC	47.19	22631337
407	Sumoylation	VEIATYRKLLEGEES HHHHHHHHHHCCCCC	47.19	-
407	Sumoylation	VEIATYRKLLEGEES HHHHHHHHHHCCCCC	47.19	-
414	Phosphorylation	KLLEGEESRINLPIQ HHHCCCCCCCCCCCC	33.87	21815630
422	Phosphorylation	RINLPIQTYSALNFR CCCCCCCEEEECCCC	21.84	28442448
423	Phosphorylation	INLPIQTYSALNFRE CCCCCCEEEECCCCC	3.90	26657352
424	Phosphorylation	NLPIQTYSALNFRET CCCCCEEEECCCCCC	29.66	28857561
431	Phosphorylation	SALNFRETSPEQRGS EECCCCCCCHHHCCC	45.38	28857561
432	Phosphorylation	ALNFRETSPEQRGSE ECCCCCCCHHHCCCC	22.99	26657352
438	O-linked_Glycosylation	TSPEQRGSEVHTKKT CCHHHCCCCCEECEE	38.34	29237092
438	Phosphorylation	TSPEQRGSEVHTKKT CCHHHCCCCCEECEE	38.34	26657352
450	Phosphorylation	KKTVMIKTIETRDGE CEEEEEEEEECCCCC	17.08	22817900
453	Phosphorylation	VMIKTIETRDGEVVS EEEEEEECCCCCEEC	30.15	26437602
460	Phosphorylation	TRDGEVVSEATQQQH CCCCCEECHHHHHHH	27.04	26437602
463	Phosphorylation	GEVVSEATQQQHEVL CCEECHHHHHHHHCC	23.90	26437602

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	Uniprot
12	S	Phosphorylation	Kinase	AURB	Q96GD4	PSP
12	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
12	S	Phosphorylation	Kinase	ROCK1	Q13464	PSP
17	T	Phosphorylation	Kinase	AURB	Q96GD4	PSP
17	T	Phosphorylation	Kinase	ROCK_GROUP	-	PhosphoELM
17	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
17	T	Phosphorylation	Kinase	ROCK1	Q13464	Uniprot
17	T	Phosphorylation	Kinase	ROCK-SUBFAMILY	-	GPS
28	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
28	S	Phosphorylation	Kinase	GSK3A	P49840	PSP
28	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
32	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
32	S	Phosphorylation	Kinase	GSK3A	P49840	PSP
32	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
60	S	Phosphorylation	Kinase	AURB	Q96GD4	PSP
60	S	Phosphorylation	Kinase	ROCK1	Q13464	PSP
76	T	Phosphorylation	Kinase	ROCK-SUBFAMILY	-	GPS
76	T	Phosphorylation	Kinase	ROCK1	Q13464	Uniprot
76	T	Phosphorylation	Kinase	ROCK_GROUP	-	PhosphoELM
76	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
77	T	Phosphorylation	Kinase	ROCK1	Q13464	Uniprot
77	T	Phosphorylation	Kinase	ROCK-SUBFAMILY	-	GPS
77	T	Phosphorylation	Kinase	ROCK_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM32	Q13049	PMID:22908310

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
7	S	Phosphorylation	-
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	24413773
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	24413773
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	12686604
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	9875213
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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
S10A1_HUMAN	S100A1	physical	8641565
HNRL1_HUMAN	HNRNPUL1	physical	22939629
RL29_HUMAN	RPL29	physical	22939629
RU17_HUMAN	SNRNP70	physical	22939629
ECHB_HUMAN	HADHB	physical	22939629
TCPH_HUMAN	CCT7	physical	22939629
MYL6_HUMAN	MYL6	physical	22939629
RL17_HUMAN	RPL17	physical	22939629
PLAK_HUMAN	JUP	physical	22939629
MLH1_HUMAN	MLH1	physical	20706999
ECHP_HUMAN	EHHADH	physical	25416956
TBA8_HUMAN	EHHADH	physical	25416956
UBC9_HUMAN	UBE2I	physical	25416956
PPR18_HUMAN	PPP1R18	physical	25416956
BRCA1_HUMAN	BRCA1	physical	25184681

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
601419	Myopathy, myofibrillar, 1 (MFM1)
604765	Cardiomyopathy, dilated 1I (CMD1I)
181400	Neurogenic scapuloperoneal syndrome Kaeser type (Kaeser syndrome)
615325	Limb-girdle muscular dystrophy 2R (LGMD2R)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DESM_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Functional significance of the specific sites phosphorylated indesmin at cleavage furrow: Aurora-B may phosphorylate and regulatetype III intermediate filaments during cytokinesis coordinatedly withRho-kinase."; Kawajiri A., Yasui Y., Goto H., Tatsuka M., Takahashi M., Nagata K.,Inagaki M.; Mol. Biol. Cell 14:1489-1500(2003). Cited for: PHOSPHORYLATION AT SER-12; THR-17 AND SER-60.	12686604 [Abstract]

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