dbPTM

SARM1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SARM1_HUMAN
UniProt AC	Q6SZW1
Protein Name	Sterile alpha and TIR motif-containing protein 1
Gene Name	SARM1
Organism	Homo sapiens (Human).
Sequence Length	724
Subcellular Localization	Cytoplasm. Cell projection, axon. Cell projection, dendrite. Cell junction, synapse. Mitochondrion. Associated with microtubules..
Protein Description	Negative regulator of MYD88- and TRIF-dependent toll-like receptor signaling pathway which plays a pivotal role in activating axonal degeneration following injury. Promotes Wallerian degeneration an injury-induced axonal death pathway which involves degeneration of an axon distal to the injury site. Can activate neuronal death in response to stress. Regulates dendritic arborization through the MAPK4-JNK pathway. Involved in innate immune response. Inhibits both TICAM1/TRIF- and MYD88-dependent activation of JUN/AP-1, TRIF-dependent activation of NF-kappa-B and IRF3, and the phosphorylation of MAPK14/p38..
Protein Sequence	MVLTLLLSAYKLCRFFAMSGPRPGAERLAVPGPDGGGGTGPWWAAGGRGPREVSPGAGTEVQDALERALPELQQALSALKQAGGARAVGAGLAEVFQLVEEAWLLPAVGREVAQGLCDAIRLDGGLDLLLRLLQAPELETRVQAARLLEQILVAENRDRVARIGLGVILNLAKEREPVELARSVAGILEHMFKHSEETCQRLVAAGGLDAVLYWCRRTDPALLRHCALALGNCALHGGQAVQRRMVEKRAAEWLFPLAFSKEDELLRLHACLAVAVLATNKEVEREVERSGTLALVEPLVASLDPGRFARCLVDASDTSQGRGPDDLQRLVPLLDSNRLEAQCIGAFYLCAEAAIKSLQGKTKVFSDIGAIQSLKRLVSYSTNGTKSALAKRALRLLGEEVPRPILPSVPSWKEAEVQTWLQQIGFSKYCESFREQQVDGDLLLRLTEEELQTDLGMKSGITRKRFFRELTELKTFANYSTCDRSNLADWLGSLDPRFRQYTYGLVSCGLDRSLLHRVSEQQLLEDCGIHLGVHRARILTAAREMLHSPLPCTGGKPSGDTPDVFISYRRNSGSQLASLLKVHLQLHGFSVFIDVEKLEAGKFEDKLIQSVMGARNFVLVLSPGALDKCMQDHDCKDWVHKEIVTALSCGKNIVPIIDGFEWPEPQVLPEDMQAVLTFNGIKWSHEYQEATIEKIIRFLQGRSSRDSSAGSDTSLEGAAPMGPT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
54	Phosphorylation	GRGPREVSPGAGTEV CCCCCCCCCCCCHHH	16.92	29255136
59	Phosphorylation	EVSPGAGTEVQDALE CCCCCCCHHHHHHHH	32.23	29396449
80	Ubiquitination	QQALSALKQAGGARA HHHHHHHHHCCCHHH	37.51	-
173	Ubiquitination	GVILNLAKEREPVEL HHHHHHHHCCCHHHH	61.54	-
290	Phosphorylation	VEREVERSGTLALVE HHHHHHHHCCEEEHH	23.71	28857561
292	Phosphorylation	REVERSGTLALVEPL HHHHHHCCEEEHHHC	15.31	28857561
329 (in isoform 2)	Ubiquitination	-	44.97	21890473
336	Phosphorylation	RLVPLLDSNRLEAQC HHHHHHCCCCHHHHH	24.66	-
361	Acetylation	AIKSLQGKTKVFSDI HHHHHCCCCCCCCCH	32.01	7366035
362	Ubiquitination	IKSLQGKTKVFSDIG HHHHCCCCCCCCCHH	38.99	-
362	Phosphorylation	IKSLQGKTKVFSDIG HHHHCCCCCCCCCHH	38.99	29449344
363 (in isoform 1)	Ubiquitination	-	44.78	21890473
363	Ubiquitination	KSLQGKTKVFSDIGA HHHCCCCCCCCCHHH	44.78	21890473
366	Phosphorylation	QGKTKVFSDIGAIQS CCCCCCCCCHHHHHH	31.16	29449344
373	Phosphorylation	SDIGAIQSLKRLVSY CCHHHHHHHHHHHHC	29.73	29449344
375	Ubiquitination	IGAIQSLKRLVSYST HHHHHHHHHHHHCCC	49.27	-
379	Phosphorylation	QSLKRLVSYSTNGTK HHHHHHHHCCCCCCH	20.25	29449344
380	Phosphorylation	SLKRLVSYSTNGTKS HHHHHHHCCCCCCHH	16.43	29449344
381	Phosphorylation	LKRLVSYSTNGTKSA HHHHHHCCCCCCHHH	14.11	29449344
382	Phosphorylation	KRLVSYSTNGTKSAL HHHHHCCCCCCHHHH	29.45	29449344
385	Phosphorylation	VSYSTNGTKSALAKR HHCCCCCCHHHHHHH	24.72	29449344
547	Phosphorylation	TAAREMLHSPLPCTG HHHHHHHCCCCCCCC	26.51	30333228
548	Phosphorylation	AAREMLHSPLPCTGG HHHHHHCCCCCCCCC	24.95	26657352
553	Phosphorylation	LHSPLPCTGGKPSGD HCCCCCCCCCCCCCC	47.21	24117733
558	Phosphorylation	PCTGGKPSGDTPDVF CCCCCCCCCCCCCEE	53.43	24117733
561	Phosphorylation	GGKPSGDTPDVFISY CCCCCCCCCCEEEEE	25.55	24117733
567	Phosphorylation	DTPDVFISYRRNSGS CCCCEEEEEECCCHH	10.92	24117733
568	Phosphorylation	TPDVFISYRRNSGSQ CCCEEEEEECCCHHH	14.58	24117733
571	Phosphorylation	VFISYRRNSGSQLAS EEEEEECCCHHHHHH	41.55	-
572	Phosphorylation	FISYRRNSGSQLASL EEEEECCCHHHHHHH	37.70	22199227
574	Phosphorylation	SYRRNSGSQLASLLK EEECCCHHHHHHHHH	23.11	22199227
578	Phosphorylation	NSGSQLASLLKVHLQ CCHHHHHHHHHHHHH	42.71	24719451
703	Phosphorylation	IRFLQGRSSRDSSAG HHHHHCCCCCCCCCC	36.23	27251275
704	Phosphorylation	RFLQGRSSRDSSAGS HHHHCCCCCCCCCCC	38.45	27251275
707	Phosphorylation	QGRSSRDSSAGSDTS HCCCCCCCCCCCCCC	22.45	22199227
708	Phosphorylation	GRSSRDSSAGSDTSL CCCCCCCCCCCCCCC	40.72	22199227
710	Phosphorylation	SSRDSSAGSDTSLEG CCCCCCCCCCCCCCC	28.18	-
711	Phosphorylation	SRDSSAGSDTSLEGA CCCCCCCCCCCCCCC	37.11	22199227
713	Phosphorylation	DSSAGSDTSLEGAAP CCCCCCCCCCCCCCC	36.59	22199227
714	Phosphorylation	SSAGSDTSLEGAAPM CCCCCCCCCCCCCCC	29.43	27251275

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
548	S	Phosphorylation	Kinase	JNK1	P45983	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
548	S	Oxidation	30333228
Phosphorylation at Ser-548 and subsequent activation takes place in response to oxidative stress conditions and inhibits mitochondrial respiration.
548	S	Phosphorylation	30333228
Phosphorylation at Ser-548 and subsequent activation takes place in response to oxidative stress conditions and inhibits mitochondrial respiration.
548	S	Phosphorylation	30333228
Phosphorylation at Ser-548 by JNK kinases (MAPK8, MAPK9 and /or MAPK10) enhance the NAD(+) hydrolase (NADase) activity.

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 SARM1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MYD88_HUMAN	MYD88	physical	17258210
TCAM2_HUMAN	TICAM2	physical	17258210
CCD47_HUMAN	CCDC47	physical	21903422
CDIPT_HUMAN	CDIPT	physical	21903422
CLGN_HUMAN	CLGN	physical	21903422
GHITM_HUMAN	GHITM	physical	21903422
HYOU1_HUMAN	HYOU1	physical	21903422
IRAK1_HUMAN	IRAK1	physical	21903422
IRAK2_HUMAN	IRAK2	physical	21903422
NFXL1_HUMAN	NFXL1	physical	21903422
NLRX1_HUMAN	NLRX1	physical	21903422
STT3A_HUMAN	STT3A	physical	21903422
PINK1_HUMAN	PINK1	physical	23885119
TRAF2_HUMAN	TRAF2	physical	23885119
TRAF6_HUMAN	TRAF6	physical	23885119

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 SARM1_HUMAN

Related Literatures of Post-Translational Modification

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