SWP70_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SWP70_HUMAN
• UniProt AC: Q9UH65
• Protein Name: Switch-associated protein 70
• Gene Name: SWAP70
• Organism: Homo sapiens (Human).
• Sequence Length: 585
• Subcellular Localization: Cytoplasm . Cell membrane. Nucleus . Cell projection, lamellipodium . Cytoplasm, cytoskeleton . In resting B-cells it is localized mainly in the cytoplasm and upon cell activation it is recruited to the plasma membrane and then translocates to the nu
• Protein Description: Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which, independently of RAS, transduces signals from tyrosine kinase receptors to RAC. It also mediates signaling of membrane ruffling. Regulates the actin cytoskeleton as an effector or adapter protein in response to agonist stimulated phosphatidylinositol (3,4)-bisphosphate production and cell protrusion (By similarity)..
• Protein Sequence: MGSLKEELLKAIWHAFTALDQDHSGKVSKSQLKVLSHNLCTVLKVPHDPVALEEHFRDDDEGPVSNQGYMPYLNRFILEKVQDNFDKIEFNRMCWTLCVKKNLTKNPLLITEEDAFKIWVIFNFLSEDKYPLIIVSEEIEYLLKKLTEAMGGGWQQEQFEHYKINFDDSKNGLSAWELIELIGNGQFSKGMDRQTVSMAINEVFNELILDVLKQGYMMKKGHRRKNWTERWFVLKPNIISYYVSEDLKDKKGDILLDENCCVESLPDKDGKKCLFLVKCFDKTFEISASDKKKKQEWIQAIHSTIHLLKLGSPPPHKEARQRRKELRKKQLAEQEELERQMKELQAANESKQQELEAVRKKLEEAASRAAEEEKKRLQTQVELQARFSTELEREKLIRQQMEEQVAQKSSELEQYLQRVRELEDMYLKLQEALEDERQARQDEETVRKLQARLLEEESSKRAELEKWHLEQQQAIQTTEAEKQELENQRVLKEQALQEAMEQLEQLELERKQALEQYEEVKKKLEMATNKTKSWKDKVAHHEGLIRLIEPGSKNPHLITNWGPAAFTEAELEEREKNWKEKKTTE

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
3	Phosphorylation	-----MGSLKEELLK -----CCCHHHHHHH	34.66	25850435
5	Ubiquitination	---MGSLKEELLKAI ---CCCHHHHHHHHH	51.33	-
17	Phosphorylation	KAIWHAFTALDQDHS HHHHHHHHHHCCCCC	27.39	20873877
24	Phosphorylation	TALDQDHSGKVSKSQ HHHCCCCCCCCCHHH	48.91	20873877
29	Ubiquitination	DHSGKVSKSQLKVLS CCCCCCCHHHHHHHH	45.25	-
33	Malonylation	KVSKSQLKVLSHNLC CCCHHHHHHHHHCCE	33.23	32601280
70	Sulfoxidation	PVSNQGYMPYLNRFI CCCCCCCHHHHHHHH	1.94	30846556
80	Ubiquitination	LNRFILEKVQDNFDK HHHHHHHHHHHCCCH	41.57	-
105	Ubiquitination	CVKKNLTKNPLLITE HHHCCCCCCCEEECH	60.79	-
141	Phosphorylation	IVSEEIEYLLKKLTE EECHHHHHHHHHHHH	24.01	-
150	Sulfoxidation	LKKLTEAMGGGWQQE HHHHHHHCCCCCCHH	4.11	30846556
162	Phosphorylation	QQEQFEHYKINFDDS CHHHHHHEECCCCCC	13.33	27642862
189	Ubiquitination	IGNGQFSKGMDRQTV HCCCCCCCCCCHHHH	60.59	-
219	Acetylation	LKQGYMMKKGHRRKN HHHCCCCCCCCCCCC	38.79	25953088
240	Phosphorylation	VLKPNIISYYVSEDL EECCCCEEEECCHHH	13.45	20068231
241	Phosphorylation	LKPNIISYYVSEDLK ECCCCEEEECCHHHC	9.47	20068231
242	Phosphorylation	KPNIISYYVSEDLKD CCCCEEEECCHHHCC	7.24	20068231
244	Phosphorylation	NIISYYVSEDLKDKK CCEEEECCHHHCCCC	14.85	20068231
264	Phosphorylation	DENCCVESLPDKDGK CCCCCCCCCCCCCCC	25.46	30108239
272	Malonylation	LPDKDGKKCLFLVKC CCCCCCCEEEEEEEE	41.52	26320211
278	Acetylation	KKCLFLVKCFDKTFE CEEEEEEEECCCEEE	31.19	25953088
282	Acetylation	FLVKCFDKTFEISAS EEEEECCCEEEECCC	34.56	26051181
289	Phosphorylation	KTFEISASDKKKKQE CEEEECCCHHHHHHH	43.08	25159151
291	Ubiquitination	FEISASDKKKKQEWI EEECCCHHHHHHHHH	65.09	-
291	Acetylation	FEISASDKKKKQEWI EEECCCHHHHHHHHH	65.09	25953088
303	Phosphorylation	EWIQAIHSTIHLLKL HHHHHHHHHHHHHHC	23.97	30622161
304	Phosphorylation	WIQAIHSTIHLLKLG HHHHHHHHHHHHHCC	9.77	30622161
312	Phosphorylation	IHLLKLGSPPPHKEA HHHHHCCCCCCCHHH	44.67	23403867
351	Ubiquitination	LQAANESKQQELEAV HHHHHHHHHHHHHHH	50.23	-
388	Phosphorylation	VELQARFSTELEREK HHHHHHHCHHHHHHH	18.54	21815630
401	Sulfoxidation	EKLIRQQMEEQVAQK HHHHHHHHHHHHHHH	4.66	30846556
408	Ubiquitination	MEEQVAQKSSELEQY HHHHHHHHHHHHHHH	46.33	-
410	Phosphorylation	EQVAQKSSELEQYLQ HHHHHHHHHHHHHHH	53.92	28555341
426	Phosphorylation	VRELEDMYLKLQEAL HHHHHHHHHHHHHHH	17.01	-
460	2-Hydroxyisobutyrylation	LLEEESSKRAELEKW HHHHHHHHHHHHHHH	65.98	-
466	Ubiquitination	SKRAELEKWHLEQQQ HHHHHHHHHHHHHHH	53.16	-
466	Acetylation	SKRAELEKWHLEQQQ HHHHHHHHHHHHHHH	53.16	26051181
482	Ubiquitination	IQTTEAEKQELENQR HCCCHHHHHHHHHHH	57.00	-
500	Sulfoxidation	EQALQEAMEQLEQLE HHHHHHHHHHHHHHH	3.12	30846556
517	Phosphorylation	RKQALEQYEEVKKKL HHHHHHHHHHHHHHH	12.51	28796482
530	Acetylation	KLEMATNKTKSWKDK HHHHHHCCCCCHHHH	53.64	7822477
533	Phosphorylation	MATNKTKSWKDKVAH HHHCCCCCHHHHHHC	44.59	-
537	Ubiquitination	KTKSWKDKVAHHEGL CCCCHHHHHHCCCCC	37.28	-
537	Acetylation	KTKSWKDKVAHHEGL CCCCHHHHHHCCCCC	37.28	26822725
553	Ubiquitination	RLIEPGSKNPHLITN HEECCCCCCCCCCCC	79.14	-
553	Acetylation	RLIEPGSKNPHLITN HEECCCCCCCCCCCC	79.14	26051181
567	Phosphorylation	NWGPAAFTEAELEER CCCCCCCCHHHHHHH	29.56	-

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
517	Y	Phosphorylation	Kinase	SYK	P43405	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SWP70_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SWP70_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NPM_HUMAN	NPM1	physical	9642267
NUCL_HUMAN	NCL	physical	9642267
PARP1_HUMAN	PARP1	physical	9642267
RANB3_HUMAN	RANBP3	physical	22863883
SPT5H_HUMAN	SUPT5H	physical	22863883
NAA20_HUMAN	NAA20	physical	26344197

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.