VPS72_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: VPS72_HUMAN
• UniProt AC: Q15906
• Protein Name: Vacuolar protein sorting-associated protein 72 homolog
• Gene Name: VPS72
• Organism: Homo sapiens (Human).
• Sequence Length: 364
• Subcellular Localization: Nucleus .
• Protein Description: Deposition-and-exchange histone chaperone specific for H2AFZ, specifically chaperones H2AFZ and deposits it into nucleosomes. As component of the SRCAP complex, mediates the ATP-dependent exchange of histone H2AFZ/H2B dimers for nucleosomal H2A/H2B, leading to transcriptional regulation of selected genes by chromatin remodeling..
• Protein Sequence: MSLAGGRAPRKTAGNRLSGLLEAEEEDEFYQTTYGGFTEESGDDEYQGDQSDTEDEVDSDFDIDEGDEPSSDGEAEEPRRKRRVVTKAYKEPLKSLRPRKVNTPAGSSQKAREEKALLPLELQDDGSDSRKSMRQSTAEHTRQTFLRVQERQGQSRRRKGPHCERPLTQEELLREAKITEELNLRSLETYERLEADKKKQVHKKRKCPGPIITYHSVTVPLVGEPGPKEENVDIEGLDPAPSVSALTPHAGTGPVNPPARCSRTFITFSDDATFEEWFPQGRPPKVPVREVCPVTHRPALYRDPVTDIPYATARAFKIIREAYKKYITAHGLPPTASALGPGPPPPEPLPGSGPRALRQKIVIK

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
7	Methylation	-MSLAGGRAPRKTAG -CCCCCCCCCCCCCC	40.27	115919861
41	Phosphorylation	YGGFTEESGDDEYQG CCCCCCCCCCCCCCC	41.09	7702631
51	Phosphorylation	DEYQGDQSDTEDEVD CCCCCCCCCCCCCCC	51.76	7702631
59	Phosphorylation	DTEDEVDSDFDIDEG CCCCCCCCCCCCCCC	45.40	7702631
71	Phosphorylation	DEGDEPSSDGEAEEP CCCCCCCCCCCCCCH	61.42	7702631
86	Phosphorylation	RRKRRVVTKAYKEPL HHHHHHHHHHHHHHH	13.70	24719451
89	Phosphorylation	RRVVTKAYKEPLKSL HHHHHHHHHHHHHHC	19.90	24719451
90	Acetylation	RVVTKAYKEPLKSLR HHHHHHHHHHHHHCC	58.68	26051181
100	Ubiquitination	LKSLRPRKVNTPAGS HHHCCCCCCCCCCCC	42.38	24816145
103	Phosphorylation	LRPRKVNTPAGSSQK CCCCCCCCCCCCCHH	19.94	25849741
107	Phosphorylation	KVNTPAGSSQKAREE CCCCCCCCCHHHHHH	31.53	25262027
108	Phosphorylation	VNTPAGSSQKAREEK CCCCCCCCHHHHHHH	34.48	25262027
115	Sumoylation	SQKAREEKALLPLEL CHHHHHHHCCCCEEC	39.31	28112733
115	Ubiquitination	SQKAREEKALLPLEL CHHHHHHHCCCCEEC	39.31	24816145
127	Phosphorylation	LELQDDGSDSRKSMR EECCCCCCCCHHHHH	39.13	30266825
129	Phosphorylation	LQDDGSDSRKSMRQS CCCCCCCCHHHHHHH	43.22	30266825
132	Phosphorylation	DGSDSRKSMRQSTAE CCCCCHHHHHHHHHH	20.35	24719451
137	Phosphorylation	RKSMRQSTAEHTRQT HHHHHHHHHHHHHHH	27.94	7702631
168	Phosphorylation	PHCERPLTQEELLRE CCCCCCCCHHHHHHH	36.30	17525332
177	Ubiquitination	EELLREAKITEELNL HHHHHHCCCCHHHCC	45.46	29967540
197	Acetylation	YERLEADKKKQVHKK HHHHHHHHHHHHCCC	69.76	30593375
198	Acetylation	ERLEADKKKQVHKKR HHHHHHHHHHHCCCC	49.32	30593381
203	Acetylation	DKKKQVHKKRKCPGP HHHHHHCCCCCCCCC	56.25	30593387
242	Phosphorylation	EGLDPAPSVSALTPH CCCCCCCCCCCCCCC	30.70	27732954
244	Phosphorylation	LDPAPSVSALTPHAG CCCCCCCCCCCCCCC	23.15	25627689
247	Phosphorylation	APSVSALTPHAGTGP CCCCCCCCCCCCCCC	16.85	25159151
252	Phosphorylation	ALTPHAGTGPVNPPA CCCCCCCCCCCCCCC	38.81	27732954
317	Acetylation	YATARAFKIIREAYK HHHHHHHHHHHHHHH	35.92	26051181
326	Phosphorylation	IREAYKKYITAHGLP HHHHHHHHHHHCCCC	10.19	-
335	Phosphorylation	TAHGLPPTASALGPG HHCCCCCCHHHCCCC	31.16	-
337	Phosphorylation	HGLPPTASALGPGPP CCCCCCHHHCCCCCC	26.89	-
352	Phosphorylation	PPEPLPGSGPRALRQ CCCCCCCCCCCHHHH	43.62	28555341

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
41	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
41	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
51	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
51	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
59	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
59	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
71	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
71	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
86	T	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
86	T	Phosphorylation	Kinase	CAM-KII_GROUP	-	PhosphoELM
132	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
132	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
137	T	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
137	T	Phosphorylation	Kinase	CAM-KII_GROUP	-	PhosphoELM
168	T	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
168	T	Phosphorylation	Kinase	CAM-KII_GROUP	-	PhosphoELM

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of VPS72_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 VPS72_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CACO2_HUMAN	CALCOCO2	physical	16189514
CC85B_HUMAN	CCDC85B	physical	16189514
ZC3H1_HUMAN	ZFC3H1	physical	22939629
ANM1_HUMAN	PRMT1	physical	23455924
HMBX1_HUMAN	HMBOX1	physical	25416956
DMAP1_HUMAN	DMAP1	physical	26344197
MYCL_HUMAN	MYCL	physical	29028833
PP2AA_HUMAN	PPP2CA	physical	29028833
RUVB2_HUMAN	RUVBL2	physical	29028833
DMAP1_HUMAN	DMAP1	physical	29028833
KAT5_HUMAN	KAT5	physical	29028833
TRRAP_HUMAN	TRRAP	physical	29028833
EP400_HUMAN	EP400	physical	29028833
ACL6A_HUMAN	ACTL6A	physical	29028833
MAX_HUMAN	MAX	physical	29028833

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-168, AND MASSSPECTROMETRY.
PubMed: 17525332