BUD31_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BUD31_HUMAN
• UniProt AC: P41223
• Protein Name: Protein BUD31 homolog {ECO:0000303|PubMed:25091737}
• Gene Name: BUD31
• Organism: Homo sapiens (Human).
• Sequence Length: 144
• Subcellular Localization: Nucleus . Detected in chromatin at the promoter of AR target genes.
• Protein Description: Involved in the pre-mRNA splicing process. [PubMed: 28502770]
• Protein Sequence: MPKVKRSRKAPPDGWELIEPTLDELDQKMREAETEPHEGKRKVESLWPIFRIHHQKTRYIFDLFYKRKAISRELYEYCIKEGYADKNLIAKWKKQGYENLCCLRCIQTRDTNFGTNCICRVPKSKLEVGRIIECTHCGCRGCSG

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
5	Ubiquitination	---MPKVKRSRKAPP ---CCCCCCCCCCCC	51.27	22817900
9	Ubiquitination	PKVKRSRKAPPDGWE CCCCCCCCCCCCCHH	67.50	21906983
9	Ubiquitination	PKVKRSRKAPPDGWE CCCCCCCCCCCCCHH	67.50	21890473
28	Ubiquitination	TLDELDQKMREAETE HHHHHHHHHHHHHCC	39.32	32015554
40	Ubiquitination	ETEPHEGKRKVESLW HCCCCCCHHHHHHHH	46.17	23000965
42	Sumoylation	EPHEGKRKVESLWPI CCCCCHHHHHHHHHH	54.57	-
42	Ubiquitination	EPHEGKRKVESLWPI CCCCCHHHHHHHHHH	54.57	23000965
42	Sumoylation	EPHEGKRKVESLWPI CCCCCHHHHHHHHHH	54.57	-
42	Ubiquitination	EPHEGKRKVESLWPI CCCCCHHHHHHHHHH	54.57	-
45	Phosphorylation	EGKRKVESLWPIFRI CCHHHHHHHHHHHEE	38.43	25999147
56	2-Hydroxyisobutyrylation	IFRIHHQKTRYIFDL HHEEECCCCHHHHHH	30.52	-
66	Ubiquitination	YIFDLFYKRKAISRE HHHHHHHHHHHHHHH	39.84	21890473
66	Ubiquitination	YIFDLFYKRKAISRE HHHHHHHHHHHHHHH	39.84	23000965
68	Ubiquitination	FDLFYKRKAISRELY HHHHHHHHHHHHHHH	46.01	23000965
71	Phosphorylation	FYKRKAISRELYEYC HHHHHHHHHHHHHHH	25.27	29414761
75	Phosphorylation	KAISRELYEYCIKEG HHHHHHHHHHHHHHC	10.49	29414761
77	Phosphorylation	ISRELYEYCIKEGYA HHHHHHHHHHHHCCC	5.97	28152594
80	Ubiquitination	ELYEYCIKEGYADKN HHHHHHHHHCCCCHH	41.34	-
80	Acetylation	ELYEYCIKEGYADKN HHHHHHHHHCCCCHH	41.34	26051181
80	Ubiquitination	ELYEYCIKEGYADKN HHHHHHHHHCCCCHH	41.34	23000965
83	Phosphorylation	EYCIKEGYADKNLIA HHHHHHCCCCHHHHH	16.84	28152594
86	Acetylation	IKEGYADKNLIAKWK HHHCCCCHHHHHHHH	45.54	26051181
86	Ubiquitination	IKEGYADKNLIAKWK HHHCCCCHHHHHHHH	45.54	23000965
91	Acetylation	ADKNLIAKWKKQGYE CCHHHHHHHHHCCCC	53.18	25953088
91	Ubiquitination	ADKNLIAKWKKQGYE CCHHHHHHHHHCCCC	53.18	23000965
93	Ubiquitination	KNLIAKWKKQGYENL HHHHHHHHHCCCCCE	34.22	23000965
94	Ubiquitination	NLIAKWKKQGYENLC HHHHHHHHCCCCCEE	48.09	-
94	Ubiquitination	NLIAKWKKQGYENLC HHHHHHHHCCCCCEE	48.09	23000965
97	Phosphorylation	AKWKKQGYENLCCLR HHHHHCCCCCEEEEE	10.11	20090780
115	Phosphorylation	TRDTNFGTNCICRVP CCCCCCCCCCEEECC	23.84	21712546
123	Ubiquitination	NCICRVPKSKLEVGR CCEEECCHHHCCCCE	58.32	33845483
125	Sumoylation	ICRVPKSKLEVGRII EEECCHHHCCCCEEE	55.59	19608861
125	Ubiquitination	ICRVPKSKLEVGRII EEECCHHHCCCCEEE	55.59	27667366
125	Sumoylation	ICRVPKSKLEVGRII EEECCHHHCCCCEEE	55.59	-
125	Acetylation	ICRVPKSKLEVGRII EEECCHHHCCCCEEE	55.59	19608861
135	Phosphorylation	VGRIIECTHCGCRGC CCEEEEECCCCCCCC	13.86	26714015
140	Methylation	ECTHCGCRGCSG--- EECCCCCCCCCC---	34.14	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of BUD31_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BUD31_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 BUD31_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
SRSF7_HUMAN	SRSF7	physical	22939629
SRSF3_HUMAN	SRSF3	physical	22939629
ZN326_HUMAN	ZNF326	physical	22939629
TRA2A_HUMAN	TRA2A	physical	22939629
VTNC_HUMAN	VTN	physical	22939629
ZCH18_HUMAN	ZC3H18	physical	22939629
TPBG_HUMAN	TPBG	physical	22939629
UT14A_HUMAN	UTP14A	physical	22939629
TRI55_HUMAN	TRIM55	physical	22939629
SON_HUMAN	SON	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
TPR_HUMAN	TPR	physical	22939629
SEPT7_HUMAN	SEPT7	physical	22939629
CTBL1_HUMAN	CTNNBL1	physical	22365833
RELB_HUMAN	RELB	physical	21988832
BEND5_HUMAN	BEND5	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
SGF29_HUMAN	CCDC101	physical	26344197
CCD12_HUMAN	CCDC12	physical	26344197
DCNL4_HUMAN	DCUN1D4	physical	26344197
LSM2_HUMAN	LSM2	physical	26344197
PRP19_HUMAN	PRPF19	physical	26344197
RCC2_HUMAN	RCC2	physical	26344197
RRBP1_HUMAN	RRBP1	physical	26344197
SNW1_HUMAN	SNW1	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.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125, AND MASS SPECTROMETRY.
PubMed: 19608861