dbPTM

UBE2H_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBE2H_HUMAN
UniProt AC	P62256
Protein Name	Ubiquitin-conjugating enzyme E2 H
Gene Name	UBE2H
Organism	Homo sapiens (Human).
Sequence Length	183
Subcellular Localization
Protein Description	Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination. Capable, in vitro, to ubiquitinate histone H2A..
Protein Sequence	MSSPSPGKRRMDTDVVKLIESKHEVTILGGLNEFVVKFYGPQGTPYEGGVWKVRVDLPDKYPFKSPSIGFMNKIFHPNIDEASGTVCLDVINQTWTALYDLTNIFESFLPQLLAYPNPIDPLNGDAAAMYLHRPEEYKQKIKEYIQKYATEEALKEQEEGTGDSSSESSMSDFSEDEAQDMEL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSPSPGKR ------CCCCCCCCC	51.46	29255136
2	Acetylation	------MSSPSPGKR ------CCCCCCCCC	51.46	19413330
3	Phosphorylation	-----MSSPSPGKRR -----CCCCCCCCCC	28.26	29255136
5	Phosphorylation	---MSSPSPGKRRMD ---CCCCCCCCCCCC	48.51	29255136
13	Phosphorylation	PGKRRMDTDVVKLIE CCCCCCCCHHHHHHH	22.73	26074081
17	Ubiquitination	RMDTDVVKLIESKHE CCCCHHHHHHHCCCE	43.53	-
39	Phosphorylation	NEFVVKFYGPQGTPY CEEEEEEECCCCCCC	23.37	28152594
60	Acetylation	VRVDLPDKYPFKSPS EEEECCCCCCCCCCC	53.54	21791702
60	Ubiquitination	VRVDLPDKYPFKSPS EEEECCCCCCCCCCC	53.54	21890473
60	Ubiquitination	VRVDLPDKYPFKSPS EEEECCCCCCCCCCC	53.54	21890473
60	Ubiquitination	VRVDLPDKYPFKSPS EEEECCCCCCCCCCC	53.54	21890473
60	Ubiquitination	VRVDLPDKYPFKSPS EEEECCCCCCCCCCC	53.54	21890473
64	Acetylation	LPDKYPFKSPSIGFM CCCCCCCCCCCCCCC	57.88	21791702
64	Ubiquitination	LPDKYPFKSPSIGFM CCCCCCCCCCCCCCC	57.88	21890473
65	Phosphorylation	PDKYPFKSPSIGFMN CCCCCCCCCCCCCCC	25.02	24719451
71	Sulfoxidation	KSPSIGFMNKIFHPN CCCCCCCCCCCCCCC	4.15	21406390
116	Ubiquitination	LPQLLAYPNPIDPLN HHHHHCCCCCCCCCC	34.22	21890473
116	Ubiquitination	LPQLLAYPNPIDPLN HHHHHCCCCCCCCCC	34.22	21890473
147	Ubiquitination	KIKEYIQKYATEEAL HHHHHHHHHHHHHHH	27.56	21890473
164	Phosphorylation	QEEGTGDSSSESSMS CCCCCCCCCCCHHHC	36.79	27251275
165	Phosphorylation	EEGTGDSSSESSMSD CCCCCCCCCCHHHCC	42.75	27251275
166	Phosphorylation	EGTGDSSSESSMSDF CCCCCCCCCHHHCCC	45.51	27251275
168	Phosphorylation	TGDSSSESSMSDFSE CCCCCCCHHHCCCCH	33.03	27251275
169	Phosphorylation	GDSSSESSMSDFSED CCCCCCHHHCCCCHH	20.46	27251275
171	Phosphorylation	SSSESSMSDFSEDEA CCCCHHHCCCCHHHH	37.13	27251275
174	Phosphorylation	ESSMSDFSEDEAQDM CHHHCCCCHHHHHHH	49.48	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
Oops, there are no upstream regulatory protein records of UBE2H_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UBE2H_HUMAN !!

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 UBE2H_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STAM2_HUMAN	STAM2	physical	17588522
EPS15_HUMAN	EPS15	physical	17588522
DPOLM_HUMAN	POLM	physical	17588522
DPOLL_HUMAN	POLL	physical	17588522
HDAC6_HUMAN	HDAC6	physical	17588522
UBS3B_HUMAN	UBASH3B	physical	17588522
RN103_HUMAN	RNF103	physical	19690564
NEUL1_HUMAN	NEURL1	physical	19690564
RN186_HUMAN	RNF186	physical	19690564
TRI56_HUMAN	TRIM56	physical	19690564
RNF37_HUMAN	UBOX5	physical	19549727
DZIP3_HUMAN	DZIP3	physical	19549727
RNF34_HUMAN	RNF34	physical	19549727
TRI27_HUMAN	TRIM27	physical	19549727
RNF4_HUMAN	RNF4	physical	19549727
TRAIP_HUMAN	TRAIP	physical	19549727
TRI36_HUMAN	TRIM36	physical	19549727
DTX3_HUMAN	DTX3	physical	19549727
RN114_HUMAN	RNF114	physical	19549727
BRAP_HUMAN	BRAP	physical	19549727
LRSM1_HUMAN	LRSAM1	physical	19549727
CBLC_HUMAN	CBLC	physical	19549727
DTX3L_HUMAN	DTX3L	physical	19549727
MKRN3_HUMAN	MKRN3	physical	19549727
TRI23_HUMAN	TRIM23	physical	19549727
RNF10_HUMAN	RNF10	physical	19549727
R113B_HUMAN	RNF113B	physical	19549727
RN133_HUMAN	RNF133	physical	19549727
RN139_HUMAN	RNF139	physical	19549727
R144A_HUMAN	RNF144A	physical	19549727
RN146_HUMAN	RNF146	physical	19549727
RN166_HUMAN	RNF166	physical	19549727
RN185_HUMAN	RNF185	physical	19549727
MARHA_HUMAN	MARCH10	physical	19549727
RING2_HUMAN	RNF2	physical	19549727
RNF38_HUMAN	RNF38	physical	19549727
RNF6_HUMAN	RNF6	physical	19549727
TRI17_HUMAN	TRIM17	physical	19549727
TRIM2_HUMAN	TRIM2	physical	19549727
TRI37_HUMAN	TRIM37	physical	19549727
TRIM5_HUMAN	TRIM5	physical	19549727
TF65_HUMAN	RELA	physical	14690596
UBP2L_HUMAN	UBAP2L	physical	22939629
UBP5_HUMAN	USP5	physical	22939629
UFC1_HUMAN	UFC1	physical	22939629
TRI72_HUMAN	TRIM72	physical	23965929
ANXA6_HUMAN	ANXA6	physical	22863883
IDHC_HUMAN	IDH1	physical	22863883
MTAP_HUMAN	MTAP	physical	22863883
FAK1_HUMAN	PTK2	physical	24344130
UBE2H_HUMAN	UBE2H	physical	20061386
WDR26_HUMAN	WDR26	physical	27173435
ARMC8_HUMAN	ARMC8	physical	27173435

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 UBE2H_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-60 AND LYS-64, AND MASSSPECTROMETRY.	19608861 [Abstract]