dbPTM

BID_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BID_HUMAN
UniProt AC	P55957
Protein Name	BH3-interacting domain death agonist
Gene Name	BID
Organism	Homo sapiens (Human).
Sequence Length	195
Subcellular Localization	Cytoplasm. Mitochondrion membrane. When uncleaved, it is predominantly cytoplasmic. BH3-interacting domain death agonist p15: Mitochondrion membrane. Translocates to mitochondria as an integral membrane protein.. BH3-interacting domain death a
Protein Description	The major proteolytic product p15 BID allows the release of cytochrome c (By similarity). Isoform 1, isoform 2 and isoform 4 induce ICE-like proteases and apoptosis. Isoform 3 does not induce apoptosis. Counters the protective effect of Bcl-2..
Protein Sequence	MDCEVNNGSSLRDECITNLLVFGFLQSCSDNSFRRELDALGHELPVLAPQWEGYDELQTDGNRSSHSRLGRIEADSESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGLALQLRNTSRSEEDRNRDLATALEQLLQAYPRDMEKEKTMLVLALLLAKKVASHTPSLLRDVFHTTVNFINQNLRTYVRSLARNGMD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDCEVNNG -------CCCCCCCC	13.85	22814378
3 (in isoform 2)	Phosphorylation	-	6.41	-
4 (in isoform 4)	Phosphorylation	-	43.97	21406692
21 (in isoform 4)	Phosphorylation	-	5.06	21406692
28 (in isoform 2)	Phosphorylation	-	3.70	24719451
54	Phosphorylation	LAPQWEGYDELQTDG ECCCCCCCCCCCCCC	8.50	19605366
59	Phosphorylation	EGYDELQTDGNRSSH CCCCCCCCCCCCCCC	59.50	26356563
62 (in isoform 4)	Ubiquitination	-	43.39	21906983
64	Phosphorylation	LQTDGNRSSHSRLGR CCCCCCCCCCCCCCC	36.08	30576142
65	Phosphorylation	QTDGNRSSHSRLGRI CCCCCCCCCCCCCCC	23.42	26434776
67	Phosphorylation	DGNRSSHSRLGRIEA CCCCCCCCCCCCCCC	31.02	28464451
76	Phosphorylation	LGRIEADSESQEDII CCCCCCCCCCHHHHH	46.31	28450419
78	Phosphorylation	RIEADSESQEDIIRN CCCCCCCCHHHHHHH	42.70	17525332
83 (in isoform 3)	Phosphorylation	-	4.22	22210691
88 (in isoform 3)	Phosphorylation	-	22.89	22210691
93 (in isoform 3)	Phosphorylation	-	8.38	22210691
96	Phosphorylation	HLAQVGDSMDRSIPP HHHHHCCCCCCCCCC	19.36	26471730
100 (in isoform 2)	Phosphorylation	-	34.87	27642862
100	Phosphorylation	VGDSMDRSIPPGLVN HCCCCCCCCCCCHHH	34.87	22210691
110 (in isoform 2)	Phosphorylation	-	8.48	27642862
113 (in isoform 2)	Phosphorylation	-	4.79	24719451
116	Phosphorylation	LALQLRNTSRSEEDR HHHHHHCCCCCHHHH	21.05	21406692
117	Phosphorylation	ALQLRNTSRSEEDRN HHHHHCCCCCHHHHH	37.04	21406692
124 (in isoform 2)	Phosphorylation	-	54.89	-
147	Phosphorylation	RDMEKEKTMLVLALL CCHHHHHHHHHHHHH	19.48	30576142
158 (in isoform 1)	Ubiquitination	-	37.11	21906983
158	Ubiquitination	LALLLAKKVASHTPS HHHHHHHHHHHCCHH	37.11	2190698
161	Phosphorylation	LLAKKVASHTPSLLR HHHHHHHHCCHHHHH	30.77	30576142
204 (in isoform 2)	Ubiquitination	-		21906983

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
59	T	Phosphorylation	Kinase	MAPK8	P45983	GPS
59	T	Phosphorylation	Kinase	MAPK9	P45984	GPS
59	T	Phosphorylation	Kinase	MAPK10	P53779	GPS
59	T	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
59	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
59	T	Phosphorylation	Kinase	CK1_GROUP	-	PhosphoELM
59	T	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
64	S	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
64	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
64	S	Phosphorylation	Kinase	CK1_GROUP	-	PhosphoELM
64	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:20392206

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TR10B_HUMAN	TNFRSF10B	physical	15659383
FADD_HUMAN	FADD	physical	15659383
TNFL6_HUMAN	FASLG	physical	15659383
MK08_HUMAN	MAPK8	physical	15659383
CASPA_HUMAN	CASP10	physical	15659383
CASP8_HUMAN	CASP8	physical	15659383
TNR1A_HUMAN	TNFRSF1A	physical	15659383
BCL2_HUMAN	BCL2	physical	15520201
BID_HUMAN	BID	physical	11805084
B2LA1_HUMAN	BCL2A1	physical	11929871
ERG28_HUMAN	C14orf1	physical	21900206
G3P_HUMAN	GAPDH	physical	21900206
ZHX1_HUMAN	ZHX1	physical	21900206
CRNL1_HUMAN	CRNKL1	physical	21900206
GBP2_HUMAN	GBP2	physical	21900206
PKHM1_HUMAN	PLEKHM1	physical	21900206
TBB2B_HUMAN	TUBB2B	physical	21900206
TLE1_HUMAN	TLE1	physical	21900206
RBM48_HUMAN	RBM48	physical	21900206
DPYL1_HUMAN	CRMP1	physical	21900206
SETB1_HUMAN	SETDB1	physical	21900206
FBN3_HUMAN	FBN3	physical	21900206
RFA1_HUMAN	RPA1	physical	21859891
RFA2_HUMAN	RPA2	physical	21859891
UBQL2_HUMAN	UBQLN2	physical	22939629
SQSTM_HUMAN	SQSTM1	physical	23333919
CAV1_HUMAN	CAV1	physical	21382479
BCL2_HUMAN	BCL2	physical	18835031
REL_HUMAN	REL	physical	25416956
SAHH2_HUMAN	AHCYL1	physical	25416956
BAK_HUMAN	BAK1	physical	25408501
B2CL1_HUMAN	BCL2L1	physical	25241761
BAX_HUMAN	BAX	physical	25241761
KC1E_HUMAN	CSNK1E	physical	25241761
TNFL6_HUMAN	FASLG	physical	25241761
RHOA_HUMAN	RHOA	physical	25241761
TNR6_HUMAN	FAS	physical	25241761

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 BID_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-78, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-54, AND MASSSPECTROMETRY.	15592455 [Abstract]