dbPTM

BAF_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BAF_HUMAN
UniProt AC	O75531
Protein Name	Barrier-to-autointegration factor
Gene Name	BANF1
Organism	Homo sapiens (Human).
Sequence Length	89
Subcellular Localization	Barrier-to-autointegration factor: Nucleus . Cytoplasm . Chromosome . Nucleus envelope . Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase.
Protein Description	Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging.; (Microbial infection) Exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD.; (Microbial infection) In case of poxvirus infection, has an antiviral activity by blocking viral DNA replication..
Protein Sequence	MTTSQKHRDFVAEPMGEKPVGSLAGIGEVLGKKLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MTTSQKHR -------CCCCHHHH	9.23	20068231
2	Acetylation	------MTTSQKHRD ------CCCCHHHHH	34.84	19413330
2	Phosphorylation	------MTTSQKHRD ------CCCCHHHHH	34.84	22617229
3	Phosphorylation	-----MTTSQKHRDF -----CCCCHHHHHH	28.06	23401153
4	Phosphorylation	----MTTSQKHRDFV ----CCCCHHHHHHC	28.24	23401153
6	Acetylation	--MTTSQKHRDFVAE --CCCCHHHHHHCCC	40.13	25825284
6	2-Hydroxyisobutyrylation	--MTTSQKHRDFVAE --CCCCHHHHHHCCC	40.13	-
18	Acetylation	VAEPMGEKPVGSLAG CCCCCCCCCCCCHHH	38.99	26051181
18	2-Hydroxyisobutyrylation	VAEPMGEKPVGSLAG CCCCCCCCCCCCHHH	38.99	-
18	Ubiquitination	VAEPMGEKPVGSLAG CCCCCCCCCCCCHHH	38.99	-
22	Phosphorylation	MGEKPVGSLAGIGEV CCCCCCCCHHHHHHH	18.45	25867546
32	Succinylation	GIGEVLGKKLEERGF HHHHHHHHHHHHCCC	50.45	23954790
32	Acetylation	GIGEVLGKKLEERGF HHHHHHHHHHHHCCC	50.45	25953088
32	2-Hydroxyisobutyrylation	GIGEVLGKKLEERGF HHHHHHHHHHHHCCC	50.45	-
32	Ubiquitination	GIGEVLGKKLEERGF HHHHHHHHHHHHCCC	50.45	21890473
37	Methylation	LGKKLEERGFDKAYV HHHHHHHCCCCHHHE	41.52	-
41	Ubiquitination	LEERGFDKAYVVLGQ HHHCCCCHHHEEHHE	39.08	-
43	Phosphorylation	ERGFDKAYVVLGQFL HCCCCHHHEEHHEEE	9.24	23822953
54	Acetylation	GQFLVLKKDEDLFRE HEEEEEECCHHHHHH	63.29	26051181
54	Ubiquitination	GQFLVLKKDEDLFRE HEEEEEECCHHHHHH	63.29	-
54	2-Hydroxyisobutyrylation	GQFLVLKKDEDLFRE HEEEEEECCHHHHHH	63.29	-
60	Methylation	KKDEDLFREWLKDTC ECCHHHHHHHHHHHC	41.29	-
64	Ubiquitination	DLFREWLKDTCGANA HHHHHHHHHHCCCCC	52.65	-
64	Acetylation	DLFREWLKDTCGANA HHHHHHHHHHCCCCC	52.65	25825284
64	Malonylation	DLFREWLKDTCGANA HHHHHHHHHHCCCCC	52.65	26320211
72	Acetylation	DTCGANAKQSRDCFG HHCCCCCCCHHHHHH	48.92	26051181
72	Ubiquitination	DTCGANAKQSRDCFG HHCCCCCCCHHHHHH	48.92	21890473
82	Methylation	RDCFGCLREWCDAFL HHHHHHHHHHHHHHC	39.17	-

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
2	T	Phosphorylation	Kinase	VRK1	Q99986	Uniprot
2	T	Phosphorylation	Kinase	VRK2	Q86Y07	Uniprot
2	T	Phosphorylation	Kinase	VIRAL VACV B1 KINASE	-	Uniprot
3	T	Phosphorylation	Kinase	VRK1	Q99986	Uniprot
3	T	Phosphorylation	Kinase	VRK2	Q86Y07	Uniprot
3	T	Phosphorylation	Kinase	VIRAL VACV B1 KINASE	-	Uniprot
4	S	Phosphorylation	Kinase	VRK1	Q99986	Uniprot
4	S	Phosphorylation	Kinase	VRK2	Q86Y07	Uniprot
4	S	Phosphorylation	Kinase	VRK3	Q8IV63	PSP
4	S	Phosphorylation	Kinase	VIRAL VACV B1 KINASE	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
2	T	Phosphorylation	16495336
Phosphorylation on Thr-2; Thr-3 and Ser-4 disrupts its ability to bind DNA and reduces its ability to bind LEM domain-containing proteins.
2	T	Phosphorylation	16495336
Ser-4 is the major site of phosphorylation as compared to Thr-2 and Thr-3.
3	T	Phosphorylation	16495336
Phosphorylation on Thr-2; Thr-3 and Ser-4 disrupts its ability to bind DNA and reduces its ability to bind LEM domain-containing proteins.
3	T	Phosphorylation	16495336
Ser-4 is the major site of phosphorylation as compared to Thr-2 and Thr-3.
4	S	Phosphorylation	16371512
Phosphorylation on Thr-2; Thr-3 and Ser-4 disrupts its ability to bind DNA and reduces its ability to bind LEM domain-containing proteins.
4	S	Phosphorylation	16371512
Ser-4 is the major site of phosphorylation as compared to Thr-2 and Thr-3.

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 BAF_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BAF_HUMAN	BANF1	physical	10924106
DDB1_HUMAN	DDB1	physical	19759913
DDB2_HUMAN	DDB2	physical	19759913
CHD4_HUMAN	CHD4	physical	19759913
SMOC2_HUMAN	SMOC2	physical	19759913
MDC1_HUMAN	MDC1	physical	19759913
CBX3_HUMAN	CBX3	physical	19759913
RECQ1_HUMAN	RECQL	physical	19759913
NUMA1_HUMAN	NUMA1	physical	19759913
DPY30_HUMAN	DPY30	physical	19759913
ACL6A_HUMAN	ACTL6A	physical	19759913
HDAC1_HUMAN	HDAC1	physical	19759913
HDAC2_HUMAN	HDAC2	physical	19759913
KPYM_HUMAN	PKM	physical	19759913
FLNA_HUMAN	FLNA	physical	19759913
ACINU_HUMAN	ACIN1	physical	19759913
CAF1B_HUMAN	CHAF1B	physical	19759913
CBX1_HUMAN	CBX1	physical	19759913
MTA2_HUMAN	MTA2	physical	19759913
HNRPC_HUMAN	HNRNPC	physical	19759913
RBBP7_HUMAN	RBBP7	physical	19759913
SMRC2_HUMAN	SMARCC2	physical	19759913
APTX_HUMAN	APTX	physical	19759913
SMD3_HUMAN	SNRPD3	physical	19759913
PARP1_HUMAN	PARP1	physical	19759913
EFTU_HUMAN	TUFM	physical	19759913
TRA2B_HUMAN	TRA2B	physical	19759913
LBN_HUMAN	EVC2	physical	19759913
HMGA1_HUMAN	HMGA1	physical	19759913
ATP5J_HUMAN	ATP5J	physical	19759913
LMNB2_HUMAN	LMNB2	physical	19759913
SMCA2_HUMAN	SMARCA2	physical	19759913
EHMT2_HUMAN	EHMT2	physical	19759913
TCP4_HUMAN	SUB1	physical	19759913
CD2B2_HUMAN	CD2BP2	physical	19759913
PAEP_HUMAN	PAEP	physical	19759913
BAF_HUMAN	BANF1	physical	19759913
BCL7C_HUMAN	BCL7C	physical	19759913
PSIP1_HUMAN	PSIP1	physical	19759913
ZN428_HUMAN	ZNF428	physical	19759913
LMNA_HUMAN	LMNA	physical	19759913
HNRPD_HUMAN	HNRNPD	physical	19759913
SMCE1_HUMAN	SMARCE1	physical	19759913
K1C16_HUMAN	KRT16	physical	19759913
XPC_HUMAN	XPC	physical	19759913
SET_HUMAN	SET	physical	22127260
EHMT2_HUMAN	EHMT2	physical	22127260
LAP2A_HUMAN	TMPO	physical	22939629
LAP2B_HUMAN	TMPO	physical	22939629
FBRL_HUMAN	FBL	physical	22939629
LC7L3_HUMAN	LUC7L3	physical	22939629
SOX4_HUMAN	SOX4	physical	25969425
ASPC1_HUMAN	ASPSCR1	physical	26344197
DNJC2_HUMAN	DNAJC2	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614008	Nestor-Guillermo progeria syndrome (NGPS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of BAF_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The vaccinia-related kinases phosphorylate the N' terminus of BAF,regulating its interaction with DNA and its retention in thenucleus."; Nichols R.J., Wiebe M.S., Traktman P.; Mol. Biol. Cell 17:2451-2464(2006). Cited for: PHOSPHORYLATION AT THR-2; THR-3 AND SER-4, AND SUBCELLULAR LOCATION.	16495336 [Abstract]
"Barrier-to-autointegration factor phosphorylation on Ser-4 regulatesemerin binding to lamin A in vitro and emerin localization in vivo."; Bengtsson L., Wilson K.L.; Mol. Biol. Cell 17:1154-1163(2006). Cited for: PHOSPHORYLATION AT SER-4, AND MUTAGENESIS OF SER-4.	16371512 [Abstract]

show

show

show

show

show

show