dbPTM

BAP18_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BAP18_HUMAN
UniProt AC	Q8IXM2
Protein Name	Chromatin complexes subunit BAP18
Gene Name	BAP18
Organism	Homo sapiens (Human).
Sequence Length	172
Subcellular Localization	Nucleus .
Protein Description	Component of chromatin complexes such as the MLL1/MLL and NURF complexes..
Protein Sequence	MTSASTKVGEIFSAAGAAFTKLGELTMQLHPVADSSPAGAKWTETEIEMLRAAVKRFGDDLNHISCVIKERTVAQIKATVKRKVYEDSGIPLPAESPKKGPKKVASGVLSPPPAAPPPSSSSVPEAGGPPIKKQKADVTLSALNDSDANSDVVDIEGLGETPPAKKLNFDQA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
26 (in isoform 2)	Phosphorylation	-	9.89	20873877
26	Phosphorylation	FTKLGELTMQLHPVA HHHHHHHHEEEEECC	9.89	27794612
27	Sulfoxidation	TKLGELTMQLHPVAD HHHHHHHEEEEECCC	6.62	21406390
35	Phosphorylation	QLHPVADSSPAGAKW EEEECCCCCCCCCCC	28.60	23401153
35 (in isoform 2)	Phosphorylation	-	28.60	30266825
36	Phosphorylation	LHPVADSSPAGAKWT EEECCCCCCCCCCCC	21.22	22167270
36 (in isoform 2)	Phosphorylation	-	21.22	30266825
41	Ubiquitination	DSSPAGAKWTETEIE CCCCCCCCCCHHHHH	54.45	29967540
43	Phosphorylation	SPAGAKWTETEIEML CCCCCCCCHHHHHHH	32.11	26074081
45	Phosphorylation	AGAKWTETEIEMLRA CCCCCCHHHHHHHHH	34.58	26074081
62	Phosphorylation	KRFGDDLNHISCVIK HHHCCCCCCCEEEEE	37.12	32645325
69	Ubiquitination	NHISCVIKERTVAQI CCCEEEEECCCHHHH	22.27	32015554
69	Acetylation	NHISCVIKERTVAQI CCCEEEEECCCHHHH	22.27	23749302
76	Phosphorylation	KERTVAQIKATVKRK ECCCHHHHHHHHCCH	2.06	32142685
77	Ubiquitination	ERTVAQIKATVKRKV CCCHHHHHHHHCCHH	26.40	32015554
77	Acetylation	ERTVAQIKATVKRKV CCCHHHHHHHHCCHH	26.40	25953088
85	Phosphorylation	ATVKRKVYEDSGIPL HHHCCHHHCCCCCCC	19.63	22167270
88	Phosphorylation	KRKVYEDSGIPLPAE CCHHHCCCCCCCCCC	27.04	22167270
96	Phosphorylation	GIPLPAESPKKGPKK CCCCCCCCCCCCCCC	44.09	19664994
96 (in isoform 3)	Phosphorylation	-	44.09	24719451
106	Phosphorylation	KGPKKVASGVLSPPP CCCCCCCCCCCCCCC	32.21	23401153
106 (in isoform 3)	Phosphorylation	-	32.21	27251275
110	Phosphorylation	KVASGVLSPPPAAPP CCCCCCCCCCCCCCC	32.71	23401153
110 (in isoform 3)	Phosphorylation	-	32.71	24719451
112	Phosphorylation	ASGVLSPPPAAPPPS CCCCCCCCCCCCCCC	27.99	32142685
119	Phosphorylation	PPAAPPPSSSSVPEA CCCCCCCCCCCCCCC	48.93	23927012
119	O-linked_Glycosylation	PPAAPPPSSSSVPEA CCCCCCCCCCCCCCC	48.93	21740066
120	Phosphorylation	PAAPPPSSSSVPEAG CCCCCCCCCCCCCCC	32.19	23927012
121	Phosphorylation	AAPPPSSSSVPEAGG CCCCCCCCCCCCCCC	39.43	25159151
122	Phosphorylation	APPPSSSSVPEAGGP CCCCCCCCCCCCCCC	43.57	23927012
127	Phosphorylation	SSSVPEAGGPPIKKQ CCCCCCCCCCCCCCC	47.69	32142685
131	Ubiquitination	PEAGGPPIKKQKADV CCCCCCCCCCCCCCE	11.09	32015554
132	Acetylation	EAGGPPIKKQKADVT CCCCCCCCCCCCCEE	55.73	25953088
139	Phosphorylation	KKQKADVTLSALNDS CCCCCCEEEECCCCC	18.62	20873877
141	Phosphorylation	QKADVTLSALNDSDA CCCCEEEECCCCCCC	22.73	28355574
146 (in isoform 3)	Phosphorylation	-	37.23	24719451
146	Phosphorylation	TLSALNDSDANSDVV EEECCCCCCCCCCCC	37.23	30266825
150 (in isoform 3)	Phosphorylation	-	33.24	24719451
150	Phosphorylation	LNDSDANSDVVDIEG CCCCCCCCCCCCEEC	33.24	30266825
161 (in isoform 3)	Phosphorylation	-	32.54	24719451
161	Phosphorylation	DIEGLGETPPAKKLN CEECCCCCCCCHHCC	32.54	30266825
165	Ubiquitination	LGETPPAKKLNFDQA CCCCCCCHHCCCCCC	64.66	32015554

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
96	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BAP18_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 BAP18_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RBBP4_HUMAN	RBBP4	physical	20850016
HMGX4_HUMAN	HMGXB4	physical	20850016
BPTF_HUMAN	BPTF	physical	20850016
SMCA5_HUMAN	SMARCA5	physical	20850016
SMCA1_HUMAN	SMARCA1	physical	20850016
RBBP7_HUMAN	RBBP7	physical	20850016
GRP75_HUMAN	HSPA9	physical	20850016
LMNB1_HUMAN	LMNB1	physical	20850016
HSP7C_HUMAN	HSPA8	physical	20850016
LMNA_HUMAN	LMNA	physical	20850016
BPTF_HUMAN	BPTF	physical	26496610
S38A5_HUMAN	SLC38A5	physical	26496610

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 BAP18_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASSSPECTROMETRY.	17287340 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASSSPECTROMETRY.	16964243 [Abstract]