BROX_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BROX_HUMAN
• UniProt AC: Q5VW32
• Protein Name: BRO1 domain-containing protein BROX
• Gene Name: BROX
• Organism: Homo sapiens (Human).
• Sequence Length: 411
• Subcellular Localization: Membrane ; Lipid-anchor .
• Protein Sequence: MTHWFHRNPLKATAPVSFNYYGVVTGPSASKICNDLRSSRARLLELFTDLSCNPEMMKNAADSYFSLLQGFINSLDESTQESKLRYIQNFKWTDTLQGQVPSAQQDAVFELISMGFNVALWYTKYASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHLPKLITPAEKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKADHTLSSLEPAYSAKWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKEYGETKGPGPTVKPSGHLFFRKLGNLVKNTLEKCQRENGFIYFQKIPTEAPQLELKANYGLVEPIPFEFPPTSVQWTPETLAAFDLTKRPKDDSTKPKPEEEVKPVKEPDIKPQKDTGCYIS

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
2	Acetylation	------MTHWFHRNP ------CCCCCCCCC	28.02	19413330
2	Phosphorylation	------MTHWFHRNP ------CCCCCCCCC	28.02	23401153
11	Ubiquitination	WFHRNPLKATAPVSF CCCCCCCCCCCCEEE	44.97	-
13	Phosphorylation	HRNPLKATAPVSFNY CCCCCCCCCCEEEEE	29.88	23401153
17	Phosphorylation	LKATAPVSFNYYGVV CCCCCCEEEEEEEEE	13.50	28152594
20	Phosphorylation	TAPVSFNYYGVVTGP CCCEEEEEEEEEECC	10.29	28152594
21	Phosphorylation	APVSFNYYGVVTGPS CCEEEEEEEEEECCC	12.44	21082442
25	Phosphorylation	FNYYGVVTGPSASKI EEEEEEEECCCHHHH	40.75	23401153
30	Phosphorylation	VVTGPSASKICNDLR EEECCCHHHHHHHHH	27.22	30576142
38	Phosphorylation	KICNDLRSSRARLLE HHHHHHHHHHHHHHH	31.32	30576142
48	Phosphorylation	ARLLELFTDLSCNPE HHHHHHHHCCCCCHH	48.97	28355574
51	Phosphorylation	LELFTDLSCNPEMMK HHHHHCCCCCHHHHH	18.04	28355574
79	Phosphorylation	INSLDESTQESKLRY HHHCCCCCHHHHHHH	34.02	24275569
82	Phosphorylation	LDESTQESKLRYIQN CCCCCHHHHHHHHHH	27.46	24275569
91	Methylation	LRYIQNFKWTDTLQG HHHHHHCCCCCCCCC	57.65	-
116	Ubiquitination	FELISMGFNVALWYT HHHHHHCHHHHHHHH	5.07	-
123	Ubiquitination	FNVALWYTKYASRLA HHHHHHHHHHHHHHC	13.14	21890473
126	Ubiquitination	ALWYTKYASRLAGKE HHHHHHHHHHHCCCC	6.96	-
136	Phosphorylation	LAGKENITEDEAKEV HCCCCCCCHHHHHHH	49.30	-
141	Ubiquitination	NITEDEAKEVHRSLK CCCHHHHHHHHHHHH	59.21	-
148	Malonylation	KEVHRSLKIAAGIFK HHHHHHHHHHHHHHH	31.39	26320211
148	Ubiquitination	KEVHRSLKIAAGIFK HHHHHHHHHHHHHHH	31.39	-
148	Acetylation	KEVHRSLKIAAGIFK HHHHHHHHHHHHHHH	31.39	25953088
155	Ubiquitination	KIAAGIFKHLKESHL HHHHHHHHHHHHHCC	46.22	21890473
158	Ubiquitination	AGIFKHLKESHLPKL HHHHHHHHHHCCCCC	57.82	-
158	2-Hydroxyisobutyrylation	AGIFKHLKESHLPKL HHHHHHHHHHCCCCC	57.82	-
164	Ubiquitination	LKESHLPKLITPAEK HHHHCCCCCCCHHHC	59.90	-
171	Ubiquitination	KLITPAEKGRDLESR CCCCHHHCCCCHHHH	62.44	-
171	2-Hydroxyisobutyrylation	KLITPAEKGRDLESR CCCCHHHCCCCHHHH	62.44	-
171	Ubiquitination	KLITPAEKGRDLESR CCCCHHHCCCCHHHH	62.44	-
251	Acetylation	LKMCFYTAYAYCYHG HHHHHHHHHHHHHCC	3.90	19608861
279	Ubiquitination	RSLQEAEKLYAKAEA HHHHHHHHHHHHHHH	54.57	-
281	Phosphorylation	LQEAEKLYAKAEALC HHHHHHHHHHHHHHH	19.68	21253578
283	Ubiquitination	EAEKLYAKAEALCKE HHHHHHHHHHHHHHH	32.95	19608861
283	Acetylation	EAEKLYAKAEALCKE HHHHHHHHHHHHHHH	32.95	19608861
283	Malonylation	EAEKLYAKAEALCKE HHHHHHHHHHHHHHH	32.95	26320211
295	Ubiquitination	CKEYGETKGPGPTVK HHHHCCCCCCCCCCC	59.82	-
302	Ubiquitination	KGPGPTVKPSGHLFF CCCCCCCCCCCCCHH	35.62	21890473
331	Phosphorylation	QRENGFIYFQKIPTE HHHCCEEEEEECCCC	9.55	25884760
334	Ubiquitination	NGFIYFQKIPTEAPQ CCEEEEEECCCCCCC	40.53	21890473
337	Phosphorylation	IYFQKIPTEAPQLEL EEEEECCCCCCCCHH	48.53	29978859
337	O-linked_Glycosylation	IYFQKIPTEAPQLEL EEEEECCCCCCCCHH	48.53	OGP
348	Phosphorylation	QLELKANYGLVEPIP CCHHHHCCCCCCCCC	19.39	-
408	Methylation	KPQKDTGCYIS---- CCCCCCCCCCC----	2.71	18190528
408	Farnesylation	KPQKDTGCYIS---- CCCCCCCCCCC----	2.71	18190528
408	Farnesylation	KPQKDTGCYIS---- CCCCCCCCCCC----	2.71	18190528

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BROX_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 BROX_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GAG_HV1H2	gag	physical	19403673
CHM4B_HUMAN	CHMP4B	physical	19403673
LDHA_HUMAN	LDHA	physical	26344197
PDC6I_HUMAN	PDCD6IP	physical	26344197
DHSO_HUMAN	SORD	physical	26344197
TCEA1_HUMAN	TCEA1	physical	28514442
CHM1A_HUMAN	CHMP1A	physical	28514442
IPO9_HUMAN	IPO9	physical	28514442

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-283, AND MASS SPECTROMETRY.
PubMed: 19608861

Prenylation

"Towards complete sets of farnesylated and geranylgeranylatedproteins.";
Maurer-Stroh S., Koranda M., Benetka W., Schneider G., Sirota F.L.,Eisenhaber F.;
PLoS Comput. Biol. 3:634-648(2007).
Cited for: ISOPRENYLATION AT CYS-408.
PubMed: 17411337

"Brox, a novel farnesylated Bro1 domain-containing protein thatassociates with charged multivesicular body protein 4 (CHMP4).";
Ichioka F., Kobayashi R., Katoh K., Shibata H., Maki M.;
FEBS J. 275:682-692(2008).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ISOPRENYLATION AT CYS-408, AND INTERACTIONWITH CHMP4B.
PubMed: 18190528