dbPTM

CHM4B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CHM4B_HUMAN
UniProt AC	Q9H444
Protein Name	Charged multivesicular body protein 4b
Gene Name	CHMP4B
Organism	Homo sapiens (Human).
Sequence Length	224
Subcellular Localization	Cytoplasm, cytosol . Late endosome membrane Peripheral membrane protein . Midbody . Nucleus envelope . Recruited to the nuclear envelope by CHMP7 during late anaphase (PubMed:26040712). Localizes transiently to the midbody arms immediately before a
Protein Description	Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. [PubMed: 12860994]
Protein Sequence	MSVFGKLFGAGGGKAGKGGPTPQEAIQRLRDTEEMLSKKQEFLEKKIEQELTAAKKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTNTEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFDEDELMAELEELEQEELDKNLLEISGPETVPLPNVPSIALPSKPAKKKEEEDDDMKELENWAGSM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSVFGKLFG ------CCHHHHCCC	26.59	24719451
2	Acetylation	------MSVFGKLFG ------CCHHHHCCC	26.59	22814378
6	Acetylation	--MSVFGKLFGAGGG --CCHHHHCCCCCCC	29.22	19608861
6	Ubiquitination	--MSVFGKLFGAGGG --CCHHHHCCCCCCC	29.22	23000965
14	Ubiquitination	LFGAGGGKAGKGGPT CCCCCCCCCCCCCCC	58.18	33845483
14	Acetylation	LFGAGGGKAGKGGPT CCCCCCCCCCCCCCC	58.18	25953088
17	Acetylation	AGGGKAGKGGPTPQE CCCCCCCCCCCCHHH	66.60	26051181
17	Ubiquitination	AGGGKAGKGGPTPQE CCCCCCCCCCCCHHH	66.60	33845483
17	Malonylation	AGGGKAGKGGPTPQE CCCCCCCCCCCCHHH	66.60	26320211
35	Sulfoxidation	RLRDTEEMLSKKQEF HHHHHHHHHHHHHHH	4.10	21406390
38	Ubiquitination	DTEEMLSKKQEFLEK HHHHHHHHHHHHHHH	55.29	32015554
38	Succinylation	DTEEMLSKKQEFLEK HHHHHHHHHHHHHHH	55.29	23954790
55	Acetylation	EQELTAAKKHGTKNK HHHHHHHHHHCCHHH	42.72	26051181
55	Ubiquitination	EQELTAAKKHGTKNK HHHHHHHHHHCCHHH	42.72	32015554
70	Ubiquitination	RAALQALKRKKRYEK HHHHHHHHHHHHHHH	66.25	32015554
70	2-Hydroxyisobutyrylation	RAALQALKRKKRYEK HHHHHHHHHHHHHHH	66.25	-
87	Phosphorylation	AQIDGTLSTIEFQRE HHCCCCHHHHHHHHH	27.46	-
101	Phosphorylation	EALENANTNTEVLKN HHHHHCCCCHHHHHH	40.90	25072903
103	Phosphorylation	LENANTNTEVLKNMG HHHCCCCHHHHHHHH	25.98	25072903
107	Ubiquitination	NTNTEVLKNMGYAAK CCCHHHHHHHHHHHH	50.49	23000965
111	Phosphorylation	EVLKNMGYAAKAMKA HHHHHHHHHHHHHHH	7.82	28102081
114	Acetylation	KNMGYAAKAMKAAHD HHHHHHHHHHHHHHH	40.62	19608861
114	Ubiquitination	KNMGYAAKAMKAAHD HHHHHHHHHHHHHHH	40.62	32015554
117	Methylation	GYAAKAMKAAHDNMD HHHHHHHHHHHHCCC	47.48	-
184	Phosphorylation	DKNLLEISGPETVPL HHHCHHHHCCCCCCC	38.63	29255136
188	Phosphorylation	LEISGPETVPLPNVP HHHHCCCCCCCCCCC	30.47	29255136
196	Phosphorylation	VPLPNVPSIALPSKP CCCCCCCCCCCCCCC	19.06	29514088
201	Phosphorylation	VPSIALPSKPAKKKE CCCCCCCCCCCCCCC	52.72	29514088
202	Ubiquitination	PSIALPSKPAKKKEE CCCCCCCCCCCCCCC	47.24	22817900
202	Acetylation	PSIALPSKPAKKKEE CCCCCCCCCCCCCCC	47.24	23954790
205	Ubiquitination	ALPSKPAKKKEEEDD CCCCCCCCCCCCCCC	73.27	22817900
206	Ubiquitination	LPSKPAKKKEEEDDD CCCCCCCCCCCCCCH	68.47	22817900
207	Ubiquitination	PSKPAKKKEEEDDDM CCCCCCCCCCCCCHH	70.43	22817900
223	Phosphorylation	ELENWAGSM------ HHHHHHHCC------	17.36	28355574

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 CHM4B_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CHM4B_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 CHM4B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PDC6I_HUMAN	PDCD6IP	physical	14505570
NOLC1_HUMAN	NOLC1	physical	21264300
CHM4B_HUMAN	CHMP4B	physical	16730941
CHM1B_HUMAN	CHMP1B	physical	16730941
CHM4A_HUMAN	CHMP4A	physical	16730941
CHMP3_HUMAN	CHMP3	physical	16730941
CHM4C_HUMAN	CHMP4C	physical	16730941
VPS4A_HUMAN	VPS4A	physical	16730941
PIAS2_HUMAN	PIAS2	physical	16730941
EXOS9_HUMAN	EXOSC9	physical	16730941
HIPK2_HUMAN	HIPK2	physical	16730941
UBC9_HUMAN	UBE2I	physical	16730941
STABP_HUMAN	STAMBP	physical	16730941
MVP_HUMAN	MVP	physical	22939629
CHM2A_HUMAN	CHMP2A	physical	26040713
CHM1B_HUMAN	CHMP1B	physical	26344197
IMDH2_HUMAN	IMPDH2	physical	26344197
VATA_HUMAN	ATP6V1A	physical	26496610
VATB2_HUMAN	ATP6V1B2	physical	26496610
VATE1_HUMAN	ATP6V1E1	physical	26496610
VPP1_HUMAN	ATP6V0A1	physical	26496610
BST2_HUMAN	BST2	physical	26496610
CALX_HUMAN	CANX	physical	26496610
EF1G_HUMAN	EEF1G	physical	26496610
FLOT2_HUMAN	FLOT2	physical	26496610
MPRI_HUMAN	IGF2R	physical	26496610
MECP2_HUMAN	MECP2	physical	26496610
NUP98_HUMAN	NUP98	physical	26496610
CHM1A_HUMAN	CHMP1A	physical	26496610
E2AK2_HUMAN	EIF2AK2	physical	26496610
RL6_HUMAN	RPL6	physical	26496610
SPAST_HUMAN	SPAST	physical	26496610
TAF1_HUMAN	TAF1	physical	26496610
TARB1_HUMAN	TARBP1	physical	26496610
ELOC_HUMAN	TCEB1	physical	26496610
TS101_HUMAN	TSG101	physical	26496610
CEGT_HUMAN	UGCG	physical	26496610
EVI5_HUMAN	EVI5	physical	26496610
HERC2_HUMAN	HERC2	physical	26496610
VA0D1_HUMAN	ATP6V0D1	physical	26496610
VP9D1_HUMAN	VPS9D1	physical	26496610
IST1_HUMAN	IST1	physical	26496610
PDC6I_HUMAN	PDCD6IP	physical	26496610
FLOT1_HUMAN	FLOT1	physical	26496610
TM9S1_HUMAN	TM9SF1	physical	26496610
CTCF_HUMAN	CTCF	physical	26496610
CAN7_HUMAN	CAPN7	physical	26496610
ZN281_HUMAN	ZNF281	physical	26496610
IMA7_HUMAN	KPNA6	physical	26496610
NECT3_HUMAN	PVRL3	physical	26496610
CHM2B_HUMAN	CHMP2B	physical	26496610
FBX5_HUMAN	FBXO5	physical	26496610
CHM2A_HUMAN	CHMP2A	physical	26496610
SCMC1_HUMAN	SLC25A24	physical	26496610
CHMP5_HUMAN	CHMP5	physical	26496610
CHMP3_HUMAN	CHMP3	physical	26496610
SARAF_HUMAN	SARAF	physical	26496610
KDM3B_HUMAN	KDM3B	physical	26496610
S38A2_HUMAN	SLC38A2	physical	26496610
NLE1_HUMAN	NLE1	physical	26496610
C2D1A_HUMAN	CC2D1A	physical	26496610
DAAF5_HUMAN	DNAAF5	physical	26496610
CSCL2_HUMAN	TMEM63B	physical	26496610
CK5P2_HUMAN	CDK5RAP2	physical	26496610
CHM1B_HUMAN	CHMP1B	physical	26496610
TTC7A_HUMAN	TTC7A	physical	26496610
NBEL1_HUMAN	NBEAL1	physical	26496610
DCTP1_HUMAN	DCTPP1	physical	26496610
ZMYM1_HUMAN	ZMYM1	physical	26496610
RN170_HUMAN	RNF170	physical	26496610
TLN2_HUMAN	TLN2	physical	26496610
MB12A_HUMAN	MVB12A	physical	26496610
OSBL9_HUMAN	OSBPL9	physical	26496610
MITD1_HUMAN	MITD1	physical	26496610
CA052_HUMAN	C1orf52	physical	26496610
C2D1B_HUMAN	CC2D1B	physical	26496610
METRL_HUMAN	METRNL	physical	26496610
PDC6I_HUMAN	PDCD6IP	physical	26490116

Drug and Disease Associations

Kegg Disease
H01202	Cataract
OMIM Disease
605387	Cataract 31, multiple types (CTRCT31)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CHM4B_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-6 AND LYS-114, AND MASSSPECTROMETRY.	19608861 [Abstract]