CHM1B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CHM1B_HUMAN
• UniProt AC: Q7LBR1
• Protein Name: Charged multivesicular body protein 1b
• Gene Name: CHMP1B
• Organism: Homo sapiens (Human).
• Sequence Length: 199
• Subcellular Localization: Cytoplasm, cytosol. Endosome. Late endosome membrane ; Peripheral membrane protein . Localizes to the midbody of dividing cells, colocalizing with CEP55 and CHMP5. Localized at the periphery of the Fleming body.
• Protein Description: Probable peripherally associated 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. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to the midbody of dividing cells. Involved in HIV-1 p6- and p9-dependent virus release..
• Protein Sequence: MSNMEKHLFNLKFAAKELSRSAKKCDKEEKAEKAKIKKAIQKGNMEVARIHAENAIRQKNQAVNFLRMSARVDAVAARVQTAVTMGKVTKSMAGVVKSMDATLKTMNLEKISALMDKFEHQFETLDVQTQQMEDTMSSTTTLTTPQNQVDMLLQEMADEAGLDLNMELPQGQTGSVGTSVASAEQDELSQRLARLRDQV

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	Phosphorylation	------MSNMEKHLF ------CCHHHHHHH	44.90	24719451
6	Ubiquitination	--MSNMEKHLFNLKF --CCHHHHHHHHHHH	34.53	23000965
6	Malonylation	--MSNMEKHLFNLKF --CCHHHHHHHHHHH	34.53	26320211
6	Acetylation	--MSNMEKHLFNLKF --CCHHHHHHHHHHH	34.53	26822725
6	2-Hydroxyisobutyrylation	--MSNMEKHLFNLKF --CCHHHHHHHHHHH	34.53	-
12	Ubiquitination	EKHLFNLKFAAKELS HHHHHHHHHHHHHHH	33.78	23000965
16	Acetylation	FNLKFAAKELSRSAK HHHHHHHHHHHHHHH	56.62	22424773
16	Ubiquitination	FNLKFAAKELSRSAK HHHHHHHHHHHHHHH	56.62	23000965
37	Ubiquitination	KAEKAKIKKAIQKGN HHHHHHHHHHHHHCC	35.13	23000965
38	Ubiquitination	AEKAKIKKAIQKGNM HHHHHHHHHHHHCCH	54.95	23000965
42	Malonylation	KIKKAIQKGNMEVAR HHHHHHHHCCHHHHH	46.25	26320211
42	Ubiquitination	KIKKAIQKGNMEVAR HHHHHHHHCCHHHHH	46.25	23000965
59	Ubiquitination	AENAIRQKNQAVNFL HHHHHHHHHHHHHHH	40.97	24816145
81	Phosphorylation	AVAARVQTAVTMGKV HHHHHHHHHHHHCCC	21.90	24719451
84	Phosphorylation	ARVQTAVTMGKVTKS HHHHHHHHHCCCHHH	20.10	27470641
87	Acetylation	QTAVTMGKVTKSMAG HHHHHHCCCHHHHHH	35.59	25953088
87	Ubiquitination	QTAVTMGKVTKSMAG HHHHHHCCCHHHHHH	35.59	23000965
89	Phosphorylation	AVTMGKVTKSMAGVV HHHHCCCHHHHHHHH	22.38	24719451
90	Malonylation	VTMGKVTKSMAGVVK HHHCCCHHHHHHHHH	41.02	32601280
90	Ubiquitination	VTMGKVTKSMAGVVK HHHCCCHHHHHHHHH	41.02	23000965
91	Phosphorylation	TMGKVTKSMAGVVKS HHCCCHHHHHHHHHH	12.42	24719451
97	Malonylation	KSMAGVVKSMDATLK HHHHHHHHHHHHHHH	37.34	26320211
97	Acetylation	KSMAGVVKSMDATLK HHHHHHHHHHHHHHH	37.34	27452117
97	Ubiquitination	KSMAGVVKSMDATLK HHHHHHHHHHHHHHH	37.34	23000965
102	Phosphorylation	VVKSMDATLKTMNLE HHHHHHHHHHHCCHH	25.23	24719451
104	Ubiquitination	KSMDATLKTMNLEKI HHHHHHHHHCCHHHH	41.18	23000965
110	Ubiquitination	LKTMNLEKISALMDK HHHCCHHHHHHHHHH	45.16	23000965
173	Phosphorylation	MELPQGQTGSVGTSV CCCCCCCCCCCCCHH	37.94	24275569
175	Phosphorylation	LPQGQTGSVGTSVAS CCCCCCCCCCCHHHH	22.29	29759185
178	Phosphorylation	GQTGSVGTSVASAEQ CCCCCCCCHHHHHHH	20.19	24275569
179	Phosphorylation	QTGSVGTSVASAEQD CCCCCCCHHHHHHHH	15.12	24275569

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

Oops, there are no upstream regulatory protein records of CHM1B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CHM1B_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 CHM1B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBP8_HUMAN	USP8	physical	17711858
CHM1B_HUMAN	CHMP1B	physical	16730941
VPS4A_HUMAN	VPS4A	physical	16730941
SKAP_HUMAN	KNSTRN	physical	16730941
SUCA_HUMAN	SUCLG1	physical	16730941
U520_HUMAN	SNRNP200	physical	16730941
RB11A_HUMAN	RAB11A	physical	16730941
STABP_HUMAN	STAMBP	physical	16730941
CNO10_HUMAN	CNOT10	physical	16730941
SSRP1_HUMAN	SSRP1	physical	16730941
RASF7_HUMAN	RASSF7	physical	16730941
STABP_HUMAN	STAMBP	physical	21988832
IST1_HUMAN	IST1	physical	26344197

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.