CHM1A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CHM1A_HUMAN
• UniProt AC: Q9HD42
• Protein Name: Charged multivesicular body protein 1a
• Gene Name: CHMP1A
• Organism: Homo sapiens (Human).
• Sequence Length: 196
• Subcellular Localization: Cytoplasm. Endosome membrane; Peripheral membrane protein. Nucleus matrix. The cytoplasmic form is partially membrane-associated and localizes to early endosomes. The nuclear form remains associated with the chromosome scaffold during mitosis. On ove
• 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 to the midbody of dividing cells. May also be involved in chromosome condensation. Targets the Polycomb group (PcG) protein BMI1/PCGF4 to regions of condensed chromatin. May play a role in stable cell cycle progression and in PcG gene silencing..
• Protein Sequence: MDDTLFQLKFTAKQLEKLAKKAEKDSKAEQAKVKKALLQKNVECARVYAENAIRKKNEGVNWLRMASRVDAVASKVQTAVTMKGVTKNMAQVTKALDKALSTMDLQKVSSVMDRFEQQVQNLDVHTSVMEDSMSSATTLTTPQEQVDSLIMQIAEENGLEVLDQLSQLPEGASAVGESSVRSQEDQLSRRLAALRN

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
1	Acetylation	-------MDDTLFQL -------CCCHHHHH	10.70	19413330
11	Phosphorylation	TLFQLKFTAKQLEKL HHHHHHHHHHHHHHH	31.21	28102081
13	Malonylation	FQLKFTAKQLEKLAK HHHHHHHHHHHHHHH	52.97	26320211
13	Ubiquitination	FQLKFTAKQLEKLAK HHHHHHHHHHHHHHH	52.97	29967540
17	Acetylation	FTAKQLEKLAKKAEK HHHHHHHHHHHHHHH	63.44	25953088
26	Phosphorylation	AKKAEKDSKAEQAKV HHHHHHCCHHHHHHH	44.85	29396449
27	Acetylation	KKAEKDSKAEQAKVK HHHHHCCHHHHHHHH	67.10	20167786
40	Ubiquitination	VKKALLQKNVECARV HHHHHHHCCHHHHHH	64.03	33845483
40	Acetylation	VKKALLQKNVECARV HHHHHHHCCHHHHHH	64.03	25953088
48	Phosphorylation	NVECARVYAENAIRK CHHHHHHHHHHHHHH	11.57	28152594
55	Ubiquitination	YAENAIRKKNEGVNW HHHHHHHHHCCCCCH	54.56	23000965
56	Ubiquitination	AENAIRKKNEGVNWL HHHHHHHHCCCCCHH	50.84	23000965
56 (in isoform 1)	Ubiquitination	-	50.84	21890473
67	Phosphorylation	VNWLRMASRVDAVAS CCHHHHHHHHHHHHH	24.40	28857561
75 (in isoform 1)	Ubiquitination	-	28.73	21890473
75	Ubiquitination	RVDAVASKVQTAVTM HHHHHHHHHHHHHHH	28.73	32015554
78	Phosphorylation	AVASKVQTAVTMKGV HHHHHHHHHHHHCCC	26.53	26503514
81	Phosphorylation	SKVQTAVTMKGVTKN HHHHHHHHHCCCCCC	15.65	20068231
83	Acetylation	VQTAVTMKGVTKNMA HHHHHHHCCCCCCHH	40.64	25953088
83	Ubiquitination	VQTAVTMKGVTKNMA HHHHHHHCCCCCCHH	40.64	23000965
87	Malonylation	VTMKGVTKNMAQVTK HHHCCCCCCHHHHHH	42.17	26320211
87	Acetylation	VTMKGVTKNMAQVTK HHHCCCCCCHHHHHH	42.17	7676611
87	Ubiquitination	VTMKGVTKNMAQVTK HHHCCCCCCHHHHHH	42.17	23000965
94	Ubiquitination	KNMAQVTKALDKALS CCHHHHHHHHHHHHH	48.36	23000965
98 (in isoform 1)	Ubiquitination	-	52.67	21890473
98	Malonylation	QVTKALDKALSTMDL HHHHHHHHHHHHCCH	52.67	26320211
98	Acetylation	QVTKALDKALSTMDL HHHHHHHHHHHHCCH	52.67	25953088
98	Ubiquitination	QVTKALDKALSTMDL HHHHHHHHHHHHCCH	52.67	23000965
101	Phosphorylation	KALDKALSTMDLQKV HHHHHHHHHCCHHHH	26.92	25072903
102	Phosphorylation	ALDKALSTMDLQKVS HHHHHHHHCCHHHHH	18.63	28450419
103	Sulfoxidation	LDKALSTMDLQKVSS HHHHHHHCCHHHHHH	4.32	30846556
107	Ubiquitination	LSTMDLQKVSSVMDR HHHCCHHHHHHHHHH	51.92	30230243
173	Phosphorylation	SQLPEGASAVGESSV HCCCCCCCCCCHHHC	34.05	19129479
178	Phosphorylation	GASAVGESSVRSQED CCCCCCHHHCCCHHH	28.36	-
179	Phosphorylation	ASAVGESSVRSQEDQ CCCCCHHHCCCHHHH	19.76	19581576
182	Phosphorylation	VGESSVRSQEDQLSR CCHHHCCCHHHHHHH	35.45	30278072
188	Phosphorylation	RSQEDQLSRRLAALR CCHHHHHHHHHHHHH	15.10	33259812

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

Oops, there are no upstream regulatory protein records of CHM1A_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CHM1A_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 CHM1A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LNP_HUMAN	KIAA1715	physical	17353931
VPS4A_HUMAN	VPS4A	physical	11559748
VPS4B_HUMAN	VPS4B	physical	14505570
VPS4A_HUMAN	VPS4A	physical	14505570
CHM1A_HUMAN	CHMP1A	physical	14505570
CHM1B_HUMAN	CHMP1B	physical	14505570
CHM1A_HUMAN	CHMP1A	physical	16730941
CHM1B_HUMAN	CHMP1B	physical	16730941
VPS4A_HUMAN	VPS4A	physical	16730941
UBC9_HUMAN	UBE2I	physical	16730941
STABP_HUMAN	STAMBP	physical	16730941
FXL18_HUMAN	FBXL18	physical	22939629
OAS3_HUMAN	OAS3	physical	22939629
STABP_HUMAN	STAMBP	physical	21988832

Drug and Disease Associations

• Kegg Disease
• OMIM Disease
• 614961: Pontocerebellar hypoplasia 8 (PCH8)
• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330