CHM4A_HUMAN - dbPTM
CHM4A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHM4A_HUMAN
UniProt AC Q9BY43
Protein Name Charged multivesicular body protein 4a
Gene Name CHMP4A
Organism Homo sapiens (Human).
Sequence Length 222
Subcellular Localization Cytoplasmic vesicle membrane. Late endosome membrane
Peripheral membrane protein . Membrane-associated. Localizes to large vesicle-like structures. Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fl
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. 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. When overexpressed, membrane-assembled circular arrays of CHMP4A filaments can promote or stabilize negative curvature and outward budding. Via its interaction with PDCD6IP involved in HIV-1 p6- and p9-dependent virus release. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan. [PubMed: 22660413]
Protein Sequence MSGLGRLFGKGKKEKGPTPEEAIQKLKETEKILIKKQEFLEQKIQQELQTAKKYGTKNKRAALQALRRKKRFEQQLAQTDGTLSTLEFQREAIENATTNAEVLRTMELAAQSMKKAYQDMDIDKVDELMTDITEQQEVAQQISDAISRPMGFGDDVDEDELLEELEELEQEELAQELLNVGDKEEEPSVKLPSVPSTHLPAGPAPKVDEDEEALKQLAEWVS
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 Orthologous
Protein Cluster
45PhosphorylationEFLEQKIQQELQTAK
HHHHHHHHHHHHHHH
37.4220068231
45 (in isoform 2)Phosphorylation-37.4220068231
50PhosphorylationKIQQELQTAKKYGTK
HHHHHHHHHHHHCCH
53.7427470641
58UbiquitinationAKKYGTKNKRAALQA
HHHHCCHHHHHHHHH
38.59-
68UbiquitinationAALQALRRKKRFEQQ
HHHHHHHHHHHHHHH
50.09-
97PhosphorylationREAIENATTNAEVLR
HHHHHHCCCCHHHHH
31.9727470641
112PhosphorylationTMELAAQSMKKAYQD
HHHHHHHHHHHHHHC
28.0427470641
114AcetylationELAAQSMKKAYQDMD
HHHHHHHHHHHHCCC
39.2325953088
157UbiquitinationMGFGDDVDEDELLEE
CCCCCCCCHHHHHHH
65.70-
193PhosphorylationEPSVKLPSVPSTHLP
CCCCCCCCCCCCCCC
58.0325849741
196PhosphorylationVKLPSVPSTHLPAGP
CCCCCCCCCCCCCCC
26.7225159151
197PhosphorylationKLPSVPSTHLPAGPA
CCCCCCCCCCCCCCC
22.7426657352
236Phosphorylation---------------------
---------------------
-
239Phosphorylation------------------------
------------------------
-
249Ubiquitination----------------------------------
----------------------------------
-

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 CHM4A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHM4A_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 CHM4A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYT17_HUMANSYT17physical
16189514
PDC6I_HUMANPDCD6IPphysical
14505570
CHMP3_HUMANCHMP3physical
14505570
VPS4A_HUMANVPS4Aphysical
14505570
GAG_HV1H2gagphysical
14505569
CHM4A_HUMANCHMP4Aphysical
16730941
C2D1A_HUMANCC2D1Aphysical
16730941
TTC19_HUMANTTC19physical
16730941
CDK13_HUMANCDK13physical
16730941
SYT17_HUMANSYT17physical
16730941
STABP_HUMANSTAMBPphysical
16730941
VPS4B_HUMANVPS4Bphysical
22939629
EGFR_HUMANEGFRphysical
23477725
PURA2_HUMANADSSphysical
22863883
CHRC1_HUMANCHRAC1physical
22863883
EFHD2_HUMANEFHD2physical
22863883
CH10_HUMANHSPE1physical
22863883
IDHC_HUMANIDH1physical
22863883
RANG_HUMANRANBP1physical
22863883
RBBP7_HUMANRBBP7physical
22863883
RCN1_HUMANRCN1physical
22863883
TALDO_HUMANTALDO1physical
22863883
SYT17_HUMANSYT17physical
25416956

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 CHM4A_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP