CHMP5_HUMAN - dbPTM
CHMP5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHMP5_HUMAN
UniProt AC Q9NZZ3
Protein Name Charged multivesicular body protein 5
Gene Name CHMP5
Organism Homo sapiens (Human).
Sequence Length 219
Subcellular Localization Cytoplasm, cytosol. Endosome membrane
Peripheral membrane protein . Localizes to the midbody of dividing cells. Localized in two distinct rings on either side 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 HIV-1 p6- and p9-dependent virus release..
Protein Sequence MNRLFGKAKPKAPPPSLTDCIGTVDSRAESIDKKISRLDAELVKYKDQIKKMREGPAKNMVKQKALRVLKQKRMYEQQRDNLAQQSFNMEQANYTIQSLKDTKTTVDAMKLGVKEMKKAYKQVKIDQIEDLQDQLEDMMEDANEIQEALSRSYGTPELDEDDLEAELDALGDELLADEDSSYLDEAASAPAIPEGVPTDTKNKDGVLVDEFGLPQIPAS
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
3Methylation-----MNRLFGKAKP
-----CCCCCCCCCC		30.05-
7Ubiquitination-MNRLFGKAKPKAPP
-CCCCCCCCCCCCCC		46.00-
7Acetylation-MNRLFGKAKPKAPP
-CCCCCCCCCCCCCC		46.0025953088
9MalonylationNRLFGKAKPKAPPPS
CCCCCCCCCCCCCCC		51.0026320211
16PhosphorylationKPKAPPPSLTDCIGT
CCCCCCCCHHHHCCC		50.0728985074
18PhosphorylationKAPPPSLTDCIGTVD
CCCCCCHHHHCCCCH		32.9123090842
23PhosphorylationSLTDCIGTVDSRAES
CHHHHCCCCHHHHHH		10.9623090842
23O-linked_GlycosylationSLTDCIGTVDSRAES
CHHHHCCCCHHHHHH		10.9623301498
26PhosphorylationDCIGTVDSRAESIDK
HHCCCCHHHHHHHHH		29.1125849741
30PhosphorylationTVDSRAESIDKKISR
CCHHHHHHHHHHHHH		34.7926657352
34UbiquitinationRAESIDKKISRLDAE
HHHHHHHHHHHHHHH		42.0124816145
44AcetylationRLDAELVKYKDQIKK
HHHHHHHHHHHHHHH		60.2423236377
44UbiquitinationRLDAELVKYKDQIKK
HHHHHHHHHHHHHHH		60.2421890473
44UbiquitinationRLDAELVKYKDQIKK
HHHHHHHHHHHHHHH		60.2423000965
46UbiquitinationDAELVKYKDQIKKMR
HHHHHHHHHHHHHHH		37.1223000965
50UbiquitinationVKYKDQIKKMREGPA
HHHHHHHHHHHCCCH		34.5823000965
58UbiquitinationKMREGPAKNMVKQKA
HHHCCCHHHHHHHHH		49.0224816145
86PhosphorylationRDNLAQQSFNMEQAN
HHHHHHHHHCHHHHC		13.4021945579
94PhosphorylationFNMEQANYTIQSLKD
HCHHHHCHHHHHHHC		14.2921945579
95PhosphorylationNMEQANYTIQSLKDT
CHHHHCHHHHHHHCC		16.6121945579
98PhosphorylationQANYTIQSLKDTKTT
HHCHHHHHHHCCCHH		33.2721945579
100UbiquitinationNYTIQSLKDTKTTVD
CHHHHHHHCCCHHHH		69.4721890473
100UbiquitinationNYTIQSLKDTKTTVD
CHHHHHHHCCCHHHH		69.4721906983
102PhosphorylationTIQSLKDTKTTVDAM
HHHHHHCCCHHHHHH		28.8023532336
103UbiquitinationIQSLKDTKTTVDAMK
HHHHHCCCHHHHHHH		52.9422817900
110UbiquitinationKTTVDAMKLGVKEMK
CHHHHHHHHCHHHHH		43.7533845483
114AcetylationDAMKLGVKEMKKAYK
HHHHHCHHHHHHHHH		50.7425953088
138SulfoxidationLQDQLEDMMEDANEI
HHHHHHHHHHHHHHH		2.0130846556
139SulfoxidationQDQLEDMMEDANEIQ
HHHHHHHHHHHHHHH		6.9730846556
150PhosphorylationNEIQEALSRSYGTPE
HHHHHHHHHHHCCCC		26.6526074081
152PhosphorylationIQEALSRSYGTPELD
HHHHHHHHHCCCCCC		25.2526074081
153PhosphorylationQEALSRSYGTPELDE
HHHHHHHHCCCCCCH		24.7326074081
180PhosphorylationELLADEDSSYLDEAA
HHHCCCCCCHHHHHH		20.8729759185
219PhosphorylationGLPQIPAS-------
CCCCCCCC-------		35.0925159151
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 CHMP5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHMP5_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 CHMP5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VTA1_HUMANVTA1physical
17261583
ISG15_HUMANISG15physical
20164219
CHM1B_HUMANCHMP1Bphysical
16730941
CHM4A_HUMANCHMP4Aphysical
16730941
CHM4B_HUMANCHMP4Bphysical
16730941
CHMP5_HUMANCHMP5physical
16730941
ZNF91_HUMANZNF91physical
16730941
RL38_HUMANRPL38physical
16730941
PDC10_HUMANPDCD10physical
16730941
TF3A_HUMANGTF3Aphysical
16730941
ZN142_HUMANZNF142physical
16730941
URGCP_HUMANURGCPphysical
16730941
SMCA4_HUMANSMARCA4physical
16730941
VTA1_HUMANVTA1physical
16730941
SAE2_HUMANUBA2physical
22939629
STABP_HUMANSTAMBPphysical
21988832
PAXI_HUMANPXNphysical
22863883
MITD1_HUMANMITD1physical
25416956
CHM4A_HUMANCHMP4Aphysical
26344197
CHM4B_HUMANCHMP4Bphysical
26344197
HABP4_HUMANHABP4physical
26344197
PSA4_HUMANPSMA4physical
26344197
SMD2_HUMANSNRPD2physical
26344197
SAE2_HUMANUBA2physical
26344197
RAB5A_HUMANRAB5Aphysical
27764233
RAB7A_HUMANRAB7Aphysical
27764233
VTA1_HUMANVTA1physical
28514442
TCP1L_HUMANTCP10Lphysical
28514442
CU077_HUMANTCP10Lphysical
28514442
STMN4_HUMANSTMN4physical
28514442
CHM1A_HUMANCHMP1Aphysical
28514442
CHMP3_HUMANCHMP3physical
28514442
SH3K1_HUMANSH3KBP1physical
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.
Regulatory Network of CHMP5_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory