FUND2_HUMAN - dbPTM
FUND2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FUND2_HUMAN
UniProt AC Q9BWH2
Protein Name FUN14 domain-containing protein 2
Gene Name FUNDC2
Organism Homo sapiens (Human).
Sequence Length 189
Subcellular Localization
Protein Description
Protein Sequence METSAPRAGSQVVATTARHSAAYRADPLRVSSRDKLTEMAASSQGNFEGNFESLDLAEFAKKQPWWRKLFGQESGPSAEKYSVATQLFIGGVTGWCTGFIFQKVGKLAATAVGGGFFLLQLANHTGYIKVDWQRVEKDMKKAKEQLKIRKSNQIPTEVRSKAEEVVSFVKKNVLVTGGFFGGFLLGMAS
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
10PhosphorylationTSAPRAGSQVVATTA
CCCCCCCCCEEEEEC
20.8625159151
15PhosphorylationAGSQVVATTARHSAA
CCCCEEEEECCCCHH
14.9123312004
16PhosphorylationGSQVVATTARHSAAY
CCCEEEEECCCCHHH
16.3829214152
20PhosphorylationVATTARHSAAYRADP
EEEECCCCHHHHCCC
14.7229214152
23PhosphorylationTARHSAAYRADPLRV
ECCCCHHHHCCCCCC
13.1730177828
31PhosphorylationRADPLRVSSRDKLTE
HCCCCCCCCHHHHHH
17.1430266825
32PhosphorylationADPLRVSSRDKLTEM
CCCCCCCCHHHHHHH
41.4630266825
37PhosphorylationVSSRDKLTEMAASSQ
CCCHHHHHHHHHHCC
29.4728857561
42PhosphorylationKLTEMAASSQGNFEG
HHHHHHHHCCCCCCC
17.4128857561
43PhosphorylationLTEMAASSQGNFEGN
HHHHHHHCCCCCCCC
37.0628857561
53PhosphorylationNFEGNFESLDLAEFA
CCCCCCCCCCHHHHH
24.0525693802
61UbiquitinationLDLAEFAKKQPWWRK
CCHHHHHHHCHHHHH
58.2121963094
62UbiquitinationDLAEFAKKQPWWRKL
CHHHHHHHCHHHHHH
59.15-
68UbiquitinationKKQPWWRKLFGQESG
HHCHHHHHHHCCCCC
34.1521906983
147UbiquitinationKKAKEQLKIRKSNQI
HHHHHHHHHHHHCCC
39.9123000965
150UbiquitinationKEQLKIRKSNQIPTE
HHHHHHHHHCCCCHH
58.1823000965
151PhosphorylationEQLKIRKSNQIPTEV
HHHHHHHHCCCCHHH
24.9029255136
156PhosphorylationRKSNQIPTEVRSKAE
HHHCCCCHHHHHHHH
49.0624702127
161UbiquitinationIPTEVRSKAEEVVSF
CCHHHHHHHHHHHHH
49.6121906983
167PhosphorylationSKAEEVVSFVKKNVL
HHHHHHHHHHHCCEE
29.5120833797
170UbiquitinationEEVVSFVKKNVLVTG
HHHHHHHHCCEEEEC
36.3033845483
176PhosphorylationVKKNVLVTGGFFGGF
HHCCEEEECCCCHHH
27.68-
189PhosphorylationGFLLGMAS-------
HHHHCCCC-------
31.68-

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 FUND2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FUND2_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 FUND2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FUND2_HUMANFUNDC2physical
25416956
SEC62_HUMANSEC62physical
26186194
FAF2_HUMANFAF2physical
26186194
FUND1_HUMANFUNDC1physical
26186194
FAF2_HUMANFAF2physical
28514442
FUND1_HUMANFUNDC1physical
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 FUND2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND MASSSPECTROMETRY.

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