F107B_HUMAN - dbPTM
F107B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F107B_HUMAN
UniProt AC Q9H098
Protein Name Protein FAM107B
Gene Name FAM107B
Organism Homo sapiens (Human).
Sequence Length 131
Subcellular Localization
Protein Description
Protein Sequence MAEPDYIEDDNPELIRPQKLINPVKTSRNHQDLHRELLMNQKRGLAPQNKPELQKVMEKRKRDQVIKQKEEEAQKKKSDLEIELLKRQQKLEQLELEKQKLQEEQENAPEFVKVKGNLRRTGQEVAQAQES
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
2Acetylation------MAEPDYIED
------CCCCCCCCC
36.7119413330
6Phosphorylation--MAEPDYIEDDNPE
--CCCCCCCCCCCHH
19.5425394399
25AcetylationQKLINPVKTSRNHQD
HHHCCCCCCCCCCHH
41.8825953088
25UbiquitinationQKLINPVKTSRNHQD
HHHCCCCCCCCCCHH
41.8829967540
26PhosphorylationKLINPVKTSRNHQDL
HHCCCCCCCCCCHHH
32.9029083192
27PhosphorylationLINPVKTSRNHQDLH
HCCCCCCCCCCHHHH
25.9329083192
42AcetylationRELLMNQKRGLAPQN
HHHHHHHHCCCCCCC
43.3525953088
42UbiquitinationRELLMNQKRGLAPQN
HHHHHHHHCCCCCCC
43.3529967540
43MethylationELLMNQKRGLAPQNK
HHHHHHHCCCCCCCC
35.28-
50AcetylationRGLAPQNKPELQKVM
CCCCCCCCHHHHHHH
34.3223749302
50UbiquitinationRGLAPQNKPELQKVM
CCCCCCCCHHHHHHH
34.3233845483
55UbiquitinationQNKPELQKVMEKRKR
CCCHHHHHHHHHHHH
57.0624816145
64UbiquitinationMEKRKRDQVIKQKEE
HHHHHHHHHHHHHHH
42.7529967540
68 (in isoform 2)Phosphorylation-47.47-
77UbiquitinationEEEAQKKKSDLEIEL
HHHHHHHHHHHHHHH
57.1233845483
78PhosphorylationEEAQKKKSDLEIELL
HHHHHHHHHHHHHHH
57.2028450419
81UbiquitinationQKKKSDLEIELLKRQ
HHHHHHHHHHHHHHH
39.1329967540
86UbiquitinationDLEIELLKRQQKLEQ
HHHHHHHHHHHHHHH
61.8733845483
89UbiquitinationIELLKRQQKLEQLEL
HHHHHHHHHHHHHHH
57.2333845483
90UbiquitinationELLKRQQKLEQLELE
HHHHHHHHHHHHHHH
45.7330230243
94UbiquitinationRQQKLEQLELEKQKL
HHHHHHHHHHHHHHH
6.2324816145
100AcetylationQLELEKQKLQEEQEN
HHHHHHHHHHHHHHH
64.3020167786
100UbiquitinationQLELEKQKLQEEQEN
HHHHHHHHHHHHHHH
64.3033845483
113UbiquitinationENAPEFVKVKGNLRR
HHCCCHHHCCCHHHH
43.4833845483
113AcetylationENAPEFVKVKGNLRR
HHCCCHHHCCCHHHH
43.4826051181
116UbiquitinationPEFVKVKGNLRRTGQ
CCHHHCCCHHHHHHH
41.2033845483
121PhosphorylationVKGNLRRTGQEVAQA
CCCHHHHHHHHHHHH
36.4628674419
125UbiquitinationLRRTGQEVAQAQES-
HHHHHHHHHHHHCC-
3.5333845483
129UbiquitinationGQEVAQAQES-----
HHHHHHHHCC-----
39.1130230243
131PhosphorylationEVAQAQES-------
HHHHHHCC-------
33.1828450419
139Ubiquitination---------------
---------------
33845483
152Ubiquitination----------------------------
----------------------------
33845483
200Ubiquitination----------------------------------------------------------------------------
----------------------------------------------------------------------------
29967540
217Ubiquitination---------------------------------------------------------------------------------------------
---------------------------------------------------------------------------------------------
29967540
225Ubiquitination-----------------------------------------------------------------------------------------------------
-----------------------------------------------------------------------------------------------------
33845483
230Ubiquitination----------------------------------------------------------------------------------------------------------
----------------------------------------------------------------------------------------------------------
24816145
252Ubiquitination--------------------------------------------------------------------------------------------------------------------------------
--------------------------------------------------------------------------------------------------------------------------------
33845483
261Ubiquitination-----------------------------------------------------------------------------------------------------------------------------------------
-----------------------------------------------------------------------------------------------------------------------------------------
33845483
265Ubiquitination---------------------------------------------------------------------------------------------------------------------------------------------
---------------------------------------------------------------------------------------------------------------------------------------------
30230243
275Ubiquitination-------------------------------------------------------------------------------------------------------------------------------------------------------
-------------------------------------------------------------------------------------------------------------------------------------------------------
33845483
288Ubiquitination--------------------------------------------------------------------------------------------------------------------------------------------------------------------
--------------------------------------------------------------------------------------------------------------------------------------------------------------------
33845483

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 F107B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F107B_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 F107B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of F107B_HUMAN !!

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 F107B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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 ALA-2, AND MASS SPECTROMETRY.

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