F104A_HUMAN - dbPTM
F104A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F104A_HUMAN
UniProt AC Q969W3
Protein Name Protein FAM104A
Gene Name FAM104A
Organism Homo sapiens (Human).
Sequence Length 186
Subcellular Localization
Protein Description
Protein Sequence MGGRGADAGSSGGTGPTEGYSPPAASTRAAARAKARGGGRGGRRNTTPSVPSLRGAAPRSFHPPAAMSERLRPRKRRRNGNEEDNHLPPQTKRSSRNPVFQDSWDTESSGSDSGGSSSSSSSSINSPDRASGPEGSLSQTMAGSSPNTPQPVPEQSALCQGLYFHINQTLREAHFHSLQHRGRPLT
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
4Methylation----MGGRGADAGSS
----CCCCCCCCCCC
31.2524129315
10PhosphorylationGRGADAGSSGGTGPT
CCCCCCCCCCCCCCC
27.7729255136
11PhosphorylationRGADAGSSGGTGPTE
CCCCCCCCCCCCCCC
40.0829255136
14PhosphorylationDAGSSGGTGPTEGYS
CCCCCCCCCCCCCCC
43.4429255136
17PhosphorylationSSGGTGPTEGYSPPA
CCCCCCCCCCCCCCH
43.3030266825
20PhosphorylationGTGPTEGYSPPAAST
CCCCCCCCCCCHHHH
16.2726657352
21PhosphorylationTGPTEGYSPPAASTR
CCCCCCCCCCHHHHH
34.9523401153
21 (in isoform 2)Phosphorylation-34.9524719451
26PhosphorylationGYSPPAASTRAAARA
CCCCCHHHHHHHHHH
22.1129255136
27PhosphorylationYSPPAASTRAAARAK
CCCCHHHHHHHHHHH
21.4329255136
28MethylationSPPAASTRAAARAKA
CCCHHHHHHHHHHHH
21.52-
46 (in isoform 2)Phosphorylation-37.9724719451
46PhosphorylationGRGGRRNTTPSVPSL
CCCCCCCCCCCCCCC
37.9724719451
47PhosphorylationRGGRRNTTPSVPSLR
CCCCCCCCCCCCCCC
19.6727251275
52PhosphorylationNTTPSVPSLRGAAPR
CCCCCCCCCCCCCCC
28.6624719451
54MethylationTPSVPSLRGAAPRSF
CCCCCCCCCCCCCCC
36.72-
68PhosphorylationFHPPAAMSERLRPRK
CCCCHHHHHHHCCCH
18.1628555341
108PhosphorylationQDSWDTESSGSDSGG
CCCCCCCCCCCCCCC
41.9319369195
126PhosphorylationSSSSSINSPDRASGP
CCCCCCCCCCCCCCC
26.8928985074
129 (in isoform 2)Phosphorylation-33.75-
132 (in isoform 2)Phosphorylation-24.2428348404
134 (in isoform 2)Phosphorylation-66.0128348404
137 (in isoform 2)Phosphorylation-6.9028348404
138 (in isoform 2)Phosphorylation-25.8828348404
139 (in isoform 2)Phosphorylation-40.3628348404
140 (in isoform 2)Phosphorylation-12.9528348404
144PhosphorylationLSQTMAGSSPNTPQP
CHHHHCCCCCCCCCC
32.8426074081
144 (in isoform 2)Phosphorylation-32.8427251275
145PhosphorylationSQTMAGSSPNTPQPV
HHHHCCCCCCCCCCC
22.6626074081
147 (in isoform 2)Phosphorylation-67.3628674419
148PhosphorylationMAGSSPNTPQPVPEQ
HCCCCCCCCCCCCCH
27.0426074081
166 (in isoform 2)Phosphorylation-2.6827251275

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 F104A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F104A_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 F104A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NSF1C_HUMANNSFL1Cphysical
26389662

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 F104A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASSSPECTROMETRY.

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