F199X_HUMAN - dbPTM
F199X_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F199X_HUMAN
UniProt AC Q6PEV8
Protein Name Protein FAM199X
Gene Name FAM199X
Organism Homo sapiens (Human).
Sequence Length 388
Subcellular Localization
Protein Description
Protein Sequence MSDEASAITSYEKFLTPEEPFPLLGPPRGVGTCPSEEPGCLDISDFGCQLSSCHRTDPLHRFHTNRWNLTSCGTSVASSEGSEELFSSVSVGDQDDCYSLLDDQDFTSFDLFPEGSVCSDVSSSISTYWDWSDSEFEWQLPGSDIASGSDVLSDVIPSIPSSPCLLPKKKNKHRNLDELPWSAMTNDEQVEYIEYLSRKVSTEMGLREQLDIIKIIDPSAQISPTDSEFIIELNCLTDEKLKQVRNYIKEHSPRQRPAREAWKRSNFSCASTSGVSGASASASSSSASMVSSASSSGSSVGNSASNSSANMSRAHSDSNLSASAAERIRDSKKRSKQRKLQQKAFRKRQLKEQRQARKERLSGLFLNEEVLSLKVTEEDHEADVDVLM
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
2Phosphorylation------MSDEASAIT
------CCHHHHHHH
44.1325849741
13 (in isoform 2)Ubiquitination-37.1221890473
13 (in isoform 1)Ubiquitination-37.1221890473
13UbiquitinationSAITSYEKFLTPEEP
HHHHCHHHCCCCCCC
37.1221890473
16PhosphorylationTSYEKFLTPEEPFPL
HCHHHCCCCCCCCCC
31.6127050516
35PhosphorylationRGVGTCPSEEPGCLD
CCCCCCCCCCCCEEE
57.6527050516
56PhosphorylationQLSSCHRTDPLHRFH
CCCCCCCCCCCHHCC
20.5023532336
199UbiquitinationYIEYLSRKVSTEMGL
HHHHHHHHHHHHHCH
36.84-
201PhosphorylationEYLSRKVSTEMGLRE
HHHHHHHHHHHCHHH
22.9924719451
240UbiquitinationLNCLTDEKLKQVRNY
EECCCHHHHHHHHHH
64.89-
242UbiquitinationCLTDEKLKQVRNYIK
CCCHHHHHHHHHHHH
58.79-
249UbiquitinationKQVRNYIKEHSPRQR
HHHHHHHHHHCCCCC
38.73-
265PhosphorylationAREAWKRSNFSCAST
HHHHHHHCCCCCCCC
38.2022210691
298PhosphorylationSSASSSGSSVGNSAS
HCCCCCCCCCCCCCC
24.65-
299PhosphorylationSASSSGSSVGNSASN
CCCCCCCCCCCCCCC
37.25-
305PhosphorylationSSVGNSASNSSANMS
CCCCCCCCCCCCCHH
36.75-
312PhosphorylationSNSSANMSRAHSDSN
CCCCCCHHHHCCCCC
26.56-
316PhosphorylationANMSRAHSDSNLSAS
CCHHHHCCCCCCCHH
41.5729255136
318PhosphorylationMSRAHSDSNLSASAA
HHHHCCCCCCCHHHH
42.5625159151
321PhosphorylationAHSDSNLSASAAERI
HCCCCCCCHHHHHHH
25.1629255136
323PhosphorylationSDSNLSASAAERIRD
CCCCCCHHHHHHHHH
25.3329255136
343UbiquitinationKQRKLQQKAFRKRQL
HHHHHHHHHHHHHHH
36.21-
372PhosphorylationFLNEEVLSLKVTEED
HCCHHHHEEECCCCH
31.1824719451

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 F199X_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F199X_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 F199X_HUMAN !!

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

Oops, there are no PPI records of F199X_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 F199X_HUMAN

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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-316 AND SER-321, ANDMASS SPECTROMETRY.

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