F219B_HUMAN - dbPTM
F219B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F219B_HUMAN
UniProt AC Q5XKK7
Protein Name Protein FAM219B
Gene Name FAM219B
Organism Homo sapiens (Human).
Sequence Length 198
Subcellular Localization
Protein Description
Protein Sequence MATAEPSGRALRLSTPGPRPSGARDRAPGAAGPPSGQIGNRALRLGERTPAAVEKRGPYMVTRAPSIQAKLQKHRDLAKAVLRRKGMLGASPNRPDSSGKRSVKFNKGYTALSQSPDENLVSLDSDSDGELGSRYSSGYSSAEQVNQDVSRQLLQDGYHLDEIPDDEDLDLIPPKPMASSTCSCCWCCLGDSSSCTLQ
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
14PhosphorylationSGRALRLSTPGPRPS
CCCCEECCCCCCCCC
26.5628985074
15PhosphorylationGRALRLSTPGPRPSG
CCCEECCCCCCCCCC
36.5428985074
21PhosphorylationSTPGPRPSGARDRAP
CCCCCCCCCCCCCCC
46.4928985074
35PhosphorylationPGAAGPPSGQIGNRA
CCCCCCCCCCCCHHH
46.6028674419
55UbiquitinationRTPAAVEKRGPYMVT
CCCHHHHHHCCCEEE
56.93-
59PhosphorylationAVEKRGPYMVTRAPS
HHHHHCCCEEECCHH
13.6725884760
62PhosphorylationKRGPYMVTRAPSIQA
HHCCCEEECCHHHHH
12.4623882029
66PhosphorylationYMVTRAPSIQAKLQK
CEEECCHHHHHHHHH
26.7526074081
91PhosphorylationRKGMLGASPNRPDSS
HCCCCCCCCCCCCCC
22.4029255136
97PhosphorylationASPNRPDSSGKRSVK
CCCCCCCCCCCCEEE
43.6129396449
98PhosphorylationSPNRPDSSGKRSVKF
CCCCCCCCCCCEEEE
56.5727251275
109PhosphorylationSVKFNKGYTALSQSP
EEEECCCCEECCCCC
7.1722115753
110PhosphorylationVKFNKGYTALSQSPD
EEECCCCEECCCCCC
29.7722115753
113PhosphorylationNKGYTALSQSPDENL
CCCCEECCCCCCCCC
26.5829978859
115PhosphorylationGYTALSQSPDENLVS
CCEECCCCCCCCCEE
30.8325850435
122PhosphorylationSPDENLVSLDSDSDG
CCCCCCEECCCCCCC
29.6222115753
125PhosphorylationENLVSLDSDSDGELG
CCCEECCCCCCCCCC
44.2825159151
127PhosphorylationLVSLDSDSDGELGSR
CEECCCCCCCCCCCC
52.0125159151
133PhosphorylationDSDGELGSRYSSGYS
CCCCCCCCCCCCCCC
40.4430108239
135PhosphorylationDGELGSRYSSGYSSA
CCCCCCCCCCCCCCH
14.6428796482
136PhosphorylationGELGSRYSSGYSSAE
CCCCCCCCCCCCCHH
19.0428796482
137PhosphorylationELGSRYSSGYSSAEQ
CCCCCCCCCCCCHHH
32.5828796482
139PhosphorylationGSRYSSGYSSAEQVN
CCCCCCCCCCHHHHC
11.0328796482
140PhosphorylationSRYSSGYSSAEQVNQ
CCCCCCCCCHHHHCH
26.9728796482
141PhosphorylationRYSSGYSSAEQVNQD
CCCCCCCCHHHHCHH
27.6028796482
181PhosphorylationPKPMASSTCSCCWCC
CCCCCCCCCCEEEEE
13.1230576142
196PhosphorylationLGDSSSCTLQ-----
CCCCCCCCCC-----
30.0930576142

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 F219B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F219B_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 F219B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JIP4_HUMANSPAG9physical
26186194
ELP1_HUMANIKBKAPphysical
26186194
DPH2_HUMANDPH2physical
26186194
ELP2_HUMANELP2physical
26186194
MTCH2_HUMANMTCH2physical
26186194
MTU1_HUMANTRMUphysical
26186194
ELP3_HUMANELP3physical
26186194
MTU1_HUMANTRMUphysical
28514442
DPH2_HUMANDPH2physical
28514442
ELP3_HUMANELP3physical
28514442
JIP4_HUMANSPAG9physical
28514442
MTCH2_HUMANMTCH2physical
28514442
ELP2_HUMANELP2physical
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 F219B_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-125 AND SER-127, ANDMASS SPECTROMETRY.

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