F177A_HUMAN - dbPTM
F177A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F177A_HUMAN
UniProt AC Q8N128
Protein Name Protein FAM177A1
Gene Name FAM177A1
Organism Homo sapiens (Human).
Sequence Length 213
Subcellular Localization
Protein Description
Protein Sequence MDQEPVGGVERGEAVAASGAAAAAAFGESAGQMSNERGFENVELGVIGKKKKVPRRVIHFVSGETMEEYSTDEDEVDGLEKKDVLPTVDPTKLTWGPYLWFYMLRAATSTLSVCDFLGEKIASVLGISTPKYQYAIDEYYRMKKEEEEEEEENRMSEEAEKQYQQNKLQTDSIVQTDQPETVISSSFVNVNFEMEGDSEVIMESKQNPVSVPP
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
1Acetylation-------MDQEPVGG
-------CCCCCCCC		12.3822814378
9 (in isoform 2)Phosphorylation-3.5925627689
13 (in isoform 2)Phosphorylation-46.3125627689
14 (in isoform 2)Phosphorylation-10.0825627689
16 (in isoform 2)Phosphorylation-11.7125627689
17 (in isoform 2)Phosphorylation-11.2525627689
18PhosphorylationRGEAVAASGAAAAAA
HHHHHHHHHHHHHHH		21.16-
29PhosphorylationAAAAFGESAGQMSNE
HHHHHHHCHHCCCCC		37.7728122231
34PhosphorylationGESAGQMSNERGFEN
HHCHHCCCCCCCCCC		27.8728122231
49UbiquitinationVELGVIGKKKKVPRR
EEEEEECCCCCCCCE		50.7432015554
62PhosphorylationRRVIHFVSGETMEEY
CEEEEEECCCCHHHC		29.9323401153
65PhosphorylationIHFVSGETMEEYSTD
EEEECCCCHHHCCCC		33.1529255136
69PhosphorylationSGETMEEYSTDEDEV
CCCCHHHCCCCHHHC		11.9923401153
70PhosphorylationGETMEEYSTDEDEVD
CCCHHHCCCCHHHCC		32.4429255136
71PhosphorylationETMEEYSTDEDEVDG
CCHHHCCCCHHHCCC		42.3729255136
72UbiquitinationTMEEYSTDEDEVDGL
CHHHCCCCHHHCCCC		56.2432015554
81UbiquitinationDEVDGLEKKDVLPTV
HHCCCCCCCCCCCCC		60.3525015289
82UbiquitinationEVDGLEKKDVLPTVD
HCCCCCCCCCCCCCC		43.6325015289
93 (in isoform 2)Phosphorylation-5.5324719451
94 (in isoform 2)Phosphorylation-29.9024719451
94PhosphorylationTVDPTKLTWGPYLWF
CCCCCCCCCHHHHHH		29.9020166139
98PhosphorylationTKLTWGPYLWFYMLR
CCCCCHHHHHHHHHH		16.78-
102PhosphorylationWGPYLWFYMLRAATS
CHHHHHHHHHHHHHC		5.44-
104UbiquitinationPYLWFYMLRAATSTL
HHHHHHHHHHHHCHH		1.9925015289
105UbiquitinationYLWFYMLRAATSTLS
HHHHHHHHHHHCHHH		12.9725015289
129PhosphorylationASVLGISTPKYQYAI
HHHHCCCCCHHHHHH		23.1428674419
131 (in isoform 1)Ubiquitination-45.1121890473
131UbiquitinationVLGISTPKYQYAIDE
HHCCCCCHHHHHHHH		45.1123000965
134PhosphorylationISTPKYQYAIDEYYR
CCCCHHHHHHHHHHH		11.48-
139PhosphorylationYQYAIDEYYRMKKEE
HHHHHHHHHHHHHHH		7.8228796482
140PhosphorylationQYAIDEYYRMKKEEE
HHHHHHHHHHHHHHH		11.3728796482
154UbiquitinationEEEEEENRMSEEAEK
HHHHHHHHCCHHHHH		33.0323000965
154 (in isoform 2)Ubiquitination-33.0321890473
155 (in isoform 2)Phosphorylation-9.9727642862
156PhosphorylationEEEENRMSEEAEKQY
HHHHHHCCHHHHHHH		29.1028060719
157 (in isoform 2)Phosphorylation-52.4627642862
162 (in isoform 2)Phosphorylation-32.5427642862
163 (in isoform 2)Phosphorylation-24.1227642862
163PhosphorylationSEEAEKQYQQNKLQT
CHHHHHHHHHCCCCC		24.1220736484
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 F177A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F177A_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 F177A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
F204A_HUMANFAM204Aphysical
26186194
S27A2_HUMANSLC27A2physical
26186194
ODR4_HUMANC1orf27physical
26186194
SUGP1_HUMANSUGP1physical
26186194
UFSP2_HUMANUFSP2physical
26186194
EF1A2_HUMANEEF1A2physical
26186194
STEA3_HUMANSTEAP3physical
26186194
AAGAB_HUMANAAGABphysical
26186194
NADAP_HUMANSLC4A1APphysical
26186194
F207A_HUMANFAM207Aphysical
26186194
SAR1B_HUMANSAR1Bphysical
26186194
TGS1_HUMANTGS1physical
26186194
ARMX3_HUMANARMCX3physical
26186194
PRP16_HUMANDHX38physical
26186194
RIOK1_HUMANRIOK1physical
26186194
VP13B_HUMANVPS13Bphysical
26186194
T2FB_HUMANGTF2F2physical
26186194
DCNL5_HUMANDCUN1D5physical
26186194
OSTM1_HUMANOSTM1physical
26186194
GPKOW_HUMANGPKOWphysical
26186194
CL043_HUMANC12orf43physical
26186194
CLCN7_HUMANCLCN7physical
26186194
CLCN7_HUMANCLCN7physical
28514442
F204A_HUMANFAM204Aphysical
28514442
S27A2_HUMANSLC27A2physical
28514442
VP13B_HUMANVPS13Bphysical
28514442
OSTM1_HUMANOSTM1physical
28514442
T2FB_HUMANGTF2F2physical
28514442
F207A_HUMANFAM207Aphysical
28514442
TGS1_HUMANTGS1physical
28514442
SUGP1_HUMANSUGP1physical
28514442
DCNL5_HUMANDCUN1D5physical
28514442
STEA3_HUMANSTEAP3physical
28514442
CL043_HUMANC12orf43physical
28514442
SNAG_HUMANNAPGphysical
28514442
ODR4_HUMANC1orf27physical
28514442
GPKOW_HUMANGPKOWphysical
28514442
UFSP2_HUMANUFSP2physical
28514442
NCEH1_HUMANNCEH1physical
28514442
RIOK1_HUMANRIOK1physical
28514442
PRP16_HUMANDHX38physical
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 F177A_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-70 AND THR-71, AND MASSSPECTROMETRY.
"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-70 AND THR-71, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND THR-71, AND MASSSPECTROMETRY.

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