FA76B_HUMAN - dbPTM
FA76B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FA76B_HUMAN
UniProt AC Q5HYJ3
Protein Name Protein FAM76B
Gene Name FAM76B
Organism Homo sapiens (Human).
Sequence Length 339
Subcellular Localization Nucleus speckle .
Protein Description
Protein Sequence MAASALYACTKCTQRYPFEELSQGQQLCKECRIAHPIVKCTYCRSEFQQESKTNTICKKCAQNVKQFGTPKPCQYCNIIAAFIGTKCQRCTNSEKKYGPPQTCEQCKQQCAFDRKEEGRRKVDGKLLCWLCTLSYKRVLQKTKEQRKSLGSSHSNSSSSSLTEKDQHHPKHHHHHHHHHHRHSSSHHKISNLSPEEEQGLWKQSHKSSATIQNETPKKKPKLESKPSNGDSSSINQSADSGGTDNFVLISQLKEEVMSLKRLLQQRDQTILEKDKKLTELKADFQYQESNLRTKMNSMEKAHKETVEQLQAKNRELLKQVAALSKGKKFDKSGSILTSP
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------MAASALYAC
------CHHHHHHHH		15.3222223895
4Phosphorylation----MAASALYACTK
----CHHHHHHHHCC		14.8526552605
7Phosphorylation-MAASALYACTKCTQ
-CHHHHHHHHCCCCC		10.1925159151
10PhosphorylationASALYACTKCTQRYP
HHHHHHHCCCCCCCC		22.4526552605
22PhosphorylationRYPFEELSQGQQLCK
CCCHHHHHHHHHHHH		35.2317525332
42PhosphorylationHPIVKCTYCRSEFQQ
CHHHHCCCCCHHHHH		8.71-
45PhosphorylationVKCTYCRSEFQQESK
HHCCCCCHHHHHHHC		38.92-
51PhosphorylationRSEFQQESKTNTICK
CHHHHHHHCCCHHHH		40.20-
52SumoylationSEFQQESKTNTICKK
HHHHHHHCCCHHHHH		45.07-
52SumoylationSEFQQESKTNTICKK
HHHHHHHCCCHHHHH		45.07-
69PhosphorylationQNVKQFGTPKPCQYC
HHHHHHCCCCCCCHH		29.4522617229
75PhosphorylationGTPKPCQYCNIIAAF
CCCCCCCHHHHHHHH		8.32-
147SumoylationQKTKEQRKSLGSSHS
HHHHHHHHHHCCCCC		50.13-
147SumoylationQKTKEQRKSLGSSHS
HHHHHHHHHHCCCCC		50.13-
148PhosphorylationKTKEQRKSLGSSHSN
HHHHHHHHHCCCCCC		39.9025159151
151PhosphorylationEQRKSLGSSHSNSSS
HHHHHHCCCCCCCCC		30.1228450419
152PhosphorylationQRKSLGSSHSNSSSS
HHHHHCCCCCCCCCC		29.1825159151
154PhosphorylationKSLGSSHSNSSSSSL
HHHCCCCCCCCCCCC		40.1128450419
156PhosphorylationLGSSHSNSSSSSLTE
HCCCCCCCCCCCCCH		34.3128450419
157PhosphorylationGSSHSNSSSSSLTEK
CCCCCCCCCCCCCHH		38.1928450419
158PhosphorylationSSHSNSSSSSLTEKD
CCCCCCCCCCCCHHH		24.6228450419
159PhosphorylationSHSNSSSSSLTEKDQ
CCCCCCCCCCCHHHC		31.1728450419
160PhosphorylationHSNSSSSSLTEKDQH
CCCCCCCCCCHHHCC		41.0628450419
162PhosphorylationNSSSSSLTEKDQHHP
CCCCCCCCHHHCCCC		42.8328450419
190PhosphorylationSSSHHKISNLSPEEE
CCCCCCCCCCCHHHH		36.2030266825
193PhosphorylationHHKISNLSPEEEQGL
CCCCCCCCHHHHHCH		34.2219664994
204PhosphorylationEQGLWKQSHKSSATI
HHCHHHHCHHHCCCC		29.2028122231
207PhosphorylationLWKQSHKSSATIQNE
HHHHCHHHCCCCCCC		21.5628111955
208PhosphorylationWKQSHKSSATIQNET
HHHCHHHCCCCCCCC		33.9528111955
210PhosphorylationQSHKSSATIQNETPK
HCHHHCCCCCCCCCC		25.6629396449
215PhosphorylationSATIQNETPKKKPKL
CCCCCCCCCCCCCCC		48.2123401153
224PhosphorylationKKKPKLESKPSNGDS
CCCCCCCCCCCCCCC		61.3728450419
225UbiquitinationKKPKLESKPSNGDSS
CCCCCCCCCCCCCCC		42.9917203973
227PhosphorylationPKLESKPSNGDSSSI
CCCCCCCCCCCCCCH		58.1225159151
231PhosphorylationSKPSNGDSSSINQSA
CCCCCCCCCCHHCCC		27.6425159151
232PhosphorylationKPSNGDSSSINQSAD
CCCCCCCCCHHCCCC		39.7228450419
233PhosphorylationPSNGDSSSINQSADS
CCCCCCCCHHCCCCC		29.5230108239
237PhosphorylationDSSSINQSADSGGTD
CCCCHHCCCCCCCCC		29.5628450419
240PhosphorylationSINQSADSGGTDNFV
CHHCCCCCCCCCCEE		38.5526074081
243PhosphorylationQSADSGGTDNFVLIS
CCCCCCCCCCEEEHH		31.1526074081
250PhosphorylationTDNFVLISQLKEEVM
CCCEEEHHHHHHHHH		25.8724719451
269PhosphorylationLLQQRDQTILEKDKK
HHHHHHHHHHHHHHH		31.64-
325AcetylationKQVAALSKGKKFDKS
HHHHHHHCCCCCCCC		75.5025953088
332PhosphorylationKGKKFDKSGSILTSP
CCCCCCCCCCCCCCC		39.3524719451
337PhosphorylationDKSGSILTSP-----
CCCCCCCCCC-----		36.9629396449
338PhosphorylationKSGSILTSP------
CCCCCCCCC------		25.7625159151
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 FA76B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FA76B_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 FA76B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANM5_HUMANPRMT5physical
23455924
KR107_HUMANKRTAP10-7physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR101_HUMANKRTAP10-1physical
25416956
KR10B_HUMANKRTAP10-11physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
SORL_HUMANSORL1physical
26186194
AEDO_HUMANADOphysical
26186194
SORL_HUMANSORL1physical
28514442
AEDO_HUMANADOphysical
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 FA76B_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-193, AND MASS SPECTROMETRY.
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-193, AND MASSSPECTROMETRY.
"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-193, AND MASS SPECTROMETRY.
"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-193, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"The proteomic reactor facilitates the analysis of affinity-purifiedproteins by mass spectrometry: application for identifyingubiquitinated proteins in human cells.";
Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,Haines D.S., Figeys D.;
J. Proteome Res. 6:298-305(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-225 (ISOFORM 2), AND MASSSPECTROMETRY.

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