SURF6_HUMAN - dbPTM
SURF6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SURF6_HUMAN
UniProt AC O75683
Protein Name Surfeit locus protein 6
Gene Name SURF6
Organism Homo sapiens (Human).
Sequence Length 361
Subcellular Localization Nucleus, nucleoplasm. Nucleus, nucleolus. Granular component of the nucleolus..
Protein Description Binds to both DNA and RNA in vitro, with a stronger binding capacity for RNA. May represent a nucleolar constitutive protein involved in ribosomal biosynthesis or assembly (By similarity)..
Protein Sequence MASLLAKDAYLQSLAKKICSHSAPEQQARTRAGKTQGSETAGPPKKKRKKTQKKFRKREEKAAEHKAKSLGEKSPAASGARRPEAAKEEAAWASSSAGNPADGLATEPESVFALDVLRQRLHEKIQEARGQGSAKELSPAALEKRRRRKQERDRKKRKRKELRAKEKARKAEEATEAQEVVEATPEGACTEPREPPGLIFNKVEVSEDEPASKAQRRKEKRQRVKGNLTPLTGRNYRQLLERLQARQSRLDELRGQDEGKAQELEAKMKWTNLLYKAEGVKIRDDERLLQEALKRKEKRRAQRQRRWEKRTAGVVEKMQQRQDRRRQNLRRKKAARAERRLLRARKKGRILPQDLERAGLV
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
7Ubiquitination-MASLLAKDAYLQSL
-CHHHHHHHHHHHHH		42.7522817900
72-Hydroxyisobutyrylation-MASLLAKDAYLQSL
-CHHHHHHHHHHHHH		42.75-
13PhosphorylationAKDAYLQSLAKKICS
HHHHHHHHHHHHHHC		27.9125159151
16AcetylationAYLQSLAKKICSHSA
HHHHHHHHHHHCCCC		48.2225953088
22PhosphorylationAKKICSHSAPEQQAR
HHHHHCCCCHHHHHH		29.2625159151
35PhosphorylationARTRAGKTQGSETAG
HHHHCCCCCCCCCCC		36.9330576142
38PhosphorylationRAGKTQGSETAGPPK
HCCCCCCCCCCCCCH		23.1930576142
40PhosphorylationGKTQGSETAGPPKKK
CCCCCCCCCCCCHHH		38.3128985074
53UbiquitinationKKRKKTQKKFRKREE
HHCHHHHHHHHHHHH		60.1424816145
61AcetylationKFRKREEKAAEHKAK
HHHHHHHHHHHHHHH		48.417369393
66AcetylationEEKAAEHKAKSLGEK
HHHHHHHHHHHHHCC		49.367369401
69PhosphorylationAAEHKAKSLGEKSPA
HHHHHHHHHHCCCCC		46.6024732914
73AcetylationKAKSLGEKSPAASGA
HHHHHHCCCCCCCCC		61.0025953088
74PhosphorylationAKSLGEKSPAASGAR
HHHHHCCCCCCCCCC		18.5728176443
78PhosphorylationGEKSPAASGARRPEA
HCCCCCCCCCCCHHH		34.7824732914
106PhosphorylationNPADGLATEPESVFA
CCCCCCCCCCHHHHH		58.05-
1242-HydroxyisobutyrylationLRQRLHEKIQEARGQ
HHHHHHHHHHHHCCC		38.65-
133PhosphorylationQEARGQGSAKELSPA
HHHCCCCCHHHCCHH		28.4224732914
138PhosphorylationQGSAKELSPAALEKR
CCCHHHCCHHHHHHH		17.3729255136
144UbiquitinationLSPAALEKRRRRKQE
CCHHHHHHHHHHHHH		52.64-
184PhosphorylationAQEVVEATPEGACTE
HHHHHHCCCCCCCCC		14.3625159151
202AcetylationPPGLIFNKVEVSEDE
CCCCEEECEECCCCC		29.0826051181
202UbiquitinationPPGLIFNKVEVSEDE
CCCCEEECEECCCCC		29.0832015554
206PhosphorylationIFNKVEVSEDEPASK
EEECEECCCCCCCHH		26.3123401153
212PhosphorylationVSEDEPASKAQRRKE
CCCCCCCHHHHHHHH		38.9628450419
213UbiquitinationSEDEPASKAQRRKEK
CCCCCCHHHHHHHHH		51.1232015554
229PhosphorylationQRVKGNLTPLTGRNY
HHHCCCCCCCCCHHH		21.9130266825
232PhosphorylationKGNLTPLTGRNYRQL
CCCCCCCCCHHHHHH		34.9930266825
248PhosphorylationERLQARQSRLDELRG
HHHHHHHHHHHHHCC		29.29-
260AcetylationLRGQDEGKAQELEAK
HCCCCCHHHHHHHHH		44.8626051181
267AcetylationKAQELEAKMKWTNLL
HHHHHHHHHHHHHHH		31.4725953088
271PhosphorylationLEAKMKWTNLLYKAE
HHHHHHHHHHHHHHH		15.52-
275PhosphorylationMKWTNLLYKAEGVKI
HHHHHHHHHHHCCCC		16.00-
2942-HydroxyisobutyrylationRLLQEALKRKEKRRA
HHHHHHHHHHHHHHH		69.35-
294UbiquitinationRLLQEALKRKEKRRA
HHHHHHHHHHHHHHH		69.3529967540
294AcetylationRLLQEALKRKEKRRA
HHHHHHHHHHHHHHH		69.3511793317
298AcetylationEALKRKEKRRAQRQR
HHHHHHHHHHHHHHH		50.6611793327
317UbiquitinationRTAGVVEKMQQRQDR
HHHHHHHHHHHHHHH		30.3324816145
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 SURF6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SURF6_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 SURF6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RRS1_HUMANRRS1physical
26344197
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 SURF6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND THR-229, ANDMASS 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-74; SER-138 AND THR-229,AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-138, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-138; SER-206 ANDTHR-229, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASSSPECTROMETRY.
"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 THR-229, AND MASSSPECTROMETRY.

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