SURF2_HUMAN - dbPTM
SURF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SURF2_HUMAN
UniProt AC Q15527
Protein Name Surfeit locus protein 2
Gene Name SURF2
Organism Homo sapiens (Human).
Sequence Length 256
Subcellular Localization
Protein Description
Protein Sequence MSELPGDVRAFLREHPSLRLQTDARKVRCILTGHELPCRLPELQVYTRGKKYQRLVRASPAFDYAEFEPHIVPSTKNPHQLFCKLTLRHINKCPEHVLRHTQGRRYQRALCKYEECQKQGVEYVPACLVHRRRRREDQMDGDGPRPREAFWEPTSSDEGGAASDDSMTDLYPPELFTRKDLGSTEDGDGTDDFLTDKEDEKAKPPREKATDESRRETTVYRGLVQKRGKKQLGSLKKKFKSHHRKPKSFSSCKQPG
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
9MethylationSELPGDVRAFLREHP
CCCCHHHHHHHHHCC
25.10115918041
17PhosphorylationAFLREHPSLRLQTDA
HHHHHCCCCCCCCCC
28.2024719451
29S-nitrosocysteineTDARKVRCILTGHEL
CCCCCEEEEHHCCCC
3.15-
29S-nitrosylationTDARKVRCILTGHEL
CCCCCEEEEHHCCCC
3.1519483679
38S-nitrosocysteineLTGHELPCRLPELQV
HHCCCCCCCCCCCEE
12.48-
38S-nitrosylationLTGHELPCRLPELQV
HHCCCCCCCCCCCEE
12.4819483679
59PhosphorylationYQRLVRASPAFDYAE
HHHHHHCCCCCCHHH
13.2430576142
64PhosphorylationRASPAFDYAEFEPHI
HCCCCCCHHHCCCCC
11.1123312004
74PhosphorylationFEPHIVPSTKNPHQL
CCCCCCCCCCCHHHH
40.9128348404
75PhosphorylationEPHIVPSTKNPHQLF
CCCCCCCCCCHHHHH
28.8628348404
84AcetylationNPHQLFCKLTLRHIN
CHHHHHHHHHHHHHH
36.8523749302
112AcetylationRYQRALCKYEECQKQ
HHHHHHHCHHHHHHC
57.4525953088
118UbiquitinationCKYEECQKQGVEYVP
HCHHHHHHCCCCCCC
61.7629967540
145PhosphorylationQMDGDGPRPREAFWE
CCCCCCCCCHHHCCC
48.7332645325
154PhosphorylationREAFWEPTSSDEGGA
HHHCCCCCCCCCCCC
29.3725849741
155PhosphorylationEAFWEPTSSDEGGAA
HHCCCCCCCCCCCCC
46.6525849741
156PhosphorylationAFWEPTSSDEGGAAS
HCCCCCCCCCCCCCC
42.0022115753
163PhosphorylationSDEGGAASDDSMTDL
CCCCCCCCCCCCCCC
41.2222617229
166PhosphorylationGGAASDDSMTDLYPP
CCCCCCCCCCCCCCH
28.6823663014
168PhosphorylationAASDDSMTDLYPPEL
CCCCCCCCCCCCHHH
27.1423663014
171PhosphorylationDDSMTDLYPPELFTR
CCCCCCCCCHHHCCC
21.3923663014
177PhosphorylationLYPPELFTRKDLGST
CCCHHHCCCCCCCCC
49.8120068231
183PhosphorylationFTRKDLGSTEDGDGT
CCCCCCCCCCCCCCC
35.6030266825
184PhosphorylationTRKDLGSTEDGDGTD
CCCCCCCCCCCCCCC
35.9830266825
190PhosphorylationSTEDGDGTDDFLTDK
CCCCCCCCCCCCCCH
36.8229255136
195PhosphorylationDGTDDFLTDKEDEKA
CCCCCCCCCHHHHCC
45.0529255136
197UbiquitinationTDDFLTDKEDEKAKP
CCCCCCCHHHHCCCC
62.9324816145
217PhosphorylationTDESRRETTVYRGLV
CHHHHHHHHHHHHHH
21.5429209046
218PhosphorylationDESRRETTVYRGLVQ
HHHHHHHHHHHHHHH
15.7029209046
220PhosphorylationSRRETTVYRGLVQKR
HHHHHHHHHHHHHHH
9.2529209046
221MethylationRRETTVYRGLVQKRG
HHHHHHHHHHHHHHC
27.86115918037
234PhosphorylationRGKKQLGSLKKKFKS
HCHHHHHHHHHHHHH
45.6828355574
248PhosphorylationSHHRKPKSFSSCKQP
HCCCCCCCHHHCCCC
38.6022210691
250PhosphorylationHRKPKSFSSCKQPG-
CCCCCCHHHCCCCC-
41.7521712546
251PhosphorylationRKPKSFSSCKQPG--
CCCCCHHHCCCCC--
24.2721712546

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 SURF2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SURF2_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 SURF2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NPTN_HUMANNPTNphysical
21900206
RL5_HUMANRPL5physical
21900206
ZN331_HUMANZNF331physical
21900206
A4_HUMANAPPphysical
21832049
ANKY2_HUMANANKMY2physical
22863883
GPN1_HUMANGPN1physical
22863883
HSF1_HUMANHSF1physical
22863883
HPBP1_HUMANHSPBP1physical
22863883
LPP_HUMANLPPphysical
22863883
NPL4_HUMANNPLOC4physical
22863883
OGT1_HUMANOGTphysical
22863883
PPME1_HUMANPPME1physical
22863883
RPR1A_HUMANRPRD1Aphysical
22863883
RPR1B_HUMANRPRD1Bphysical
22863883
STA5B_HUMANSTAT5Bphysical
22863883
TM1L1_HUMANTOM1L1physical
22863883
WDR4_HUMANWDR4physical
22863883
ZPR1_HUMANZPR1physical
22863883
POP1_HUMANPOP1physical
26186194
SPB1_HUMANFTSJ3physical
26186194
RL11_HUMANRPL11physical
26186194
LA_HUMANSSBphysical
26186194
RL3_HUMANRPL3physical
26186194
RL5_HUMANRPL5physical
26186194
PABP4_HUMANPABPC4physical
26186194
HEAT3_HUMANHEATR3physical
26186194
LARP1_HUMANLARP1physical
26186194
IMA7_HUMANKPNA6physical
26186194
RIOX2_HUMANMINAphysical
26186194
RRS1_HUMANRRS1physical
26186194
BRX1_HUMANBRIX1physical
26186194
DDX18_HUMANDDX18physical
26186194
MDM2_HUMANMDM2physical
26186194
HEXI1_HUMANHEXIM1physical
26186194
ZCHC9_HUMANZCCHC9physical
26186194
TRI27_HUMANTRIM27physical
26186194
LN28B_HUMANLIN28Bphysical
26186194
RS13_HUMANRPS13physical
26186194
CE022_HUMANC5orf22physical
26186194
PURA_HUMANPURAphysical
26186194
H2AX_HUMANH2AFXphysical
26186194
KBTB7_HUMANKBTBD7physical
26186194
ZCRB1_HUMANZCRB1physical
26186194
DBLOH_HUMANDIABLOphysical
26344197
CE022_HUMANC5orf22physical
28514442
H2AX_HUMANH2AFXphysical
28514442
RL11_HUMANRPL11physical
28514442
HEXI1_HUMANHEXIM1physical
28514442
RIOX2_HUMANMINAphysical
28514442
RL5_HUMANRPL5physical
28514442
LA_HUMANSSBphysical
28514442
ZCHC9_HUMANZCCHC9physical
28514442
HEAT3_HUMANHEATR3physical
28514442
RRS1_HUMANRRS1physical
28514442
ZCRB1_HUMANZCRB1physical
28514442
IMA7_HUMANKPNA6physical
28514442
MDM2_HUMANMDM2physical
28514442
KBTB7_HUMANKBTBD7physical
28514442
LN28B_HUMANLIN28Bphysical
28514442
LARP1_HUMANLARP1physical
28514442
YBOX1_HUMANYBX1physical
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 SURF2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-154; SER-155; SER-156;SER-163; THR-190 AND THR-195, AND MASS SPECTROMETRY.
"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-190 AND THR-195, ANDMASS SPECTROMETRY.
"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 THR-190 AND THR-195, 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 THR-190 AND THR-195, ANDMASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-195, AND MASSSPECTROMETRY.

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