SPAG7_HUMAN - dbPTM
SPAG7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPAG7_HUMAN
UniProt AC O75391
Protein Name Sperm-associated antigen 7
Gene Name SPAG7
Organism Homo sapiens (Human).
Sequence Length 227
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MADLLGSILSSMEKPPSLGDQETRRKAREQAARLKKLQEQEKQQKVEFRKRMEKEVSDFIQDSGQIKKKFQPMNKIERSILHDVVEVAGLTSFSFGEDDDCRYVMIFKKEFAPSDEELDSYRRGEEWDPQKAEEKRKLKELAQRQEEEAAQQGPVVVSPASDYKDKYSHLIGKGAAKDAAHMLQANKTYGCVPVANKRDTRSIEEAMNEIRAKKRLRQSGEELPPTS
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------MADLLGSIL
------CHHHHHHHH
19.0322223895
7Phosphorylation-MADLLGSILSSMEK
-CHHHHHHHHHHCCC
21.9622199227
10PhosphorylationDLLGSILSSMEKPPS
HHHHHHHHHCCCCCC
26.4322199227
11PhosphorylationLLGSILSSMEKPPSL
HHHHHHHHCCCCCCC
27.7622199227
17PhosphorylationSSMEKPPSLGDQETR
HHCCCCCCCCCHHHH
54.2125159151
23PhosphorylationPSLGDQETRRKAREQ
CCCCCHHHHHHHHHH
30.0927732954
45UbiquitinationQEQEKQQKVEFRKRM
HHHHHHHHHHHHHHH
41.04-
57PhosphorylationKRMEKEVSDFIQDSG
HHHHHHHHHHHHCCC
28.0920068231
63PhosphorylationVSDFIQDSGQIKKKF
HHHHHHCCCHHHHHC
19.0720068231
67UbiquitinationIQDSGQIKKKFQPMN
HHCCCHHHHHCCCCC
41.8621890473
103PhosphorylationGEDDDCRYVMIFKKE
CCCCCCCEEEEEECC
10.7419413330
109UbiquitinationRYVMIFKKEFAPSDE
CEEEEEECCCCCCHH
47.52-
114PhosphorylationFKKEFAPSDEELDSY
EECCCCCCHHHHHHH
54.9830266825
120PhosphorylationPSDEELDSYRRGEEW
CCHHHHHHHHCCCCC
32.9128152594
121PhosphorylationSDEELDSYRRGEEWD
CHHHHHHHHCCCCCC
12.1928152594
139UbiquitinationAEEKRKLKELAQRQE
HHHHHHHHHHHHHHH
54.43-
158PhosphorylationQQGPVVVSPASDYKD
HHCCEEECCCHHCHH
11.7919664994
161PhosphorylationPVVVSPASDYKDKYS
CEEECCCHHCHHHHH
44.8730266825
163PhosphorylationVVSPASDYKDKYSHL
EECCCHHCHHHHHHH
20.7030266825
164AcetylationVSPASDYKDKYSHLI
ECCCHHCHHHHHHHH
53.3826051181
166AcetylationPASDYKDKYSHLIGK
CCHHCHHHHHHHHCC
44.4919608861
166UbiquitinationPASDYKDKYSHLIGK
CCHHCHHHHHHHHCC
44.4919608861
167PhosphorylationASDYKDKYSHLIGKG
CHHCHHHHHHHHCCC
16.0823927012
168PhosphorylationSDYKDKYSHLIGKGA
HHCHHHHHHHHCCCH
19.9823927012
173UbiquitinationKYSHLIGKGAAKDAA
HHHHHHCCCHHHHHH
38.0821890473
177MethylationLIGKGAAKDAAHMLQ
HHCCCHHHHHHHHHH
47.57115980669
187AcetylationAHMLQANKTYGCVPV
HHHHHCCCCCCEEEC
46.2526051181
188PhosphorylationHMLQANKTYGCVPVA
HHHHCCCCCCEEECC
25.5928152594
189PhosphorylationMLQANKTYGCVPVAN
HHHCCCCCCEEECCC
15.3328152594
197UbiquitinationGCVPVANKRDTRSIE
CEEECCCCCCCCCHH
41.74-
197AcetylationGCVPVANKRDTRSIE
CEEECCCCCCCCCHH
41.7425953088
200PhosphorylationPVANKRDTRSIEEAM
ECCCCCCCCCHHHHH
30.2828450419
202PhosphorylationANKRDTRSIEEAMNE
CCCCCCCCHHHHHHH
36.1223401153
207SulfoxidationTRSIEEAMNEIRAKK
CCCHHHHHHHHHHHH
5.3821406390
219PhosphorylationAKKRLRQSGEELPPT
HHHHHHHCCCCCCCC
41.5623401153
226PhosphorylationSGEELPPTS------
CCCCCCCCC------
45.1625159151
227O-linked_GlycosylationGEELPPTS-------
CCCCCCCC-------
43.9523301498
227PhosphorylationGEELPPTS-------
CCCCCCCC-------
43.9529396449

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 SPAG7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPAG7_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 SPAG7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SPAG7_HUMAN !!

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 SPAG7_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, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-166, 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-114, 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-114 AND SER-158, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-121, AND MASSSPECTROMETRY.

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