SSFA2_HUMAN - dbPTM
SSFA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SSFA2_HUMAN
UniProt AC P28290
Protein Name Sperm-specific antigen 2
Gene Name SSFA2
Organism Homo sapiens (Human).
Sequence Length 1259
Subcellular Localization Cytoplasm . Located near the plasma membrane. Associated with actin filaments. May also exist as a membrane-bound form with extracellular regions.
Protein Description
Protein Sequence MDRPLSSSAEAEEELEWQVASRRRKAWAKCRSSWQASETEDLSTEATTQDEEEDEEEDLPGAQLPAAGGRGNVPNEKIAIWLKDCRTPLGASLDEQSSSTLKGVLVRNGGSFEDDLSLGAEANHLHESDAQIENCNNILAKERRLQFHQKGRSMNSTGSGKSSGTVSSVSELLELYEEDPEEILYNLGFGRDEPDIASKIPSRFFNSSSFAKGIDIKVFLSAQMQRMEVENPNYALTSRFRQIEVLTTVANAFSSLYSQVSGTPLQRIGSMSSVTSNKETDPPPPLTRSNTANRLMKTLSKLNLCVDKTEKGESSSPSPSAEKGKILNVSVIEESGNKNDQKSQKIMKKKESSSMLATVKEEVSGSSAAVTENADSDRISDEANSNFNQGTENEQSKETQSHESKLGEESGIVESKLDSDFNISSHSELENSSELKSVHISTPEKEPCAPLTIPSIRNIMTQQKDSFEMEEVQSTEGEAPHVPATYQLGLTKSKRDHLLRTASQHSDSSGFAEDSTDCLSLNHLQVQESLQAMGSSADSCDSETTVTSLGEDLATPTAQDQPYFNESEEESLVPLQKGLEKAAAVADKRKSGSQDFPQCNTIENTGTKQSTCSPGDHIIEITEVEEDLFPAETVELLREASAESDVGKSSESEFTQYTTHHILKSLASIEAKCSDMSSENTTGPPSSMDRVNTALQRAQMKVCSLSNQRMGRSLLKSKDLLKQRYLFAKAGYPLRRSQSLPTTLLSPVRVVSSVNVRLSPGKETRCSPPSFTYKYTPEEEQELEKRVMEHDGQSLVKSTIFISPSSVKKEEAPQSEAPRVEECHHGRTPTCSRLAPPPMSQSTCSLHSIHSEWQERPLCEHTRTLSTHSVPNISGATCSAFASPFGCPYSHRHATYPYRVCSVNPPSAIEMQLRRVLHDIRNSLQNLSQYPMMRGPDPAAAPYSTQKSSVLPLYENTFQELQVMRRSLNLFRTQMMDLELAMLRQQTMVYHHMTEEERFEVDQLQGLRNSVRMELQDLELQLEERLLGLEEQLRAVRMPSPFRSSALMGMCGSRSADNLSCPSPLNVMEPVTELMQEQSYLKSELGLGLGEMGFEIPPGESSESVFSQATSESSSVCSGPSHANRRTGVPSTASVGKSKTPLVARKKVFRASVALTPTAPSRTGSVQTPPDLESSEEVDAAEGAPEVVGPKSEVEEGHGKLPSMPAAEEMHKNVEQDELQQVIREIKESIVGEIRREIVSGLLAAVSSSKASNSKQDYH
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
46 (in isoform 2)Ubiquitination-18.9421890473
59 (in isoform 2)Ubiquitination-4.8221890473
77 (in isoform 3)Ubiquitination-44.0421890473
77 (in isoform 1)Ubiquitination-44.0421890473
102 (in isoform 3)Ubiquitination-47.2421890473
102 (in isoform 1)Ubiquitination-47.2421890473
125 (in isoform 2)Ubiquitination-4.8721890473
148 (in isoform 2)Ubiquitination-18.5821890473
158 (in isoform 2)Ubiquitination-33.9321890473
172 (in isoform 2)Ubiquitination-3.3321890473
199 (in isoform 1)Ubiquitination-50.0021890473
199 (in isoform 3)Ubiquitination-50.0021890473
212 (in isoform 3)Ubiquitination-55.1521890473
212 (in isoform 1)Ubiquitination-55.1521890473
244 (in isoform 2)Ubiquitination-24.1221890473
252 (in isoform 2)Ubiquitination-8.9221890473
263 (in isoform 2)Ubiquitination-17.2021890473
278 (in isoform 1)Ubiquitination-62.8521890473
278 (in isoform 3)Ubiquitination-62.8521890473
301 (in isoform 1)Ubiquitination-44.5021890473
301 (in isoform 3)Ubiquitination-44.5021890473
308AcetylationKLNLCVDKTEKGESS
HHCEEEECCCCCCCC
37.8826051181
311 (in isoform 3)Ubiquitination-73.5321890473
311 (in isoform 1)Ubiquitination-73.5321890473
325 (in isoform 3)Ubiquitination-55.9021890473
325 (in isoform 1)Ubiquitination-55.9021890473
360SumoylationSSMLATVKEEVSGSS
HHHHHHHHHHHCCCC
43.7528112733
397 (in isoform 3)Ubiquitination-65.5621890473
397 (in isoform 1)Ubiquitination-65.5621890473
405 (in isoform 3)Ubiquitination-58.4921890473
405 (in isoform 1)Ubiquitination-58.4921890473
416 (in isoform 3)Ubiquitination-42.6921890473
416 (in isoform 1)Ubiquitination-42.6921890473
445AcetylationVHISTPEKEPCAPLT
CEECCCCCCCCCCCC
69.0626051181
511 (in isoform 2)Ubiquitination-7.9021890473
632 (in isoform 2)Ubiquitination-54.3321890473
644 (in isoform 2)Ubiquitination-36.9921890473
655 (in isoform 2)Ubiquitination-19.3321890473
664 (in isoform 3)Ubiquitination-42.7021890473
664 (in isoform 1)Ubiquitination-42.7021890473
785 (in isoform 3)Ubiquitination-64.0221890473
785 (in isoform 1)Ubiquitination-64.0221890473
794 (in isoform 2)Ubiquitination-40.4321890473
797 (in isoform 3)Ubiquitination-47.3721890473
797 (in isoform 1)Ubiquitination-47.3721890473
808 (in isoform 3)Ubiquitination-57.3121890473
808 (in isoform 1)Ubiquitination-57.3121890473
947 (in isoform 3)Ubiquitination-44.8021890473
947 (in isoform 1)Ubiquitination-44.8021890473
1047 (in isoform 2)Ubiquitination-3.0921890473
1059 (in isoform 2)Ubiquitination-6.0021890473
1097 (in isoform 2)Ubiquitination-24.5221890473
1102 (in isoform 2)Ubiquitination-29.5921890473
1200 (in isoform 3)Ubiquitination-52.1021890473
1200 (in isoform 1)Ubiquitination-52.1021890473
1212 (in isoform 1)Ubiquitination-62.4721890473
1212 (in isoform 3)Ubiquitination-62.4721890473
1250 (in isoform 1)Ubiquitination-58.7521890473
1255 (in isoform 1)Ubiquitination-51.9821890473

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 SSFA2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SSFA2_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 SSFA2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LC7L2_HUMANLUC7L2physical
16169070
1433Z_HUMANYWHAZphysical
21988832
1433T_HUMANYWHAQphysical
21988832
CBL_HUMANCBLphysical
26186194
FKB15_HUMANFKBP15physical
26186194
SGF29_HUMANCCDC101physical
26186194
PIGR_HUMANPIGRphysical
26186194
PCM1_HUMANPCM1physical
26186194
VP33B_HUMANVPS33Bphysical
26186194
FKB15_HUMANFKBP15physical
28514442
SGF29_HUMANCCDC101physical
28514442
VP33B_HUMANVPS33Bphysical
28514442
CBL_HUMANCBLphysical
28514442
PCM1_HUMANPCM1physical
28514442
PIGR_HUMANPIGRphysical
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 SSFA2_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-92 AND SER-739, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-330; SER-737 ANDSER-739, AND MASS 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 SER-739, 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 THR-87; SER-92; SER-668;SER-737; SER-739; SER-746; SER-1131 AND SER-1134, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-739, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; TYR-725 ANDTYR-732, AND MASS SPECTROMETRY.
"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-163; THR-165; SER-167;SER-168; SER-610; SER-1055; SER-1060 AND SER-1063, AND MASSSPECTROMETRY.

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