SPAT2_HUMAN - dbPTM
SPAT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPAT2_HUMAN
UniProt AC Q9UM82
Protein Name Spermatogenesis-associated protein 2
Gene Name SPATA2
Organism Homo sapiens (Human).
Sequence Length 520
Subcellular Localization Nucleus.
Protein Description May have a role in the regulation of spermatogenesis..
Protein Sequence MGKPSSMDTKFKDDLFRKYVQFHESKVDTTTSRQRPGSDECLRVAASTLLSLHKVDPFYRFRLIQFYEVVESSLRSLSSSSLRALHGAFSMLETVGINLFLYPWKKEFRSIKTYTGPFVYYVKSTLLEEDIRAILSCMGYTPELGTAYKLRELVETLQVKMVSFELFLAKVECEQMLEIHSQVKDKGYSELDIVSERKSSAEDVRGCSDALRRRAEGREHLTASMSRVALQKSASERAAKDYYKPRVTKPSRSVDAYDSYWESRKPPLKASLSLRKEPVATDVGDDLKDEIIRPSPSLLTMASSPHGSPDVLPPASPSNGPALLRGTYFSTQDDVDLYTDSEPRATYRRQDALRPDVWLLRNDAHSLYHKRSPPAKESALSKCQSCGLSCSSSLCQRCDSLLTCPPASKPSAFPSKASTHDSLAHGASLREKYPGQTQGLDRLPHLHSKSKPSTTPTSRCGFCNRPGATNTCTQCSKVSCDACLSAYHYDPCYKKSELHKFMPNNQLNYKSTQLSHLVYR
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
6Phosphorylation--MGKPSSMDTKFKD
--CCCCCCCCHHHCH		29.2529449344
9PhosphorylationGKPSSMDTKFKDDLF
CCCCCCCHHHCHHHH		29.7329449344
18MalonylationFKDDLFRKYVQFHES
HCHHHHHHHHHHHHH		42.3032601280
38PhosphorylationTSRQRPGSDECLRVA
CCCCCCCCHHHHHHH		32.6829083192
113PhosphorylationKEFRSIKTYTGPFVY
HHHHCCCCCCCCCEE		25.33-
114PhosphorylationEFRSIKTYTGPFVYY
HHHCCCCCCCCCEEE		12.51-
115PhosphorylationFRSIKTYTGPFVYYV
HHCCCCCCCCCEEEE		43.54-
120PhosphorylationTYTGPFVYYVKSTLL
CCCCCCEEEECCCCC		11.7029759185
121PhosphorylationYTGPFVYYVKSTLLE
CCCCCEEEECCCCCH		8.9729759185
163PhosphorylationTLQVKMVSFELFLAK
HHHHHHHHHHHHHHH		14.9828355574
186UbiquitinationIHSQVKDKGYSELDI
HHHHHCCCCCCCCCH		54.77-
222PhosphorylationAEGREHLTASMSRVA
HHCHHHHHHHHHHHH		20.7028857561
224PhosphorylationGREHLTASMSRVALQ
CHHHHHHHHHHHHHH		16.4428857561
226PhosphorylationEHLTASMSRVALQKS
HHHHHHHHHHHHHHH		22.5523312004
232UbiquitinationMSRVALQKSASERAA
HHHHHHHHHHHHHHH		49.17-
242PhosphorylationSERAAKDYYKPRVTK
HHHHHHHHHCCCCCC		16.8129496907
243PhosphorylationERAAKDYYKPRVTKP
HHHHHHHHCCCCCCC		25.34-
244UbiquitinationRAAKDYYKPRVTKPS
HHHHHHHCCCCCCCC		21.81-
251PhosphorylationKPRVTKPSRSVDAYD
CCCCCCCCCCCCCCH		38.4528634298
253PhosphorylationRVTKPSRSVDAYDSY
CCCCCCCCCCCCHHH		28.7825159151
257PhosphorylationPSRSVDAYDSYWESR
CCCCCCCCHHHHHHC		10.8520090780
259PhosphorylationRSVDAYDSYWESRKP
CCCCCCHHHHHHCCC		21.3328857561
260PhosphorylationSVDAYDSYWESRKPP
CCCCCHHHHHHCCCC		15.4220090780
269MethylationESRKPPLKASLSLRK
HHCCCCCEECEECCC		41.52115980637
271PhosphorylationRKPPLKASLSLRKEP
CCCCCEECEECCCCC		19.5317081983
273PhosphorylationPPLKASLSLRKEPVA
CCCEECEECCCCCCC		24.5129514088
281PhosphorylationLRKEPVATDVGDDLK
CCCCCCCCCCCCHHC		31.30-
295PhosphorylationKDEIIRPSPSLLTMA
CCCCCCCCCCHHHHC		19.78-
303PhosphorylationPSLLTMASSPHGSPD
CCHHHHCCCCCCCCC		33.31-
316PhosphorylationPDVLPPASPSNGPAL
CCCCCCCCCCCCCCC		34.3426074081
318PhosphorylationVLPPASPSNGPALLR
CCCCCCCCCCCCCCC		52.5026074081
338PhosphorylationTQDDVDLYTDSEPRA
CCCCCCCCCCCCCCH		12.2027642862
366PhosphorylationLLRNDAHSLYHKRSP
EEECCHHHHHHCCCC		32.1327251275
368PhosphorylationRNDAHSLYHKRSPPA
ECCHHHHHHCCCCCH		14.33-
382UbiquitinationAKESALSKCQSCGLS
HHHHHHHHHHHCCCC		36.82-
389PhosphorylationKCQSCGLSCSSSLCQ
HHHHCCCCCCHHHHH		9.3828348404
391PhosphorylationQSCGLSCSSSLCQRC
HHCCCCCCHHHHHHC		21.4228348404
392PhosphorylationSCGLSCSSSLCQRCD
HCCCCCCHHHHHHCC		31.4928348404
393PhosphorylationCGLSCSSSLCQRCDS
CCCCCCHHHHHHCCH		19.5028348404
400PhosphorylationSLCQRCDSLLTCPPA
HHHHHCCHHCCCCCC		28.9828348404
408O-linked_GlycosylationLLTCPPASKPSAFPS
HCCCCCCCCCCCCCC		51.3730379171
416MethylationKPSAFPSKASTHDSL
CCCCCCCCCCCCCHH		46.74115980645
422PhosphorylationSKASTHDSLAHGASL
CCCCCCCHHHHCHHH		21.6123312004
428PhosphorylationDSLAHGASLREKYPG
CHHHHCHHHHHHCCC		32.3323312004
432UbiquitinationHGASLREKYPGQTQG
HCHHHHHHCCCCCCC		50.76-
487PhosphorylationCDACLSAYHYDPCYK
CCCCHHHCCCCCCCC		9.50-
489PhosphorylationACLSAYHYDPCYKKS
CCHHHCCCCCCCCHH		14.6520090780
493PhosphorylationAYHYDPCYKKSELHK
HCCCCCCCCHHHHHH		27.17-
509PhosphorylationMPNNQLNYKSTQLSH
CCCCCCCCCHHHHHH		18.2127642862
510AcetylationPNNQLNYKSTQLSHL
CCCCCCCCHHHHHHH		46.058259985
510MethylationPNNQLNYKSTQLSHL
CCCCCCCCHHHHHHH		46.058259985
519PhosphorylationTQLSHLVYR------
HHHHHHHCC------		19.5725159151
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 SPAT2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPAT2_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 SPAT2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CEP72_HUMANCEP72physical
16189514
CYLD_HUMANCYLDphysical
19615732
GNAL_HUMANGNALphysical
19615732
PFD4_HUMANPFDN4physical
19615732
CSKP_HUMANCASKphysical
19615732
SSNA1_HUMANSSNA1physical
19615732
PFD6_HUMANPFDN6physical
19615732
BABA1_HUMANBABAM1physical
19615732
UIMC1_HUMANUIMC1physical
19615732
LIN7C_HUMANLIN7Cphysical
19615732
A4_HUMANAPPphysical
21832049
LZTS2_HUMANLZTS2physical
25416956
CYLD_HUMANCYLDphysical
27458237
RNF31_HUMANRNF31physical
27458237
CYLD_HUMANCYLDphysical
27591049
RNF31_HUMANRNF31physical
27591049
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 SPAT2_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-253, 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-253, AND MASSSPECTROMETRY.

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