SPAS2_HUMAN - dbPTM
SPAS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPAS2_HUMAN
UniProt AC Q86XZ4
Protein Name Spermatogenesis-associated serine-rich protein 2
Gene Name SPATS2
Organism Homo sapiens (Human).
Sequence Length 545
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MSRKQNQKDSSGFIFDLQSNTVLAQGGAFENMKEKINAVRAIVPNKSNNEIILVLQHFDNCVDKTVQAFMEGSASEVLKEWTVTGKKKNKKKKNKPKPAAEPSNGIPDSSKSVSIQEEQSAPSSEKGGMNGYHVNGAINDTESVDSLSEGLETLSIDARELEDPESAMLDTLDRTGSMLQNGVSDFETKSLTMHSIHNSQQPRNAAKSLSRPTTETQFSNMGMEDVPLATSKKLSSNIEKSVKDLQRCTVSLARYRVVVKEEMDASIKKMKQAFAELESCLMDREVALLAEMDKVKAEAMEILLSRQKKAELLKKMTHVAVQMSEQQLVELRADIKHFVSERKYDEDLGRVARFTCDVETLKKSIDSFGQVSHPKNSYSTRSRCSSVTSVSLSSPSDASAASSSTCASPPSLTSANKKNFAPGETPAAIANSSGQPYQPLREVLPGNRRGGQGYRPQGQKSNDPMNQGRHDSMGRYRNSSWYSSGSRYQSAPSQAPGNTIERGQTHSAGTNGTGVSMEPSPPTPSFKKGLPQRKPRTSQTEAVNS
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
10PhosphorylationRKQNQKDSSGFIFDL
CCCCCCCCCCCEEEC
39.1230576142
11PhosphorylationKQNQKDSSGFIFDLQ
CCCCCCCCCCEEECC
48.1024719451
47PhosphorylationRAIVPNKSNNEIILV
EEECCCCCCCEEEEE
52.0727251275
93AcetylationKKKNKKKKNKPKPAA
CCCCCCCCCCCCCCC
78.1830592593
97AcetylationKKKKNKPKPAAEPSN
CCCCCCCCCCCCCCC
49.2330592599
112PhosphorylationGIPDSSKSVSIQEEQ
CCCCCCCCCCCCCCC
24.0523403867
114PhosphorylationPDSSKSVSIQEEQSA
CCCCCCCCCCCCCCC
26.1621815630
120PhosphorylationVSIQEEQSAPSSEKG
CCCCCCCCCCCCCCC
45.4823403867
123PhosphorylationQEEQSAPSSEKGGMN
CCCCCCCCCCCCCCC
51.3423403867
124PhosphorylationEEQSAPSSEKGGMNG
CCCCCCCCCCCCCCC
42.1221815630
132PhosphorylationEKGGMNGYHVNGAIN
CCCCCCCEEECCCCC
9.5220068231
141PhosphorylationVNGAINDTESVDSLS
ECCCCCCCCCCHHHH
26.1820068231
143PhosphorylationGAINDTESVDSLSEG
CCCCCCCCCHHHHHC
33.0625137130
146PhosphorylationNDTESVDSLSEGLET
CCCCCCHHHHHCHHE
31.4725137130
148PhosphorylationTESVDSLSEGLETLS
CCCCHHHHHCHHEEE
33.3020068231
153PhosphorylationSLSEGLETLSIDARE
HHHHCHHEEECCHHH
30.7426074081
155PhosphorylationSEGLETLSIDARELE
HHCHHEEECCHHHCC
26.3320068231
168SulfoxidationLEDPESAMLDTLDRT
CCCHHHHHHHHHHHH
4.9121406390
175PhosphorylationMLDTLDRTGSMLQNG
HHHHHHHHHCHHHHC
33.0228857561
177PhosphorylationDTLDRTGSMLQNGVS
HHHHHHHCHHHHCCC
18.7328857561
190PhosphorylationVSDFETKSLTMHSIH
CCCCCCCCCCHHHHH
36.1729116813
192PhosphorylationDFETKSLTMHSIHNS
CCCCCCCCHHHHHCC
21.6729514088
195PhosphorylationTKSLTMHSIHNSQQP
CCCCCHHHHHCCCCH
18.0829514088
199PhosphorylationTMHSIHNSQQPRNAA
CHHHHHCCCCHHHHH
18.9428555341
207UbiquitinationQQPRNAAKSLSRPTT
CCHHHHHHHCCCCCC
49.90-
208PhosphorylationQPRNAAKSLSRPTTE
CHHHHHHHCCCCCCC
27.1828348404
210PhosphorylationRNAAKSLSRPTTETQ
HHHHHHCCCCCCCHH
43.2228348404
213PhosphorylationAKSLSRPTTETQFSN
HHHCCCCCCCHHHCC
35.8318491316
214PhosphorylationKSLSRPTTETQFSNM
HHCCCCCCCHHHCCC
39.4518491316
216PhosphorylationLSRPTTETQFSNMGM
CCCCCCCHHHCCCCC
32.5928857561
219PhosphorylationPTTETQFSNMGMEDV
CCCCHHHCCCCCCCC
18.9830576142
230PhosphorylationMEDVPLATSKKLSSN
CCCCCHHHCHHHHHH
49.0828555341
233UbiquitinationVPLATSKKLSSNIEK
CCHHHCHHHHHHHHH
54.06-
240UbiquitinationKLSSNIEKSVKDLQR
HHHHHHHHHHHHHHH
57.67-
279PhosphorylationQAFAELESCLMDREV
HHHHHHHHHHHHHHH
25.7726270265
294UbiquitinationALLAEMDKVKAEAME
HHHHHHHHHHHHHHH
44.30-
296UbiquitinationLAEMDKVKAEAMEIL
HHHHHHHHHHHHHHH
46.37-
336AcetylationVELRADIKHFVSERK
HHHHHHHHHHHHHCC
31.3826051181
336UbiquitinationVELRADIKHFVSERK
HHHHHHHHHHHHHCC
31.38-
362UbiquitinationTCDVETLKKSIDSFG
ECCHHHHHHHHHHCC
52.47-
363UbiquitinationCDVETLKKSIDSFGQ
CCHHHHHHHHHHCCC
56.61-
367PhosphorylationTLKKSIDSFGQVSHP
HHHHHHHHCCCCCCC
29.6124719451
375UbiquitinationFGQVSHPKNSYSTRS
CCCCCCCCCCCCCCC
53.77-
378PhosphorylationVSHPKNSYSTRSRCS
CCCCCCCCCCCCCCC
24.3724719451
379PhosphorylationSHPKNSYSTRSRCSS
CCCCCCCCCCCCCCC
19.7122210691
380PhosphorylationHPKNSYSTRSRCSSV
CCCCCCCCCCCCCCC
25.1624719451
382PhosphorylationKNSYSTRSRCSSVTS
CCCCCCCCCCCCCEE
37.4122817900
385PhosphorylationYSTRSRCSSVTSVSL
CCCCCCCCCCEEEEE
27.0827273156
386PhosphorylationSTRSRCSSVTSVSLS
CCCCCCCCCEEEEEC
32.8027273156
388PhosphorylationRSRCSSVTSVSLSSP
CCCCCCCEEEEECCC
25.9229978859
389PhosphorylationSRCSSVTSVSLSSPS
CCCCCCEEEEECCCC
13.9325159151
391PhosphorylationCSSVTSVSLSSPSDA
CCCCEEEEECCCCCC
23.4629978859
393PhosphorylationSVTSVSLSSPSDASA
CCEEEEECCCCCCCC
32.4729978859
394PhosphorylationVTSVSLSSPSDASAA
CEEEEECCCCCCCCC
33.4425159151
396PhosphorylationSVSLSSPSDASAASS
EEEECCCCCCCCCCC
47.9930576142
399PhosphorylationLSSPSDASAASSSTC
ECCCCCCCCCCCCCC
29.3823312004
402PhosphorylationPSDASAASSSTCASP
CCCCCCCCCCCCCCC
25.2527174698
403PhosphorylationSDASAASSSTCASPP
CCCCCCCCCCCCCCC
25.5830576142
404PhosphorylationDASAASSSTCASPPS
CCCCCCCCCCCCCCC
25.6327174698
405PhosphorylationASAASSSTCASPPSL
CCCCCCCCCCCCCCC
17.6530576142
408PhosphorylationASSSTCASPPSLTSA
CCCCCCCCCCCCCCC
39.2230576142
411PhosphorylationSTCASPPSLTSANKK
CCCCCCCCCCCCCCC
47.8927174698
413PhosphorylationCASPPSLTSANKKNF
CCCCCCCCCCCCCCC
30.0827174698
414PhosphorylationASPPSLTSANKKNFA
CCCCCCCCCCCCCCC
34.8327174698
418UbiquitinationSLTSANKKNFAPGET
CCCCCCCCCCCCCCC
58.04-
425PhosphorylationKNFAPGETPAAIANS
CCCCCCCCCHHHHCC
24.9227050516
432PhosphorylationTPAAIANSSGQPYQP
CCHHHHCCCCCCCCC
27.1629978859
433PhosphorylationPAAIANSSGQPYQPL
CHHHHCCCCCCCCCH
41.0528796482
437PhosphorylationANSSGQPYQPLREVL
HCCCCCCCCCHHHHC
18.1828796482
449MethylationEVLPGNRRGGQGYRP
HHCCCCCCCCCCCCC
58.5630761157
455MethylationRRGGQGYRPQGQKSN
CCCCCCCCCCCCCCC
24.72115387495
472PhosphorylationMNQGRHDSMGRYRNS
CCCCCCCCCCCCCCC
19.6024719451
476PhosphorylationRHDSMGRYRNSSWYS
CCCCCCCCCCCCCCC
14.3930576142
479PhosphorylationSMGRYRNSSWYSSGS
CCCCCCCCCCCCCCC
17.1622167270
480PhosphorylationMGRYRNSSWYSSGSR
CCCCCCCCCCCCCCC
33.3223401153
482PhosphorylationRYRNSSWYSSGSRYQ
CCCCCCCCCCCCCCC
8.5628796482
483PhosphorylationYRNSSWYSSGSRYQS
CCCCCCCCCCCCCCC
23.2028796482
484PhosphorylationRNSSWYSSGSRYQSA
CCCCCCCCCCCCCCC
25.7028796482
486PhosphorylationSSWYSSGSRYQSAPS
CCCCCCCCCCCCCCC
29.7528796482
488PhosphorylationWYSSGSRYQSAPSQA
CCCCCCCCCCCCCCC
14.44-
490PhosphorylationSSGSRYQSAPSQAPG
CCCCCCCCCCCCCCC
32.9622210691
493PhosphorylationSRYQSAPSQAPGNTI
CCCCCCCCCCCCCCC
38.4028555341
499PhosphorylationPSQAPGNTIERGQTH
CCCCCCCCCCCCCCC
30.0827251275
507PhosphorylationIERGQTHSAGTNGTG
CCCCCCCCCCCCCCC
31.61-
516PhosphorylationGTNGTGVSMEPSPPT
CCCCCCCCCCCCCCC
20.8328555341
520PhosphorylationTGVSMEPSPPTPSFK
CCCCCCCCCCCCCHH
30.1526055452
523PhosphorylationSMEPSPPTPSFKKGL
CCCCCCCCCCHHCCC
34.6426055452
525PhosphorylationEPSPPTPSFKKGLPQ
CCCCCCCCHHCCCCC
52.7720068231
537PhosphorylationLPQRKPRTSQTEAVN
CCCCCCCCCCCCCCC
33.4422199227
538PhosphorylationPQRKPRTSQTEAVNS
CCCCCCCCCCCCCCC
36.0630576142
540PhosphorylationRKPRTSQTEAVNS--
CCCCCCCCCCCCC--
26.1930576142
545O-linked_GlycosylationSQTEAVNS-------
CCCCCCCC-------
34.6923301498
545PhosphorylationSQTEAVNS-------
CCCCCCCC-------
34.6925159151

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 SPAS2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPAS2_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 SPAS2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049

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 SPAS2_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-146, 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-520 AND THR-523, ANDMASS SPECTROMETRY.

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