SPAG1_HUMAN - dbPTM
SPAG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPAG1_HUMAN
UniProt AC Q07617
Protein Name Sperm-associated antigen 1
Gene Name SPAG1
Organism Homo sapiens (Human).
Sequence Length 926
Subcellular Localization Cytoplasm . Colocalizes with tubulin.
Protein Description May play a role in the cytoplasmic assembly of the ciliary dynein arms (By similarity). May play a role in fertilization. Binds GTP and has GTPase activity..
Protein Sequence MTTKDYPSLWGFGTTKTFKIPIEHLDFKYIEKCSDVKHLEKILCVLRSGEEGYYPELTEFCEKHLQALAPESRALRKDKPAATAASFTAEEWEKIDGDIKSWVSEIKKEEDKMHFHETETFPAMKDNLPPVRGSNSCLHVGKEKYSKRPTKKKTPRDYAEWDKFDVEKECLKIDEDYKEKTVIDKSHLSKIETRIDTAGLTEKEKDFLATREKEKGNEAFNSGDYEEAVMYYTRSISALPTVVAYNNRAQAEIKLQNWNSAFQDCEKVLELEPGNVKALLRRATTYKHQNKLREATEDLSKVLDVEPDNDLAKKTLSEVERDLKNSEAASETQTKGKRMVIQEIENSEDEEGKSGRKHEDGGGDKKPAEPAGAARAAQPCVMGNIQKKLTGKAEGGKRPARGAPQRGQTPEAGADKRSPRRASAAAAAGGGATGHPGGGQGAENPAGLKSQGNELFRSGQFAEAAGKYSAAIALLEPAGSEIADDLSILYSNRAACYLKEGNCSGCIQDCNRALELHPFSMKPLLRRAMAYETLEQYGKAYVDYKTVLQIDCGLQLANDSVNRLSRILMELDGPNWREKLSPIPAVPASVPLQAWHPAKEMISKQAGDSSSHRQQGITDEKTFKALKEEGNQCVNDKNYKDALSKYSECLKINNKECAIYTNRALCYLKLCQFEEAKQDCDQALQLADGNVKAFYRRALAHKGLKNYQKSLIDLNKVILLDPSIIEAKMELEEVTRLLNLKDKTAPFNKEKERRKIEIQEVNEGKEEPGRPAGEVSMGCLASEKGGKSSRSPEDPEKLPIAKPNNAYEFGQIINALSTRKDKEACAHLLAITAPKDLPMFLSNKLEGDTFLLLIQSLKNNLIEKDPSLVYQHLLYLSKAERFKMMLTLISKGQKELIEQLFEDLSDTPNNHFTLEDIQALKRQYEL
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--MTTKDYPSLWGFG
--CCCCCCCCCCCCC		9.04-
72PhosphorylationLQALAPESRALRKDK
HHHHCHHHHHHHCCC		23.07-
158PhosphorylationKKKTPRDYAEWDKFD
CCCCCCCHHHHHCCC		14.0127642862
168AcetylationWDKFDVEKECLKIDE
HHCCCHHHHHCCCCC		54.28156793
177PhosphorylationCLKIDEDYKEKTVID
HCCCCCCHHCCEEEC		20.9922817900
186PhosphorylationEKTVIDKSHLSKIET
CCEEECHHHHHHHHH		26.3926074081
189PhosphorylationVIDKSHLSKIETRID
EECHHHHHHHHHHHC		26.6026074081
201PhosphorylationRIDTAGLTEKEKDFL
HHCCCCCCHHHHHHH		44.0630576142
210PhosphorylationKEKDFLATREKEKGN
HHHHHHHHCHHHHCC		41.3230576142
225PhosphorylationEAFNSGDYEEAVMYY
CCCCCCCHHHHHHHH		21.1322817900
284PhosphorylationKALLRRATTYKHQNK
HHHHHHHHHHHHHHH		28.9327174698
285PhosphorylationALLRRATTYKHQNKL
HHHHHHHHHHHHHHH		29.5927174698
286PhosphorylationLLRRATTYKHQNKLR
HHHHHHHHHHHHHHH		11.3427174698
315PhosphorylationDNDLAKKTLSEVERD
CCHHHHHHHHHHHHH		34.5124905233
317PhosphorylationDLAKKTLSEVERDLK
HHHHHHHHHHHHHHH		44.8411517287
326PhosphorylationVERDLKNSEAASETQ
HHHHHHCCHHHHHHH		27.33-
330PhosphorylationLKNSEAASETQTKGK
HHCCHHHHHHHCCCC		48.50-
347PhosphorylationVIQEIENSEDEEGKS
EEEECCCCCCCCCCC		33.3729255136
354PhosphorylationSEDEEGKSGRKHEDG
CCCCCCCCCCCCCCC		55.4729978859
366UbiquitinationEDGGGDKKPAEPAGA
CCCCCCCCCCCHHHH		54.95-
387AcetylationCVMGNIQKKLTGKAE
CCCCCHHHHHCCCCC		46.0524469485
392UbiquitinationIQKKLTGKAEGGKRP
HHHHHCCCCCCCCCC		37.7233845483
409PhosphorylationGAPQRGQTPEAGADK
CCCCCCCCCCCCCCC		26.3923403867
416AcetylationTPEAGADKRSPRRAS
CCCCCCCCCCHHHHH		55.002520369
418PhosphorylationEAGADKRSPRRASAA
CCCCCCCCHHHHHHH		28.6226055452
423PhosphorylationKRSPRRASAAAAAGG
CCCHHHHHHHHHHCC		19.3429255136
433PhosphorylationAAAGGGATGHPGGGQ
HHHCCCCCCCCCCCC		39.0223927012
520PhosphorylationALELHPFSMKPLLRR
HHHHCCCCHHHHHHH		30.2825159151
531PhosphorylationLLRRAMAYETLEQYG
HHHHHHHHHHHHHHC		9.0727642862
537PhosphorylationAYETLEQYGKAYVDY
HHHHHHHHCCEECCH		15.9527642862
560PhosphorylationGLQLANDSVNRLSRI
CCHHCCHHHHHHHHH		22.5430266825
565PhosphorylationNDSVNRLSRILMELD
CHHHHHHHHHHHHCC		17.6530266825
581PhosphorylationPNWREKLSPIPAVPA
CCHHHHCCCCCCCCC		31.6725159151
603PhosphorylationHPAKEMISKQAGDSS
CCHHHHHHHHCCCCH		19.8722210691
609PhosphorylationISKQAGDSSSHRQQG
HHHHCCCCHHHHCCC		32.5922210691
618PhosphorylationSHRQQGITDEKTFKA
HHHCCCCCCHHHHHH		44.95-
624MethylationITDEKTFKALKEEGN
CCCHHHHHHHHHHCC		59.03-
639PhosphorylationQCVNDKNYKDALSKY
CCCCCCCHHHHHHHH		18.9122817900
640UbiquitinationCVNDKNYKDALSKYS
CCCCCCHHHHHHHHH		46.0129967540
645UbiquitinationNYKDALSKYSECLKI
CHHHHHHHHHHHHHC		54.3629967540
646PhosphorylationYKDALSKYSECLKIN
HHHHHHHHHHHHHCC		13.3122817900
647PhosphorylationKDALSKYSECLKINN
HHHHHHHHHHHHCCC		26.10-
655UbiquitinationECLKINNKECAIYTN
HHHHCCCEEEEHHHC		50.0829967540
660PhosphorylationNNKECAIYTNRALCY
CCEEEEHHHCHHHHH		4.5728796482
661PhosphorylationNKECAIYTNRALCYL
CEEEEHHHCHHHHHH		16.4728796482
669MethylationNRALCYLKLCQFEEA
CHHHHHHHHHCHHHH		22.27-
692UbiquitinationQLADGNVKAFYRRAL
HHHCCCHHHHHHHHH		36.4629967540
705MethylationALAHKGLKNYQKSLI
HHHHHCHHHHHHHHH		63.3823644510
705"N6,N6-dimethyllysine"ALAHKGLKNYQKSLI
HHHHHCHHHHHHHHH		63.38-
709"N6,N6-dimethyllysine"KGLKNYQKSLIDLNK
HCHHHHHHHHHHHCC		36.55-
709MethylationKGLKNYQKSLIDLNK
HCHHHHHHHHHHHCC		36.5523644510
728UbiquitinationDPSIIEAKMELEEVT
CHHHHHHHHHHHHHH		21.8129967540
741UbiquitinationVTRLLNLKDKTAPFN
HHHHHCCCCCCCCCC		56.9829967540
744O-linked_GlycosylationLLNLKDKTAPFNKEK
HHCCCCCCCCCCHHH		50.0930379171
788PhosphorylationASEKGGKSSRSPEDP
ECCCCCCCCCCCCCH		33.9725627689
789PhosphorylationSEKGGKSSRSPEDPE
CCCCCCCCCCCCCHH		40.0225627689
791PhosphorylationKGGKSSRSPEDPEKL
CCCCCCCCCCCHHHC		34.2925159151
870PhosphorylationEKDPSLVYQHLLYLS
CCCHHHHHHHHHHHH		8.77-
875PhosphorylationLVYQHLLYLSKAERF
HHHHHHHHHHHHHHH		18.45-
887PhosphorylationERFKMMLTLISKGQK
HHHHHHHHHHHHHHH		12.2630622161
890PhosphorylationKMMLTLISKGQKELI
HHHHHHHHHHHHHHH		33.5730622161
921UbiquitinationLEDIQALKRQYEL--
HHHHHHHHHHHCC--		40.2329967540
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 SPAG1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPAG1_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 SPAG1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GBB1_HUMANGNB1physical
16368546
CL045_HUMANC12orf45physical
27173435
PR38A_HUMANPRPF38Aphysical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615505Ciliary dyskinesia, primary, 28 (CILD28)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPAG1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-347 AND SER-791, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of capacitated human sperm. Evidence oftyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation.";
Ficarro S., Chertihin O., Westbrook V.A., White F., Jayes F.,Kalab P., Marto J.A., Shabanowitz J., Herr J.C., Hunt D.F.,Visconti P.E.;
J. Biol. Chem. 278:11579-11589(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-177, AND MASSSPECTROMETRY.

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