ANX11_HUMAN - dbPTM
ANX11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANX11_HUMAN
UniProt AC P50995
Protein Name Annexin A11
Gene Name ANXA11
Organism Homo sapiens (Human).
Sequence Length 505
Subcellular Localization Cytoplasm. Melanosome. Nucleus envelope. Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, spindle. Found throughout the nucleoplasm at interphase and during mitosis concentrates around the mitotic apparatus (By similarity). Elevation of intracellular c
Protein Description Binds specifically to calcyclin in a calcium-dependent manner (By similarity). Required for midbody formation and completion of the terminal phase of cytokinesis..
Protein Sequence MSYPGYPPPPGGYPPAAPGGGPWGGAAYPPPPSMPPIGLDNVATYAGQFNQDYLSGMAANMSGTFGGANMPNLYPGAPGAGYPPVPPGGFGQPPSAQQPVPPYGMYPPPGGNPPSRMPSYPPYPGAPVPGQPMPPPGQQPPGAYPGQPPVTYPGQPPVPLPGQQQPVPSYPGYPGSGTVTPAVPPTQFGSRGTITDAPGFDPLRDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSFKTAYGKDLIKDLKSELSGNFEKTILALMKTPVLFDIYEIKEAIKGVGTDEACLIEILASRSNEHIRELNRAYKAEFKKTLEEAIRSDTSGHFQRLLISLSQGNRDESTNVDMSLAQRDAQELYAAGENRLGTDESKFNAVLCSRSRAHLVAVFNEYQRMTGRDIEKSICREMSGDLEEGMLAVVKCLKNTPAFFAERLNKAMRGAGTKDRTLIRIMVSRSETDLLDIRSEYKRMYGKSLYHDISGDTSGDYRKILLKICGGND
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
53PhosphorylationAGQFNQDYLSGMAAN
HHHCCHHHHHHHCCC		7.9412312629
181UbiquitinationPGSGTVTPAVPPTQF
CCCCCCCCCCCCCCC		27.24-
214UbiquitinationEVLRKAMKGFGTDEQ
HHHHHHHCCCCCCHH		56.82-
215AcetylationVLRKAMKGFGTDEQA
HHHHHHCCCCCCHHH		17.09-
215UbiquitinationVLRKAMKGFGTDEQA
HHHHHHCCCCCCHHH		17.09-
215AcetylationVLRKAMKGFGTDEQA
HHHHHHCCCCCCHHH		17.0919608861
222AcetylationGFGTDEQAIIDCLGS
CCCCCHHHHHHHHCC		9.92-
222UbiquitinationGFGTDEQAIIDCLGS
CCCCCHHHHHHHHCC		9.92-
222AcetylationGFGTDEQAIIDCLGS
CCCCCHHHHHHHHCC		9.9219608861
231PhosphorylationIDCLGSRSNKQRQQI
HHHHCCCCHHHHHHH		50.5030622161
231UbiquitinationIDCLGSRSNKQRQQI
HHHHCCCCHHHHHHH		50.5021890473
238UbiquitinationSNKQRQQILLSFKTA
CHHHHHHHHHHHHHH		2.94-
241PhosphorylationQRQQILLSFKTAYGK
HHHHHHHHHHHHHCH		22.6624719451
243AcetylationQQILLSFKTAYGKDL
HHHHHHHHHHHCHHH		28.9525953088
248AcetylationSFKTAYGKDLIKDLK
HHHHHHCHHHHHHHH		36.3619608861
248UbiquitinationSFKTAYGKDLIKDLK
HHHHHHCHHHHHHHH		36.3619608861
2482-HydroxyisobutyrylationSFKTAYGKDLIKDLK
HHHHHHCHHHHHHHH		36.36-
248MalonylationSFKTAYGKDLIKDLK
HHHHHHCHHHHHHHH		36.3626320211
249UbiquitinationFKTAYGKDLIKDLKS
HHHHHCHHHHHHHHH		49.62-
252UbiquitinationAYGKDLIKDLKSELS
HHCHHHHHHHHHHHC		65.3921906983
2522-HydroxyisobutyrylationAYGKDLIKDLKSELS
HHCHHHHHHHHHHHC		65.39-
252MalonylationAYGKDLIKDLKSELS
HHCHHHHHHHHHHHC		65.3926320211
253UbiquitinationYGKDLIKDLKSELSG
HCHHHHHHHHHHHCC		52.95-
255AcetylationKDLIKDLKSELSGNF
HHHHHHHHHHHCCCH		52.6019608861
255SumoylationKDLIKDLKSELSGNF
HHHHHHHHHHHCCCH		52.60-
255SumoylationKDLIKDLKSELSGNF
HHHHHHHHHHHCCCH		52.6019608861
255UbiquitinationKDLIKDLKSELSGNF
HHHHHHHHHHHCCCH		52.6019608861
2552-HydroxyisobutyrylationKDLIKDLKSELSGNF
HHHHHHHHHHHCCCH		52.60-
255MalonylationKDLIKDLKSELSGNF
HHHHHHHHHHHCCCH		52.6026320211
259PhosphorylationKDLKSELSGNFEKTI
HHHHHHHCCCHHHHH		27.86113309987
264MethylationELSGNFEKTILALMK
HHCCCHHHHHHHHHC		36.41-
264UbiquitinationELSGNFEKTILALMK
HHCCCHHHHHHHHHC		36.4121890473
271UbiquitinationKTILALMKTPVLFDI
HHHHHHHCCCEEEEH		50.9921906983
272PhosphorylationTILALMKTPVLFDIY
HHHHHHCCCEEEEHH		12.5015995497
279PhosphorylationTPVLFDIYEIKEAIK
CCEEEEHHHHHHHHC		17.2875329
282AcetylationLFDIYEIKEAIKGVG
EEEHHHHHHHHCCCC		29.2023954790
282UbiquitinationLFDIYEIKEAIKGVG
EEEHHHHHHHHCCCC		29.202190698
282SumoylationLFDIYEIKEAIKGVG
EEEHHHHHHHHCCCC		29.20-
282UbiquitinationLFDIYEIKEAIKGVG
EEEHHHHHHHHCCCC		29.20-
286UbiquitinationYEIKEAIKGVGTDEA
HHHHHHHCCCCCCHH		55.37-
287UbiquitinationEIKEAIKGVGTDEAC
HHHHHHCCCCCCHHH		19.58-
290PhosphorylationEAIKGVGTDEACLIE
HHHCCCCCCHHHHHH		28.41310709053
294S-nitrosocysteineGVGTDEACLIEILAS
CCCCCHHHHHHHHHH		3.56-
294S-nitrosylationGVGTDEACLIEILAS
CCCCCHHHHHHHHHH		3.5622178444
301PhosphorylationCLIEILASRSNEHIR
HHHHHHHHCCHHHHH		32.5626699800
303PhosphorylationIEILASRSNEHIREL
HHHHHHCCHHHHHHH		44.0426699800
314PhosphorylationIRELNRAYKAEFKKT
HHHHHHHHHHHHHHH		13.9026074081
315UbiquitinationRELNRAYKAEFKKTL
HHHHHHHHHHHHHHH		40.22-
315MalonylationRELNRAYKAEFKKTL
HHHHHHHHHHHHHHH		40.2226320211
315AcetylationRELNRAYKAEFKKTL
HHHHHHHHHHHHHHH		40.2225953088
320UbiquitinationAYKAEFKKTLEEAIR
HHHHHHHHHHHHHHH		64.76-
320MalonylationAYKAEFKKTLEEAIR
HHHHHHHHHHHHHHH		64.7626320211
321PhosphorylationYKAEFKKTLEEAIRS
HHHHHHHHHHHHHHC		39.7436013345
340PhosphorylationHFQRLLISLSQGNRD
HHHHHHHHHHCCCCC		23.1826270265
342PhosphorylationQRLLISLSQGNRDES
HHHHHHHHCCCCCCC		29.2926270265
345UbiquitinationLISLSQGNRDESTNV
HHHHHCCCCCCCCCC		40.36-
346MethylationISLSQGNRDESTNVD
HHHHCCCCCCCCCCC		56.76-
352UbiquitinationNRDESTNVDMSLAQR
CCCCCCCCCHHHHHH		7.0921890473
354SulfoxidationDESTNVDMSLAQRDA
CCCCCCCHHHHHHHH		2.8521406390
364UbiquitinationAQRDAQELYAAGENR
HHHHHHHHHHHHCCC		2.0421890473
365PhosphorylationQRDAQELYAAGENRL
HHHHHHHHHHHCCCC		8.1520090780
371UbiquitinationLYAAGENRLGTDESK
HHHHHCCCCCCCHHH		30.1421890473
374PhosphorylationAGENRLGTDESKFNA
HHCCCCCCCHHHHHH		40.9829507054
375AcetylationGENRLGTDESKFNAV
HCCCCCCCHHHHHHH		57.27-
375UbiquitinationGENRLGTDESKFNAV
HCCCCCCCHHHHHHH		57.27-
377PhosphorylationNRLGTDESKFNAVLC
CCCCCCHHHHHHHHH		45.4129507054
378SumoylationRLGTDESKFNAVLCS
CCCCCHHHHHHHHHC		40.36-
378UbiquitinationRLGTDESKFNAVLCS
CCCCCHHHHHHHHHC		40.36-
378SumoylationRLGTDESKFNAVLCS
CCCCCHHHHHHHHHC		40.36-
378AcetylationRLGTDESKFNAVLCS
CCCCCHHHHHHHHHC		40.3625953088
382UbiquitinationDESKFNAVLCSRSRA
CHHHHHHHHHCCCCH		6.0921890473
384S-nitrosocysteineSKFNAVLCSRSRAHL
HHHHHHHHCCCCHHH		2.27-
384S-nitrosylationSKFNAVLCSRSRAHL
HHHHHHHHCCCCHHH		2.2719483679
394UbiquitinationSRAHLVAVFNEYQRM
CCHHHHHHHHHHHHH		4.06-
397UbiquitinationHLVAVFNEYQRMTGR
HHHHHHHHHHHHHCC		31.42-
398PhosphorylationLVAVFNEYQRMTGRD
HHHHHHHHHHHHCCC		11.5229209046
400MethylationAVFNEYQRMTGRDIE
HHHHHHHHHHCCCHH		24.59-
402PhosphorylationFNEYQRMTGRDIEKS
HHHHHHHHCCCHHHH		31.1129209046
408AcetylationMTGRDIEKSICREMS
HHCCCHHHHHHHHHC		45.5123749302
408UbiquitinationMTGRDIEKSICREMS
HHCCCHHHHHHHHHC		45.51-
4082-HydroxyisobutyrylationMTGRDIEKSICREMS
HHCCCHHHHHHHHHC		45.51-
414SulfoxidationEKSICREMSGDLEEG
HHHHHHHHCCCHHHH		2.5430846556
415PhosphorylationKSICREMSGDLEEGM
HHHHHHHCCCHHHHH		25.1320068231
422SulfoxidationSGDLEEGMLAVVKCL
CCCHHHHHHHHHHHH		2.1630846556
427UbiquitinationEGMLAVVKCLKNTPA
HHHHHHHHHHHCCHH		27.53-
428S-nitrosylationGMLAVVKCLKNTPAF
HHHHHHHHHHCCHHH		4.4024105792
430UbiquitinationLAVVKCLKNTPAFFA
HHHHHHHHCCHHHHH		69.14-
439MethylationTPAFFAERLNKAMRG
CHHHHHHHHHHHHCC		39.88-
446AcetylationRLNKAMRGAGTKDRT
HHHHHHCCCCCCCHH		18.44-
446UbiquitinationRLNKAMRGAGTKDRT
HHHHHHCCCCCCCHH		18.44-
446AcetylationRLNKAMRGAGTKDRT
HHHHHHCCCCCCCHH		18.4419608861
460PhosphorylationTLIRIMVSRSETDLL
HHEEEEECCCCCCHH		16.8322496350
462PhosphorylationIRIMVSRSETDLLDI
EEEEECCCCCCHHHH		37.0222496350
464PhosphorylationIMVSRSETDLLDIRS
EEECCCCCCHHHHHH		32.9420068231
466UbiquitinationVSRSETDLLDIRSEY
ECCCCCCHHHHHHHH		6.38-
470MethylationETDLLDIRSEYKRMY
CCCHHHHHHHHHHHH		24.09-
471PhosphorylationTDLLDIRSEYKRMYG
CCHHHHHHHHHHHHC		45.6820068231
473PhosphorylationLLDIRSEYKRMYGKS
HHHHHHHHHHHHCCC		12.7320068231
479AcetylationEYKRMYGKSLYHDIS
HHHHHHCCCCCCCCC		21.5719608861
479UbiquitinationEYKRMYGKSLYHDIS
HHHHHHCCCCCCCCC		21.5719608861
4792-HydroxyisobutyrylationEYKRMYGKSLYHDIS
HHHHHHCCCCCCCCC		21.57-
480PhosphorylationYKRMYGKSLYHDISG
HHHHHCCCCCCCCCC		29.7830804283
482PhosphorylationRMYGKSLYHDISGDT
HHHCCCCCCCCCCCC		12.4421082442
486PhosphorylationKSLYHDISGDTSGDY
CCCCCCCCCCCCCCH		36.3528152594
489PhosphorylationYHDISGDTSGDYRKI
CCCCCCCCCCCHHHH		37.8328152594
490PhosphorylationHDISGDTSGDYRKIL
CCCCCCCCCCHHHHH		34.1128152594
493PhosphorylationSGDTSGDYRKILLKI
CCCCCCCHHHHHHHH		19.8223403867
499SumoylationDYRKILLKICGGND-
CHHHHHHHHHCCCC-		32.29-
499UbiquitinationDYRKILLKICGGND-
CHHHHHHHHHCCCC-		32.29-
499SumoylationDYRKILLKICGGND-
CHHHHHHHHHCCCC-		32.29-
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 ANX11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANX11_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 ANX11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLS1_HUMANPLSCR1physical
16189514
PDCD6_HUMANPDCD6physical
11883939
ALG2_HUMANALG2physical
12445460
S10A6_HUMANS100A6physical
10037139
STXB2_HUMANSTXBP2physical
22939629
ANXA3_HUMANANXA3physical
22939629
RS21_HUMANRPS21physical
22939629
PDCD6_HUMANPDCD6physical
25416956
TFG_HUMANTFGphysical
25416956
CEP55_HUMANCEP55physical
25416956
ANXA2_HUMANANXA2physical
26344197
ASSY_HUMANASS1physical
26344197
CK054_HUMANC11orf54physical
26344197
CISD1_HUMANCISD1physical
26344197
LDHA_HUMANLDHAphysical
26344197
MIF_HUMANMIFphysical
26344197
NDUV1_HUMANNDUFV1physical
26344197
PCBP1_HUMANPCBP1physical
26344197
ODPA_HUMANPDHA1physical
26344197
PEF1_HUMANPEF1physical
26344197
PRDX2_HUMANPRDX2physical
26344197
RAC1_HUMANRAC1physical
26344197
STX12_HUMANSTX12physical
26344197
CYTM_HUMANCST6physical
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 ANX11_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-248; LYS-255 AND LYS-479,AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-482, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-365 AND TYR-482, ANDMASS SPECTROMETRY.

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