Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Protein S100-A11  

UniProtKB / Swiss-Prot ID :  S10AB_HUMAN

Gene Name (Synonyms) : 
S100A11, MLN70, S100C  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. 

Protein Function :  Facilitates the differentiation and the cornification of keratinocytes. 

Protein Sequence MAKISSPTETERCIESLIAVFQKYAGKDGYNYTLSKTEFLSFMNTELAAFTKNQKDPGVLDRMMKKLDTN...
Predicted Secondary Structure CCCCCCHHHHHHHHHHHHHHHHHHHHHCCCCCCCCHHHHHHHHHHHHHHHCCCCCCHHHHHHHHHHHCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
3N6-acetyllysine--MAKISSP
--CCCCCCH
41.65HPRD
Link
3N6-acetyllysine--MAKISSP
--CCCCCCH
41.65Phosphositeplus
Link
3N6-acetyllysine.--MAKISSP
--CCCCCCH
41.65UniProtKB
Link
5PhosphoserineMAKISSPTE
CCCCCCHHH
29.56HPRD
Link
5PhosphoserineMAKISSPTE
CCCCCCHHH
29.56PhosphoELM
Link
5PhosphoserineMAKISSPTE
CCCCCCHHH
29.56Phosphositeplus
Link
6PhosphoserineAKISSPTET
CCCCCHHHH
39.04HPRD
Link
6PhosphoserineAKISSPTET
CCCCCHHHH
39.04PhosphoELM
Link
6PhosphoserineAKISSPTET
CCCCCHHHH
39.04Phosphositeplus
Link
6PhosphoserineAKISSPTET
CCCCCHHHH
39.04SysPTM
Link
6Phosphoserine.AKISSPTET
CCCCCHHHH
39.04UniProtKB
Link
10PhosphothreonineSPTETERCI
CHHHHHHHH
31.07HPRD
Link
10PhosphothreonineSPTETERCI
CHHHHHHHH
31.07PhosphoELM
Link
10PhosphothreonineSPTETERCI
CHHHHHHHH
31.07Phosphositeplus
Link
10Phosphothreonine.SPTETERCI
CHHHHHHHH
31.07UniProtKB
Link
13S-nitrosocysteineETERCIESL
HHHHHHHHH
3.09dbSNO
Link
13S-nitrosocysteineETERCIESL
HHHHHHHHH
3.09HPRD
Link
23Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AVFQKYAGK
HHHHHHHHH
26.13Phosphositeplus
Link-
24PhosphotyrosineVFQKYAGKD
HHHHHHHHC
15.14Phosphositeplus
Link-
27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KYAGKDGYN
HHHHHCCCC
39.55Phosphositeplus
Link-
30PhosphotyrosineGKDGYNYTL
HHCCCCCCC
18.35HPRD
Link-
30PhosphotyrosineGKDGYNYTL
HHCCCCCCC
18.35PhosphoELM
Link-
30PhosphotyrosineGKDGYNYTL
HHCCCCCCC
18.35Phosphositeplus
Link-
30Phosphotyrosine.GKDGYNYTL
HHCCCCCCC
18.35UniProtKB
Link-
32PhosphotyrosineDGYNYTLSK
CCCCCCCCH
10.69HPRD
Link-
32PhosphotyrosineDGYNYTLSK
CCCCCCCCH
10.69PhosphoELM
Link-
32PhosphotyrosineDGYNYTLSK
CCCCCCCCH
10.69Phosphositeplus
Link-
32Phosphotyrosine.DGYNYTLSK
CCCCCCCCH
10.69UniProtKB
Link-
55Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TKNQKDPGV
CCCCCCHHH
75.24Phosphositeplus
Link-
69PhosphothreonineKKLDTNSDG
HHHCCCCCC
47.24HPRD
Link-
69PhosphothreonineKKLDTNSDG
HHHCCCCCC
47.24SysPTM
Link-
71PhosphoserineLDTNSDGQL
HCCCCCCEE
45.25PhosphoELM
Link-
78PhosphoserineQLDFSEFLN
EECHHHHHH
27.40HPRD
Link-
78PhosphoserineQLDFSEFLN
EECHHHHHH
27.40SysPTM
Link-
94PhosphoserineACHDSFLKA
HHHHHHHHH
14.60HPRD
Link-
94PhosphoserineACHDSFLKA
HHHHHHHHH
14.60PhosphoELM
Link-
94PhosphoserineACHDSFLKA
HHHHHHHHH
14.60Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
S10AB_HUMANphysical interactionEBI-945567
intact10913138
ACTB_HUMANin vitro
in vivo
HPRD:04385HPRD14623863
10851017
ANXA1_HUMANin vitro
in vivo
HPRD:04385HPRD12645011
8557678
NUCL_HUMANin vitro
in vivo
HPRD:04385HPRD14623863
S100B_HUMANin vivo
yeast 2-hybrid
HPRD:04385HPRD10913138
S10AB_HUMANin vitroHPRD:04385HPRD10673436
ANXA1_HUMANENSP00000271638STRING
NUCL_HUMANENSP00000271638STRING
ANXA6_HUMANENSP00000271638STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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-3, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, 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-30 AND TYR-32, 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-6, AND MASSSPECTROMETRY.
"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-30, AND MASSSPECTROMETRY.
"The structure of S100A11 fragment explains a local structural changeinduced by phosphorylation.";
Kouno T., Mizuguchi M., Sakaguchi M., Makino E., Mori Y., Shinoda H.,Aizawa T., Demura M., Huh N.H., Kawano K.;
J. Pept. Sci. 14:1129-1138(2008).
Cited for: STRUCTURE BY NMR OF 1-19, DISULFIDE BOND, PHOSPHORYLATION AT THR-10,FUNCTION, AND SUBCELLULAR LOCATION.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures