S10A4_HUMAN - dbPTM
S10A4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S10A4_HUMAN
UniProt AC P26447
Protein Name Protein S100-A4
Gene Name S100A4
Organism Homo sapiens (Human).
Sequence Length 101
Subcellular Localization
Protein Description
Protein Sequence MACPLEKALDVMVSTFHKYSGKEGDKFKLNKSELKELLTRELPSFLGKRTDEAAFQKLMSNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGFPDKQPRKK
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
2Acetylation------MACPLEKAL
------CCCCHHHHH
12.02-
7Acetylation-MACPLEKALDVMVS
-CCCCHHHHHHHHHH
63.0319608861
7Ubiquitination-MACPLEKALDVMVS
-CCCCHHHHHHHHHH
63.0333845483
72-Hydroxyisobutyrylation-MACPLEKALDVMVS
-CCCCHHHHHHHHHH
63.03-
12SulfoxidationLEKALDVMVSTFHKY
HHHHHHHHHHHHHHH
1.6530846556
14PhosphorylationKALDVMVSTFHKYSG
HHHHHHHHHHHHHCC
13.7828348404
15PhosphorylationALDVMVSTFHKYSGK
HHHHHHHHHHHHCCC
20.5328348404
18UbiquitinationVMVSTFHKYSGKEGD
HHHHHHHHHCCCCCC
36.6033845483
182-HydroxyisobutyrylationVMVSTFHKYSGKEGD
HHHHHHHHHCCCCCC
36.60-
18AcetylationVMVSTFHKYSGKEGD
HHHHHHHHHCCCCCC
36.6023954790
22AcetylationTFHKYSGKEGDKFKL
HHHHHCCCCCCCCCC
53.2126051181
222-HydroxyisobutyrylationTFHKYSGKEGDKFKL
HHHHHCCCCCCCCCC
53.21-
22UbiquitinationTFHKYSGKEGDKFKL
HHHHHCCCCCCCCCC
53.2133845483
22SumoylationTFHKYSGKEGDKFKL
HHHHHCCCCCCCCCC
53.21-
22SumoylationTFHKYSGKEGDKFKL
HHHHHCCCCCCCCCC
53.21-
26AcetylationYSGKEGDKFKLNKSE
HCCCCCCCCCCCHHH
56.0826051181
28SumoylationGKEGDKFKLNKSELK
CCCCCCCCCCHHHHH
57.82-
31SuccinylationGDKFKLNKSELKELL
CCCCCCCHHHHHHHH
56.6023954790
31SumoylationGDKFKLNKSELKELL
CCCCCCCHHHHHHHH
56.60-
31AcetylationGDKFKLNKSELKELL
CCCCCCCHHHHHHHH
56.6025825284
31SumoylationGDKFKLNKSELKELL
CCCCCCCHHHHHHHH
56.60-
31UbiquitinationGDKFKLNKSELKELL
CCCCCCCHHHHHHHH
56.6022817900
32PhosphorylationDKFKLNKSELKELLT
CCCCCCHHHHHHHHH
47.2720068231
35AcetylationKLNKSELKELLTREL
CCCHHHHHHHHHHHC
42.1119608861
35UbiquitinationKLNKSELKELLTREL
CCCHHHHHHHHHHHC
42.1121906983
44PhosphorylationLLTRELPSFLGKRTD
HHHHHCHHHHCCCCC
45.8121712546
48AcetylationELPSFLGKRTDEAAF
HCHHHHCCCCCHHHH
55.0326051181
48SuccinylationELPSFLGKRTDEAAF
HCHHHHCCCCCHHHH
55.0323954790
482-HydroxyisobutyrylationELPSFLGKRTDEAAF
HCHHHHCCCCCHHHH
55.03-
48UbiquitinationELPSFLGKRTDEAAF
HCHHHHCCCCCHHHH
55.0321963094
57AcetylationTDEAAFQKLMSNLDS
CCHHHHHHHHHCCCC
39.4426051181
57UbiquitinationTDEAAFQKLMSNLDS
CCHHHHHHHHHCCCC
39.4421906983
59SulfoxidationEAAFQKLMSNLDSNR
HHHHHHHHHCCCCCC
3.0030846556
60PhosphorylationAAFQKLMSNLDSNRD
HHHHHHHHCCCCCCC
44.6824850871
64PhosphorylationKLMSNLDSNRDNEVD
HHHHCCCCCCCCCCC
36.6121815630
84SulfoxidationVFLSCIAMMCNEFFE
HHHHHHHHHHHHHHC
1.2730846556
85SulfoxidationFLSCIAMMCNEFFEG
HHHHHHHHHHHHHCC
1.3230846556
96UbiquitinationFFEGFPDKQPRKK--
HHCCCCCCCCCCC--
63.54-
96SumoylationFFEGFPDKQPRKK--
HHCCCCCCCCCCC--
63.54-
96SumoylationFFEGFPDKQPRKK--
HHCCCCCCCCCCC--
63.54-

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 S10A4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S10A4_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 S10A4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BAG6_HUMANBAG6physical
16169070
U119A_HUMANUNC119physical
16169070
P53_HUMANTP53physical
11527429
LIPB1_HUMANPPFIBP1physical
11836260
S10A1_HUMANS100A1physical
10753920
SMAD3_HUMANSMAD3physical
20070253
SMAD2_HUMANSMAD2physical
20070253
P53_HUMANTP53physical
20070253
TM1L2_HUMANTOM1L2physical
22939629
UNK_HUMANUNKphysical
22939629
SGT1_HUMANSUGT1physical
22939629
SBP1_HUMANSELENBP1physical
22939629
S100B_HUMANS100Bphysical
25416956
S100B_HUMANS100Bphysical
21516116
XIAP_HUMANXIAPphysical
26496610
NPAT_HUMANNPATphysical
26496610
S10A6_HUMANS100A6physical
26496610
SUV91_HUMANSUV39H1physical
26496610
DYL1_HUMANDYNLL1physical
26496610
DNJA3_HUMANDNAJA3physical
26496610
DNJB6_HUMANDNAJB6physical
26496610
RPP29_HUMANPOP4physical
26496610
CNTRL_HUMANCNTRLphysical
26496610
KAT7_HUMANKAT7physical
26496610
WDFY3_HUMANWDFY3physical
26496610
SYNE2_HUMANSYNE2physical
26496610
BRD1_HUMANBRD1physical
26496610
QCR9_HUMANUQCR10physical
26496610
BBX_HUMANBBXphysical
26496610
CORO7_HUMANCORO7physical
26496610
PTGR2_HUMANPTGR2physical
26496610
ESCO2_HUMANESCO2physical
26496610

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
DB00831Trifluoperazine
Regulatory Network of S10A4_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-7 AND LYS-35, AND MASSSPECTROMETRY.

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