S100P_HUMAN - dbPTM
S100P_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S100P_HUMAN
UniProt AC P25815
Protein Name Protein S100-P
Gene Name S100P
Organism Homo sapiens (Human).
Sequence Length 95
Subcellular Localization Nucleus. Cytoplasm. Cell projection, microvillus membrane. Colocalizes with S100PBP in the nucleus. Colocolizes with EZR in the microvilli in a calcium-dependent manner.
Protein Description May function as calcium sensor and contribute to cellular calcium signaling. In a calcium-dependent manner, functions by interacting with other proteins, such as EZR and PPP5C, and indirectly plays a role in physiological processes like the formation of microvilli in epithelial cells. May stimulate cell proliferation in an autocrine manner via activation of the receptor for activated glycation end products (RAGE)..
Protein Sequence MTELETAMGMIIDVFSRYSGSEGSTQTLTKGELKVLMEKELPGFLQSGKDKDAVDKLLKDLDANGDAQVDFSEFIVFVAAITSACHKYFEKAGLK
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
2Phosphorylation------MTELETAMG
------CCHHHHHHH
49.6421060948
6Phosphorylation--MTELETAMGMIID
--CCHHHHHHHHHHH
34.2725072903
16PhosphorylationGMIIDVFSRYSGSEG
HHHHHHHHHCCCCCC
30.1125072903
18PhosphorylationIIDVFSRYSGSEGST
HHHHHHHCCCCCCCC
19.0420068231
19PhosphorylationIDVFSRYSGSEGSTQ
HHHHHHCCCCCCCCE
34.4320068231
21PhosphorylationVFSRYSGSEGSTQTL
HHHHCCCCCCCCEEE
32.6126657352
24PhosphorylationRYSGSEGSTQTLTKG
HCCCCCCCCEEECHH
17.1925159151
25PhosphorylationYSGSEGSTQTLTKGE
CCCCCCCCEEECHHH
36.1128450419
27PhosphorylationGSEGSTQTLTKGELK
CCCCCCEEECHHHHH
36.1628450419
29PhosphorylationEGSTQTLTKGELKVL
CCCCEEECHHHHHHH
40.1520068231
30UbiquitinationGSTQTLTKGELKVLM
CCCEEECHHHHHHHH
54.2021963094
30AcetylationGSTQTLTKGELKVLM
CCCEEECHHHHHHHH
54.2026051181
34AcetylationTLTKGELKVLMEKEL
EECHHHHHHHHHCCC
29.0827452117
34UbiquitinationTLTKGELKVLMEKEL
EECHHHHHHHHHCCC
29.0822817900
39SuccinylationELKVLMEKELPGFLQ
HHHHHHHCCCCCHHH
51.0623954790
39AcetylationELKVLMEKELPGFLQ
HHHHHHHCCCCCHHH
51.0626051181
39UbiquitinationELKVLMEKELPGFLQ
HHHHHHHCCCCCHHH
51.0633845483
49UbiquitinationPGFLQSGKDKDAVDK
CCHHHCCCCHHHHHH
67.8429967540
49AcetylationPGFLQSGKDKDAVDK
CCHHHCCCCHHHHHH
67.8427452117
49SuccinylationPGFLQSGKDKDAVDK
CCHHHCCCCHHHHHH
67.8423954790
56UbiquitinationKDKDAVDKLLKDLDA
CCHHHHHHHHHHHCC
49.4729967540
91UbiquitinationACHKYFEKAGLK---
HHHHHHHHCCCC---
37.5433845483
91AcetylationACHKYFEKAGLK---
HHHHHHHHCCCC---
37.5427178108

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
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:23344957

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S100P_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 S100P_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
S100P_HUMANS100Pphysical
10924150
RAGE_HUMANAGERphysical
14617629
EZRI_HUMANEZRphysical
12808036
S100Z_HUMANS100Zphysical
11747429
S100P_HUMANS100Pphysical
1633809
S100P_HUMANS100Pphysical
12507480
SGT1_HUMANSUGT1physical
22939629
CHIP_HUMANSTUB1physical
23344957
TFP11_HUMANTFIP11physical
25416956

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
DB01003Cromoglicic acid
Regulatory Network of S100P_HUMAN

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Related Literatures of Post-Translational Modification

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