CSEN_HUMAN - dbPTM
CSEN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSEN_HUMAN
UniProt AC Q9Y2W7
Protein Name Calsenilin
Gene Name KCNIP3
Organism Homo sapiens (Human).
Sequence Length 256
Subcellular Localization Cytoplasm . Cell membrane
Lipid-anchor. Endoplasmic reticulum . Golgi apparatus . Nucleus . Also membrane-bound, associated with the plasma membrane (PubMed:15485870). In the presence of PSEN2 associated with the endoplasmic reticulum and Golgi. Th
Protein Description Calcium-dependent transcriptional repressor that binds to the DRE element of genes including PDYN and FOS. Affinity for DNA is reduced upon binding to calcium and enhanced by binding to magnesium. Seems to be involved in nociception (By similarity).; Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels, such as KCND2/Kv4.2 and KCND3/Kv4.3. Modulates channel expression at the cell membrane, gating characteristics, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner.; May play a role in the regulation of PSEN2 proteolytic processing and apoptosis. Together with PSEN2 involved in modulation of amyloid-beta formation..
Protein Sequence MQPAKEVTKASDGSLLGDLGHTPLSKKEGIKWQRPRLSRQALMRCCLVKWILSSTAPQGSDSSDSELELSTVRHQPEGLDQLQAQTKFTKKELQSLYRGFKNECPTGLVDEDTFKLIYAQFFPQGDATTYAHFLFNAFDADGNGAIHFEDFVVGLSILLRGTVHEKLKWAFNLYDINKDGYITKEEMLAIMKSIYDMMGRHTYPILREDAPAEHVERFFEKMDRNQDGVVTIEEFLEACQKDENIMSSMQLFENVI
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
8PhosphorylationMQPAKEVTKASDGSL
CCCCHHCCCCCCCCC
23.2222115753
11PhosphorylationAKEVTKASDGSLLGD
CHHCCCCCCCCCCCC
44.0222115753
14PhosphorylationVTKASDGSLLGDLGH
CCCCCCCCCCCCCCC
25.9722115753
22PhosphorylationLLGDLGHTPLSKKEG
CCCCCCCCCCCHHCC
24.9126091039
25PhosphorylationDLGHTPLSKKEGIKW
CCCCCCCCHHCCCCC
42.7722115753
26SumoylationLGHTPLSKKEGIKWQ
CCCCCCCHHCCCCCC
63.63-
26SumoylationLGHTPLSKKEGIKWQ
CCCCCCCHHCCCCCC
63.6321070824
45S-palmitoylationSRQALMRCCLVKWIL
HHHHHHHHHHHHHHH
1.00-
46S-palmitoylationRQALMRCCLVKWILS
HHHHHHHHHHHHHHH
3.27-
60PhosphorylationSSTAPQGSDSSDSEL
HCCCCCCCCCCCCCE
29.13-
63PhosphorylationAPQGSDSSDSELELS
CCCCCCCCCCCEEHH
50.5816112838
86PhosphorylationLDQLQAQTKFTKKEL
HHHHHHHCCCCHHHH
31.0129083192
89PhosphorylationLQAQTKFTKKELQSL
HHHHCCCCHHHHHHH
42.6429083192
90SumoylationQAQTKFTKKELQSLY
HHHCCCCHHHHHHHH
47.5921070824
90SumoylationQAQTKFTKKELQSLY
HHHCCCCHHHHHHHH
47.59-
95PhosphorylationFTKKELQSLYRGFKN
CCHHHHHHHHHHHCC
39.7417102134
156PhosphorylationEDFVVGLSILLRGTV
HHHHHHHHHHHHCCH
12.7824719451
174PhosphorylationLKWAFNLYDINKDGY
HHHHHHHCCCCCCCC
18.84-
241SumoylationEFLEACQKDENIMSS
HHHHHHHCCCCHHHH
67.88-

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
63SPhosphorylationKinaseCSNK1A1P48729
GPS
63SPhosphorylationKinaseCK1-FAMILY-GPS
63SPhosphorylationKinaseCK1-Uniprot
95SPhosphorylationKinaseGRK2P25098
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
63SPhosphorylation

12837631

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 CSEN_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD177_HUMANCD177physical
16189514
PSN2_HUMANPSEN2physical
9771752
PSN1_HUMANPSEN1physical
9771752
CREM_HUMANCREMphysical
11094064
PSN1_HUMANPSEN1physical
10854253
CREB1_HUMANCREB1physical
12198160
PHS2_HUMANPCBD2physical
20211142
UBC9_HUMANUBE2Iphysical
21070824
GRK6_HUMANGRK6physical
17102134
ARBK1_HUMANADRBK1physical
17102134
CSEN_HUMANKCNIP3physical
17102134
CLN3_HUMANCLN3physical
17189291
KCND2_HUMANKCND2physical
23692269
CD177_HUMANCD177physical
25416956
MAVS_HUMANMAVSphysical
25416956
CTBP1_HUMANCTBP1physical
16787403
CTBP2_HUMANCTBP2physical
16787403

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 CSEN_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphorylation of calsenilin at Ser63 regulates its cleavage bycaspase-3.";
Choi E.K., Miller J.S., Zaidi N.F., Salih E., Buxbaum J.D., Wasco W.;
Mol. Cell. Neurosci. 23:495-506(2003).
Cited for: PHOSPHORYLATION AT SER-63.

TOP