KCC1D_HUMAN - dbPTM
KCC1D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCC1D_HUMAN
UniProt AC Q8IU85
Protein Name Calcium/calmodulin-dependent protein kinase type 1D
Gene Name CAMK1D
Organism Homo sapiens (Human).
Sequence Length 385
Subcellular Localization Cytoplasm . Nucleus . Predominantly cytoplasmic. Nuclear localization increases upon activation by KCl treatment in hippocampal neurons.
Protein Description Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, activates CREB-dependent gene transcription, regulates calcium-mediated granulocyte function and respiratory burst and promotes basal dendritic growth of hippocampal neurons. In neutrophil cells, required for cytokine-induced proliferative responses and activation of the respiratory burst. Activates the transcription factor CREB1 in hippocampal neuron nuclei. May play a role in apoptosis of erythroleukemia cells. In vitro, phosphorylates transcription factor CREM isoform Beta..
Protein Sequence MARENGESSSSWKKQAEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWIAGDTALNKNIHESVSAQIRKNFAKSKWRQAFNATAVVRHMRKLHLGSSLDSSNASVSSSLSLASQKDCLAPSTLCSFISSSSGVSGVGAERRPRPTTVTAVHSGSK
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
8PhosphorylationMARENGESSSSWKKQ
CCCCCCCCCHHHHHH		36.60-
43UbiquitinationEVVLAEEKATGKLFA
EEEEEEHHHCCCEEE		42.63-
52UbiquitinationTGKLFAVKCIPKKAL
CCCEEEEEEECHHHH		24.02-
62UbiquitinationPKKALKGKESSIENE
CHHHHCCCCCCHHHH		53.49-
64PhosphorylationKALKGKESSIENEIA
HHHCCCCCCHHHHHH		39.8528122231
65PhosphorylationALKGKESSIENEIAV
HHCCCCCCHHHHHHH		34.7124076635
113SumoylationLFDRIVEKGFYTEKD
HHHHHHHCCCCCHHH		43.3525218447
113SumoylationLFDRIVEKGFYTEKD
HHHHHHHCCCCCHHH		43.35-
122PhosphorylationFYTEKDASTLIRQVL
CCCHHHHHHHHHHHH		33.6018669648
123PhosphorylationYTEKDASTLIRQVLD
CCHHHHHHHHHHHHH		28.1129083192
152PhosphorylationLKPENLLYYSQDEES
CCHHHCEEECCCCCC		12.3027642862
153PhosphorylationKPENLLYYSQDEESK
CHHHCEEECCCCCCC		10.3823312004
154PhosphorylationPENLLYYSQDEESKI
HHHCEEECCCCCCCE		20.0023312004
159PhosphorylationYYSQDEESKIMISDF
EECCCCCCCEEEEHH		25.9923312004
174AcetylationGLSKMEGKGDVMSTA
CCCCCCCCCCHHCCC		38.337678613
179PhosphorylationEGKGDVMSTACGTPG
CCCCCHHCCCCCCCC		16.8323401153
180PhosphorylationGKGDVMSTACGTPGY
CCCCHHCCCCCCCCC		14.1023401153
184PhosphorylationVMSTACGTPGYVAPE
HHCCCCCCCCCCCHH		17.2725627689
187PhosphorylationTACGTPGYVAPEVLA
CCCCCCCCCCHHHHC		8.4723312004
196UbiquitinationAPEVLAQKPYSKAVD
CHHHHCCCCCCCHHH		40.07-
196AcetylationAPEVLAQKPYSKAVD
CHHHHCCCCCCCHHH		40.077678625
238PhosphorylationEQILKAEYEFDSPYW
HHHHHHHCCCCCCCC		27.1021951684
262AcetylationFIRNLMEKDPNKRYT
HHHHHHHHCCCCCCC		65.607462123
268PhosphorylationEKDPNKRYTCEQAAR
HHCCCCCCCHHHHHH		19.8328176443
269PhosphorylationKDPNKRYTCEQAARH
HCCCCCCCHHHHHHC		17.3828176443
287UbiquitinationAGDTALNKNIHESVS
CCCHHHCCCHHHHHH		59.12-
292PhosphorylationLNKNIHESVSAQIRK
HCCCHHHHHHHHHHH		13.7522210691
294PhosphorylationKNIHESVSAQIRKNF
CCHHHHHHHHHHHHH		24.6022210691
313PhosphorylationWRQAFNATAVVRHMR
HHHHHHHHHHHHHHH		22.5328857561
326PhosphorylationMRKLHLGSSLDSSNA
HHHHCCCCCCCCCCC		33.8025159151
327PhosphorylationRKLHLGSSLDSSNAS
HHHCCCCCCCCCCCC		34.1025159151
331PhosphorylationLGSSLDSSNASVSSS
CCCCCCCCCCCHHHH		35.7625307156
338PhosphorylationSNASVSSSLSLASQK
CCCCHHHHHHHHHCC		17.9322817900
349 (in isoform 2)Phosphorylation-11.4326552605
352O-linked_GlycosylationKDCLAPSTLCSFISS
CCCCCHHHHHHHHHH		30.6323301498
355 (in isoform 2)Phosphorylation-28.8221712546
355PhosphorylationLAPSTLCSFISSSSG
CCHHHHHHHHHHCCC		28.8228348404
357 (in isoform 2)Phosphorylation-1.9328674419
358PhosphorylationSTLCSFISSSSGVSG
HHHHHHHHHCCCCCC		23.3528348404
375PhosphorylationAERRPRPTTVTAVHS
CCCCCCCCEEEEEEC		34.8723312004
376PhosphorylationERRPRPTTVTAVHSG
CCCCCCCEEEEEECC		20.6727732954
378PhosphorylationRPRPTTVTAVHSGSK
CCCCCEEEEEECCCC		22.3727732954
382PhosphorylationTTVTAVHSGSK----
CEEEEEECCCC----		37.8627732954
384PhosphorylationVTAVHSGSK------
EEEEECCCC------		37.9029214152
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
180TPhosphorylationKinaseKKCC1Q8N5S9
PhosphoELM
180TPhosphorylationKinaseCAMKK2Q96RR4
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCC1D_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 KCC1D_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
TNF13_HUMANTNFSF13physical
21988832
MPIP1_HUMANCDC25Aphysical
21988832
CUL3_HUMANCUL3physical
21988832
GMFG_HUMANGMFGphysical
21988832
DCPS_HUMANDCPSphysical
22863883
HS71L_HUMANHSPA1Lphysical
22863883
ULA1_HUMANNAE1physical
22863883
NUCB2_HUMANNUCB2physical
22863883
PCY2_HUMANPCYT2physical
22863883
TBB6_HUMANTUBB6physical
22863883
EFTU_HUMANTUFMphysical
22863883
UBA3_HUMANUBA3physical
22863883
XPO1_HUMANXPO1physical
22863883
KCC1A_HUMANCAMK1physical
26186194
KCC1G_HUMANCAMK1Gphysical
26186194
ZG16B_HUMANZG16Bphysical
26186194
QPCTL_HUMANQPCTLphysical
26186194
MUC7_HUMANMUC7physical
26186194
CKS2_HUMANCKS2physical
26186194
CYTS_HUMANCST4physical
26186194
XYLT2_HUMANXYLT2physical
26186194
KCC1A_HUMANCAMK1physical
28514442
KCC1G_HUMANCAMK1Gphysical
28514442
MUC7_HUMANMUC7physical
28514442
CKS2_HUMANCKS2physical
28514442
CYTN_HUMANCST1physical
28514442
ZG16B_HUMANZG16Bphysical
28514442
QPCTL_HUMANQPCTLphysical
28514442
XYLT2_HUMANXYLT2physical
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 KCC1D_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-122 AND THR-180, ANDMASS SPECTROMETRY.
"Identification and characterization of novel components of aCa2+/calmodulin-dependent protein kinase cascade in HeLa cells.";
Ishikawa Y., Tokumitsu H., Inuzuka H., Murata-Hori M., Hosoya H.,Kobayashi R.;
FEBS Lett. 550:57-63(2003).
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1), CATALYTIC ACTIVITY, ENZYMEREGULATION, PHOSPHORYLATION AT THR-180, PHOSPHORYLATION BY CAMKK1 ANDCAMKK2, MUTAGENESIS OF THR-180, AND TISSUE SPECIFICITY.

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