NALCN_HUMAN - dbPTM
NALCN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NALCN_HUMAN
UniProt AC Q8IZF0
Protein Name Sodium leak channel non-selective protein
Gene Name NALCN
Organism Homo sapiens (Human).
Sequence Length 1738
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Voltage-independent, cation-nonselective channel which is permeable to sodium, potassium and calcium ions. Regulates the resting membrane potential and controls neuronal excitability. [PubMed: 17448995 Neuropeptides such as neurotensin and substance P (SP) stimulate the firing of action potentials by activating NALCN through a SRC family kinases-dependent pathway. In addition to its baseline activity, NALCN activity is enhanced/modulated by several GPCRs. Required for normal respiratory rhythm and neonatal survival. Involved in systemic osmoregulation by controlling the serum sodium concentration. NALCN is partly responsible for the substance P-induced depolarization and regulation of the intestinal pace-making activity in the interstitial cells of Cajal. Plays a critical role in both maintenance of spontaneous firing of substantia nigra pars reticulata (SNr) neurons and physiological modulation of SNr neuron excitability (By similarity]
Protein Sequence MLKRKQSSRVEAQPVTDFGPDESLSDNADILWINKPWVHSLLRICAIISVISVCMNTPMTFEHYPPLQYVTFTLDTLLMFLYTAEMIAKMHIRGIVKGDSSYVKDRWCVFDGFMVFCLWVSLVLQVFEIADIVDQMSPWGMLRIPRPLIMIRAFRIYFRFELPRTRITNILKRSGEQIWSVSIFLLFFLLLYGILGVQMFGTFTYHCVVNDTKPGNVTWNSLAIPDTHCSPELEEGYQCPPGFKCMDLEDLGLSRQELGYSGFNEIGTSIFTVYEAASQEGWVFLMYRAIDSFPRWRSYFYFITLIFFLAWLVKNVFIAVIIETFAEIRVQFQQMWGSRSSTTSTATTQMFHEDAAGGWQLVAVDVNKPQGRAPACLQKMMRSSVFHMFILSMVTVDVIVAASNYYKGENFRRQYDEFYLAEVAFTVLFDLEALLKIWCLGFTGYISSSLHKFELLLVIGTTLHVYPDLYHSQFTYFQVLRVVRLIKISPALEDFVYKIFGPGKKLGSLVVFTASLLIVMSAISLQMFCFVEELDRFTTFPRAFMSMFQILTQEGWVDVMDQTLNAVGHMWAPVVAIYFILYHLFATLILLSLFVAVILDNLELDEDLKKLKQLKQSEANADTKEKLPLRLRIFEKFPNRPQMVKISKLPSDFTVPKIRESFMKQFIDRQQQDTCCLLRSLPTTSSSSCDHSKRSAIEDNKYIDQKLRKSVFSIRARNLLEKETAVTKILRACTRQRMLSGSFEGQPAKERSILSVQHHIRQERRSLRHGSNSQRISRGKSLETLTQDHSNTVRYRNAQREDSEIKMIQEKKEQAEMKRKVQEEELRENHPYFDKPLFIVGREHRFRNFCRVVVRARFNASKTDPVTGAVKNTKYHQLYDLLGLVTYLDWVMIIVTICSCISMMFESPFRRVMHAPTLQIAEYVFVIFMSIELNLKIMADGLFFTPTAVIRDFGGVMDIFIYLVSLIFLCWMPQNVPAESGAQLLMVLRCLRPLRIFKLVPQMRKVVRELFSGFKEIFLVSILLLTLMLVFASFGVQLFAGKLAKCNDPNIIRREDCNGIFRINVSVSKNLNLKLRPGEKKPGFWVPRVWANPRNFNFDNVGNAMLALFEVLSLKGWVEVRDVIIHRVGPIHGIYIHVFVFLGCMIGLTLFVGVVIANFNENKGTALLTVDQRRWEDLKSRLKIAQPLHLPPRPDNDGFRAKMYDITQHPFFKRTIALLVLAQSVLLSVKWDVEDPVTVPLATMSVVFTFIFVLEVTMKIIAMSPAGFWQSRRNRYDLLVTSLGVVWVVLHFALLNAYTYMMGACVIVFRFFSICGKHVTLKMLLLTVVVSMYKSFFIIVGMFLLLLCYAFAGVVLFGTVKYGENINRHANFSSAGKAITVLFRIVTGEDWNKIMHDCMVQPPFCTPDEFTYWATDCGNYAGALMYFCSFYVIIAYIMLNLLVAIIVENFSLFYSTEEDQLLSYNDLRHFQIIWNMVDDKREGVIPTFRVKFLLRLLRGRLEVDLDKDKLLFKHMCYEMERLHNGGDVTFHDVLSMLSYRSVDIRKSLQLEELLAREQLEYTIEEEVAKQTIRMWLKKCLKRIRAKQQQSCSIIHSLRESQQQELSRFLNPPSIETTQPSEDTNANSQDNSMQPETSSQQQLLSPTLSDRGGSRQDAADAGKPQRKFGQWRLPSAPKPISHSVSSVNLRFGGRTTMKSVVCKMNPMTDAASCGSEVKKWWTRQLTVESDESGDDLLDI
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
40PhosphorylationINKPWVHSLLRICAI
ECCHHHHHHHHHHHH
21.3424719451
165PhosphorylationFRFELPRTRITNILK
EEECCCCCHHHHHHH
25.20-
489PhosphorylationVVRLIKISPALEDFV
HHHHHCCCHHHHHHH
10.10-
497PhosphorylationPALEDFVYKIFGPGK
HHHHHHHHHHHCCCC
9.8122817900
623PhosphorylationQSEANADTKEKLPLR
HHHCCCCCCCCCCHH
38.40-
651PhosphorylationVKISKLPSDFTVPKI
EEEECCCCCCCHHHH
56.65-
740PhosphorylationCTRQRMLSGSFEGQP
HHHHHHHCCCCCCCC
24.0523663014
742PhosphorylationRQRMLSGSFEGQPAK
HHHHHCCCCCCCCCH
19.4223663014
795PhosphorylationDHSNTVRYRNAQRED
CCCCHHHHHHCCCCC
12.1328152594
803PhosphorylationRNAQREDSEIKMIQE
HHCCCCCHHHHHHHH
36.1530619164
886PhosphorylationYDLLGLVTYLDWVMI
HHHHHHHHHHHHHHH
24.3323401153
902PhosphorylationVTICSCISMMFESPF
HHHHHHHHHHHCCCH
14.4423401153
907PhosphorylationCISMMFESPFRRVMH
HHHHHHCCCHHHHHC
20.3423401153
917PhosphorylationRRVMHAPTLQIAEYV
HHHHCCCHHHHHHHH
31.8821403953
923PhosphorylationPTLQIAEYVFVIFMS
CHHHHHHHHHHHHHH
7.0821403953
962PhosphorylationGVMDIFIYLVSLIFL
HHHHHHHHHHHHHHH
7.1223401153
965PhosphorylationDIFIYLVSLIFLCWM
HHHHHHHHHHHHHHC
17.1023401153
980PhosphorylationPQNVPAESGAQLLMV
CCCCCCCCHHHHHHH
41.3523401153
1066PhosphorylationGIFRINVSVSKNLNL
CEEEEEEEEECCCCC
19.04-
1068PhosphorylationFRINVSVSKNLNLKL
EEEEEEEECCCCCEE
14.34-
1069AcetylationRINVSVSKNLNLKLR
EEEEEEECCCCCEEC
64.4020167786
1113PhosphorylationLALFEVLSLKGWVEV
HHHHHHHHCCCCEEE
32.9624719451
1169PhosphorylationNKGTALLTVDQRRWE
CCCEEEEEECHHHHH
23.9222210691
1228PhosphorylationLAQSVLLSVKWDVED
HHHHHHHHCCCCCCC
19.9324719451
1298PhosphorylationHFALLNAYTYMMGAC
HHHHHHHHHHHHHHH
9.42-
1327PhosphorylationTLKMLLLTVVVSMYK
HHHHHHHHHHHHHHH
15.9526270265
1331PhosphorylationLLLTVVVSMYKSFFI
HHHHHHHHHHHHHHH
12.5626270265
1333PhosphorylationLTVVVSMYKSFFIIV
HHHHHHHHHHHHHHH
8.9326270265
1362PhosphorylationVLFGTVKYGENINRH
HHHCCCCCCCCCCCC
25.9024927040
1571PhosphorylationEEEVAKQTIRMWLKK
HHHHHHHHHHHHHHH
15.1627422710
1590PhosphorylationIRAKQQQSCSIIHSL
HHHHHHHHHHHHHHH
12.9024114839
1596PhosphorylationQSCSIIHSLRESQQQ
HHHHHHHHHHHHHHH
20.7924719451
1600PhosphorylationIIHSLRESQQQELSR
HHHHHHHHHHHHHHH
27.1922210691
1680PhosphorylationPSAPKPISHSVSSVN
CCCCCCCCCCCCEEE
20.4529507054
1682PhosphorylationAPKPISHSVSSVNLR
CCCCCCCCCCEEEEE
19.5329507054
1684PhosphorylationKPISHSVSSVNLRFG
CCCCCCCCEEEEEEC
31.4229507054
1685PhosphorylationPISHSVSSVNLRFGG
CCCCCCCEEEEEECC
16.9329507054

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 NALCN_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NALCN_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 NALCN_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSD11_HUMANPSMD11physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615419Hypotonia, infantile, with psychomotor retardation and characteristic facies (IHPRF)
616266Congenital contractures of the limbs and face, hypotonia, and developmental delay (CLIFAHDD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NALCN_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-497, AND MASSSPECTROMETRY.

TOP