SCLT1_HUMAN - dbPTM
SCLT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCLT1_HUMAN
UniProt AC Q96NL6
Protein Name Sodium channel and clathrin linker 1
Gene Name SCLT1
Organism Homo sapiens (Human).
Sequence Length 688
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Localizes to the distal appendage region of the centriole, which anchors the mother centriole to the plasma membrane.
Protein Description Adapter protein that links SCN10A to clathrin. Regulates SCN10A channel activity, possibly by promoting channel internalization (By similarity)..
Protein Sequence MAAEIDFLREQNRRLNEDFRRYQMESFSKYSSVQKAVCQGEGDDTFENLVFDQSFLAPLVTEYDKHLGELNGQLKYYQKQVGEMKLQLENVIKENERLHSELKDAVEKKLEAFPLGTEVGTDIYADDETVRNLQEQLQLANQEKTQAVELWQTVSQELDRLHKLYQEHMTEAQIHVFESQKQKDQLFDFQQLTKQLHVTNENMEVTNQQFLKTVTEQSVIIEQLRKKLRQAKLELRVAVAKVEELTNVTEDLQGQMKKKEKDVVSAHGREEASDRRLQQLQSSIKQLEIRLCVTIQEANQLRTENTHLEKQTRELQAKCNELENERYEAIVRARNSMQLLEEANLQKSQALLEEKQKEEDIEKMKETVSRFVQDATIRTKKEVANTKKQCNIQISRLTEELSALQMECAEKQGQIERVIKEKKAVEEELEKIYREGRGNESDYRKLEEMHQRFLVSERSKDDLQLRLTRAENRIKQLETDSSEEISRYQEMIQKLQNVLESERENCGLVSEQRLKLQQENKQLRKETESLRKIALEAQKKAKVKISTMEHEFSIKERGFEVQLREMEDSNRNSIVELRHLLATQQKAANRWKEETKKLTESAEIRINNLKSELSRQKLHTQELLSQLEMANEKVAENEKLILEHQEKANRLQRRLSQAEERAASASQQLSVITVQRRKAASLMNLENI
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------MAAEIDFLR
------CHHHHHHHH
17.5022814378
22PhosphorylationLNEDFRRYQMESFSK
HCHHHHHHHHHHHHC
14.1429759185
26PhosphorylationFRRYQMESFSKYSSV
HHHHHHHHHHCCCHH
29.4924719451
28PhosphorylationRYQMESFSKYSSVQK
HHHHHHHHCCCHHHH
39.7123532336
29UbiquitinationYQMESFSKYSSVQKA
HHHHHHHCCCHHHHH
47.33-
75UbiquitinationGELNGQLKYYQKQVG
HHHHHHHHHHHHHHC
33.74-
79UbiquitinationGQLKYYQKQVGEMKL
HHHHHHHHHHCCHHH
30.72-
93UbiquitinationLQLENVIKENERLHS
HHHHHHHHHHHHHHH
50.64-
109UbiquitinationLKDAVEKKLEAFPLG
HHHHHHHHHHHCCCC
37.75-
183UbiquitinationVFESQKQKDQLFDFQ
HHHCHHHHHHCCCHH
55.25-
261AcetylationGQMKKKEKDVVSAHG
HHHHHHHHCHHHHCC
65.787711431
265PhosphorylationKKEKDVVSAHGREEA
HHHHCHHHHCCCHHH
17.88-
294PhosphorylationLEIRLCVTIQEANQL
HHHHHHHHHHHHHHH
18.8827174698
303PhosphorylationQEANQLRTENTHLEK
HHHHHHHCCCHHHHH
42.0327174698
306PhosphorylationNQLRTENTHLEKQTR
HHHHCCCHHHHHHHH
22.9327174698
312PhosphorylationNTHLEKQTRELQAKC
CHHHHHHHHHHHHHH
36.8627174698
336PhosphorylationAIVRARNSMQLLEEA
HHHHHHHHHHHHHHH
11.4428555341
347UbiquitinationLEEANLQKSQALLEE
HHHHCHHHHHHHHHH
47.93-
367PhosphorylationDIEKMKETVSRFVQD
HHHHHHHHHHHHHHH
20.4726074081
369PhosphorylationEKMKETVSRFVQDAT
HHHHHHHHHHHHHCH
27.6726074081
376PhosphorylationSRFVQDATIRTKKEV
HHHHHHCHHHHHHHH
21.2026074081
379PhosphorylationVQDATIRTKKEVANT
HHHCHHHHHHHHHCC
42.4926074081
386PhosphorylationTKKEVANTKKQCNIQ
HHHHHHCCHHHHCCH
29.85-
398PhosphorylationNIQISRLTEELSALQ
CCHHHHHHHHHHHHH
26.72-
422AcetylationIERVIKEKKAVEEEL
HHHHHHHHHHHHHHH
40.827707155
423AcetylationERVIKEKKAVEEELE
HHHHHHHHHHHHHHH
59.777707163
431AcetylationAVEEELEKIYREGRG
HHHHHHHHHHHCCCC
58.637707171
431UbiquitinationAVEEELEKIYREGRG
HHHHHHHHHHHCCCC
58.63-
445TrimethylationGNESDYRKLEEMHQR
CCHHHHHHHHHHHHH
54.76-
445UbiquitinationGNESDYRKLEEMHQR
CCHHHHHHHHHHHHH
54.76-
445MethylationGNESDYRKLEEMHQR
CCHHHHHHHHHHHHH
54.7623644510
475UbiquitinationTRAENRIKQLETDSS
HHHHHHHHHHCCCCH
45.66-
494UbiquitinationRYQEMIQKLQNVLES
HHHHHHHHHHHHHHH
40.91-
521UbiquitinationLKLQQENKQLRKETE
HHHHHHHHHHHHHHH
50.38-
553PhosphorylationSTMEHEFSIKERGFE
EECCCEEEHHHCCEE
29.7524719451
569PhosphorylationQLREMEDSNRNSIVE
EHHCCCCCCCCCHHH
25.12-
573PhosphorylationMEDSNRNSIVELRHL
CCCCCCCCHHHHHHH
25.44-
586UbiquitinationHLLATQQKAANRWKE
HHHHHHHHHHHHHHH
39.38-
597AcetylationRWKEETKKLTESAEI
HHHHHHHHHHHHHHH
68.9724848985
639UbiquitinationEKVAENEKLILEHQE
HHHHHHHHHHHHHHH
53.03-
656PhosphorylationNRLQRRLSQAEERAA
HHHHHHHHHHHHHHH
26.0729255136
681PhosphorylationVQRRKAASLMNLENI
HHHHHHHHHHCCCCC
32.7723401153

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 SCLT1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCLT1_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 SCLT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SSBP_HUMANSSBP1physical
26638075
CCD22_HUMANCCDC22physical
26638075
COMD2_HUMANCOMMD2physical
26638075
DNJC7_HUMANDNAJC7physical
26638075
HSBP1_HUMANHSBP1physical
26638075
HS74L_HUMANHSPA4Lphysical
26638075
KIF23_HUMANKIF23physical
26638075
LRC45_HUMANLRRC45physical
26638075
KIZ_HUMANKIZphysical
26638075
TBK1_HUMANTBK1physical
26638075
TPP2_HUMANTPP2physical
26638075
LUZP1_HUMANLUZP1physical
26638075
BRK1_HUMANBRK1physical
26638075
HSP74_HUMANHSPA4physical
26638075
AKA12_HUMANAKAP12physical
26638075
COMD1_HUMANCOMMD1physical
26638075
RINT1_HUMANRINT1physical
26638075
CS025_HUMANC19orf25physical
26638075
WASC3_HUMANCCDC53physical
26638075
COMD8_HUMANCOMMD8physical
26638075
EXOC4_HUMANEXOC4physical
26638075
GRPE1_HUMANGRPEL1physical
26638075
ACOT9_HUMANACOT9physical
26638075
ARP2_HUMANACTR2physical
26638075
AIFM1_HUMANAIFM1physical
26638075
AP3M1_HUMANAP3M1physical
26638075
ARHG2_HUMANARHGEF2physical
26638075
ARL2_HUMANARL2physical
26638075
PRAF3_HUMANARL6IP5physical
26638075
ASSY_HUMANASS1physical
26638075
AT1A2_HUMANATP1A2physical
26638075
ATX10_HUMANATXN10physical
26638075
BCAS3_HUMANBCAS3physical
26638075
CA198_HUMANC1orf198physical
26638075
CC85C_HUMANCCDC85Cphysical
26638075
CDK16_HUMANCDK16physical
26638075
CENPH_HUMANCENPHphysical
26638075
CE170_HUMANCEP170physical
26638075
CHTOP_HUMANCHTOPphysical
26638075
CPNE3_HUMANCPNE3physical
26638075
CATB_HUMANCTSBphysical
26638075
NB5R3_HUMANCYB5R3physical
26638075
DCTN2_HUMANDCTN2physical
26638075
DD19B_HUMANDDX19Bphysical
26638075
DRG2_HUMANDRG2physical
26638075
DYHC1_HUMANDYNC1H1physical
26638075
ECHD1_HUMANECHDC1physical
26638075
4ET_HUMANEIF4ENIF1physical
26638075
ERLN2_HUMANERLIN2physical
26638075
WAC2A_HUMANFAM21Aphysical
26638075
FR1OP_HUMANFGFR1OPphysical
26638075
FSD1_HUMANFSD1physical
26638075
GALK1_HUMANGALK1physical
26638075
NIPS2_HUMANGBASphysical
26638075
GLOD4_HUMANGLOD4physical
26638075
GTPB1_HUMANGTPBP1physical
26638075
HINT1_HUMANHINT1physical
26638075
1A02_HUMANHLA-Aphysical
26638075
1A03_HUMANHLA-Aphysical
26638075
1A01_HUMANHLA-Aphysical
26638075
1A26_HUMANHLA-Aphysical
26638075
IFT20_HUMANIFT20physical
26638075
IFT27_HUMANIFT27physical
26638075
KDM1A_HUMANKDM1Aphysical
26638075
VWA8_HUMANVWA8physical
26638075
KIF3A_HUMANKIF3Aphysical
26638075
KTAP2_HUMANKRTCAP2physical
26638075
LASP1_HUMANLASP1physical
26638075
LMCD1_HUMANLMCD1physical
26638075
LYPL1_HUMANLYPLAL1physical
26638075
LZIC_HUMANLZICphysical
26638075
MISSL_HUMANMAPK1IP1Lphysical
26638075
MK09_HUMANMAPK9physical
26638075
TAU_HUMANMAPTphysical
26638075
MS18A_HUMANMIS18Aphysical
26638075
MLEC_HUMANMLECphysical
26638075
MTAP_HUMANMTAPphysical
26638075
MYEF2_HUMANMYEF2physical
26638075
SYNC_HUMANNARSphysical
26638075
NDUAD_HUMANNDUFA13physical
26638075
NEBL_HUMANNEBLphysical
26638075
NECP2_HUMANNECAP2physical
26638075
NEDD1_HUMANNEDD1physical
26638075
NMT1_HUMANNMT1physical
26638075
NSF_HUMANNSFphysical
26638075
NUP54_HUMANNUP54physical
26638075
OCRL_HUMANOCRLphysical
26638075
PAK2_HUMANPAK2physical
26638075
PALLD_HUMANPALLDphysical
26638075
PEBP1_HUMANPEBP1physical
26638075
PFD4_HUMANPFDN4physical
26638075
PF21A_HUMANPHF21Aphysical
26638075
PHLB3_HUMANPHLDB3physical
26638075
PKHA1_HUMANPLEKHA1physical
26638075
PLSI_HUMANPLS1physical
26638075
PREB_HUMANPREBphysical
26638075
AAPK1_HUMANPRKAA1physical
26638075
KAP2_HUMANPRKAR2Aphysical
26638075
PSME1_HUMANPSME1physical
26638075
PYGL_HUMANPYGLphysical
26638075
RB11B_HUMANRAB11Bphysical
26638075
RAB2A_HUMANRAB2Aphysical
26638075
RCOR1_HUMANRCOR1physical
26638075
KS6A1_HUMANRPS6KA1physical
26638075
RIR2_HUMANRRM2physical
26638075
SDCB1_HUMANSDCBPphysical
26638075
SC24B_HUMANSEC24Bphysical
26638075
SHC1_HUMANSHC1physical
26638075
SNX4_HUMANSNX4physical
26638075
SNX5_HUMANSNX5physical
26638075
SRP09_HUMANSRP9physical
26638075
SRSF2_HUMANSRSF2physical
26638075
SSRG_HUMANSSR3physical
26638075
STAU1_HUMANSTAU1physical
26638075
SWP70_HUMANSWAP70physical
26638075
TES_HUMANTESphysical
26638075
TYB10_HUMANTMSB10physical
26638075
TNR6B_HUMANTNRC6Bphysical
26638075
ASPP2_HUMANTP53BP2physical
26638075
UN45A_HUMANUNC45Aphysical
26638075
RENT1_HUMANUPF1physical
26638075
YTHD1_HUMANYTHDF1physical
26638075
ABLM1_HUMANABLIM1physical
26638075
CP131_HUMANCEP131physical
26638075
BL1S1_HUMANBLOC1S1physical
26638075
VPS51_HUMANVPS51physical
26638075
CC138_HUMANCCDC138physical
26638075
COMD3_HUMANCOMMD3physical
26638075
COMD4_HUMANCOMMD4physical
26638075
COMD6_HUMANCOMMD6physical
26638075
DCTN3_HUMANDCTN3physical
26638075
RB6I2_HUMANERC1physical
26638075
IFT57_HUMANIFT57physical
26638075
NUP58_HUMANNUPL1physical
26638075
PHAR4_HUMANPHACTR4physical
26638075
SIR2_HUMANSIRT2physical
26638075
SNAPN_HUMANSNAPINphysical
26638075
TNR6C_HUMANTNRC6Cphysical
26638075
VPS50_HUMANCCDC132physical
26638075

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 SCLT1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-681, AND MASSSPECTROMETRY.

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